Literature DB >> 9631288

Chaperonins.

K Braig1.   

Abstract

Molecular chaperones are essential to all living organisms. Their key role consists of mediating protein folding within the cell. Recent functional studies have provided more detailed information about the function and regulation of the chaperone network. Highlights of the past year include the crystal structure determinations of the asymmetric GroEL-GroES complex and of their isolated peptide-binding domains.

Entities:  

Mesh：

Substances：

Year:  1998        PMID： 9631288     DOI： 10.1016/s0959-440x(98)80033-x

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  10 in total

1.  Chaperonin function: folding by forced unfolding.

Authors:  M Shtilerman; G H Lorimer; S W Englander
Journal:  Science       Date:  1999-04-30       Impact factor: 47.728

2.  GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori.

Authors:  Gabriela E Bergonzelli; Dominique Granato; Raymond D Pridmore; Laure F Marvin-Guy; Dominique Donnicola; Irène E Corthésy-Theulaz
Journal:  Infect Immun       Date:  2006-01       Impact factor: 3.441

Review 3.  A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.

Authors:  Komal Fatima; Fatima Naqvi; Hooria Younas
Journal:  Cell Biochem Biophys       Date:  2021-02-25       Impact factor: 2.194

4.  An insecticidal GroEL protein with chitin binding activity from Xenorhabdus nematophila.

Authors:  Mohan Chandra Joshi; Animesh Sharma; Sashi Kant; Ajanta Birah; Gorakh Prasad Gupta; Sharik R Khan; Rakesh Bhatnagar; Nirupama Banerjee
Journal:  J Biol Chem       Date:  2008-07-30       Impact factor: 5.157

5.  Facilitating chromophore formation of engineered Ca(2+) binding green fluorescent proteins.

Authors:  Angela N Holder; April L Ellis; Jin Zou; Ning Chen; Jenny J Yang
Journal:  Arch Biochem Biophys       Date:  2009-04-07       Impact factor: 4.013

6.  Protein disorder is positively correlated with gene expression in Escherichia coli.

Authors:  Oleg Paliy; Shawn M Gargac; Yugong Cheng; Vladimir N Uversky; A Keith Dunker
Journal:  J Proteome Res       Date:  2008-05-09       Impact factor: 4.466

7.  Molecular characterization of the Corynebacterium pseudotuberculosis hsp60-hsp10 operon, and evaluation of the immune response and protective efficacy induced by hsp60 DNA vaccination in mice.

Authors:  Marcilia P Costa; John A McCulloch; Síntia S Almeida; Fernanda A Dorella; Cristina T Fonseca; Diana M Oliveira; Maria Fs Teixeira; Ewa Laskowska; Barbara Lipinska; Roberto Meyer; Ricardo W Portela; Sérgio C Oliveira; Anderson Miyoshi; Vasco Azevedo
Journal:  BMC Res Notes       Date:  2011-07-20

8.  Novel lipolytic enzymes identified from metagenomic library of deep-sea sediment.

Authors:  Jeong Ho Jeon; Jun Tae Kim; Hyun Sook Lee; Sang-Jin Kim; Sung Gyun Kang; Sang Ho Choi; Jung-Hyun Lee
Journal:  Evid Based Complement Alternat Med       Date:  2011-08-07       Impact factor: 2.629

Review 9.  GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?

Authors:  Victor V Marchenkov; Gennady V Semisotnov
Journal:  Int J Mol Sci       Date:  2009-05-12       Impact factor: 6.208

10.  Transient increase of ATP as a response to temperature up-shift in Escherichia coli.

Authors:  Jaakko Soini; Christina Falschlehner; Christina Mayer; Daniela Böhm; Stefan Weinel; Johanna Panula; Antti Vasala; Peter Neubauer
Journal:  Microb Cell Fact       Date:  2005-04-01       Impact factor: 5.328
  10 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.