X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster-Reference-Cited by-同舟云学术

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X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster

Published:2011-03 Issue:3 Volume:19 Page:397-408
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Lee Chi F.,Hauenstein Arthur V.,Fleming Jonathan K.,Gasper William C.,Engelke Valerie,Sankaran Banumathi,Bernstein Sanford I.,Huxford Tom

Funder

California Metabolic Research Foundation

National Institutes of Health

American Cancer Society

U.S. Department of Energy

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference46 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallogr. D Biol. Crystallogr.,2010

2. Comparison of ARM and HEAT protein repeats;Andrade;J. Mol. Biol.,2001

3. Electrostatics of nanosystems: application to microtubules and the ribosome;Baker;Proc. Natl. Acad. Sci. USA,2001

4. unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly;Barral;J. Cell Biol.,1998

5. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin;Barral;Science,2002

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

4. Putting AlphaFold models to work with phenix.process_predicted_model and ISOLDE;Acta Crystallographica Section D Structural Biology;2022-10-27

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