D
David L. Gard
Researcher at University of California, San Francisco
Publications - 8
Citations - 1035
David L. Gard is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Microtubule & Desmin. The author has an hindex of 7, co-authored 8 publications receiving 1011 citations.
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Journal ArticleDOI
A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end.
David L. Gard,Marc W. Kirschner +1 more
TL;DR: XMAP is phosphorylated during M-phase of both meiotic and mitotic cycles, suggesting that its activity may be regulated during the cell cycle.
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A polymer-dependent increase in phosphorylation of beta-tubulin accompanies differentiation of a mouse neuroblastoma cell line.
David L. Gard,Marc W. Kirschner +1 more
TL;DR: The observed increase in beta- tubulin phosphorylation during differentiation then reflects developmental regulation of microtubule assembly during neurite outgrowth, rather than developmentalregulation of a tubulin kinase activity.
Journal ArticleDOI
Coexistence of desmin and the fibroblastic intermediate filament subunit in muscle and nonmuscle cells: identification and comparative peptide analysis.
TL;DR: Peptide analyses of 32P-labeled intermediate filament subunits suggest that there is considerable similarity in the phosphorylation sites of these proteins, indicating that F-IFP and desmin might be evolutionally related.
Journal ArticleDOI
Microtubule assembly in cytoplasmic extracts of Xenopus oocytes and eggs.
David L. Gard,Marc W. Kirschner +1 more
TL;DR: The results suggest that there is a plus-end-specific inhibitor of microtubule assembly in the oocyte and aPlus- end-specific promoter ofAssembly in the eggs, which may serve to regulate microtubules assembly during early development in Xenopus.
Journal ArticleDOI
Cyclic AMP-modulated phosphorylation of intermediate filament proteins in cultured avian myogenic cells.
David L. Gard,Elias Lazarides +1 more
TL;DR: The data strongly suggest that in vivo phosphorylation of the intermediate filament proteins desmin and vimentin is catalyzed by the cAMP-dependent protein kinases and that suchosphorylation may be regulated during muscle differentiation.