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The Role of Protein-Ligand Contacts in Allosteric Regulation of the Escherichia coli Catabolite Activator Protein.

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Title: The Role of Protein-Ligand Contacts in Allosteric Regulation of the Escherichia coli Catabolite Activator Protein.
Authors: Townsend PD; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and., Rodgers TL; the School of Chemical Engineering and Analytical Science, University of Manchester, Manchester M13 9PL, United Kingdom., Glover LC; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and the Departments of Chemistry and., Korhonen HJ; the Biophysical Sciences Institute, and the Departments of Chemistry and the Department of Chemistry, University of Turku, 20014 Turku, Finland, and., Richards SA; From the School of Biological and Biomedical Sciences., Colwell LJ; the Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom., Pohl E; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and the Departments of Chemistry and., Wilson MR; the Biophysical Sciences Institute, and the Departments of Chemistry and., Hodgson DR; the Biophysical Sciences Institute, and the Departments of Chemistry and., McLeish TC; the Biophysical Sciences Institute, and the Departments of Chemistry and Physics, Durham University, Durham DH1 3LE, United Kingdom., Cann MJ; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and m.j.cann@durham.ac.uk.
Source: The Journal of biological chemistry [J Biol Chem] 2015 Sep 04; Vol. 290 (36), pp. 22225-35. Date of Electronic Publication: 2015 Jul 16.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: The Role of Protein-Ligand Contacts in Allosteric Regulation of the Escherichia coli Catabolite Activator Protein.
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  Data: <searchLink fieldCode="AU" term="%22Townsend+PD%22">Townsend PD</searchLink>; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and.<br /><searchLink fieldCode="AU" term="%22Rodgers+TL%22">Rodgers TL</searchLink>; the School of Chemical Engineering and Analytical Science, University of Manchester, Manchester M13 9PL, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Glover+LC%22">Glover LC</searchLink>; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and the Departments of Chemistry and.<br /><searchLink fieldCode="AU" term="%22Korhonen+HJ%22">Korhonen HJ</searchLink>; the Biophysical Sciences Institute, and the Departments of Chemistry and the Department of Chemistry, University of Turku, 20014 Turku, Finland, and.<br /><searchLink fieldCode="AU" term="%22Richards+SA%22">Richards SA</searchLink>; From the School of Biological and Biomedical Sciences.<br /><searchLink fieldCode="AU" term="%22Colwell+LJ%22">Colwell LJ</searchLink>; the Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Pohl+E%22">Pohl E</searchLink>; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and the Departments of Chemistry and.<br /><searchLink fieldCode="AU" term="%22Wilson+MR%22">Wilson MR</searchLink>; the Biophysical Sciences Institute, and the Departments of Chemistry and.<br /><searchLink fieldCode="AU" term="%22Hodgson+DR%22">Hodgson DR</searchLink>; the Biophysical Sciences Institute, and the Departments of Chemistry and.<br /><searchLink fieldCode="AU" term="%22McLeish+TC%22">McLeish TC</searchLink>; the Biophysical Sciences Institute, and the Departments of Chemistry and Physics, Durham University, Durham DH1 3LE, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Cann+MJ%22">Cann MJ</searchLink>; From the School of Biological and Biomedical Sciences, the Biophysical Sciences Institute, and m.j.cann@durham.ac.uk.
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2015 Sep 04; Vol. 290 (36), pp. 22225-35. <i>Date of Electronic Publication: </i>2015 Jul 16.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1083-351X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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