Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain (Q28588643)

Creative Commons Attribution 4.0 International

GOA release 2020-03-11

author name string

Rajani Srikakulam

series ordinal

1

1 reference

31 January 2017

Li Liu

series ordinal

2

1 reference

31 January 2017

Donald A. Winkelmann

series ordinal

3

1 reference

31 January 2017

language of work or name

English

0 references

publication date

14 May 2008

1 reference

31 January 2017

1 reference

31 January 2017

3

1 reference

31 January 2017

5

1 reference

31 January 2017

e2137

1 reference

31 January 2017

start time

14 May 2008

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

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The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans

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Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin

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Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A

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Maternal UNC-45 is involved in cytokinesis and colocalizes with non-muscle myosin in the early Caenorhabditis elegans embryo

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The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0002137

Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans

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Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

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12 December 2020

Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis

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Mutations in the motor domain modulate myosin activity and myofibril organization

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Probing myosin head structure with monoclonal antibodies

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10.1371/JOURNAL.PONE.0002137

Identifiers

DOI

1 reference

3146359

ADS bibcode

2008PLoSO...3.2137S

0 references

3146359

1 reference

1 reference

1 reference