Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation.

scientific article published on 23 May 2005

Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M503934200
P698PubMed publication ID15911614

P50authorWeizhe HongQ47918622
P2093author name stringBin Xia
Jicheng Hu
Dan Shen
Chong Liu
Zengyi Chang
Xinmiao Fu
Junrui Zhang
Wangwang Jiao
P2860cites workIntrinsically unstructured proteins and their functionsQ22061731
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Crystal structure of Escherichia coli HdeAQ27765274
Intrinsically disordered proteinQ28191444
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The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coliQ34403212
The role of gastric acid in preventing foodborne disease and how bacteria overcome acid conditionsQ35180934
The role of structural disorder in the function of RNA and protein chaperonesQ35850848
Escherichia coli acid resistance: tales of an amateur acidophileQ35923268
Acid and base resistance in Escherichia coli and Shigella flexneri: role of rpoS and growth pH.Q36106069
Gene expression profiling of the pH response in Escherichia coliQ39680649
Identification of sigma S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneriQ42642088
alpha-B- and alpha-A-crystallin prevent irreversible acidification-induced protein denaturationQ43742562
Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high saltQ46978560
Periplasmic proteins of Escherichia coli are highly resistant to aggregation: reappraisal for roles of molecular chaperones in periplasm.Q47918518
A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins.Q51580906
P433issue29
P407language of work or nameEnglishQ1860
P921main subjectmolecular chaperonesQ422496
P304page(s)27029-27034
P577publication date2005-05-23
P1433published inJournal of Biological ChemistryQ867727
P1476titlePeriplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation.
P478volume280

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