Structure-function analyses of metal-binding sites of HypA reveal residues important for hydrogenase maturation in Helicobacter pylori.

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Title: Structure-function analyses of metal-binding sites of HypA reveal residues important for hydrogenase maturation in Helicobacter pylori.
Authors: Blum FC; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America., Hu HQ; Department of Chemistry and Program in Molecular and Cellular Biology, University of Massachusetts Amherst, Amherst, MA, United States of America., Servetas SL; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America., Benoit SL; Department of Microbiology, University of Georgia, Athens, GA, United States of America., Maier RJ; Department of Microbiology, University of Georgia, Athens, GA, United States of America., Maroney MJ; Department of Chemistry and Program in Molecular and Cellular Biology, University of Massachusetts Amherst, Amherst, MA, United States of America., Merrell DS; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America.
Source: PloS one [PLoS One] 2017 Aug 15; Vol. 12 (8), pp. e0183260. Date of Electronic Publication: 2017 Aug 15 (Print Publication: 2017).
Publication Type: Journal Article
Journal Info: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Structure-function analyses of metal-binding sites of HypA reveal residues important for hydrogenase maturation in Helicobacter pylori.
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  Data: <searchLink fieldCode="AU" term="%22Blum+FC%22">Blum FC</searchLink>; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America.<br /><searchLink fieldCode="AU" term="%22Hu+HQ%22">Hu HQ</searchLink>; Department of Chemistry and Program in Molecular and Cellular Biology, University of Massachusetts Amherst, Amherst, MA, United States of America.<br /><searchLink fieldCode="AU" term="%22Servetas+SL%22">Servetas SL</searchLink>; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America.<br /><searchLink fieldCode="AU" term="%22Benoit+SL%22">Benoit SL</searchLink>; Department of Microbiology, University of Georgia, Athens, GA, United States of America.<br /><searchLink fieldCode="AU" term="%22Maier+RJ%22">Maier RJ</searchLink>; Department of Microbiology, University of Georgia, Athens, GA, United States of America.<br /><searchLink fieldCode="AU" term="%22Maroney+MJ%22">Maroney MJ</searchLink>; Department of Chemistry and Program in Molecular and Cellular Biology, University of Massachusetts Amherst, Amherst, MA, United States of America.<br /><searchLink fieldCode="AU" term="%22Merrell+DS%22">Merrell DS</searchLink>; Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America.
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  Data: <searchLink fieldCode="JN" term="%22101285081%22">PloS one</searchLink> [PLoS One] 2017 Aug 15; Vol. 12 (8), pp. e0183260. <i>Date of Electronic Publication: </i>2017 Aug 15 (<i>Print Publication: </i>2017).
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