Re: Dr. Boyd Haley
- From: "Jan Drew" <jdrew1374@xxxxxxxxxxxxx>
- Date: Sun, 12 Jul 2009 21:26:19 -0400
"Jan Drew" <jdrew1374@xxxxxxxxxxxxx> wrote in message news:rqd6m.16074$OF1.2039@xxxxxxxxxxxxxxxxxxxxxxx
Here is what Peter Said:
A professor of chemistry deliberately talks about two different chemical
compounds (ethylmercury and methylmercury) as if they are interchangeable
and have identical properties.
That is a LIE.
Dr Haley said NO such thing.
He said:
(methylmercury, ethylmercury, thimerosal dental amalgams, Hg vapor, Hg2+,
etc.) have been reported to be extremely toxic.
He is absolutely correct.
Ethylmercury has also been shown, like methylmercury, to accumulate in the
brain and causes tissue damage methylmercury, to accumulate in the brain
and
causes tissue damage
Like methylmercury, ethylmercury is toxic to the brain and crosses the
blood-brain barrier. (9) "Higher-dose exposure to ethylmercury from
Thimerosal results in toxicity comparable to that observed after high-dose
exposure to methylmercury."
==
Fact *** Scientific Studies Concerning Mercury Dental Fillings
Prepared by the International Academy of Oral Medicine and Toxicology
www.iaomt.org 1. Mercury is a very toxic substance-- more toxic than lead,
cadmium, or arsenic. Sharma, RP; Obersteiner, EJ., Metals and Neurotoxic
Effects: Cytotoxicity of Selected Metallic Compounds on Chick Ganglia
Cultures, J Comp Pathol, 91(2):235-44 (1981). 2. At least seventeen separate
studies have confirmed that dental patients absorb a daily dose of mercury
derived from their mercury fillings. Mercury is not rendered chemically
inert in dental fillings. These studies were recently summarized in the
following paper: Richardson, G.M., Inhalation of Mercury-Contaminated
Particulate Matter by Dentists: An Overlooked Occupational Risk, Human and
Ecological Risk Assessment, 9:1519-1531 (2003). A fact *** on ADA's
website says, "Minute amounts of mercury vapor (between 1-3 micrograms per
day) may be released from amalgam under the pressure of chewing or
grinding."
http://www.ada.org/public/media/releases/0207_release01.asp 3. On average,
eighty percent of the mercury inhaled into the lungs is absorbed into the
bloodstream. Kudsk, F.N., Absorption of Mercury Vapour from the Respiratory
Tract in Man, Acta Pharmacol. et Toxicol. 23:250-262 (1965). 4. The general
population in America absorbs more mercury from dental fillings than from
any other source. Studies demonstrate that two-thirds of the mercury
absorbed by non-occupationally exposed populations is derived from amalgam
fillings. Aposhian, H.V., et al., Urinary mercury after administration of
2,3-dimercap-topropaane-1-sufonic acid: correlation with dental amalgam
score, FASEB J, vol. 6 (April 1992), pp. 2472-2476. See also,
Sandborgh-Englund, et al., Mercury in Biological Fluids After Amalgam
Removal, J Dent Res, 77(4): 615-24 (Apr. 1998); World Health Organization,
Environmental Health Criteria 118: Inorganic Mercury (1991) p. 36; Clarkson,
T.W.; et al., Biological Monitoring of Toxic Metals: The Prediction of
Intake of Mercury Vapor From Amalgams (1988) p. 256. ("The release of
mercury from dental amalgams makes the predominant contribution to human
exposure to inorganic mercury including mercury vapor in the general
population."); Lorscheider, FL; et al., Mercury Exposure from Silver Tooth
Fillings: Emerging Evidence Questions a Traditional Dental Paradigm, FASEB
J., 9:504-8 (1995). ("[D]ental amalgam tooth fillings are the major source
of Hg exposure for the general population.") 5. The mercury absorbed from
dental fillings exceeds published government toxic thresholds for mercury.
The Agency for Toxic Substances & Disease Registry minimum risk level for
mercury is 2.4 ?gs/day. (ATSDR, Toxicological Profile for Mercury.) The EPA's
reference dose for mercury is 3.84 ?gs/day. (U.S. EPA. "Health Effects
Assessment Summary Tables: FY-1997 Update" (1997).) Health Canada's
tolerable daily intake for mercury is 1.4 ugs/day. (Health Canada,
Assessment of Mercury Exposure and Risks From Dental Amalgam: Final Report,
Medical Devices Bureau, Environmental Health Directorate.) The World Health
Organization, Environmental Health Criteria 118: Inorganic Mercury (1991) p.
36, concludes that persons with mercury fillings absorb 3 to 17 micrograms
of mercury per day. This document reflects that the concensus average
estimate of 10 ?gs absorbed per day, an uptake corroborated by a more recent
daily estimate of 12 ?gs/day. Skare, I, et al., Human Exposure to Mercury
and Silver Released from Dental Amalgam Restorations, Archives of
Environmental Health, vol. 49, no. 5, pp. 384-394 (Sept.-Oct. 1994). Levels
for some individuals may be as high as 100 ?gs/day. Lorscheider, FL; et al.,
Mercury Exposure from Silver Tooth Fillings: Emerging Evidence Questions a
Traditional Dental Paradigm. FASEB J., 9:504-8 (1995). 6. A specific
no-observed-effect level (NOEL) cannot be established, meaning that no level
can be established at which mercury does not adversely affect the body.
World Health Organization, Environmental Health Criteria 118: Inorganic
Mercury (1991) p. 36. 7. Peer-reviewed studies have established that adverse
health affects have been associated with mercury vapor derived from amalgam
fillings. Summarized in: Lorscheider, FL; et al., Mercury Exposure from
Silver Tooth Fillings: Emerging Evidence Questions a Traditional Dental
Paradigm. FASEB J., 9:504-8 (1995). Ziff, M.F., Documented Clinical
Side-Effects to Dental Amalgam, Advanced Dental Research, 6:131-4, 1992. An
extensive list of diseases that have been linked to amalgam in the
peer-reviewed scientific literature, including periodontal disease (gum
disease).
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1292453&dopt=Abstract
8. Mercury is transferred from a mother to her fetus during pregnancy and is
transferred post-natally through breast milk. Vimy, M.J.; Takahashi, Y.;
Lorscheider, F.L., Maternal-fetal distribution of mercury (203 Hg) released
from dental amalgam fillings, The American Physiology Society, 0363-6119/90
R939-945.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2331037
Vimy, M.J.; Hooper, D.E.; King, W.W.; Lorscheider, F.L., Mercury from
Maternal "Silver" Tooth Fillings in Sheep and Human Breast Milk, Biological
Trace Element Research, 56, 1997.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?
cmd=Retrieve&db=PubMed&list_uids=9164660&dopt=Abstract 9. The developing
fetus and young children are disproportionately affected by mercury
exposure, because many aspects of development, particularly brain
maturation, can be disturbed by the presence of mercury. Goldman LR, Shannon
MW, Technical Report: Mercury in the Environment: Implications for
Pediatricians. American Academy of Pediatrics: Committee on Environmental
Health. Pediatrics (2001) Jul;108(1):197-205. 10. Mercury derived from
mercury fillings may impair kidney function. Boyd, N.D.; Benediktsson, H.;
Vimy, M.J.; Hooper, D.E.; Lorscheider, F.L., Mercury from dental "silver"
tooth fillings impairs sheep kidney function, The American Physiological
Society, 11: 1010-1014, 1991.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1928419&dopt=Abstract
11. Mercury has been linked to Alzheimer's Disease. Ehmann, et al., Brain
Trace Elements in Alzheimer's Disease, Neurotoxicology, 7(1):195-206 (Spring
1986); Thompson, et al., Regional Brain Trace-element Studies in Alzheimer's
Disease, Neurotoxicology, 9(1):107 (Spring 1988); Vance, Trace Element
Imbalances in Hair and Nails of Alzheimer's Disease Patients,
Neurotoxicology, 9(2):197-208 (Summer 1988); Wenstrup, et al., Trace Element
Imbalances in Isolated Subcellular Fractions of Alzheimer's Disease Brains,
Brain Res, 12;533(1): 125-31 (Nov. 1990); Cornett, et al., Imbalances of
Trace Elements Related to Oxidative Damage in Alzheimer's Disease Brain,
Neurotoxicology, 19(3):339-45 (June 1998); Mutter, Alzheimer Disease:
Mercury as a Pathogenetic Factor and
Apolipoprotein E as a Moderator, Neuroendocrinol Lett. 2004; 25(5):275-283.
( "Inorganic mercury [found in dental amalgam] may play a major role [in the
pathogenesis of Alzheimer's Disease."]) Pendergrass, J. C., et al., Mercury
Vapor Inhalation Inhibits Binding of GTP to Tubulin in Rat Brain: Similarity
to a Molecular Lesion in Alzheimer's Disease Brain. Neurotoxicology 18(2),
315-324 (1997); Pendergrass, J.C., Inhibition of Brain Tubulin-Guanosine
5'-Triphosphate Interactions by Mercury: Similarity to Observations in
Alzheimer's Diseased Brain, Metal Ions in Biological Systems V34, Mercury
and Its Effects on Environment and Biology, Chapter 16. Edited by H. Sigel
and A. Sigel (1996); Duhr, E.F., et al., HgEDTA Complex Inhibits GTP
Interactions With The E-Site of Brain b-Tubulin, Toxicology and Applied
Pharmacology 122, 273-288 (1993); Leong, CCW, et al., Retrograde
Degeneration of Neurite Membrane Structural Integrity of Nerve Growth Cones
Following In Vitro Exposure to Mercury, Neuroreport, vol.12, pps. 733-737
(2001); Duhr, E.; Pendergrass, C.; Kasarskis, E.; Slevin, J.; Haley, B.,
Hg2+ Induces GTP-Tubulin Interactions in Rat Brain Similar to Those Observed
in Alzheimer's Disease, Federation of American Societies for Experimental
Biology (FASEB). 75th Annual Meeting. Atlanta, GA 21-25 April 1991. Abstract
493; Palkiewicz, P.l; Zwiers, H.; Lorscheider, FL, ADP-Ribosilation of Brain
Neuronal Proteins Is Altered by In Vitro and In vivo Exposure to Inorganic
Mercury, Journal of Neurochemistry 62: 2049-2052, 1994.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?md=Retrieve&db=PubMed&list_uids=8158153&dopt=Abstract
12. Mercury has been linked to Parkinson's Disease. Ngim, C., Epidemiologic
Study on the Association between Body Burden Mercury Level and Idiopathic
Parkinson's Disease, Neuroepidemiology, 8:128-141 (1989). 13. Mercury
released from dental "silver" fillings provokes an increase in mercury and
antibiotic resistant bacteria in oral and intestinal flora. Summers, A.O.;
Wireman, J.; Vimy, M.J.; Lorscheider, F.L.; Marshall, B.; Levy, S.B.;
Bennett, S.; and Billard, L. "Mercury released from dental "silver" fillings
provokes an increase in mercury and antibiotic resistant bacteria in
primates oral and intestinal flora," Antimicrobial Agents and Chemotherapy,
37: 825-834, 1993;
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Ab
stract&list_uids=8280208; See also, Wireman, J.; Liebert, C.A.; Smith, T.;
and Summers, A.O., Association of mercury resistance with antibiotic
resistance in the gram-negative fecal bacteria of primates, Applied
Environmental Microbiology, 63/11: 4494-4503, Nov 1997.
http://aem.asm.org/cgi/content/abstract/63/11/4494 14. Animal studies
demonstrate that exposure to mercury vapor can induce
autoimmunity. Hultman, P; et al., Adverse Immunological Effects and
Autoimmunity Induced by Dental Amalgam and Alloy in Mice, FASEB J, 8:1183-90
(1994); Warfvinge, et al., Systemic Autoimmunity Due to Mercury Vapor
Exposure in Genetically Susceptible Mice: Dose-Response Studies, Toxicol
Appl Pharmacol, 132:299-309 (1995). 15. Mercury causes adverse health
effects in dentists and dental personnnel. Echeverria, et al.,
Neurobehavioral Effects from Exposure to Dental Amalgam HgE: New
Distinctions Between Recent Exposure and Hg Body Burden, FASEB J. 12,
971-980 (1998); Ngim, CH; et al., Chronic Neurobehavioral Effects of
Elemental Mercury in Dentists, Brit J Indust Med, 49:782-90, 1992.
Gonzalez-Ramirez, D; et al. Sodium 2,3-Dimercaptopropane-1-Sulfonate
Challenge Test for Mercury in Humans: II. Urinary Mercury, Porphyrins and
Neurobehavioral Changes of Dental Workers in Monterrey, Mexico. J Pharmocol
Exper Therap, 272(1):264-74 (1995); Echeverria, D; et al., Behavioral
Effects of Low-Level Exposure to HgE Among Dentists. Neurotoxicol Teratol,
17(2):161-8 (1995); Shapiro, I.M., et al., Neurophysiological and
neuropsychological function in mercury-exposed dentists. The Lancet 1,
1147-1150 (1982); Uzzell, B.P., et al., Chronic low-level mercury exposure
and neuropsychological functioning. J of Clin and Exper Neuropsych. 8,
581-593.
http://www.fasebj.org/cgi/content/full/12/11/971 16. The National Academy of
Sciences estimates that 60,000 newborns a year could be at risk of learning
disabilities because of mercury their mothers absorbed during pregnancy.
Mercury in the tissues of fetuses and infants (11-50 weeks of life)
correlates significantly with the number of dental amalgam fillings of the
mother. Drasch et. al., "Mercury Burden of Human Fetal and Infant Tissues,"
European Journal of Pediatrics (August 1994). 17. IAOMT's science
contributed to Germany's ban on mercury fillings for women and children.
Germany's Ministry of Health decided to ban the use of mercury fillings in
women and children in that country, following the International Academy of
Oral Medicine and Toxicology conference in Düsseldorf in 1992. Members of
the dental profession had asked for an opportunity to present evidence of
mercury fillings' safety. This conference consisted of 25 presenters and two
moderators who are experts in mercury. The peer-reviewed conclusions
supported the German ban on exposure of children and women of childbearing
age to mercury from mercury fillings.
Seven representatives of the IAOMT participated in the conference, giving
peer-reviewed presentations as follows: F.L. Lorscheider, "Mercury Exposure
from 'Silver' Dental Fillings: Current Research Findings about Uptake,
Tissue Distribution, and Pathophysiology." D.J. Pleva, "Mercury Release From
Dental Amalgam." D.C. Kennedy, "Biocompatible Restorative Dentistry,"
davidkennedy-dds@xxxxxxx B.E. Haley & J.C. Pendergrass, "Mercury-EDTA
Complex Specifically Blocks Brain b-Tubulin-GTP Interactions: Similarity to
Observations in Alzheimer's Disease," behaley@xxxxxxx M.F. Ziff, "Dental
amalgam: Status Quo, Political Aspects, International Situation." J.V. Masi,
"Corrosion of amalgams in restorative materials: the problem and the
promise," jmasi@xxxxxxxx 18. Mercury vapor released by fillings is routinely
measured in dentists' offices. The Arizona Instrument Co. manufactures and
sells a device that measures mercury vapor releases, the Jerome Mercury
Vapor Analyzer. This device is used in dental offices nationwide and
routinely records mercury vapors released from mercury fillings in the
dental offices in which it is used. http://www.azic.com/products_431.aspx
The American Dental Association recommends that its members purchase such a
device to determine their exposure to the vapor released by mercury
fillings.
http://www.ada.org/prof/resources/pubs/jada/reports/report_mercury.pdf
The Jerome Mercury Vapor Analyzer is also widely relied on by government
agencies such as Brookhaven National Laboratory and the U.S. Environmental
Protection Agency. See for example
http://www.bnl.gov/esh/shsd/ih/PDF/IH75530.pdf 19. There is more mercury in
dental fillings than in all other products sold in America. The U.S.
Environmental Protection Agency states that 55% of all mercury in commerce
today in the United States - an estimated 1,088 tons of mercury - resides in
Americans' dental fillings, which have a typical lifespan of 10 years. An
additional 34 tons of mercury is added in Americans' dental fillings every
year. United States EPA International Mercury Market Study and the Role and
Impact of US Environmental Policy 2004, referenced in Nov. 30, 2004
presentation by Linda Barr, EPA Office of Solid Waste, "EPA's Draft Mercury
Use Reduction Program." See
http://www.epa.gov/region5/air/mercury/meetings/Nov04/barr.pdf 20. The U.S.
government has never tested mercury fillings for safety. The U.S. Food and
Drug Administration (FDA) regulates the constituents of dental filling
materials, not mixed dental amalgam, the product used as a dental
restorative material. Because mercury fillings were in use prior to passage
of the 1976 Medical Devices Act, manufacturers were not required to present
any evidence of safety and effectiveness, as is required of new materials.
http://www.cdc.gov/oralhealth/factsheets/amalgam.htm See also Washington
State Department of Health, "Amalgam Dental Fillings."
http://www.doh.wa.gov/ehp/oehas/amalgam_dental_fillings_12-2003.htm
CURRICULUM VITAE
BOYD E. HALEY, Ph.D. Born 22-09-40 Greensburg, Indiana
ADDRESS: Advanced Science Technology Commercialization Center, ASTeCC
Room A057
University of Kentucky
Lexington, KY 40506-0286
Laboratory: Telephone; (606) 257-2300 ext 246 FAX; (606) 257-3040
Chemistry Office: Telephone; (606) 257-7082
EDUCATION:
Institution Year Degree/Area
Franklin College 1963 B.A./Chemistry-Physics
University of Idaho 1967 M.S./Organic Chemistry
Washington State University 1971 Ph.D./Chemistry-Biochemistry
Yale University Medical Center 1971-74 Postdoctoral Fellow
RESEARCH AND PROFESSIONAL EXPERIENCE:
1963-1964 Research Scholar, Food and Drug Administration.
1964-1966 U.S. Army Medic
1966-1967 Graduate Student, University of Idaho
1967-1971 Graduate Student, Washington State University
1971-1974 Postdoctoral Scholar, Yale University
1974-1979 Assistant Professor, Department of Biochemistry, University of
Wyoming, Laramie, WY
1979-1981 Associate Professor, Department of Biochemistry, University of
Wyoming, Laramie, WY
1981-1985 Professor, Department of Biochemistry, University of Wyoming,
Laramie, WY
1985-1997 Professor of Medicinal Chemistry, College of Pharmacy, University
of Kentucky, with
joint appointments in Biochemistry & Chemistry
1997-present Chairman & Professor, Department of Chemistry with joint
appointment in College of
Pharmacy
PROFESSIONAL ORGANIZATIONS, SOCIETIES, HONORS AND RESPONSIBILITIES
1959 President's Scholarship, Franklin College, Indiana
1962 Chi Beta Phi, Franklin College
1962 James M. Sprague Award - $400 award to outstanding
undergraduate junior majoring in science.
1963 Kennedy Scholar, Food and Drug Administration,
Washington, D.C.
1970 Sigma Xi
1975 Dreyfus Foundation Visiting Researcher, Enzyme Institute University of
Wisconsin
1977 American Society of Biological Chemists
1981 Biophysical Society
1981 Served on NIH Physiological Chemistry Study Section
1981 Research was presented as a "highlight" in NIH report on
"Cellular and Molecular Basis of Disease Program"
1984 "TOP" Professor Award, University of Wyoming
1982 Served on NIH Physiological Chemistry Study Section
1983 Served on NIH Physiological Chemistry Study Section
1985 Permanent member NIH Biomedical Sciences, Study Section
1991 Honorary Doctorate in Arts & Sciences, Franklin College
1992 Society for Neuroscience
GRANT SUPPORT
1975 - 1978 National Institutes of Health, "Application of Photoaffinity
Nucleotide Analogs", $82,000, Prinicipal Investigator
1975 Research Coordination Committee, University of Wyoming $1,800
1978 - 1981 National Institutes of Health, "Application of Photoaffinity
Nucleotide Analogs", $183,696, Prinicipal Investigator
1978 - 1981 Eleanor Roosevelt Cancer Institute Grant, $11,400
1979 - 1983 PHS Research Career Development Award, $185,000
1981 - 1986 National Institutes of Health, "Application of Photoaffinity
Nucleotide Analogs", $434,000, Prinicipal Investigator
1982 ASBC Travel Award to attend 12th IVB Congress, Perth, Australia
1983 - 1984 National Science Foundation, "Melatonin Photoaffinity Probe",
$84,000, Co-Principal Investigator
1983 - 1985 National Institutes of Health, "Epididymal Sperm Nucleotide
Binding proteins", $190,000, Co-Principal Investigator
1985 - 1988 U.S. Army Mycotoxin Photoprobes, $390,000, Co-Principal
Investigator
1986 - 1989 NIH, "Forskolin Photoaffinity Probes", $170,000, Co-Principal
Investigator
1986 - 1991 NIH, "Application of Photoaffinity Nucleotide Analogs" $781,661,
Principal Investigator
1989 - 1994 NIH, "Nucleotide-Tubulin Interactions in Alzheimer's Disease",
$405,259, Co-Prinicipal Investigator
1990 - 1996 Lexington Clinic Foundation For Medical Education and Research,
"Inhibition of Neoplastic Cell Proliferation Through Utilization of
Photoactive DNA & RNA Synthesis, $100,000, P.I.
1990 - 1993 Eli Lilly, "Development of a Diagnostic Test for Alzheimer's
Disease, $378,000, P.I.
1995 - 1997 Wallace Research Foundation, "Development of Diagnostic Tests
Using Nucleotide Photoaffinity Probes". $109,000 for two years.
1997-1998 Wallace Research Foundation, "Development of Diagnostic Tests
Using Nucleotide Photoaffinity Probes". $74,344.
1997-2000 NIH, "Application of Photoaffinity Nucleotide Analogs", $378,081,
P.I.
1997-1998 Isostent, Inc. "Photoattachment of 32P to angioplastic ballon
cathers" $52,000.
Pending NIH, "Identification of CSF proteins Related to ALS"
NIH, "Photomodification of Antibodies for Diagnostic and Therapeutic
Applications".
TEACHING EXPERIENCE
Introductory Comparative Biochemistry
General Biochemistry
Problems and Topics in Biochemistry
Mercury Toxicity: Chemistry and Biochemistry Involved
Advanced Problems and Topics in Biochemistry
Nucleic Acids and Protein Biosynthesis
Nucleotides in Regulation of Biological Phenomena
Bioenergetics
Medicinal Chemistry
Natural Products and Bio-organics
Graduate level Biochemistry, Protein Chemistry
INVITED LECTURES:
1975 - Sloan Kettering Memorial Cancer Institute, New York
thru Colorado State University (3)
1979 Albert Einstein University, New York
Hoffman-LaRoche Research Institute, Nutley, New Jersey
University of Colorado Medical School Denver (3)
University of Colorado, Boulder (2)
Yale University Medical School (2)
The Salk Institute, San Diego
University of California, Davis
Stanford University Medical School
University of California, San Diego
University of Washington, Seattle
Washington State University
Kansas State University
1979 Symposium Speaker, ASBC Meeting, Dallas, Texas
1979 Symposium Speaker, New York Academy of Sciences Meeting, New York
Department of Molecular Biology, National Jewish Hospital, Denver
University of California, Riverside
Workshop Speaker, ICN-UCLA Conference on Adenylyl Cyclase
1982 Symposium Speaker, 1982 FASEB Meeting, New Orleans
1982 Guest Lecturer and Scientist, German Cancer Research Center,
Institute of Cell and Tumor Biology, Heidelberg, West Germany,
May
1982 Centre National De La Recherche Scientifique, Laboratoire
D'Enzymologie, Gif Sur Yvette, France, June
1982 Workshop Speaker, ASBC Meeting in New Orleans (Photoprobe
utilization, sponsored by Schwarz-Mann)
1982 Symposium Speaker, Society for the Study of Reproduction, Madison
Wisconsin, August
1982 Department of Biochemistry, University of Wisconsin, November
1982 Department of Chemistry, New Mexico State University, November
1982 Department of Chemistry, University of Colorado, December
1983 Institute of Infectious Diseases, U.S. Army Medical Research
Institute, Ft. Detrick, Michigan, January
1983 Department of Biochemistry and Biophysics, Oregon State University
1983 Department of Biochemistry, Texas Health Science Center, San Antonio,
TX
1983 Department of Biochemistry, University of Mississippi Medical Center
1984 Department of Biochemistry, University of Kentucky, Lexington, KY
1985 Department of Physiology and Biophysics, Northwestern University
Medical School, Chicago, Illinois
1985 Department of Chemistry, University of Southern California, Los
Angeles, California
1985 Department of Physiology, University of Illionis at Chicago,
Chicago, Illinois
1985 Department of Biochemistry, Ohio State University, Columbus, Ohio
1985 Department of Physiology, Yale University Medical School, New
Haven, Connecticut
1986 Department of Biochemistry, Case Western University, School of
Medicine, Cleveland, Ohio
1986 Department of Biochemistry, Indiana University, School of Medicine,
Indianapolis, Indiana
1986 Department of Biochemistry, Washington University, School of
Medicine, St. Louis, Missouri
1987 Division Fermentation Products Research Division, Eli Lilly
Research Laboratories, Indianapolis, Indiana
1987 Department of Chemistry, University of South Florida, Tampa, Florida
1987 Department of Molecular Biology and Biochemistry, University of
Wyoming, Laramie, Wyoming
1988 Worcester Foundation, Shrewsbury, Massachusetts
1988 Department of Biochemistry, University of Colorado, Denver, Colorado
1988 Department of Biochemistry, University of Delaware, Newark, Delaware
1989 University of California at San Diego
1989 University of California at Los Angeles
1989 Texas College of Osteopathic Medicine, Fort Worth, Texas
1990 Wright State University, Dayton, Ohio
1990 Athena Neurosciences, S. San Francisco, California
1990 Eli Lilly & Co., Indianapolis, Indiana
1990 Connaught Laboratories, Toronto, Canada
1990 University of East Carolina Medical School, Greenville, North Carolina
1990 Hoffman-LaRoche Research Center, Nutley, New Jersey
1991 Eli Lilly & Co., Indianapolis, Indiana
1991 City University of New York, New York, New York
1991 University of Cincinnati, Cincinnati, Ohio
1991 University of Colorado, Boulder, Colorado
1991 University of Missouri at Kansas, Kansas City, Missouri
1992 Williams College at Williamsburg, Massachusetts
1992 Centre College at Danville, Kentucky
1992 University of Colorado, Boulder, Colorado
1992 Eli Lilly & Co., Indianapolis, Indiana
1992 Merck Laboratories, West Point, Pennsylvania
1993 NIH Rocky Mountain Laboratory, Hamilton, MT
1993 Intern. Acad. Oral & Medical Toxicology, Chicago, IL
1993 Univ. Tenn. at Memphis, Memphis, TN
1993 Penn State University, College Station, PN
1993 University California, Riverside, Riverside, CA
1993 Mayo Clinic, Jacksonville, FL
1993 Washington University, St. Louis, MO
1993 University of Arkansas, Little Rock, AR
1994 European Academy of Science, Otzenhausen, Germany
1994 Intern. Acad. Oral & Medical Toxicology, London, England.
1994 Great Lakes College for Advancement of Medicine, Cincinnati, OH
1995 American College for the Advancement of Medicine, Colorado Springs, CO.
1995 Pfizer Pharmaceuticals, Groton, CN
1995 Ohio State University, Dept,. Chemistry, Columbus, OH
1996 Intern. Acad. Oral & Medical Toxicology, Tuscon, AZ
1996 University of Wyoming, Laramie WY
1996 American College for the Advancement of Medicine, Colorado Springs, CO.
1997 American Academy Biological Dentistry, Carmel, CA March 7-9.
1997 International Academy of Oral and Medical Toxicology, Louisville, KY
March 14-16
1997 Washington State University, Dept. of Chemistry and Biophysics,
Pullman, WA, March 27-30.
1997 American Society of Biochemistry and Molecular Biology, Symposium talk,
August 24-28.
1997 Canadian Academy Oral and Medical Toxicology, Toronto, Canada.
September 19-21.
1997 Capital University of Integrative Medicine, Washington, DC, October
16-18
1997 American Academy Environmental Medicine, San Diego, CA, October 24-26.
1997 University of Missouri at Kansas City, Dept. Biology & Biophysics,
November 20-22.
SERVICE TO DEPARTMENT, COLLEGE AND UNIVERSITY:
1975-1979 Faculty Senate
Biological Interdepartmental Seminar Committee
University Grievance Procedure Committee
College of Agriculture Teaching Improvement Committee
College of Agriculture Academic Planning Committee
Faculty Senate Nominating Committee
Division of Biochemistry Undergraduate Teaching Committee
Division of Biochemistry Graduate Program Committee
University Research Coordination Committee
Chairman of the Graduate Committee, Biochemistry Department
1979-1982 College of Agriculture Tenure and Promotion Committee
1979 College of Agriculture Dean Search Committee
1981 Vice-President for Research Search Committee
1981 College of Human Medicine Evaluation Committee
1981-1982 Biomedical Research Funding Committee
1982 Chairman, Department of Zoology and Physiology Review Committee
1986 Research Committee College of Medicine
Ad Hoc Committee to Review Center on Aging
Ad Hoc Medical Center Research Advisory Committee
Working Group for Biotechnology Center
Center for Pharmaceutical Science and Technology Advisory Committee
College of Pharmacy Graduate Program
College of Pharmacy Research and Seminar
1987 Markey Cancer Center Internal Advisory Committee
College of Medicine Research Committee
Tobacco and Health Advisory Committee
1988 College of Pharmacy BRSG Committee, Tenure and Promotion
1989 Chairman, College of Medicine BRSG Committee
Member, Tobacco & Health Advisory Committee
Member, Markey Cancer Center Advisory Committee
1990 Chairman, College of Medicine BRSG Committee
1991-1992 Member, Intellectual Properties Committee
Member, Search Committee Cancer Center Director
Member, Cancer Center Advisory Committee
Member, Search Committee Diagnostic Radiology Chair
Member, Academic Area Committee, Biological Sciences
1993-1995 Chair, Research and Seminar Committee
Member, Appointment, Tenure and Promotion Committee
1996-1997 Chair, Graduate Program task force, College of Pharmacy
Chair, Physical Plant section, College of Pharmacy self-study
University Chemical Safety Committee
College of Medicine Academic Council
College of Pharmacy Tenure and Promotion Committee
PUBLICATIONS (REFEREED JOURNALS)
1. Haley, B. and Yount, R. Gamma-fluoradenosine Triphosphate.Synthesis,
Properties and Interaction with Myosin and Heavy Meromyosin. Biochemistry
II, 2863-2871 (1972).
2. Haley, B., Yount and Hoffman, J. Selective Inhibition of Divalent Metal
Ion Requiring ATPase Activity of Human Red Cell Ghost by an Analog of ATP.
The Physiologist 16, 333-334 (1973).
3. Haley, B. and Hoffman, J. Interactions of Photo-Affinity ATP Analog with
Cation-Stimulated ATPase Activities of Human Red Cell Ghost. Proc. Natl.
Acad. Sci. 71, 3367-3371 (1974).
4. Staros, J.V., Haley, B. and Richards, F.M. Human Erythrocytes and
Resealed Ghost: A Comparison of Membrane Topology. J. Biol. Chem. 249,
5004-5007 (1974).
5. Pomerantz, A., Rudolph, S.A., Haley, B. and Greengard, P. Photoaffinity
Labeling of a Protein Kinase from Bovine Brain with 8-Azido-adenosine-3',
5'-monophosphate. Biochemistry 14, 3852-3857 (1975).
6. Haley, B. Photoaffinity Labeling of cAMP Binding Sites of Human Red Blood
Cell Membranes. Biochemistry 14, 3852-3857 (1975).
7. Staros, J.V., Richards, F.M. and Haley, B. Photochemical Labeling of the
Cytoplasmic Surface of the Membranes of Intact Human Erythrocytes. J. Biol.
Chem. 250, 8174-8178 (1975).
8. Malkinson, A.M., Krueger, B.V., Rudolph, S.A., Casnelli, J.E., Haley, B.
and Greengard, P. Widespread Occurrence of a Specific Protein in Vertebrate
Tissues and Regulation by cAMP of its Endogenous Phosphorylation and
Dephosphorylation. Metabolism 24, 331-341 (1975).
9. Haley, B. Photoaffinity Labeling of Adenosine 3', 5'-Cyclic Monophosphate
Binding Sites. Methods in Enzymology, Jacoby and Wilchek, Editors. V 46, pp.
339-346 (1976).
10. Owens, J.R. and Haley, B.E. A Study of Adenosine 3', 5'-Cyclic
Monophosphate Binding Sites of Human Erythrocyte Membranes Using
8-Azido-adenosine-3'-5' Cyclic Monophosphate. J. Supra. Mole. Structure 5,
91-102 (1976).
11. Skare, K., Black, J.L., Pancoe, W.L. and Haley, B. Determination of the
Cellular Location of Cyclic Nucleotide Binding Sites Using
8-Azido-adenosine-3', 5'-monophosphate, A Photoaffinity Probe. Arch.
Biochem. Biophy. 180, 409-415 (1977).
12. Lau, E., Haley, B. and Barden, R. Interactions of a Photoaffinity Analog
of CoA with CoA Enzymes. Biochemistry 16, 2581-2585 (1977).
13. Owens, J.R. and Haley, B. A Study of Adenosine 3', 5'-Cyclic Nucleotide
Binding Sites of Human Erythrocyte Membranes Using 8-Azido-adenosine
3'-5'-Cyclic Monophosphate. Cell Shape and Surface Architecture: Progress in
Clinical and Biological Research 17, 65-76 (1977)
14. Lau, E.P., Haley, B. and Barden, R. The 8-Azidoadenine Analog of
S-Benzoyl (3'-dephospho) Coenzyme A-A Photoaffinity Label for Acyl CoA;
Glycine N-Acyltransferase. Biochem. Biophys. Res. Commun 76, 843-849 (1977).
15. Geahlen, R.T. and Haley, B. Interactions of a Photoaffinity Analog of
GTP with the Proteins of Microtubules. Proc. Natl. Acad. Sci. 74, 4375-4377
(1977).
16. Owens, J.R. and Haley, B. Use of Photoaffinity Nucleotide Analogs to
Determine the Mechanism of ATP Regulation of a Membrane Bound, cAMP
Activated Protein Kinase. J. Supra. Mole. Structure 9, 57-68 (1978).
17. Czarnecki, J., Geahlen, R.T. and Haley, B. Synthesis and Use of Azido
Photoaffinity Analogs of Adenine and Guanine Nucleotides. Methods in
Enzymology 56, 642-653 (1979).
18. Marcus, F. and Haley, B. Inhibition of Fructose 1,6-biphosphatase by the
Photoreactive AMP Analog, 8-Azido-AMP. J. Biol. Chem. 254, 259-261 (1979).
19. Geahlen, R., Haley, B. and Krebs, E.G. Synthesis and Use of
8-azidoguanosine 3', 5'-cyclic Monophosphate as a Photoaffinity Label for
Cyclic GMP-dependent Protein Kinase. Proc. Natl. Acad. Sci. 76, 2213-2217
(1979).
20. Geahlen, R. and Haley, B. Use of GTP Photoaffinity Probe to Resolve
Aspects of the Mechanism of Tubulin Polymerization. J. Biol. Chem. 254,
11982-11987 (1979).
21. Haley, B. Application of Photoaffinity Nucleotide Analogs to Biological
Membrane Research. Selected Aspects of Cancer-Related Protein, Carbohydrate,
Lipid and other Biochemistry, International Cancer Research Data Bank, p. 87
(1979).
22. Owens, J. and Haley, B. Mechanism of MgATP Regulation of Membrane Bound
Type I cAMP Activated Protein Kinase. Transmembrane Signaling. Alan R. Liss,
Inc. New York, New York, pp. 149-160 (1979).
23. Forrester, I.T., P.K. Schoff, B.E. Haley and R.G. Atherton.
Determination of Protein Kinase Activity in Intact Mammalian Sperm. J. of
Andrology 1, 70 (1980).
24. Briggs, F. Norman, Al-Jumaily, Walid and Haley, Boyd. Photoaffinity
Labeling of the (Ca+Mg) ATPase of Skeletal and Cardiac Sarcoplasmic
Reticulum with [32P-]-8-Azido ATP. Cell Calcium 1, 205-215 (1980).
25. Hoyer, P., Owens, J.R. and Haley, B.E. Use of Nucleotide Photoaffinity
Probes to Elucidate Molecular Mechanisms of Nucleotide Regulated Phenomena.
Annals of New York Academy of Science 346, 280-301 (1980).
26. Takemoto, D.J., B.E. Haley, J. Hanse, P. Pinbett and L.J. Takemoto.
GTPase from Rod Outer Segments: Characterization by Photoaffinity Labeling
and Tryptic Peptide Mapping. Biochem. Biophys. Res. Commun. 102, 341-347
(1981).
27. Leichtling, B.H., Coffman, D.S., Yaeger, E.S., Rickenberg, H.V.,
Al-Jumaily, W. and Haley, B.E. Occurrence of the Adenylate Cyclase
"G-Protein" in Membranes of Dictyostelium discoidium, Biochem. Biophys. Res.
Commun. 102, 1187-1195 (1981).
28. Schoff, P.K., Forester, I.T., Haley, B.E. and Atherton, R. A Study of
cAMP Binding Proteins on Intact and Distrupted Sperm Cells Using
8-Azidoadenosine-3', 5'-Cyclic Monophosphate. J. Supra. Molecular Structure
19, 1-15 (1982).
29. King, M.M., Carlson, G. and Haley, B.E. Photoaffinity-Labeling of the
Subunit of Phosphorylase Kinase by 8-Azidoadenosine-5'-Triphosphate and its
2', 3' -Dialdehyde Derivative. J. Biol. Chem. 257, 14058-14065 (1982).
30. Potter, R. and Haley, B.E. Photoaffinity Labeling of Nucleotide Binding
Sites with 8-Azidopurine Analogs. Meth. Enzymol. 91, 613-633 (1982).
31. Hoyer, P.B. and Haley, B.E. Utilization of Nucleotide Photoaffinity
Probes to Study Protein-Nucleotide Interactions in Cell Fractions. J.
Cellular Biochemistry, submitted. (1983)
32. Haley, Boyd. Development and Utilization of 8-Azidopurine Nucleotide
Photoaffinity Probes. Federation Proceedings 42, 2831-2836 (1983).
33. Khatoon, S., Atherton, R. Al-Jumaily, W. and Haley, B.E. Use of
Nucleotide Photoaffinity Probes to Study Hormone Action. Biology of
Reproduction 28, 61-73 (1983).
34. Kaiser, I.I., Kladianos, D.M., Van Kirk, E.A., and Haley, B.E.
Photoaffinity Labeling of catechol-o-methyltransferase with
8'-Azido-S-adenosylmethionine. J. Biol. Chem. 258, 1747-1751 (1983).
35. Abraham, K., Haley, B. and Modak, M. Biochemistry of Terminal
Deoxynucleotidyl Transferase: 8-Azido ATP as A Substrate Binding
Site-Directed Photoaffinity Labeling Prob. Biochemistry 22, 4197-4203
(1983).
36. Haley, B.E., Ponstingl, H. and Doenges, K.H. Photoaffinity Labeling of
Pure Tubulin Using 8-Azidoguanosine triphosphate at the b-Subunit.
Hoppe-Seylers J. Physiol. Chem. 364, 1137 (1983).
37. Woody, A.M., Vader, C.R., Woody, R.W. and Haley, B.E. Photoaffinity
Labeling of DNA-dependent RNA polymerase from E. coli with
8-azidoadenosine-5'-triphosphate. Biochemistry 23, 2843-2848 (1984).
38. Owens, J.R. and Haley, B.E. Synthesis and Utilization of
[5'-32P]-8-Azidoguanosine-3'-phosphate-5'-phosphate: Photoaffinity Studies
on Cytosolic Proteins of E. coli. J. Biol. Chem. 259, 14843-14848 (1984).
39. Pfister, K.K. , Haley, B.E. and Witman, G.B. The Photoaffinity Probe
8-azidoadenosine-5'-triphosphate. Selectivity Labels the Heavy Chain of
Chlamydomonas 12S Dynein. J. Biol. Chem. 259, 8499-8504 (1984).
40. Atherton, R.W., Khatoon, S., Schoff, P.K. and Haley, B.E. A Study of Rat
Epididymal Sperm Adenosine-3', 5'-monophosphate-dependent Protein Kinase:
Maturation Differences and Cellular Location. Biol. of Reproduction 32,
155-172 (1985).
41. McMurray, M.M., Hansen, J.S., Haley, B.E., Takemoto, D.J. and Takemoto,
L.J. Interspecies Conservation of Retinal Guanosine-5'-triphosphatase:
Characterization by Photoaffinity Labeling and Tryptic Peptide Mapping.
Biochemical Journal 225, 227-232 (1985).
42. Khatoon, S., Haley, B.E. and Atherton, R.W. A Comparative Analysis of
cAMP-dependent Protein Kinase Regulatory Subunits in Sea Urchin and Rat
Sperm. J. Andrology 6, 251-260 (1985).
43. DeBortoli, M.E., Issa, H.A., Haley, B.E. and Cho-Chung, Y.S. Elevated
Levels of p2l ras Protein in Hormone-Dependent Mammary Carcinomas of Humans
and Rodents. Bioch. Biophys. Res. Commun. 127, 699-709 (1985).
44. Evans, R., Haley, B. and Roth, D. Photoaffinity Labeling of a Viral
Induced Protein from Tobacco. J. Biol. Chem. 260, 7800-7804 (1985).
45. Nunamaker, R.A., Wilson, W.T. and Haley, B.E. Electrophoretic Detection
of Africanized Honey Bees (Apis mellifera scutellata) in Guatemala and
Mexico Based on Malate Dehydrogenase Allozyme Patterns. Journal of the
Entomological Society 57, 622-631 (1985).
46. Pfister, K.K., Haley, B.E. and Witman, G.B. Labeling of Chlamydomonas
18S Dynein Polypeptides by 8-Azidoadenosine 5'-Triphosphate, a Photoaffinity
Analog of ATP. J. Biol. Chem. 260, 12844-12850 (1985).
47. Hoyer, P.B., Fletcher, P. and Haley, B.E. Synthesis of 2',
3'-0-(2,4,6,-trinitrocyclohexadienylidine) guanosine 5'-Triphosphate and
study of its Inhibitory Properties with Adenylate Cyclase. Arch. Biochem.
Biophys. 245, 368-378 (1986).
48. Evans, R.K., Johnson, J.D. and Haley, B.E.
5'-Azido-2'-deoxyuridine-5'-triphosphate: A Novel Photoaffinity Labeling
Reagent and Tool for the Enzymatic Synthesis of Photoactive DNA. Proc. Natl.
Acad. Sci. USA. 83, pp. 5382-5386 (1986).
49. Jeganathan, A., Richardson, S.K., Mani, R.S., Haley, B.E. and Watt, D.S.
Selective Reactions of Azide-substituted a-Diazoamides with Olefins and
Alcohols Using Rhodium (II) Catalysts. J. Org. Chem. 51, 5362-5367 (1986).
50. Malkinson, A.M., Haley, B.E., Macintyre, B.E. and Buthy, M.S. Changes in
Pulmonary Adenosine Triphosphate Binding Proteins Detected by Nucleotide
Photoaffinity Labeling Following Treatment of Mice with the Tumor-Modulatory
Agent Butylated Hydroxytoluene. Cancer Res. 46, 4626-4630 (1986).
51. Evans, R.K. and Haley, B.E. Synthesis and Biological Properties of
5-Azido-2'-deoxyuridine-5'-triphosphate: A Photoactive Nucleotide Suitable
for Making Light Sensitive DNA. Biochemistry 26, 269-276 (1987).
52. Richardson, S.K., Jeganathan, A., Mani, R.S., Haley, B.E. and Watt, D.S.
Synthesis and Biological Activity of C-4 and C-15 Aryl Azide Derivatives of
Anguidine. Tetrahedron Letters 43, 2925 (1987).
53. Droms, K.A., Haley, B.E. and Malkinson, A.M. Decreased Incorporation of
the Photoaffinity Probe [g3232P]-8N3 GTP into a 45KD Protein in Lung Tumors.
Bioch. Biophys. Res. Commun. 144, 591-597 (1987).
54. Karpel, R.L., Levin, V.Y. and Haley, B.E. Photoaffinity Labeling of T4
Bacteriophage 32Protein. J.Biol.Chem. 262, 9359-66 (1987).
55. Suhadolnik, R.J., Li, Shi Wu, Sobol, Jr. R.W., and Haley, B.E. 2-and
8-Azido Photoaffinity Probes. II. Studies on the Binding Process of 2-5A
Synthetase. Biochemistry 27, 8846-8851 (1988).
56. Suhadolnik, R.J., Kariko, K., Sobol, Jr., R.W., Shi Wu, Richenbach, N.L.
and Haley, B.E. 2- and 8-Azido Photoaffinity Probes. I. Enzymatic Synthesis,
Characterization and Biological Properties of 2- and 8-Azido Photoprobes of
2-5A & Photolabeling of 2-5A Binding Proteins. Biochemistry 27, 8840-8846
(1988).
57. Droms, K.A., Haley, B.E., Smith, G.J. and Malkinson, A.M. Decreased
Photolabeling of Gsa With [a-32P]8N3-GTP in Tumorigenic Lung Epithelial Cell
Lines: Association with Decreased Hormone Responsiveness and Loss of
Contact-Inhibited Growth. Experimental Cell Research 182, 330-339 (1989).
58. Francis, B., Overmeyer, J., John, W., Marshall, E. and Haley, B.
Prevalence of Nucleoside Diphosphate Kinase Autophosphorylation in Human
Colon Carcinoma versus Normal Colon Homogenates. Molecular Carcinogenesis 2,
168-178 (1989).
59. King, S.M., Haley, B.E. and Witman, G.B. Structure of the a and b Heavy
Chains of the Outer Arm Dynein from Chlamydomonas Flagella. J. Biol. Chem.
264, 10210-10218 (1989).
60. Khatoon, S., Campbell, S.R., Haley, B.E. and Slevin, J.T. Aberrant GTP
b-Tubulin Interaction in Alzheimer's Disease. Annals of Neurology 26,
210-215 (1989).
61. Lawson, S.G., Mason, T.L., Sabin, R.D., Sloan, M.E., Drake, R.R., Haley,
B.E. and Wasserman, B.P. UDP-Glucose: (1,3)-B-Glucan Synthase from Daucas
carota L.: Characterization, Photoaffinity Labeling and Solubilization.
Journal of Plant Physiology 90, 101-108 (1989).
62. Lewis, C.T., Haley, B.E. and Carlson, G.M. Formation of an
Intramolecular Cystine Disulfide During the Reaction of 8-Azido-GTP with
Cytosolic Phosphoenolpyruvate Carboxykinase (GTP) Causes Inactivation
without Photolabeling. Biochemistry 28, 9248-9255 (1989).
63. Ho, L.T., Nie, Z.M., Mende, T.J., Richardson, S., Chavan, A.,
Kolaczkowska, E., Watt, D.S., Haley, B.E. and Ho, R.J. Modification of
Adenylate Cyclase by Photoaffinity Analogs of Forskolin. J. Second
Messengers and Phosphoproteins 12, 209-223 (1989).
64. Wasserman, B.P., Read, S.M., Frost, D.J., Mason, T.L., Drake, R.R. and
Haley, B.E. Potential use of Affinity Labels in Subunit Identification
Studies of (1,3)-b-Glucan Synthase. J.Applied Polymer Science Symposium
(Proceeding of the Tenth Cellulose Conference, Syracuse, NY). C. Schuerch
and T. Timell, Eds. 43, 827-837 (1989).
65. Drake, R.R., Evans, R.K., Wolf, M.J. and Haley, B.E. Synthesis and
Properties of 5-Azido-UDP-Glucose: Development of Photoaffinity Probes for
Nucleotide Diphosphate Sugar Binding Sites. J. Biol. Chem. 264, 11928-11933
(1989).
66. Dholakia, J.N., Francis, B.R., Haley, B.E. and Wahba, A. Photoaffinity
Labeling of the Rabbit Reticulocyte Guanine Nucleotide Exchange Factor and
Eukaryotic Initiation Factor 2 with 8-Azidopurine Nucleotides. J. Biol.
Chem. 264, 20638-20642 (1989).
67. Campbell,S., Kim, H., Doukas, M. and Haley, B. Photoaffinity Labeling of
ATP and NAD+ Binding Sites on Recombinant Human Interleukin-2. Proc. Natl.
Acad. Sci. 87, 1243-1246 (1990).
68. Kim, H. and Haley, B. Synthesis and Properties of 2-Azido-NAD+: A Study
of Interactions with Glutamate Dehydrogenase. J. Biol. Chem. 265, 3636-3641
(1990).
69. Drake, R., Palamarczyk, G., Haley, B. and Lennarz, W.J. Evidence for the
Involvement of a 35-kDa Membrane Protein in the Synthesis of
Glucosylphosphoryldolichol. Bioscience Reports 10, 61-68 (1990).
70. Marchase, R.B., Richardson, K.L., Srisomsap, C., Drake, R. and Haley,
B.E. Resolution of Phosphoglucomutase and the 62 kDa Acceptor for the
Glucosylphosphotransferase. Arch. Biochim. Biophys. 280, 122-129. (1990).
71. Salvucci, M.E. and Haley, B.E. Photoaffinity Labeling of Ribulose
Bisphosphate Carboxylase/Oxygenase With 8-Azidoadenosine 5'-Triphosphate.
Planta 181, 287-295 (1990).
72. Salvucci, M.E., Drake, R., Broadbent, K.P., Haley, B.E., Hanson, K.R.
and McHale, N.A. Identification of the 64 Kilodalton Chloroplast Stromal
Phosphoprotein as Phosphoglucomutase. Plant Physiology 93, 105-109 (1990).
73. Frost, D.J., Read, S.M., Drake, R., Haley, B.E. and Wasserman, B.P.
Identification of the UDPG Binding Polypeptide of (1,3)-b-Glucan Synthase
From A Higher Plant by Photoaffinity Labeling with 5-AzidoUDP-Glucose. J.
Biol. Chem. 265, 2162-2167 (1990).
74. Lin, F.C., Brown, R.M. Jr., Drake, R.R. and Haley, B.E. Characterization
of Cellulose Synthase Catalytic Subunit of Acetobacter xylinum Using
5-Azido-UDP-glc, A Photoaffinity Probe. J. Biol. Chem. 265, 4782-4784
(1990).
75. Salvucci, M.E., Drake, R.R., and Haley, B.E. Purification and
Photoaffinity Labeling of Sucrose Phosphate Synthase from Spinach Leaves.
Arch. Biochem. Biophys. 281, 212-218 (1990).
76. Chavan, A.J., Kim, H., Haley, B.E., and Watt, D.S. A Photoactive
Phosphonamide Derivative of GTP for the Identification of the GTP Binding
Domain of b-Tubulin. Bioconjugate Chemistry, 1, No. 5, 337-344 (1990).
77. Kwiatkowski, S., Crocker, P.J., Chavan, A.J., Nobuyuki, I., Haley, B.E.
and Watt, D.S. Thiazolidine and Thiazoline Derivatives of 3-Aryl
3-Trifluormethyl Diazirines for the Preparation of Fluorescent or
35S-Radiolabeled Photoaffinity Probes. Tetrahedron Lett, 31, 2093-2096
(1990).
78. Palamarczyk, G., Drake, R., Haley, B. and Lennarz, W.J. Evidence that
the Synthesis of Glucosylphosphoryl Dolichol in Yeast Involves a 35 kDa
Membrane Protein. Proc. Natl. Acad. Sci. 87, 2666-2670 (1990).
79. King, S., Kim, H., and Haley, B. Strategies and Reagents for
Photoaffinity Labeling of Mechanochemical Proteins. Meth. Enzymol. 196,
449-466 (1991).
80. Kim, H. and Haley, B. Identification of Peptides in the Adenine Ring
Binding Domain of Glutamate and Lactate Dehydrogenase Using 2-AzidoNAD+.
Bioconjugate Chemistry 2, 1142-147 (1991).
81. Mann, D., Haley, B., and Greenberg, R. Photoaffinity Labeling of Atrial
Natriurtic Factor Analog Atriopeptin III woith [g32P]8N3GTP. Peptide
Research 4, #2, 79-83 (1991).
82. Drake, R.R., Zimniak, P., Haley, B.E., Lester, R., Elbein, A.D. and
Radominska, A. Synthesis and Characterization of5-Azido-UDP-Glucuronic Acid.
J. Biol. Chem., 266, 23257-23260 (1991).
83. Drake, R.R., Zimniak, P., Haley, B.E., Lester, R., Elbein, A.D. and
Radominska, A. Synthesis and Characterization of5-Azido-UDP-Glucuronic Acid.
J. Biol. Chem., 266, 23257-23260 (1991).
84. Hiestand, D., Haley, B., and Kindy, M. Role of Calcium inInactivation of
Calcium/Calmodulin Dependent Protein Kinase II After Cerebral Ischemia.
Journal of the Neurological Sciences, 113, 31-37 (1992).
85. Salvucci, M., Chavan, A. and Haley, B. Identification of Peptides for
the Adenine Binding Domains of ATP and AMP in Adenylate Kinase: Isolation of
Photoaffinity Labeled Peptides by Metal Chelate Chromatography. Biochemistry
31 4479-4487 (1992).
86. Shoemaker, M., Lin, P.C., and Haley, B. Identification of the Guanine
Binding Domain Peptide of the GTP Binding Site of Glucagon. Protein Science
1, 884-891 (1992).
87. Doukas, M., Chavan, A., Gass, C., Boone, T. and Haley, B. Identification
and charaterization of a Nucleotide Binding Site on Recombinant Murine
Granulocyte/Macrophage-Colony Stimulating Factor. Bioconjugate Chemistry 3,
484-492 (1992).
88. Segal, A., West, I., Wientjes, F., Nugent, J., Chavan, A., Haley, B.,
Garcia, R., Rosen, H. and Scrace, G. Cytochrome b-245 is a Flavocytochrome
Containing FAD and the NADPH Binding Site of the Microbicidal Oxidase of
Phagocytes. Biochem. J. 284, 781-788 (1992).
89. Hammond, D., Haley, B. and Lesnaw, J. Identification and
Characterization of Serine/Threonine Protein Kinase ActivityIntrinsic to the
L Protein of Vesicular Stomatitis Virus New Jersey. Journal of General
Virology 73, 67-75 (1992)
90. Chavan, A., Nemoto, Y., Narumiya, S., Kozaki, S., and Haley, B. NAD+
Binding Site of Clostridium botulinum C3 ADP-ribosyltransferase:
Identification of Peptide in the Adenine Ring Binding Domain using 2-Azido
NAD+. J. Biol. Chem. 267, 14866-14870 (1992).
91. Gunnersen, D.J. and Haley, B.E. Detection of Glutamine Synthetase in the
Cerebrospinal Fluid of Alzheimer's Diseased Patients: A Potential Diagnostic
Biochemical Marker. Proc. Natl. Acad. Sci. USA, 89 pp. 11949-11953 (1992).
92. Shoemaker, M., and Haley, B. Identification of a Guanine Binding Domain
Peptide of the GTP Binding Site of Glutamate Dehydrogenase: Isolation with
Metal-Chelate Affinity Chromatography. Biochemistry 32, 1883-1890 (1993).
93. Churn, S.B., Sankaran, B., Haley, B.E. and Delorenzo, R.J. Ischemic
Brain Injury Selectively Alters ATP Binding of Calcium and
Calmodulin-Dependent Protein Kinase-II. Biochem. Biophys. Res. Comm. 193:3,
934-940 (1993).
94. Salvucci, M., Rajagopalan, K., Sievert, G., Haley, B. and Watt, D.
Photoaffinity Labeling of Rubisco Activase with ATP-g-benzophenone:
Identification of the ATP g-Phosphate Binding Domain J. Biol. Chem. 268,
14239-14244 (1993).
95. Rajagopalan, K., Chavan, A., Haley, B. and Watt, D. Bidentate
Cross-Linking Reagents: Non-Hydrolyzable Nucleotide Photoaffinity Probes
with Two Photoactive Groups J. Biol. Chem. 268, 14245-14253 (1993).
96. Trad, C., Chavan, A., Clemens, J., and Haley, B. Identification and
Characterization of an NADH Binding Site of Prolactin with 2-Azido-NAD+
Arch. Biochem. Biophys. 304, 58-64 (1993).
97. Chavan, A., Ensor, C., Wu, P., Haley, B. and Tai, H. Photoaffinity
Labeling of Human Placental NAD+-Linked 15-Hydroxyprostaglandin
Dehydrogenase with [a32P]-2N3NAD+: Identification of a Peptide in the
Adenine Ring Binding Domain J. Biol. Chem. 268, 16437-16442 (1993).
98. Chavan, A., Richardson, S., Kim, H., Haley, B. and Watt, D. Forskolin
Photoaffinity Probes for the Evaluation of Tubulin Binding Sites
Bioconjugate Chem. 4, 268-274 (1993).
99. Duhr, E.F., Pendergrass, J. C., Slevin, J.T., and Haley, B. HgEDTA
Complex Inhibits GTP Interactions With The E-Site of Brain b-Tubulin
Toxicology and Applied Pharmacology 122, 273-288 (1993).
100. Jayaram, B. and Haley, B. Identification of Peptides Within the Base
Binding Domains of the GTP and ATP Specific Binding Sites of Tubulin. J.
Biol. Chem. 269 (5) 3233-3242 (1994).
101. A. Chavan, B. Haley, D. Volkin, K. Marfia, A. Verticelli, M. Bruner, J.
Draper, C. Burke and R. Middaugh. Interaction of Nucleotides with Acidic
Fibroblast Growth Factor (FGF-1). Biochemistry 33,7193-7202 (1994).
102. Logan, J., Hiestand, D., Daram, P., Huang, Z., Muccio, D., Hartman, J.,
Haley, B., Cook, W., and Sorscher, E. Cystic Fibrosis Transmembrane
Conductance Regulator Mutations That Disrupt Nucleotide Binding. J. Clin.
Invest. 94, 228-236 (1994).
103. Olcott, M. and Haley, B. Identification of Two Peptides From the
ATP-Binding Domain of Creatine Kinase. Biochemistry, 33, 11935-11941 (1994).
104. Bhattacharyya, A., Chavan, A., Shuffett, M., Haley, B. and Collins, D.
Photoaffinity Labeling of Rat Liver Microsomal 5a-Reductase by
2-Azido-NADP+. Steroids 59, 634-641 (1994).
105. Salvucci, M., Chavan, A., Klein, R., Rajagopalan, K. and Haley, B.
Photoaffinity Labeling of the ATP Binding Domain of Rubisco Activase and a
Separate Domain Involved in the Activation of Ribulose-1,5-Bisphosphate
Carboxylase/Oxygenase. Biochemistry 33, 14879-14886 (1994).
106. Pendergrass, J.C. and Haley, B.E. Mercury-EDTA Complex Specifically
Blocks Brain b-Tubulin-GTP Interactions: Similarity to Observations in
Alzheimer"s Disease. pp98-105 in Status Quo and Perspective of Amalgam and
Other Dental Materials (International Symposium Proceedings ed. by L. T.
Friberg and G. N. Schrauzer) Georg Thieme Verlag, Stuttgart-New York (1995).
107. Doukas, M., Chavan, A., Gass, C., Nickel, P., Boone, T. and Haley, B.
Inhibition of GM-CSF Activity by Suramine and Suramin Analogues is
Correlated to Interaction with the GM-CSF Nucleotide Binding Site. Cancer
Research 55:5161-5163 (1995).
108. Bhattacharyya, A. K., Chavan, A.J., Haley, B., Taylor, M.F., and
Collins, D.C. Identification of the NADP(H) Binding Site of Rat Liver
Microsomal 5a-Reductase (Isozyme-1): Purification of a Photolabeled Peptide
Corresponding to the Adenine Binding Domain. Biochemistry 34, 3663-3669
(1995)
109. Chavan, A., Gass, C., Haley, B., Boone, T. and Doukas, M. A.
Identification of N-Terminus Peptide of Human Granulocyte/Macrophage Colony
Stimulating Factor as the Site of Nucleotide Interaction. Biochem. Biophys.
Res. Commun. 208,#1 390-396 (1995).
110. Shoemaker, M., and Haley, B. Identification of the Adenine Binding
Domain Peptides of the ADP Binding Site of Glutamate Dehydrogenase.
Bioconjugate Chemistry 7, 302-310 (1996).
111. Rajagopalan, K., Pavlinkova, G., Levy, S., Pokkuluri, R., Schiffer, M.,
Haley, B., and Kohler, H. Novel Unconventional Binding Site in the Variable
Region of Immunoglobulins. Proc. Natl. Acad. Sci. 93, 6019-6024 (1996).
112. Pavlinkova, G., Rajagopalan, K., Muller, S., Chavan, A., Sievert, G.,
Lou, D., O'Tolle, C., Haley, B., and Kohler, H. Site-Specific
Photobiotinylation of Immunoglobins, Fragments and Light Chain Dimers. J.
Immunological Methods 201, 77-88 (1997).
113. Pendergrass, J.C. and Haley, B.E. Inhibition of Brain Tubulin-Guanosine
5'-Triphosphate Interactions by Mercury: Similarity to Observations in
Alzheimer's Diseased Brain. In Metal Ions in Biological Systems V34, Mercury
and Its Effects on Environment and Biology, Chapter 16. Edited by H. Sigel
and A. Sigel. Marcel Dekker, Inc. 270 Madison Ave., N.Y., N.Y. 10016 (1996).
114. McGuire, M., Carroll, L. J., Yankie, L., Thrall, S. H.,
Dunaway-Mariano, D., Hertzberg, O., Jayaram, B. and Haley, B. Determination
of the Nucleotide Binding Site within Clostridium symbiosum Pyruvate
Phosphate Dikinase by Photoaffinity Labeling, Site-Directed Mutagenesis, and
Structural Analysis. Biochemistry 35, 8544-8552 (1996).
115. Kohler, H., Pavlinkova, G., and Haley, B. Immunoglobulin Nucleotide
Binding Site: A Possible Superantigen Receptor. In Human B Cell
Superantigens, edited by Moncei Zouali, Chapter 13, pp 189-194 (1996).
116. Sankaran, B., Chavan, A. and Haley, B. Identification of Adenine
Binding Domain Peptides of the NADP+ Active Site within Porcine Heart
NADP+-Dependent Isocitrate Dehydrogenase. Biochemistry 35, 13501-13510
(1996).
117. Sankaran, B., Clemens, J., and Haley, B. A Comparison of Changes in
Nucleotide-Protein Interactions in the Striatal, Hippocampus and Paramedian
Cortex After Cerebral Ischemia and Reperfusion: Correlations to Regional
Vulnerability. Molecular Brain Research 47, 237-250 (1997).
118. Hensley, K., Cole, P. ,Aksenov, M., Aksenova, M., Bummer, P.E., Carney,
J.M., Haley, B.E., and Butterfield, D.A. Oxidatively-Induced Structural
Alteration of Glutamine Synthetase Assessed by Analysis of Spin Label
Incorporation Kinetics. J. of Neurochemistry 68, 2451-2457 (1997).
119. Pendergrass, J. C., Haley, B.E., Vimy, M. J., Winfield, S.A. and
Lorscheider, F.L. Mercury Vapor Inhalation Inhibits Binding of GTP to
Tubulin in Rat Brain: Similarity to a Molecular Lesion in Alzheimer's
Disease Brain. Neurotoxicology 18(2), 315-324 (1997).
120. Olcott, M.C. and Haley, B.E. Identification of an Adenine-nucleotide
Binding Site on Interferon-a2. Eur. J. Biochem. 247/3, 762-769 (1997).
121. David, S., Shoemaker, M., and Haley, B. Abnormal Properties of Creatine
kinase in Alzheimer's Disease Brain: Correlation of Reduced Enzyme Activity
and Active Site Photolabeling with Aberrant Cytosol-Membrane Partitioning.
Molecular Brain Research accepted (1997).
RESEARCH PAPERS (ABSTRACTS)
1. Haley, B. and Yount, R. Inhibition of Myosin by Gamma-Fluoroadenosine
Triphosphate, Abstracts Pacific Slope Biochemistry Conference, Seattle,
Washington (1969).
2. Haley, B. Synthesis of Photoaffinity Analogs of ATP and AMP and Their Use
as Membrane Probes. Mount Sinai School of Medicine & Rockefeller University
School of Medicine, (Invited paper)(1974)
3. Haley, B. and Hoffman, J. Photoaffinity Labeling of ATP Binding Sites of
Human Erythrocyte Membrane, FASEB Meeting, Atlantic City (1974).
4. Haley, B. Photoaffinity Labeling of cAMP Binding Sites of Human
Erythrocyte Membranes, Abstracts 1975 ICN-UCLA Biochemistry Conference on
Energy Transduction (1975).
5. Haley, B. Photoaffinity Labeling of Human Red Cell Membrane Binding Sites
Using 8-Azido-cAMP, Abstracts 1975 FASEB Meeting, Atlantic City (1975).
6. Owens, J.R. and Haley, B. A Study of cAMP Stimulated Phosphorylation and
cAMP Binding Sites of Human Erythrocyte Membrane Proteins using
32P-8-Azido-cAMP, a Photoaffinity Probe. ICN-UCLA Conference on Molecular
and Cellular Biology (1975).
7. Owens, J. and Haley, B. Properties of cAMP Binding Proteins of the Human
Erythrocyte Membrane, Abstracts 1976 ICN-UCLA Biochemistry Conference on
Cell Shape and Surface Architecture (1976).
8. Seery, V. and Haley, B. Activation of Glycogen Phosphorylase by
8-Azidoadenosine 5'-Monophosphate, Abstracts ASBC Meeting, San Francisco
(1976).
9. Waterson, R. and Haley, B. Interactions of Photoaffinity AMP and ATP
Analogs with E. coli Aminoacyl-tRNA Synthetases, Abstracts ASBC Meeting, San
Francisco (1976).
10. Fletcher, P., Kaltenback, C. and Haley, B. Photoaffinity Labeling of
Adenosine-3', 5' Cyclic Monophosphate Binding Sites in Ovine Corpus Lutea.
Abstracts, Society for the Study of Reproduction, Philadelphia, Pennsylvania
(1976).
11. Geahlen, R.L., Moore, V.G., Kaiser, I.I. and Haley, B.E. Synthesis and
Biological Activity of Photoactive 8-Azidoguanosine Nucleotide Analogs.
Abstracts, 1977 FASEB Meeting, Chicago (1977).
12. Owens, J. and Haley, B. Mechanism of Action of Membrane Bound cAMP
Activated Protein Kinase. 1977 ICN-UCLA Conference on Molecular Aspects of
Membrane Transport (1977).
13. Hahn, G.L., Metz, K.W., Atherton, R.W. and Haley, B.E. Labeling of a
Surface Cyclic-AMP Receptor Site on Rabbit Sperm Utilizing a Photoaffinity
Analog. American Society of Andrology, Nashville, Tennessee (1978).
14. Owens, J. and Haley, B.E. Mechanism of Mg-ATP Regulation of Membrane
Bound Type 1 cAMP Activated Protein Kinase, Transmembrane Signaling,
ICN-UCLA Symposia (1978).
15. Czarnecki, J. and Haley, B. Interaction of
8-Azido-2'-Deoxyadenosine-5'-Triphosphate, A Photoaffinity Label, with a
DNA-Dependent DNA Polymerase. ASBC Meeting, Atlanta (1978).
16. Hoyer, P.B. and Haley, B.E. Partial Characterization of Rat Brain cAMP
Binding Proteins: Cellular Location, Molecular Weights, and Nucleotide
Effects. 1979 ICN-UCLA Conference on Covalent Modification of Proteins
(1979).
17. Schoff, P., Atherton, R.W. and Haley, B.E. A Study of the cAMP Receptor
Proteins of Human Ejaculated Sperm Using a Photoaffinity Analog. 1979 Soc.
Study of Reproduction (1979).
18. Briggs, F.N., Al-Jumaily, W. and Haley, B.E. Interactions of the
Photoaffinity Analog of ATP, 8-Azido-ATP, 8-Azido-ATP, with Vesicles of
Skeletal and Cardiac Sarcoplasmic Reticulum (1980).
19. Hoyer, P.B. and Haley, B.E. Use of Photoaffinity Probes to Study cAMP
Dependent Membrane Partitioning of ATP Binding and Phosphorylated Proteins
(1980).
20. Owens, J.R. and Haley, B.E. Photoaffinity Labeling of Guanosine
Polyphosphate (Magic Spot) Binding Proteins. Fed. Proc. 40, St. Louis,
Missouri (1981).
21. Khatoon, S., Schoff, P.L., Haley, B.E. and Atherton, R.W. A Comparative
Study of Sperm cAMP Dependent Protein Kinases by a Photoaffinity Analysis.
American Society of Andrology Meeting, New Orleans, Louisiana (1981).
22. Woody, A-Young, M., Vader, C.R., Reisbig, R.R., Woody, R.W. and Haley,
B.E. Photoaffinity Labeling of DNA-dependent RNA Polymerase from E. coli
with 8-Azido-Adenosine 5'-Triphosphate. Biophysical Society Meeting, Denver,
Colorado (1981).
23. Schoff, P.K., Khatoon, S., Haley, B.E. and Atherton, R.W. Protein
Kinases: Control by Ca and cAMP in Rat Caudal Epididymal Sperm. American
Society of Andrology Meeting, New Orleans, Louisiana (1981).
24. Kaiser, I.I., Moore, V.G., Van Kirk, E. and Haley, B.E. The Enzymatic
Synthesis of an 8-Azido-Adenosine-Containing Analog of
OS-adenosylmethionine. Fed. Proc. 40, St. Louis, Missouri (1981).
25. Hoyer, P.B. Phosphorylation of the cAMP Dependent Protein Kinases
Catalytic Subunit Inhibits Phosphorylation of Endogenous Substrates. Fed.
Proc. 40, St. Louis, Missouri (1981).
26. Haley, B.E. and Al-Jumaily, W. Utilization of Nucleotide Probes to Study
Adenylyl Cyclase in Biological Membranes. 1982 UCLA Symposium: "Evolution of
Hormone-Receptor Systems", Squaw Valley, California (1982).
27. Khatoon, S., Haley, B.E. and Atherton, R.W. A Photolabeling Analysis of
the cAMP-Dependent Protein Kinase Regulatory Subunits in Sea Urchin and Rat
Sperm. Society for the Study of Reproduction, Madison, Wisconsin (1982).
28. Owens, J.R. and Haley, B.E. Labeling of Nucleotide Binding Sites in E.
coli and B. subtilis with "Magic Spot" Photoaffinity Analogs. FASEB Meeting,
New Orleans, Louisiana (1982).
29. Owens, M., Haley, B.E. and Barden, R.E. Photolibile Multisubstrate
Analogues as Photoaffinity Probes for Adenylate Kinase: Synthesis and
Kinetic Studies. FASEB Meeting, New Orleans, Louisiana (1982).
30. Haley, Boyd. Utilization of Nucleotide Photoaffinity Probes to Study
Adenylyl Cyclase and Protein Kinases in Biological Systems. 12th
International Congress of Biochemistry. Perth, Australia (1982).
31. Khatoon, S., Atherton, R. and Haley, B. Studies on Rat Epidimal Sperm
Phosphorylating Systems Using Nucleotide Photoaffinity Analogs. ASBC
Meetings, San Francisco, California (1983).
32. Haley, B., Hoyer, P. and Middaugh, C.R. Studies on Adenylyl Cyclase
Using Fluorescent and Photoaffinity GTP Analogs. ASBC Meeting, San
Francisco, California (1983).
33. Owens, M., Barden, R. and Haley, B. Labeling of the Active Site of
Adenylate Kinase Using a Multisubstrate Photoaffinity Probe. ASBC Meetings,
San Francisco, California (1983).
34. Owens, J., Woody, A.-J. and Haley, B. Photoaffinity Labeling of RNA
Polymerase with [5'-32P] 8-Azidoguanosine-3'-phosphate-5'-phosphate, A
Transcriptional Inhibitor. ASBC Meeting, San Francisco, California (1983).
35. Middlebrook, J.L., Evans, G.R., Smith, L.A. and Haley, B.E. Interaction
of Azido-ATP with Botulinum Neurotoxin. 3rd International Congress on Cell
Biology (1984).
36. Khatoon, S. and Haley, B.E. Autophosphorylation of cAMP Dependent
Protein Kinase Catalytic Subunit Inhibits its Ability to Bind Nucleotide
Triphosphates. ASBC Meeting, St. Louis, Missouri (1984).
37. Karpel, R.L., Levin, V.Y. and Haley, B.E. Photoaffinity Labeling of a
Nucleic Acid Helix-Destabilizing Protein. USLA Symposia on Protein
Structure, Folding and Design (1985).
38. Haley, B.E., Evans, R.K. and Roth, D.A. Studies on Viral Induced
Nucleotide Binding Proteins in Tobacco. ASBC Meetings, Anaheim, California
(1985).
39. Evans, R.K., Johnson, J.D. and Haley, B.E. Synthesis of
5-azido-2'-deoxyuridine-5'-triphosphate: Enzymatic Incorporation into DNA.
ASBC Meetings, Anaheim, California (1985).
40. Duhr, E., Leppla, S.H. and Haley, B. Studies on Bacillus anthracis and
Staphyloccoccal Protein Toxins Using Nucleotide Photoaffinity Analogs. ASBC
Meetings, Anaheim, California (1985).
41. Francis, B., Mackenzie, III, C.W. and Haley, B.E. Photoaffinity Labeling
and Phosphorylation Studies of cGMP Dependent Protein Kinase. ASBC Meetings,
Anaheim, California (1985).
42. Toner, J.A., Haley, B. and Taylor, S.J. Scoichiometric Autophosphoration
of the Catalytic Subunit of cAMP-dependent Protein Kinase II. ASBC Meetings,
Anaheim, California (1985).
43. Khatoon, S., Haley, B. and Coleman, M.S. Interactions of Deoxynucleotide
Photoaffinity Analog with Terminal Deoxynucleotidyl Transferase (TdT). ASBC
Meetings, Anaheim, California (1985).
44. Shi, Q.H., Ruiz, J., Ho, R.J. and Haley, B.E. Evaluation of Inhibition
of Forskolin-activated Adenylate Cyclase by GDP or TNP-GTP. ASBC Meetings,
Anaheim, California (1985).
45. Khatoon, S., Beach, C., Haley, B. and Coleman, M.S. Active Site
Characterization of Terminal Deoxynucleotidyl Transferase (TdT):
Modification with Deoxynucleotide Photoaffinity Analogs. ASBC Meetings,
Washington, D.C. (1986).
46. Karpel, R.L., Levin, V.Y. and Haley, B. Characterization of a
Crosslinked Nucleic Acid: Helix Destabilizing Protein Complex. ASBC
Meetings, Washington, D.C. (1986).
47. Khatoon, S., Haley, B.E. and Slevin, J.T. Decreased Availability of the
Exchangeable GTP Binding Site of the b-Subunit of Brain Tubulin in
Alzheimer's Disease. AAN Scientific Program, New York, New York (1987).
48. Lewis, C., Haddad, R., Carlson, G.M. and Haley, B.E. Photoaffinity
Labeling of Phosphoenolpyruvate Carboxykinase (GTP) by 8-Azido-GTP. ASBC
Meetings, Philadelphia, Pennsylvania (1987).
49. Kim, H., Ponstingl, H. and Haley, B.E. Identification of the Guanosine
Interacting Peptide of the GTP Binding Site of b-Tubulin Using 8N3GTP. ASBC
Meetings, Philadelphia, Pennsylvania (1987).
50. Khatoon, S., Slevin, J.T. and Haley, B.E. GTP Binding to the b-Subunit
of Tubulin is Greatly Reduced in Alzheimers Disease. ASBC Meetings,
Philadelphia, Pennsylvania (1987).
51. Campbell, S.R., Khatoon, S., Haley, B.E. and Slevin, J.T. Inability of
Brain Microtubules in Alzheimers Disease to Cold-Depolymerize. Neuroscience
Meeting, New Orleans, Louisiana (1987).
52. Ho, L.T., Nie, Z.M., Mende, T.J., Richardson, S., Lee, H., Watt, D.S.,
Haley, B.E. and Ho, R.J. Photoaffinity-Analogs of Forskolin and their
Effects on Adenylate Cyclase. APS Meeting, San Diego, California (1987).
53. Li, S.W., Sobol, R.W., Kariko, K., Haley, B.E. and Suhadolnik, R.J.
Photoaffinity Labeling of 2-5A Synthetase by 2- and 8-azido-ATP. FASEB
Meeting, Las Vegas, Nevada (1988).
54. Francis, B.R. and Haley, B.E. Regulation of Protein Phosphorylation in
Colon Carcinoma Homogenates by Metabolic Products of Glycolysis and IP3.
FASEB Meeting, Las Vegas, Nevada (1988).
55. Drake, R.R., Evans, R.K. and Haley, B.E. Synthesis and Properties of
5-azido-UDP-glucose, an Active Site-directed Photoaffinity Probe. FASEB
Meeting, Las Vegas, Nevada (1988).
56. Nie, Z.M., Ho, L.T., Lee, D.S., Bowdan, J.B., Mende, T.M., Watt, D.S.,
Haley, B.E. and Ho, R.J. Photoaffinity Analogs of Adenylate Cyclase
Activator, Forskolin. FASEB Meeting, Las Vegas, Nevada (1988).
57. Salvucci, M.E. and Haley, B.E. Photoaffinity Labeling of the Large and
Small Subunits of Ribulose Bisphosphate Carboxylase with 8-Azido-ATP. Plant
Physiology (1988).
58. Droms, K.A., Smith, G.J., Malkinson, A.M. and Haley, B.E. Gsa and Lung
Epithelial Cell Growth. American Association for Cancer Research Meeting,
Miami, Florida (1988).
59. Lewis, C.T., Haley, B.E. and Carlson, G.M. Evidence for Formation of a
Transient Sulfenamide Bond During Photoaffinity Labeling by 8-Azido-GTP of
Phosphoenolpyruvate Carboxykinase. American Chemical Society, San Diego,
California (1988).
60. Chavan, A.J., Watt, A.J., Kim, H. and Haley, B.E. Synthesis and
Application of GTP Phosphonamide Photoaffinity Reagents. American Chemical
Society Meeting, Los Angeles, California (1988).
61. Lee, H., Watt, D.S., Kim, H. and Haley, B.E. Synthesis and Application
of a Forskolin Photoaffinity Probe to a Tubulin Binding Site. American
Chemical Society Meeting, Atlanta, Georgia (1988).
62. Drake, R.R. and Haley, B.E. Covalent Labeling of Phosphoglucomutase by
[32P]UDP-GLC AND [32P]5N3UDP-GLC. ASBMB Meeting, Los Angeles, California
(1989).
63. Watt, D.S., Lee, H.-W., Kim, H.-T. and Haley, B.E. Detection of a
Forskolin Binding Site Using a Photoaffinity Probe. ASBMB Meeting, Los
Angeles, California (1989).
64. Dholakia, J.N., Francis, B.R., Haley, B.E. and Wahba, A.J.
Characterization of the Guanine Nucleotide Exchange Factor as a GTP Binding
Protein. ASBMB Meeting, Los Angeles, California (1989).
65. Parker, K.W., Drake, R.R., Haley, B.E. and Salvucci, M.E. Photoaffinity
Labeling of Tobacco Subcellular Fractions with [32P]-Azido-UDP-Glucose.
ASPP/CSPP Toronto, Ontario, Canada (1989).
66. Campbell, S., Kim, H., Haley, B.E. and Doukas, M. Photoaffinity Labeling
of Nucleotide Binding Sites on Interleukin-2. Second International Workshop
on Cytokines. Hilton Head, North Carolina (1989).
67. Wasserman, B.P., Frost, D.J., Wu, A., Read, S.M., Drake, R.R. and Haley,
B.E. Identification of the UDPG-Binding Polypeptide of (1,3)-b-Glucan
Synthase of Higher Plants by Photoaffinity Labeling with 5-Azido-UDPG. Fifth
Cell Wall Meeting, Edinburgh (1989).
68. Gunnersen, D.J., Slevin, J.T. and Haley, B.E. Novel Proteins in
Alzheimer's Diseased Brain May be Due to Pathological Modification of
b-Tubulin. ASBMB Meeting, New Orleans, Louisiana (1990).
69. Drake, R., Hiestand, D., Sharp, J. and Haley, B. Nucleotide Binding and
Autophosphorylation Properties of IL-1b. ASBMB Meeting, New Orleans,
Louisiana (1990).
70. Kim, H. and Haley, B. Identification of Active Site Peptides of
Glutamate and Lactate Dehydrogenases by Photoaffinity Labeling. ASBMB
Meeting, New Orleans, Louisiana (1990).
71. Lin, P.P-C., Shoemaker, M.T. and Haley, B.E. Observation of a Specific
Nucleotide Binding Site on Glucagon by Photoaffinity Labeling with
Azido-GTP. ASBMB Meeting, New Orleans, Louisiana (1990).
72. Olcott, M. and Haley, B. Identification of a Nucleotide Binding Site on
Interferon-a. ASBMB Meeting, New Orleans, Louisiana (1990).
73. Campbell, S., Kim, H., Hiestand, D. and Haley, B. Photoaffinity Labeling
of Nucleotide Binding Sites on Tumor Necrosis Factor. ASBMB Meeting, New
Orleans, Louisiana (1990).
74. Duhr, E., Slevin, J. and Haley, B. Low Level HgEDTA Complex Specifically
Blocks [32P]8N3GTP Interaction with Human Brain Tubulin. ASBMB Meeting, New
Orleans, Louisiana (1990).
75. Mann, D.M., Haley, B.E. and Greenberg, R.N. GTP Binding to Atrial
Natriuretic Factor as Determined by Photoaffinity Labeling with
[g-32P]8N3GTP. ASBMB Meeting, New Orleans, Louisiana (1990).
76. Droms, K.A., Haley, B.E. and Malkinson, A.M. Mechanism of Decreased
b-Adrenergic Stimulation of Adenylate Cyclase in Neoplastic Mouse Lung
Epithelial Cell Lines. FASEB Meeting, Washington, D.C. (1990).
77. Manning, E.L., Kim, H., Haley, B.E. and Jacobson, M.K. Utilization of
2-Azido-NAD for Studies of ADP-Ribose Polymer Metabolism. ASBMB Meeting, New
Orleans, Louisiana (1990).
78. Watt, D.S., Chavan, A.J., Kim, H.-T. and Haley, B.E. A Novel GTP
Photoaffinity Probe for the Identification of the Exchangeable GTP-Binding
Domain in Tubulin. ASBMB Meeting, New Orleans, Louisiana (1990).
79. Doukas, M., Chavan, A.J., Campbell, S. and Haley, B.E.Photolabeling of
the Granulocyte/Macrophage-Colony StimulatingFactor (GM-CSF) Eliminates Its
Biological Activity. FASEBMeeting, Atlanta, Georgia (1991), FASEB J., 5 (4),
A424.
80. Duhr, E., Pendergrass, C., Kasarskis, E., Slevin, J. and Haley, B.E.
Hg2+ Induces GTP-Tubulin Interactions in Rat Brain Similar to those Observed
in Alzheimer's Disease. FASEB Meeting, Atlanta, Georgia (1991), FASEB J., 5,
(4), A456.
81. Trad, C.H., Chavan, A.J. and Haley, B.E. Detection of an NAD+/NADH
Binding Site on Prolactin Using [32P]2N3NAD+. FASEB Meeting, Atlanta,
Georgia (1991), FASEB J., 5, (4), A795.
82. Shoemaker, M.T., Jayaram, B. and Haley, B.E. Glucagon-GTP Interactions:
Identification of a Binding Domain Peptide. FASEB Meeting, Atlanta, Georgia
(1991), FASEB J., 5, (4), A795.
83. Jayaram, B., Sankaran, B., Watt, D.S. and Haley, B.E. Synthesis and Use
of Radiolabeled, Non-Hydrolyzable GTP Photoaffinity Probes. FASEB Meeting,
Atlanta, Georgia (1991), FASEB J., 5, (6), A1508.
84. Campbell, S., Doukas, M. and Haley, B.E. Identification of the
[a-32P]8-Azido-ATP Photolabeled Peptides of rhIL-2. FASEB Meeting, Atlanta,
Georgia (1991), FASEB J., 5, (6), A1521.
85. Gunnersen, D.J., Slevin, J.T. and Haley, B.E. Preliminary
Characterization of a Novel Alzheimer's Disease Associated Protein. FASEB
Meeting, Atlanta, Georgia (1991), FASEB J., 5, (4), A456.
86. Hiestand, D.M., Haley, B.E. and Kindy, M.S. Nucleotide Binding and
Phosphorylation Properties of Proteins from Control and Ischemic Brains.
FASEB Meeting, Atlanta, Georgia (1991), FASEB J., 5, (4), A458.
87. Rajagopalan, K., Chavan, A.J., Haley, B.E. and Watt, D.S. Bidentate GTP
Photoaffinity Probes: Cross-Linking Agents with Two Photoactive Groups.
FASEB Meeting, Atlanta, Georgia (1991), FASEB J., 5, (6), A1522.
88. Bradley, M., Olcott, M. and Haley, B. Characterizaton of the ATP Binding
Domain of Creatine Kinase Using Photoaffinity Probes. ASBMB Meeting,
Houston, Texas (1992)
89. Doukas, M., Chavan, A., Boone, T., Gass, C. and Haley, B. Nucleotide
Binding Site of Granulocyte/Macrophage-Colony Stimulating Factor (GM-CSF) is
Preserved Across Species Barriers. ASH Annual Meeting, Anaheim, California
(1992)
90. Sankaran, B., Haley, B. and Clemens, J. Identification of Changes in
Nucleotide Interacting Proteins in Control vs Ischemic Rat Brains. Society
for Neuroscience Meeting, Anaheim, California (1992)
91. Gunnersen, D., and Haley, B. Detection of Glutamine Synthetase in the
CSF of Alzheimer's Diseased Patients: A Potential Diagnostic Biochemical
Marker. Society for Neuroscience Meeting, Anaheim, California (1992)
92. Hiestand, D., Cha]van, A. and Haley, B. Identification of a Nucleotide
Binding Domain on Recombinant Human IL-1b. FASEB Meeting, New Orleans,
Louisiana (1993)
93. Olcott, M., Haley, B. Identification of Two Peptides in the Adenine
Binding Domain of Creatine Kinase Using Immobilized Al3+ Affinity
Chromatography. FASEB Meeting, New Orleans, Louisiana (1993)
94. Rajagopalan, K., Chavan, A., Haley, B., and Watt, D. Synthesis and
Application of Bidentate Nucleotide Photoaffinity Cross-linking Reagents
with Two Photoactive Groups. FASEB Meeting, New Orleans, Louisiana (1993)
95. Shoemaker, M., and Haley, B. Identification of the Adenine Binding
Domain of ADP Regulatory Site within GDH. FASEB Meeting, New Orleans,
Louisiana (1993)
96. Chavan, A., Doukas, M., Gass, C., Haley, B. and Boone, T. Covalent
Linkage of [a32P]ATP or [g32P]ATP to rmGM-CSF in the Absence of Light. FASEB
Meeting, New Orleans, Louisiana (1993)
97. Doukas, M., Chavan, A., Gass, C., Boone, T. and Haley, B. Nucleotide
Binding Sites of Human and Murine Granulocyte/Macrophage-Colony Stimulating
Factor (GM-CSF) are Identical. FASEB Meeting, New Orleans, Louisiana (1993)
98. Pendergrass, J., Duhr, E., Slevin, J., and Haley, B. meso-2,
3-Dimercaptosuccinic (DMSA) Acid to both Alzheimer's Diseased (AD) Brains
and to HgEDTA Treated Control Brains. FASEB Meeting, New Orleans, Louisiana
(1993)
99. Sorscher, E.J., Daram, P., Hiestand, D., Huang, Z., Peng, S., Muccio,
D., Haley, B., and Logan, J. Mutations in CFTR Nucleotide Binding Domains
(NBD's) Disrupt Trinitrophemyl ATP Binding. FASEB Meeting, New Orleans,
Louisiana (1993).
100. Logan, J., Hiestand, D., Huang, Z., Muccio, D., Haley, B., and
Sorscher, E. 3-Isobutyl-1-methylxanthine (IBMX) Blocks Binding of ATP
Analogs to the CFTR First Nucleotide Binding Domain (NBD-1). FASEB Meeting,
New Orleans, Louisana (1993).
101. Rajagopalan, K., Chavan, A.J., Cockle, S., Haley, B. and Watt, D.
Identification of ATP-g-Phosphate Binding Domain of Pertussis Toxin By
Photoaffinity Labeling. FASEB Meeting, New Orleans, Louisiana (1993).
102. Kasarskis, E, Haley, B., and Gunnerson, D. GTP-binding Proteins in
Amyotrophic Lateral Sclerosis Cerebrospinal Fluid. Abstracts American
Neurological Assoc., Ann. Neurology 34, 297 (1993).
103. Pendergrass, J., Duhr, E., Haley, B., and Slevin, J. Effect of Chronic
Ingestion of Micromolar HgCl2 and HgEDTA Complex on Rodent Neuronal
Cytoskeleton. Society for Neuroscience 23rd Annual Meeting, Abstracts, p193,
#81.6 Washington, DC (1993).
104. Haley, B., Duhr, E., and David, S. Identification of an
8-Hydroxyguanosine Nucleotide in CSF that Blocks GTP Binding to b-Tubulin.
Abstracts Annual Meeting Soc. For Neuroscience (1994).
105. Shoemaker, M., and Haley, B. Creatine Kinase is Generally Depleted and
Inactive in Alzheimer's Diseased Brain. ASBMB Abstracts, FASEB J. 8, #7
(1994)
106. Sankaran, B., and Haley, B. Identification of the Coenzyme Binding Site
of NADP+-Dependent Isocitrate Dehydrogenase. ASBMB Abstracts, FASEB J. 8, #7
(1994).
107. Hiestand, D., Sorscher, E., and Haley, B. Use of 2N3ATP to Identify the
Site of ATP Interaction on Nucleotide Binding Domain-2 From the Cystic
Fibrosis Transmembrane Conductance Regulator. ASBMB Abstracts, FASEB J. 8,
#7 (1994).
108. Hiestand, D., Sorscher, E., Huang, Z., Wang, Y., and Haley, B. Use of
2N3ATP to Identify the Site of ATP Interaction on Nucleotide Binding
Domain-2 From the Cystic Fibrosis Transmembrane Conductance Regulator.
Abstracts 8th Annual N. American Cystic Fibrosis Conference, Orlando, FL
(1994).
109. Kohler, H., Pavlinkova, G., Rajagopalan, K., Wang, H-T., Chatterjee,
S., and Haley, B. Specific Photoaffinity Labeling Locus on Antibodies: Use
for Chelation, Protein Conjugation and Gene Delivery. Abstracts Annual
meeting Exper. Biol., Anaheim, CA, FASEB J. 8, #4 pA236 (1994)
110. Lorscheider, F., Vimy, M., Pendergrass, J., and Haley, B. Toxicity of
Ionic Mercury and Elemental Mercury Vapor on Brain Neuronal protein
Metabolism. Abstracts 12th Intern. Neurotoxicology Conf. Univ. Arkansas Med.
Ctr., Hot Springs, AR (1994).
111. Lorscheider, F., Vimy, M., Pendergrass, J. and Haley, B. Mercury Vapor
Exposure Inhibits Tubulin Binding to GTP in Rat Brain: A Molecular Lesion
Also Present in Alzheimer's Diseased Brain. Expt. Biol. Annual Meeting
Abstracts, Atlanta, GA, FASEB J. 9, #4 pA663 (1995)
112. Chavan, A., Doukas, M., Gass, C., Haley, B., and Collins, D. Inhibition
of Nucleotide Binding to Recombinant GM-CSF by Suramin and it's Analogs
Correlates with Inhibition of Biological Activity. Annual ASBMB Meeting, San
Francisco, CA FASEB J. 9, #6 pA1417 (1995).
113. Lorscheider, F., Vimy, M., Pendergrass, J., and Haley, B. Mercury Vapor
Inhalation inhibits Binding of GTP to Tubulin in Rat Brain: A Molecular
Lesion Present in Alzheimer's Diseased Brain. 25th Annual meeting of Society
for Neuroscience, San Diego, CA Soc. Neurosci. 21, #3, p1723 (1995).
114. Hicks, R., Pendergrass, J. and Haley, B. Identification of the Guanine
Binding Domain Peptide of Myelin Basic Protein Using [32P]8N3GTP. Abstracts
PGSRM Meeting, Madison, WI (1995).
115. Pendergrass, J., Israel, M., and Haley, B. Use of Photoaffinity
Labeling and 2-D Electrophoresis to Identify Changes in Nucleotide Binding
Proteins in Brain and CSF: A Potential Diagnostic Technique for Neurological
Diseases. Annual Meeting AAPS Miami, FL (1995)
116. Hicks, R., Pendergrass, J., and Haley, B. Identification of the Guanine
Binding Domain peptide of Myelin Basic Protein Using [32P]8N3GTP. Annual
Meeting AAPS Miami, Fl. (1995).
117. Pendergrass, J., Isarel, M., Borths, C., Chavan, A., and haley, B.
Detection of Multiple Cytodines and Growth Factors in Human CSF Using
Photochemistry. 6th International Congress on Cell Biology & 36th Amer. Soc.
Cell Biol. Annual Meeting, San Francisco, CA (1996).
118. Kohler, H., Pavlinkova, G., Sievert, G., Freeman, J., and Haley, B.
Tumor-Targeting of Oligonucleotides Using Affinity Linked Antibodies.
Abstracts FASEB Meeting, New Orleans, Louisiana, FASEB J. 10, #6 pA1350
(1996).
119. Chavan, A., Doukas, M., Gass, C., Boone, T., and Haley, B. Probing
Anti-Growth Factor Activity of Suramin Using Azido Nucleotides. 6th
International Congress on Cell Biology & 36th Amer. Soc. Cell Biol. Annual
Meeting, San Francisco, CA (1996).
120. Doukas, M., Chavan, A., Gass, C., Boone, T., Nickel, P., and Haley, B.
Suramin and Suramin Analog Activity Against Leukemic Cell Lines: Correlation
to Interaction with the Granulocyte/Macrophage Colony Stimulating Factor
Nucleotide-Binding Site. Abstracts AACR Meeting (1996).
Boyd Haley
CURRICULUM VITAE
The basic research interest of our laboratory centers on biochemical and
biomedical problems involving control at the molecular level. Specifically,
we are most interested in biological systems regulated by protein-nucleotide
interactions where the bioenergetics involved are expressed through
site-specific nucleotide binding of high affinity or through protein
substrate phosphorylation. Our approach to the study of this general
phenomenon is to synthesize novel nucleotide analogs that are photoactive or
fluorescent, or both. The analogs are then used to study various aspects of
protein-nucleotide interactions which regulate enzyme activity. Analogs used
may be modifications of the commonly known nucleotides such as ATP, cAMP,
GTP, dUTP, NAD+, UDP-Glc, etc. or probes of the more unusual nucleotides
such as the proposed alarmones guanosine-3'-phosphate-5'phosphate (magic
spot compounds) and diadenosine-P1, P4-tetraphosphate.
These nucleotide analogs are used to study a wide variety of enzymes that
either use or are regulated by nucleotides including cyclases, kinases, and
polymerases. Certain of these probes have proven useful in the study of the
differences between normal and diseased tissues as observed through changes
in nucleotide binding proteins. Alzheimer's disease, Amyotrophic Lateral
Sclerosis and Multiple Sclerosis are some of the diseases we are currently
investigating. I am currently interested in the several low molecular weight
nucleotide binding proteins that we have detected in human cerebrolspinal
fluid that seem to vary in presence and concentration with various disease
states. One of these is aFGF (binds ATP) and another is myelin basic protein
(binds GTP, is phosphorylated and ADP-ribosylated).
We have also done studies that implicate low levels of Hg as being capable
of being involved in certain neurological diseases. This is based on our
observation that Hg2+ chelated with EDTA is a more potent inhibitor of
tubulin polymerization than is free Hg2+. Addition of Hg-EDTA complex to
non-demented human brain homogenates renders the photolabeling profile to be
identical to that of Alzheimer's diseased brain homogenates. Further,
exposure of rats to low level mercury vapor causes a great increase in rat
brain mercury levels and a marked decrease in brain tubulin photolabeling as
is observed in Alzheimer's diseased brain. These results support the
contention that mercury vapor would exacerbate the symptoms associated with
Alzheimer's disease. This is a major concern since substantial levels of
mercury vapor is known to be released from dental amalgams and EDTA is a
common food additive.
Additionally, we have found that several of the large polypeptide hormones
(or biological response modifiers) have nucleotide binding sites. These
include GM-CSF, aFGF,IL-1, IL-2, Interferon-alpha, TNF (tumor necrosis
factor), glucagon and GH (growth hormone). We therefore feel that the
transmembrane signaling effected by these proteins may, at least be
expressed partially by an activity associated with the "hormone" itself.
This is supported by the observation that IL-1 and IL-2 also
autophosphorylate using ATP.
.
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