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Arp2/3 complex: Advances on the inner workings of a molecular machine

Journal

CELL
Volume 107, Issue 6, Pages 703-705

Publisher

CELL PRESS
DOI: 10.1016/S0092-8674(01)00605-5

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Funding

  1. NIGMS NIH HHS [R01 GM038542-13, R01 GM047337-10, R01 GM038542] Funding Source: Medline

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Several new papers report progress on the structure and function of Arp2/3 complex. A crystal structure, a cryo-EM structure, and a reconstitution of the complex from subunits have been reported. New results also address the nucleation mechanism and the role of bound nucleotide.

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