H
Holly V. Goodson
Researcher at University of Notre Dame
Publications - 93
Citations - 6578
Holly V. Goodson is an academic researcher from University of Notre Dame. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 35, co-authored 89 publications receiving 5963 citations. Previous affiliations of Holly V. Goodson include Stanford University & University of Geneva.
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Journal ArticleDOI
Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis.
TL;DR: Phylogenetic analysis of bacterial HDAC relatives suggests that all three HDAC classes precede the evolution of histone proteins and raises the possibility that the primary activity of some "histone deacetylase" enzymes is directed against non-histone substrates.
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A standardized kinesin nomenclature.
Carolyn J. Lawrence,R. Kelly Dawe,Karen R. Christie,Don W. Cleveland,Scott C. Dawson,Sharyn A. Endow,Lawrence S.B. Goldstein,Holly V. Goodson,Nobutaka Hirokawa,Jonathon Howard,Russell L. Malmberg,J. Richard McIntosh,Harukata Miki,Timothy J. Mitchison,Yasushi Okada,Anireddy S. N. Reddy,William M. Saxton,Manfred Schliwa,Jonathan M. Scholey,Ronald D. Vale,Claire E. Walczak,Linda Wordeman +21 more
TL;DR: A standardized kinesin nomenclature based on 14 family designations is set forth, which unifies all previous phylogenies and nomenClature proposals, while allowing individual sequence names to remain the same, and for expansion to occur as new sequences are discovered.
Journal ArticleDOI
Late endosome motility depends on lipids via the small GTPase Rab7.
Cécile Lebrand,Michela Corti,Holly V. Goodson,Holly V. Goodson,Pierre Cosson,Valeria Cavalli,Nathalie Mayran,Julien Fauré,Jean Gruenberg +8 more
TL;DR: It is concluded that motor functions can be regulated by the membrane lipid composition via the Rab7 cycle, and that Rab7 in turn controls the net movement of late endocytic elements.
Journal ArticleDOI
Microtubules and Microtubule-Associated Proteins.
TL;DR: How dynamic instability is central to the assembly of many microtubules-based structures and to the robust functioning of the microtubule cytoskeleton is reviewed.
Journal ArticleDOI
Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton.
TL;DR: Results indicate that MYO3 and MYO5 encode classical myosin I proteins with overlapping functions and suggest a role for Myo3p and Myo5p in organization of the actin cytoskeleton of Saccharomyces cerevisiae.