J
Jenny E. Hinshaw
Researcher at National Institutes of Health
Publications - 75
Citations - 8759
Jenny E. Hinshaw is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Dynamin & GTPase. The author has an hindex of 34, co-authored 70 publications receiving 7977 citations. Previous affiliations of Jenny E. Hinshaw include Scripps Research Institute.
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Journal ArticleDOI
Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization.
Ann Cassidy-Stone,Jerry E. Chipuk,Elena Ingerman,Cheng Song,Choong Yoo,Tomomi Kuwana,Mark J. Kurth,Jared T. Shaw,Jenny E. Hinshaw,Douglas R. Green,Jodi Nunnari +10 more
TL;DR: Data indicate the mitochondrial division dynamin directly regulates mitochondrial outer membrane permeabilization independent of Drp1-mediated division, raising the interesting possibility that mdivi-1 represents a class of therapeutics for stroke, myocardial infarction, and neurodegenerative diseases.
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Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding.
TL;DR: It is shown that dynamin spontaneously self-assembles into rings and stacks of interconnected rings, comparable in dimension to the 'collars' observed at the necks of invaginated coated pits that accumulate at synaptic terminals in shibire flies.
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Dynamin and its Role in Membrane Fission
TL;DR: Purified dynamin readily self-assembles into rings or spirals, which supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission.
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Dynamin Undergoes a GTP-Dependent Conformational Change Causing Vesiculation
TL;DR: Data presented here demonstrate that purified recombinant dynamin binds to a lipid bilayer in a regular pattern to form helical tubes that constrict and vesiculate upon GTP addition, suggesting that dynamin alone is sufficient for the formation of constricted necks of coated pits and supports the hypothesis that dynamIn is the force-generating molecule responsible for membrane fission.
Journal ArticleDOI
Dnm1 forms spirals that are structurally tailored to fit mitochondria
Elena Ingerman,Edward M. Perkins,Michael Marino,Jason A. Mears,J. Michael McCaffery,Jenny E. Hinshaw,Jodi Nunnari +6 more
TL;DR: Evidence is provided that Dnm1 likely functions through self-assembly to drive the membrane constriction event that is associated with mitochondrial division and extended spirals formed, which possessed diameters greater than those of dynamin-1 spirals but whose sizes were equal to those of mitochondrial constriction sites in vivo.