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Wenxiang Cao
Researcher at Yale University
Publications - 46
Citations - 2153
Wenxiang Cao is an academic researcher from Yale University. The author has contributed to research in topics: Protein filament & Cofilin. The author has an hindex of 25, co-authored 41 publications receiving 1864 citations. Previous affiliations of Wenxiang Cao include Northeastern University.
Papers
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Journal ArticleDOI
Actin Network Architecture Can Determine Myosin Motor Activity
Anne-Cécile Reymann,Rajaa Boujemaa-Paterski,Jean-Louis Martiel,Christophe Guérin,Wenxiang Cao,Harvey F. Chin,Enrique M. De La Cruz,Manuel Théry,Laurent Blanchoin +8 more
TL;DR: In vitro work in vitro shows that myosins can use a “selection orientation” mechanism to pull selectively on actin filaments, contract the actin network and disassemble it, and suggests how the dynamics of the cellular actin cytoskeleton can be spatially controlled by actomyosin contractility.
Journal ArticleDOI
Architecture and Connectivity Govern Actin Network Contractility.
Hajer Ennomani,Gaëlle Letort,Christophe Guérin,Jean-Louis Martiel,Wenxiang Cao,François Nédélec,Enrique M. De La Cruz,Manuel Théry,Laurent Blanchoin +8 more
TL;DR: The concept of "network connectivity" is introduced and it is shown that the contractions of distinct actin architectures are described by the same master curve when considering their degree of connectivity, making it possible to predict the dynamic response of defined actin structures to transient changes in connectivity.
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Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing
Brannon R. McCullough,Elena E. Grintsevich,Christine Chen,Hyeran Kang,Alan L. Hutchison,Arnon Henn,Wenxiang Cao,Cristian Suarez,Jean-Louis Martiel,Laurent Blanchoin,Emil Reisler,Enrique M. De La Cruz +11 more
TL;DR: Measurements support a coFilin-severing mechanism in which mechanical asymmetry promotes local stress accumulation and fragmentation at boundaries of bare and cofilin-decorated segments, analogous to failure of some nonprotein materials.
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The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
TL;DR: The presented analysis of the DbpA ATPase cycle reaction mechanism provides a rigorous kinetic and thermodynamic foundation for developing testable hypotheses regarding the functions and molecular mechanisms of DEAD-box helicases.
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Energetics and kinetics of cooperative cofilin-actin filament interactions.
TL;DR: It is suggested that the dissociation of actin-associated ions weakens intersubunit interactions in the actin filament lattice that enhance cofilin-binding site accessibility, favor cooperative binding and promote filament severing.