Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis–trans Isomerase and Chaperone-like Activities-Reference-Cited by-同舟云学术

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Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis–trans Isomerase and Chaperone-like Activities

Published:2003-05 Issue:5 Volume:328 Page:1149-1160
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Suzuki Rintaro,Nagata Koji,Yumoto Fumiaki,Kawakami Masaru,Nemoto Nobuaki,Furutani Masahiro,Adachi Kyoko,Maruyama Tadashi,Tanokura Masaru

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference61 articles.

1. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis–trans isomerism of proline residues;Brandts;Biochemistry,1975

2. Prolyl isomerases;Schmid;Advan. Protein Chem.,2001

3. Peptidyl-prolyl cis–trans isomerases, a superfamily of ubiquitous folding catalysts;Göthel;Cell. Mol. Life Sci.,1999

4. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent;Ranganathan;Cell,1997

5. NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein;Sekerina;J. Mol. Biol.,2000

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