The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.
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GroEL2 of Mycobacterium tuberculosis Reveals the Importance of Structural Pliability in Chaperonin Function.Multiple chaperonins in bacteria--novel functions and non-canonical behaviorsMycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions.Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation.
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P2860
The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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name
The unusual mycobacterial chap ...... nd specialization of function.
@en
The unusual mycobacterial chap ...... nd specialization of function.
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type
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The unusual mycobacterial chap ...... nd specialization of function.
@en
The unusual mycobacterial chap ...... nd specialization of function.
@nl
prefLabel
The unusual mycobacterial chap ...... nd specialization of function.
@en
The unusual mycobacterial chap ...... nd specialization of function.
@nl
P2093
P2860
P50
P1476
The unusual mycobacterial chap ...... nd specialization of function.
@en
P2093
Anshuman Shukla
Elsa Zacco
Joanna Freeke
M Tabish Ahmed
MingQi Fan
P2860
P304
P356
10.1111/J.1365-2958.2012.08150.X
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P577
2012-07-26T00:00:00Z