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Daniel L. Purich
Researcher at University of Florida
Publications - 133
Citations - 4649
Daniel L. Purich is an academic researcher from University of Florida. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 38, co-authored 133 publications receiving 4487 citations. Previous affiliations of Daniel L. Purich include University of Florida Health Science Center & University of California, Santa Barbara.
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Journal ArticleDOI
N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility.
Scott B. Snapper,Scott B. Snapper,Fuminao Takeshima,Inés M. Antón,Inés M. Antón,Ching-Hui Liu,Ching-Hui Liu,Sheila M. Thomas,Sheila M. Thomas,Deanna Nguyen,Darryll D. Dudley,Hunter B. Fraser,Daniel L. Purich,Marco Lopez-Ilasaca,Christoph Klein,Christoph Klein,Laurie Davidson,Roderick T. Bronson,Richard C. Mulligan,Richard C. Mulligan,Frederick S. Southwick,Raif S. Geha,Raif S. Geha,Marcia B. Goldberg,Fred S. Rosen,Fred S. Rosen,John H. Hartwig,John H. Hartwig,Frederick W. Alt,Frederick W. Alt,Frederick W. Alt +30 more
TL;DR: A crucial and non-redundant role for N-WASP in murine embryogenesis and in the actin-based motility of certain pathogens but not in the general formation of actin -containing structures is implied.
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Intracellular pathogenesis of listeriosis.
TL;DR: Listeria monocytogenes, an aerobic and facultatively anaerobic gram-positive bacillus, can be readily isolated from soil, dust, fertilizer, sewage, stream water, plants, and even processed foods stored at 4°C and is present in the intestinal tract of numerous mammals, birds, fish, and crustaceans.
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Profilin promotes barbed-end actin filament assembly without lowering the critical concentration.
TL;DR: It is indicated that profilin serves as a polymerization catalyst that captures actin monomers from Thymosin-β4·Actin and ushers actin as a Profilin· actin complex onto growing barbed filament ends.
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Clamped-filament elongation model for actin-based motors.
TL;DR: A new mechanochemical model for force generation by means of affinity-modulated, clamped-filament elongation, which exploits actin's intrinsic ATPase activity to provide a simple, high-fidelity enzymatic reaction cycle for force production that does not require elongating filaments to dissociate from the motile surface.
Journal ArticleDOI
Force Generation by Cytoskeletal Filament End-Tracking Proteins
TL;DR: An additional cofactor-assisted end-tracking motor is described to account for suggested roles of cofactors in the affinity-modulated interactions, such as profilin in actin-filament end- Tracking motors and EB1 in microtubule end- tracking motors.