Mutational Analysis of the Structure and Function of the Chaperoning Domain of UNC-45B-Reference-Cited by-同舟云学术

Mutational Analysis of the Structure and Function of the Chaperoning Domain of UNC-45B

Published:2020-08 Issue:4 Volume:119 Page:780-791
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Gaziova Ivana,Moncrief Taylor,Christian Courtney J.,Villarreal Michael,Powell Simon,Lee Hubert^ORCID,Qadota Hiroshi,White Mark A.,Benian Guy M.,Oberhauser Andres F.

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Biophysics

Reference57 articles.

1. Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle;Crawford;Biophys. Rev,2011

2. Caenorhabditis elegans muscle: a genetic and molecular model for protein interactions in the heart;Benian;Circ. Res,2011

3. Paradigm shifts in cardiovascular research from Caenorhabditis elegans muscle;Epstein;Trends Cardiovasc. Med,2012

4. Folding of the striated muscle myosin motor domain;Chow;J. Biol. Chem,2002

5. Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain;Srikakulam;PLoS One,2008

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1. UNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome;Nature Communications;2024-07-25

2. Beyond Chaperoning: UCS Proteins Emerge as Regulators of Myosin-Mediated Cellular Processes;Subcellular Biochemistry;2022-12-16

3. UNC-45 assisted myosin folding depends on a conserved FX₃HY motif implicated in Freeman Sheldon Syndrome;2022-08-08

4. Mutations in conserved residues of the myosin chaperone UNC ‐45 result in both reduced stability and chaperoning activity;Protein Science;2021-09-28

5. Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity;2021-05-07