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Plasticity and transient binding are key ingredients of the periplasmic chaperone network.

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Title: Plasticity and transient binding are key ingredients of the periplasmic chaperone network.
Authors: Chum AP; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Shoemaker SR; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Fleming PJ; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Fleming KG; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.
Source: Protein science : a publication of the Protein Society [Protein Sci] 2019 Jul; Vol. 28 (7), pp. 1340-1349. Date of Electronic Publication: 2019 May 23.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
Journal Info: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Plasticity and transient binding are key ingredients of the periplasmic chaperone network.
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  Data: <searchLink fieldCode="AU" term="%22Chum+AP%22">Chum AP</searchLink>; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.<br /><searchLink fieldCode="AU" term="%22Shoemaker+SR%22">Shoemaker SR</searchLink>; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.<br /><searchLink fieldCode="AU" term="%22Fleming+PJ%22">Fleming PJ</searchLink>; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.<br /><searchLink fieldCode="AU" term="%22Fleming+KG%22">Fleming KG</searchLink>; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.
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  Data: <searchLink fieldCode="JN" term="%229211750%22">Protein science : a publication of the Protein Society</searchLink> [Protein Sci] 2019 Jul; Vol. 28 (7), pp. 1340-1349. <i>Date of Electronic Publication: </i>2019 May 23.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Cold+Spring+Harbor+Laboratory+Press%22">Cold Spring Harbor Laboratory Press </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>9211750 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1469-896X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2209618368%22">09618368 </searchLink><i>NLM ISO Abbreviation: </i>Protein Sci <i>Subsets: </i>MEDLINE
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        Value: 10.1002/pro.3641
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        Text: English
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        StartPage: 1340
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      – TitleFull: Plasticity and transient binding are key ingredients of the periplasmic chaperone network.
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            NameFull: Chum AP
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            NameFull: Shoemaker SR
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            NameFull: Fleming PJ
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              Text: 2019 Jul
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              Y: 2019
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