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Dr. Charles G. Glabe (Ph.D., University of California, Davis, 1977)
Amyloid Publications via PubMed
(NIH National Library of Medicine)
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Dr. Charles G. Glabe (Ph.D., University of California, Davis, 1977)
Amyloid Publications via PubMed
(NIH National Library of Medicine)
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peptide in Alzheimers disease and the molecular basis
for species-specific gamete recognition in sea urchin fertilization.
Recently, we have defined some of the critical biochemical properties of
A that are important for the self assembly of the
peptide into the fibrillar deposits that are characteristic of senile plaque lesions in
Alzheimers disease. We also found that the aggregated peptide is
resistant to degradation by cells and this may be an important reason why
the peptide accumulates in the disease (1) and once these aggregates have
formed inside cells it stimulates the accumulation of more A by providing a nucleus onto which other non-aggregated
A can aassemble onto, rather being degraded normally (2). Current research is focused on
how this mechanism of amyloid accumulation could contribute to
pathogenesis. Other lines of research are directed at understanding the
structure of fibrillar amyloid and how it assembles with the goal of
identifying ways of interfering with the self assembly process.
Sperm adhesion in sea urchins is mediated by the interaction of a sperm
protein, bindin, with complementary egg surface receptors. We have
cloned the genes for bindin and the receptor and we are analyzing which
parts of the molecules interact during adhesion and why the interaction
is species specific (3). The interaction of these molecules controls
which individuals are members of the same gene pool, and understanding
how bindin and its receptor interact may provide important clues about
how new species diverge during evolution.
1) Molecular Biology, Genetics, and Biochemistry
2) Email: gp-mbgb@uci.edu or call (949) 824-8145
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