Structural Basis for Actin Assembly, Activation of ATP Hydrolysis, and Delayed Phosphate Release (Q27665032)

https://api.crossref.org/works/10.1016/J.CELL.2010.09.034

2 August 2024

2

Takuo Yasunaga

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2 August 2024

author name string

Kenji Murakami

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Yuki Gomibuchi

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Takeyuki Wakabayashi

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Taro Q. P. Noguchi

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:20946985

2 August 2024

Kien X. Ngo

5

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:20946985

2 August 2024

Taro Q. P. Uyeda

6

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full work available at URL

2 August 2024

language of work or name

English

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publication date

15 October 2010

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http://www.cell.com/article/S0092867410010822/pdf

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https://api.elsevier.com/content/article/PII:S0092867410010822?httpAccept=text/plain

2 August 2024

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https://api.crossref.org/works/10.1016/J.CELL.2010.09.034

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143

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issue

2

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page(s)

275-87

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Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding

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A change in actin conformation associated with filament instability after Pi release.

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Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin

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Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization. Rate of dissociation of Pi from actin filaments

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Effect of Phosphates on the Structure of the Actin Filament1

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