Literature DB >> 7788290

Thioredoxin--a fold for all reasons.

J L Martin1.   

Abstract

The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common property of interacting with cysteine-containing substrates.

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Year:  1995        PMID： 7788290     DOI： 10.1016/s0969-2126(01)00154-x

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  221 in total

1.  Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.

Authors:  J W Cave; H S Cho; A M Batchelder; H Yokota; R Kim; D E Wemmer
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

2.  On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.

Authors:  L Debarbieux; J Beckwith
Journal:  J Bacteriol       Date:  2000-02       Impact factor: 3.490

Review 3.  Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

Authors:  Robert B Freedman; Peter Klappa; Lloyd W Ruddock
Journal:  EMBO Rep       Date:  2002-02       Impact factor: 8.807

4.  Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins.

Authors:  Jérémy Couturier; Elke Ströher; Angela-Nadia Albetel; Thomas Roret; Meenakumari Muthuramalingam; Lionel Tarrago; Thorsten Seidel; Pascale Tsan; Jean-Pierre Jacquot; Michael K Johnson; Karl-Josef Dietz; Claude Didierjean; Nicolas Rouhier
Journal:  J Biol Chem       Date:  2011-06-01       Impact factor: 5.157

5.  Optimizing doped libraries by using genetic algorithms.

Authors:  D Tomandl; A Schober; A Schwienhorst
Journal:  J Comput Aided Mol Des       Date:  1997-01       Impact factor: 3.686

6.  Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases.

Authors:  Jiann-Kae Luo; Judith A T Hornby; Louise A Wallace; Jihong Chen; Richard N Armstrong; Heini W Dirr
Journal:  Protein Sci       Date:  2002-09       Impact factor: 6.725

7.  Non-animal origin of animal thioredoxin reductases: implications for selenocysteine evolution and evolution of protein function through carboxy-terminal extensions.

Authors:  Sergey V Novoselov; Vadim N Gladyshev
Journal:  Protein Sci       Date:  2003-02       Impact factor: 6.725

8.  CxxS: fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase function.

Authors:  Dmitri E Fomenko; Vadim N Gladyshev
Journal:  Protein Sci       Date:  2002-10       Impact factor: 6.725

9.  The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.

Authors:  Peter W Haebel; David Goldstone; Federico Katzen; Jon Beckwith; Peter Metcalf
Journal:  EMBO J       Date:  2002-09-16       Impact factor: 11.598

10.  Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.

Authors:  Begoña Heras; Melissa A Edeling; Horst J Schirra; Satish Raina; Jennifer L Martin
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-07       Impact factor: 11.205
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