Literature DB >> 15777275

Protein folding assisted by chaperones.

Júlio C Borges1, Carlos H I Ramos.   

Abstract

Molecular chaperones are one of the most important cell defense mechanisms against protein aggregation and misfolding. These specialized proteins bind non-native states of other proteins and assist them in reaching a correctly folded and functional conformation. Chaperones also participate in protein translocation by membranes, in the stabilization of unstable protein conformers and regulatory factors, in the delivery of substrates for proteolysis and in the recovery of proteins from aggregates.

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Year:  2005        PMID: 15777275     DOI: 10.2174/0929866053587165

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  30 in total

1.  Spectroscopic and thermodynamic properties of recombinant heat shock protein A6 from Camelus dromedarius.

Authors:  Ajamaluddin Malik; Abuzar Haroon; Haseeb Jagirdar; Abdulrahman M Alsenaidy; Mohamed Elrobh; Wajahatullah Khan; Mohammed S Alanazi; Mohammad D Bazzi
Journal:  Eur Biophys J       Date:  2014-11-14       Impact factor: 1.733

2.  Proteomic study of calpeptin-induced differentiation on calpain-interacting proteins of C2C12 myoblast.

Authors:  N K Singh; S Shiwani; I H Hwang
Journal:  In Vitro Cell Dev Biol Anim       Date:  2012-01-21       Impact factor: 2.416

3.  Analysis of stress responsive genes induced by single-walled carbon nanotubes in BJ Foreskin cells.

Authors:  Shubhashish Sarkar; Chidananda Sharma; Rajeshwari Yog; Adaikkappan Periakaruppan; Olufisayo Jejelowo; Renard Thomas; Enrique V Barrera; Allison C Rice-Ficht; Bobby L Wilson; Govindarajan T Ramesh
Journal:  J Nanosci Nanotechnol       Date:  2007-02

4.  The folding competence of HIV-1 Tat mediated by interaction with TAR RNA.

Authors:  Jung Min Kim; Hee Sun Choi; Baik Lin Seong
Journal:  RNA Biol       Date:  2017-04-18       Impact factor: 4.652

Review 5.  A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.

Authors:  Júlio C Borges; Thiago V Seraphim; Paulo R Dores-Silva; Leandro R S Barbosa
Journal:  Biophys Rev       Date:  2016-03-04

Review 6.  Role of the heat shock protein family in bone metabolism.

Authors:  Kai Hang; Chenyi Ye; Erman Chen; Wei Zhang; Deting Xue; Zhijun Pan
Journal:  Cell Stress Chaperones       Date:  2018-09-05       Impact factor: 3.667

7.  Metabolites of Lactobacillus plantarum 2142 prevent oxidative stress-induced overexpression of proinflammatory cytokines in IPEC-J2 cell line.

Authors:  Erzsebet Paszti-Gere; Krisztina Szeker; Edina Csibrik-Nemeth; Rita Csizinszky; Andras Marosi; Orsolya Palocz; Orsolya Farkas; Peter Galfi
Journal:  Inflammation       Date:  2012-08       Impact factor: 4.092

Review 8.  Bacterial Heat Shock Protein Activity.

Authors:  Farajollah Maleki; Afra Khosravi; Ahmad Nasser; Hamid Taghinejad; Mitra Azizian
Journal:  J Clin Diagn Res       Date:  2016-03-01

9.  Cell-surface HSP70 associates with thrombomodulin in endothelial cells.

Authors:  Gabriela Venturini; Ana I S Moretti; Thaís L S Araujo; Leonardo Y Tanaka; Alexandre Costa Pereira; Francisco R M Laurindo
Journal:  Cell Stress Chaperones       Date:  2019-01-15       Impact factor: 3.667

10.  The microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro.

Authors:  Lindsay M Faircloth; Perry F Churchill; Guy A Caldwell; Kim A Caldwell
Journal:  Cell Stress Chaperones       Date:  2008-07-15       Impact factor: 3.667

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