Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain (Q36787617)

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12 February 2020

title

Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain (English)

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12 February 2020

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7

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author name string

Ewa Prochniewicz

1

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12 February 2020

Anaëlle Pierre

2

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12 February 2020

Brannon R McCullough

3

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12 February 2020

Harvey F Chin

4

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12 February 2020

Wenxiang Cao

5

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12 February 2020

Lauren P Saunders

6

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12 February 2020

Enrique M De La Cruz

8

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12 February 2020

language of work or name

English

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publication date

6 September 2011

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Journal of Molecular Biology

12 February 2020

published in

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volume

413

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issue

3

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12 February 2020

page(s)

584-592

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describes a project that uses

12 February 2020

ImageJ

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3633491/fullTextXML

inferred from PubMed Central ID database lookup

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Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics

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Thermodynamics of nucleotide binding to actomyosin V and VI: a positive heat capacity change accompanies strong ADP binding.

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The structure of the myosin VI motor reveals the mechanism of directionality reversal

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Mechanism of nucleotide binding to actomyosin VI: evidence for allosteric head-head communication

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The unique insert in myosin VI is a structural calcium-calmodulin binding site.

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Myosin isoforms show unique conformations in the actin-bound state

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

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Identifiers

DOI

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12 February 2020

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12 February 2020

PubMed publication ID

21910998

1 reference