Literature DB >> 2866934

Active-site ligand binding and subunit interactions in glutamine synthetase from Escherichia coli.

M R Maurizi, A Ginsburg.   

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Year:  1985        PMID： 2866934     DOI： 10.1016/b978-0-12-152826-3.50022-x

Source DB:  PubMed          Journal:  Curr Top Cell Regul        ISSN： 0070-2137


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  3 in total

1.  Thermal unfolding of dodecameric glutamine synthetase: inhibition of aggregation by urea.

Authors:  N J Nosworthy; A Ginsburg
Journal:  Protein Sci       Date:  1997-12       Impact factor: 6.725

2.  Peroxynitrite-mediated nitration of tyrosine residues in Escherichia coli glutamine synthetase mimics adenylylation: relevance to signal transduction.

Authors:  B S Berlett; B Friguet; M B Yim; P B Chock; E R Stadtman
Journal:  Proc Natl Acad Sci U S A       Date:  1996-03-05       Impact factor: 11.205

3.  Urea-induced dissociation and unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric and spectral studies.

Authors:  M Zolkiewski; N J Nosworthy; A Ginsburg
Journal:  Protein Sci       Date:  1995-08       Impact factor: 6.725
  3 in total

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