Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone-Reference-Cited by-同舟云学术

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

Published:2014-05-09 Issue:6184 Volume:344 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Saio Tomohide¹,Guan Xiao¹,Rossi Paolo¹,Economou Anastassios²³,Kalodimos Charalampos G.¹

Affiliation:

1. Center for Integrative Proteomics Research and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.

2. Laboratory of Molecular Bacteriology, Rega Institute, Department of Microbiology and Immunology, KU Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.

3. Institute of Molecular Biology and Biotechnology-FORTH and Department of Biology, University of Crete, P.O. Box 1385, GR-71110, Iraklio, Crete, Greece.

Abstract

Nuclear magnetic resonance data show how molecular chaperones recognize and prevent aggregation and misfolding of unfolded proteins. [Also see Perspective by Gamerdinger and Deuerling ]

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference93 articles.

1. Molecular Chaperones and Protein Quality Control

2. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

3. Converging concepts of protein folding in vitro and in vivo

4. Protein folding in the cell: an inside story

5. Molecular chaperones in protein folding and proteostasis

Cited by 262 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. The Dynamic Triage Interplay of Hsp90 with its Chaperone Cycle and Client Binding;2024-08-12

2. Statistical Survey of Chemical and Geometric Patterns on Protein Surfaces as a Blueprint for Protein‐Mimicking Nanoparticles;Small Structures;2024-08-06

3. Bayesian reweighting of biomolecular structural ensembles using heterogeneous cryo-EM maps with the cryoENsemble method;Scientific Reports;2024-08-05

4. Ca²⁺-driven PDIA6 phase separation to ensure proinsulin quality control;2024-07-30

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