Members: External Advisory Council
Website: http://www.ucsf.edu/dbps/faculty/pages/babbitt.html
Website: http://www.chembio.umich.edu/people/banerjee.html
Website: http://www.biochem.wisc.edu/faculty/frey
Website: http://www.biochem.duke.edu/faculty/irwin-fridovich
Website: http://www.bio.brandeis.edu/faculty01/petsko.html
Website: http://hora.cpmc.columbia.edu/dept/eye/research/fac_spector.html
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Patsy
Babbitt, Ph.D. is a Professor in the Department of Biopharmacuetical
Sciences and Pharmaceutical Chemistry at UCSF and Associate
Director for Bioinformatics for the Biological and Medical
Informatics Graduate Program. She also serves as an Associate
Editor for the journal, PLoS Computational Biology. Her research
is focused on understanding how protein structures deliver
function. The laboratory has examined very distantly related
protein sequences and structures for clues to understanding
how structural scaffolds associated with some specific protein
superfamilies evolved to deliver common elements of function
as well as specificity. Results from analysis of several such
enzyme superfamilies suggest that chemistry, rather than ability
to bind a specific substrate type, is the critical determinant
in the evolution of new enzyme functions within each superfamily.
These results also suggest that new types of functional description,
tuned specifically to the explicit mappings between conserved
elements of structure and function, will be important for the
inference of function from sequence information in non-trivial
cases. The laboratory is developing a "Structure-Function
Linkage Database" to achieve this goal. The laboratory
is also interested in extending their approaches to other classes
of proteins besides enzymes and in examining the roles of superfamily
members in metabolic pathways and other cellular circuits for
clues in understanding the evolution of complex systems. 
Ruma Banerjee, Ph.D. is the Vincent Massey Collegiate Professor
of Biological Chemistry at the University of Michigan. Her
laboratory studies the coordinate regulation of methylation
and redox homeostasis at the organismal, cellular, molecular
and computational levels to elucidate key switchpoints and
the traffic lights that regulate this metabolic nexus. We also
study the gene-nutrient interactions that influence flux of
sulfur metabolites by virtue of the B-vitamin dependence of
several pathway enzymes. In addition, we are studying the co-dependence
of cell types for their energy and redox metabolic needs. Specifically,
we are interested in the mechanism of autoimmunity by which
regulatory T cells can suppress the proliferation and clonal
expansion of effector T cells following activation by antigen
presenting cells such as dendritic cells. We are interested
in how biology exploits the reactivity of radicals on the one
hand while containing it on the other to turnover substrates
to products with high fidelity. We use a variety of biophysical
(EPR spectroscopy, stopped-flow kinetics) approaches together
with biochemical analysis of patient mutations to elucidate
the mechanisms of these clinically important enzymes and understand
the biochemical basis of metabolic defects caused by their
impairments. 
Perry
Frey, Ph.D. currently holds the Robert H. Abeles chair
in Biochemistry at the University of Wisconsin, and has been
a co-director of the world renowned "Institute for Enzyme Research"
over the last two decades. Professor Frey received his B.S.
from Ohio State University and his Ph.D. from Brandeis University.
In 1999, his research endeavors earned him election to the
National Academy of Sciences. He is also a fellow in the American
Association for the Advancement of Science and the American
Academy of Arts and Sciences and has served on several editorial
boards including Biochemical and Molecular Biology Education,
Bioorganic Chemistry, and Journal of Biological Chemistry.
Among his many contributions to the understanding of enzymatic
reactions, Professor Frey was one of the pioneers in the field
of the radical-mediated enzyme reactions. He was the first
to characterize the mechanism of action of coenzyme B12 in
collaboration with the late Robert Abeles, and is the current
leader in the study of enzymes that use S-adenosylmethionine
to carry out coenzyme B12-like catalysis. In addition to the
study of many radical mediated enzyme reactions, Professor
Frey has made tremendous contributions to the understanding
of phosphoryl transfer reactions as well as the enzymology
of carbohydrate metabolism and peptide bond hydrolysis. 
Irwin
Fridovich, Ph.D. received his B.S. degree from the City College
of New York in 1951 and his Ph.D. in Biochemistry in 1955.
He has been associated with Duke University since 1956 and
has been the James B. Duke Professor of Biochemistry since
1976. He is currently an emeritus professor of biochemistry
at Duke and still has an active laboratory. He has served on
several editorial boards including Journal of Biological Chemistry,
Biochemistry, Biochemical Pharmacology, Advances in Free Radicals
in Biology and Medicine, and Biochimica Biophysica Acta, is
a member of the New York Academy of Sciences, the National
Academy of Sciences, and the American Academy of Arts and Sciences.
He was named the Senior Passano Foundation Laureate in 1987,
received the Elliot Cresson Medal from the Franklin Institute
in 1997 (a national award considered to be on par with the
Nobel Prize0 and the Anlyan Lifetime Achievement Award from
the Duke University Medical Center in 1998. His professional
memberships include Phi Beta Kappa, The American Society of
Biological Chemists and the American Academy of Arts and Sciences.
He is considered the father of the field of oxygen free-radical
biology due to the discovery in 1968 when his lab discovered
a class of enzymes called superoxide dismutases (SOD). The
SOD enzymes clean up toxic oxygen free radicals that are formed
during normal body processes which protect essential cell components
to resist cancer and slow the aging process. This discovery
led to the new field of study on free radical biology. 
Gregory
A. Petsko, PhD, is the Gyula and Katica Tauber Professor
of Biochemistry and Chemistry and Director of the Rosenstiel
Basic Medical Sciences Research Center at Brandies University.
He is also a member of the External Advisory Board for the
Nebraska Redox Biology Center. Dr. Petsko received his bachelor’s
degree in classical literature and chemistry from Princeton
University and his PhD in molecular biophysics from Oxford
University, which he attended as a Rhodes Scholar. After 13
years on the faculty at MIT, he moved to Brandeis in 1990.
He has been Director of the Rosenstiel Center since 1995. He
and his colleague Professor Dagmar Ringe pioneered the study
of enzyme mechanisms by X-ray crystallography and developed
the methods for time-resolved protein crystallography and the
analysis of protein motions. He is a winner of the Pfizer Award
of the American Chemical Society, the Max Planck Prize, and
the Fyodor Lynen Medal, among other honors. He is a member
of the National Academy of Sciences, the Institute of Medicine,
and the American Academy of Arts and Sciences. He writes a
monthly column for the journal "Genome Biology", and he and
Dr. Ringe are co-authors of the new book: "Protein Structure
and Function", published by Sinauer Press. 
Dr.
Abraham Spector, Ph.D. is the Malcolm P. Aldrich Research
Professor of Ophthalmology Emeritus and Research Director,
Director of Molecular Biology and Biochemistry Laboratory at
Columbia University College of Physicians and Surgeons Edward
S. Harkness Eye Institute. His laboratory is attempting to
develop techniques to prevent maturity onset cataract (MOC).
Since his laboratory and others established that oxidation
is an initiating or critically related factor in the development
of this disease, approaches to prevent or reduce oxidative
stress are being explored. Dr. Spector's laboratory has used
conditioned lens epithelial cell lines resistant to specific
oxidative stresses to elucidate their gene expression. Antioxidative
defense elements that may control gene expression have been
found in the vicinity of some of these genes which are now
being tested for their effectiveness by transfecting lens epithelial
cell lines and then subjecting them to different peroxide stresses.
The laboratory is also planning on preparing screening arrays
to detect mutations in key antioxidative genes in cataract
patients. Since his retirement in 2003, Dr. Spector's research
work is going forward through collaborative studies. Dr. Spector
has received many awards and honors including the Proctor Medal
of the Association for Research in Vision and Ophthalmology
in 1983, The Japanese Cooperative Cataract Research Group International
Award in 1987, the Alcon Research Institute Award in 1994 and
the National Foundation for Eye Research Kinoshita Lectureship
in 1997. 
