Area:
cytoskeleton, neurofilaments, biomarkers, antibodies
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High-probability grants
According to our matching algorithm, Gerry Shaw is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1985 — 1991 |
Shaw, Gerry |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Neurofilament Modifications: Extent and Significance
Neurofilaments are major, but nonetheless poorly understood, neuron specific 10nm filaments. They are composed of three subunit proteins usually referred to as NF-1, NF-M and NF-H. NF-M and NF-H differ from other characterized 10 nm filament proteins in that they contain long heavily phosphorylated carboxyterminal extensions. These carboxyterminal regions have recently been shown to contain two distinct segments, probably corresponding to two types of functional domain. The first contains multiple repeats of 5-8 amino acid segments each containing the sequence lysine-serine-proline, and is here referred to as KSP segment. The second domain, at the extreme carboxyterminus, has a high content of lysine and glutamic acid, and is called the KE segment. In the present proposal I wish to test two hypotheses I have proposed which assign functions to these unusual segments. These hypotheses are; 1. That some or all of the KE segments are responsible for a strong interaction which binds neurofilaments together into bundles. i will search for such an interaction using isolated KE domains and fusion proteins containing KE segments. Detection of a binding interaction will be followed by characterization of his interaction in detail and proof that this interaction is actually responsible for filament bundling in vivo. 2. That phosphorylation of the KSP regions of the NF-H and NF-M molecules is responsible for modulating the spacing of neurofilaments from one another in bundles. Evidence for or against this hypothesis will not detract from the importance of identifying and characterizing the KSP kinase activity, which may phosphorylate other axonal proteins besides neurofilaments and appears to change in activity following neuronal injury and in various disease states. I will make use of the new sequence data to isolate this enzyme. In summary the studies proposed will increase our understanding of the function of two unusual regions of the neurofilament molecules, and will characterize a kinase activity of great potential importance in recovery from injury and in the maintenance of differences between axons and dendrites.
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1 |
1989 — 1995 |
Shaw, Gerry |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Neurofilament Modifications--Extent and Significance
Neurofilaments (NF) are the major structures of many parts of the nervous system, but are rather poorly understood in functional terms. We plan to further elucidate the function and expression of these proteins by; 1. Producing recombinant fusion proteins containing defined NF sequences and also a panel of highly specific epitope-mapped antibodies to all known NF subunits for use in a host of studies including but not limited to those described in this proposal. 2. To use the novel antibodies to study CNS microanatomy, now concentrating on the detailed distribution and co-distributions of the triplet proteins, alpha-internexin, peripherin and vimentin and the definitive identification and ultrastructural characterization of neurons and fibre tracts containing particular NF protein combinations. These studies will provide novel cell-type specific markers and perhaps suggest relationships between particular NF patterns and particular neuron classes. 3. Search for and characterize NF-associated proteins in detail and try to understand their function, with particular emphasis of proteins that may be involved in NF cross-linking, phosphorylation, transport and interaction with other neuronal constituents. We can now perform these studies much more efficiently thanks to our newly developed computer program, called FINDER, which allows us to identify proteins rapidly and cheaply from their amino acid composition. These studies will throw light on several aspects of NF function. Since NF accumulations and modifications are seen in a variety of damage and disease states, understanding more about NF will undoubtedly have medical impact. Finally, this work is already generating a battery of novel antibodies, constructs and methods which have been and will continue to be made freely available for as yet unimagined studies in future.
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1 |