Literature DB >> 7979362

Thioredoxin: a multifunctional regulatory protein with a bright future in technology and medicine.

B B Buchanan1, P Schürmann, P Decottignies, R M Lozano.   

Abstract

Thioredoxins are proteins, typically with a molecular mass of 12 kDa, that are widely, if not universally, distributed in the animal, plant, and bacterial kingdoms. Thioredoxins undergo reversible redox change through a disulfide group (S-S-->2 SH). Two cellular reductants--reduced ferredoxin and NADPH--supply the equivalents for reduction via different enzymes. The nature of the reductant serves as a basis for distinguishing and naming the two thioredoxin systems, which are discussed below in relation to their possible application in technology and medicine. Most of the discussion is referenced by general reviews. In the section dealing with animal cells, however, much of the material is quite recent. Thus, there, and elsewhere to a lesser extent, previously uncited studies are assigned specific references.

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Year:  1994        PMID: 7979362     DOI: 10.1006/abbi.1994.1439

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  28 in total

1.  A strategy for the identification of proteins targeted by thioredoxin.

Authors:  H Yano; J H Wong; Y M Lee; M J Cho; B B Buchanan
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-27       Impact factor: 11.205

2.  Thiocalsin: a thioredoxin-linked, substrate-specific protease dependent on calcium.

Authors:  I Besse; J H Wong; K Kobrehel; B B Buchanan
Journal:  Proc Natl Acad Sci U S A       Date:  1996-04-16       Impact factor: 11.205

3.  The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond.

Authors:  Bob B Buchanan; P Schürmann; Ricardo A Wolosiuk; Jean-Pierre Jacquot
Journal:  Photosynth Res       Date:  2002       Impact factor: 3.573

4.  The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.

Authors:  P T Chivers; M C Laboissière; R T Raines
Journal:  EMBO J       Date:  1996-06-03       Impact factor: 11.598

5.  Engineering a domain-locking disulfide into a bacterial malate dehydrogenase produces a redox-sensitive enzyme.

Authors:  E H Muslin; D Li; F J Stevens; M Donnelly; M Schiffer; L E Anderson
Journal:  Biophys J       Date:  1995-06       Impact factor: 4.033

6.  Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.

Authors:  M Saitoh; H Nishitoh; M Fujii; K Takeda; K Tobiume; Y Sawada; M Kawabata; K Miyazono; H Ichijo
Journal:  EMBO J       Date:  1998-05-01       Impact factor: 11.598

7.  AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1.

Authors:  K Hirota; M Matsui; S Iwata; A Nishiyama; K Mori; J Yodoi
Journal:  Proc Natl Acad Sci U S A       Date:  1997-04-15       Impact factor: 11.205

8.  Increased intracellular survival of Mycobacterium smegmatis containing the Mycobacterium leprae thioredoxin-thioredoxin reductase gene.

Authors:  B Wieles; T H Ottenhoff; T M Steenwijk; K L Franken; R R de Vries; J A Langermans
Journal:  Infect Immun       Date:  1997-07       Impact factor: 3.441

9.  Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study.

Authors:  Emilia Pedone; Simonetta Bartolucci; Mosè Rossi; Francesco Maria Pierfederici; Andrea Scirè; Tiziana Cacciamani; Fabio Tanfani
Journal:  Biochem J       Date:  2003-08-01       Impact factor: 3.857

10.  Redox regulation of Arabidopsis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.

Authors:  Robert Entus; Michael Poling; Klaus M Herrmann
Journal:  Plant Physiol       Date:  2002-08       Impact factor: 8.340

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