The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity
about
Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallinAntagonists of Hsp16.3, a low-molecular-weight mycobacterial chaperone and virulence factor, derived from phage-displayed peptide librariesFunctional characterization of a small heat shock protein from Mycobacterium lepraeUnfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneA tricistronic heat shock operon is important for stress tolerance of Pseudomonas putida and conserved in many environmental bacteria.Recognition between flexible protein molecules: induced and assisted folding.Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium tuberculosis transcription pattern characteristic of nonreplicating persistence.On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii.A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases Also Exhibit Chaperone like Activity In-Vitro and In-VivoProteomic analysis of drug-resistant Mycobacterium tuberculosis by one-dimensional gel electrophoresis and charge chromatography.Key role for the alternative sigma factor, SigH, in the intracellular life of Mycobacterium avium subsp. paratuberculosis during macrophage stress.Crystallization and heavy-atom derivatization of StHsp14.0, a small heat-shock protein from Sulfolobus tokodaiiPosttranslational modulation on the biological activities of molecular chaperones.Immunodominant protein MIP_05962 from Mycobacterium indicus pranii displays chaperone activity.The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function.Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride.Small heat shock protein AgsA forms dynamic fibrils.Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure.
P2860
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P2860
The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity
description
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Januar 1999 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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vedecký článok (publikovaný 1999/01/01)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/01/01)
@nl
наукова стаття, опублікована в січні 1999
@uk
مقالة علمية (نشرت عام 1999)
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name
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@ast
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@en
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@nl
type
label
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@ast
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@en
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@nl
prefLabel
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@ast
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@en
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@nl
P2093
P2860
P921
P356
P1433
P1476
The Mycobacterium tuberculosis ...... d molecular chaperone activity
@en
P2093
P2860
P304
P356
10.1110/PS.8.1.174
P577
1999-01-01T00:00:00Z