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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.

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Actin Network Architecture Can Determine Myosin Motor Activity

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.
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Architecture and Connectivity Govern Actin Network Contractility.

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

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.