Cryoelectron Microscopy Analysis of Small Heat Shock Protein 16.5 (Hsp16.5) Complexes with T4 Lysozyme Reveals the Structural Basis of Multimode Binding-Reference-Cited by-同舟云学术

Cryoelectron Microscopy Analysis of Small Heat Shock Protein 16.5 (Hsp16.5) Complexes with T4 Lysozyme Reveals the Structural Basis of Multimode Binding

Published:2013-02 Issue:7 Volume:288 Page:4819-4830
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shi Jian,Koteiche Hanane A.,McDonald Ezelle T.,Fox Tara L.,Stewart Phoebe L.,Mchaourab Hassane S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

1. Small heat shock proteins and α-crystallins. Dynamic proteins with flexible functions;Basha;Trends Biochem. Sci.,2012

2. Structure and mechanism of protein stability sensors. Chaperone activity of small heat shock proteins;McHaourab;Biochemistry,2009

3. Characterization of a new, dominant V124E mutation in the mouse αA-crystallin-encoding gene;Graw;Invest. Ophthalmol. Vis. Sci.,2001

4. Autosomal dominant congenital cataract associated with a missense mutation in the human α crystallin gene CRYAA;Litt;Hum. Mol. Genet.,1998

5. A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy;Vicart;Nat. Genet.,1998

Cited by 44 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Catchers of folding gone awry: a tale of small heat shock proteins;Trends in Biochemical Sciences;2024-09

2. Chaperone regulation of biomolecular condensates;Frontiers in Biophysics;2024-05-07

3. Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM;2024-03-27

4. Cryo-EM structure of a 16.5-kDa small heat-shock protein from Methanocaldococcus jannaschii;International Journal of Biological Macromolecules;2024-02

5. HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface;International Journal of Molecular Sciences;2023-12-29