Literature DB >> 8603749

The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum.

X Chen1, D Easton, H J Oh, D S Lee-Yoon, X Liu, J Subjeck.   

Abstract

The existence of a family of unusually large and highly diverged hsp70-like proteins (the hsp110/SSE family) has recently been described. The 170 kDa glucose regulated stress protein (grp170) is a retained endoplasmic reticulum glycoprotein that may be involved in immunoglobulin folding and/or assembly. We describe here the cloning of the cDNA for grp170 and show that it, like hsp110, is a large and highly diverged hsp70-like polypeptide which shares specific features with hsp70 (the dnaK family) and the hsp110/SSE family, while also differing from both. Grp170 contains an ATP binding domain and binds ATP, it possesses a carboxyl terminal NDEL sequence, and its mRNA is anoxia inducible.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 8603749     DOI: 10.1016/0014-5793(96)00011-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  26 in total

1.  LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.

Authors:  J R Tyson; C J Stirling
Journal:  EMBO J       Date:  2000-12-01       Impact factor: 11.598

Review 2.  All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.

Authors:  Lance Shaner; Kevin A Morano
Journal:  Cell Stress Chaperones       Date:  2007       Impact factor: 3.667

Review 3.  Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential.

Authors:  Amy S Lee
Journal:  Nat Rev Cancer       Date:  2014-04       Impact factor: 60.716

4.  Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

Authors:  Zdravko Dragovic; Sarah A Broadley; Yasuhito Shomura; Andreas Bracher; F Ulrich Hartl
Journal:  EMBO J       Date:  2006-05-11       Impact factor: 11.598

5.  Tumour secreted grp170 chaperones full-length protein substrates and induces an adaptive anti-tumour immune response in vivo.

Authors:  Hilal Arnouk; Evan R Zynda; Xiang-Yang Wang; Bonnie L Hylander; Masoud H Manjili; Elizabeth A Repasky; John R Subjeck; A Latif Kazim
Journal:  Int J Hyperthermia       Date:  2010       Impact factor: 3.914

6.  Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.

Authors:  B L Lin; J S Wang; H C Liu; R W Chen; Y Meyer; A Barakat; M Delseny
Journal:  Cell Stress Chaperones       Date:  2001-07       Impact factor: 3.667

Review 7.  How antibodies fold.

Authors:  Matthias J Feige; Linda M Hendershot; Johannes Buchner
Journal:  Trends Biochem Sci       Date:  2009-12-21       Impact factor: 13.807

8.  From stress protein biochemistry to novel immunotherapeutics.

Authors:  Stuart K Calderwood
Journal:  Int J Hyperthermia       Date:  2013-08       Impact factor: 3.914

Review 9.  High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy.

Authors:  Xiang-Yang Wang; John R Subjeck
Journal:  Int J Hyperthermia       Date:  2013-07-05       Impact factor: 3.914

10.  Discovering genes associated with dormancy in the monogonont rotifer Brachionus plicatilis.

Authors:  Nadav Y Denekamp; Michael A S Thorne; Melody S Clark; Michael Kube; Richard Reinhardt; Esther Lubzens
Journal:  BMC Genomics       Date:  2009-03-13       Impact factor: 3.969

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.