Literature DB >> 11430763

1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state.

D M Jacobs, J Messens, R W Wechselberger, E Brosens, R Willem, L Wyns, J C Martin.   

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Year:  2001        PMID： 11430763     DOI： 10.1023/a:1011207007790

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


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  7 in total

1.  Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli.

Authors:  J Messens; G Hayburn; E Brosens; G Laus; L Wyns
Journal:  J Chromatogr B Biomed Sci Appl       Date:  2000-01-14

2.  Separate resistances to arsenate and arsenite (antimonate) encoded by the arsenical resistance operon of R factor R773.

Authors:  C M Chen; H L Mobley; B P Rosen
Journal:  J Bacteriol       Date:  1985-02       Impact factor: 3.490

3.  The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.

Authors:  J Messens; G Hayburn; A Desmyter; G Laus; L Wyns
Journal:  Biochemistry       Date:  1999-12-21       Impact factor: 3.162

4.  Genes for all metals--a bacterial view of the periodic table. The 1996 Thom Award Lecture.

Authors:  S Silver
Journal:  J Ind Microbiol Biotechnol       Date:  1998-01       Impact factor: 3.346

5.  Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258.

Authors:  G Ji; S Silver
Journal:  J Bacteriol       Date:  1992-06       Impact factor: 3.490

6.  The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.

Authors:  D S Wishart; B D Sykes
Journal:  J Biomol NMR       Date:  1994-03       Impact factor: 2.835

7.  Arsenate reductase of Staphylococcus aureus plasmid pI258.

Authors:  G Ji; E A Garber; L G Armes; C M Chen; J A Fuchs; S Silver
Journal:  Biochemistry       Date:  1994-06-14       Impact factor: 3.162
  7 in total
  3 in total

1.  All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.

Authors:  Joris Messens; José C Martins; Karolien Van Belle; Elke Brosens; Aline Desmyter; Marjan De Gieter; Jean-Michel Wieruszeski; Rudolph Willem; Lode Wyns; Ingrid Zegers
Journal:  Proc Natl Acad Sci U S A       Date:  2002-06-18       Impact factor: 11.205

2.  Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases.

Authors:  M S Bennett; Z Guan; M Laurberg; X D Su
Journal:  Proc Natl Acad Sci U S A       Date:  2001-11-06       Impact factor: 11.205

3.  Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop.

Authors:  Christin L T Gustafson; Cynthia V Stauffacher; Klaas Hallenga; Robert L Van Etten
Journal:  Protein Sci       Date:  2005-10       Impact factor: 6.725
  3 in total

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