Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
about
Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identifiedThe effect of macromolecular crowding on chaperonin-mediated protein foldingMycobacterium tuberculosis Chaperonin 10 Heptamers Self-Associate through Their Biologically Active LoopsCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleInterplay of structure and disorder in cochaperonin mobile loopsP. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coliDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleOligomeric interfaces under the lens: geminiMycobacterium tuberculosis chaperonin 10 is secreted in the macrophage phagosome: is secretion due to dissociation and adoption of a partially helical structure at the membrane?Overview of protein structural and functional folds.Chaperonins GroEL and GroES: views from atomic force microscopy.Submolecular resolution of single macromolecules with atomic force microscopy.Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.Differential T-cell recognition of native and recombinant Mycobacterium tuberculosis GroESIdentification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of the co-chaperonin XoGroES from Xanthomonas oryzae pv. oryzae.Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.Catalysis of protein folding by symmetric chaperone complexes.Symmetry, stability, and dynamics of multidomain and multicomponent protein systems.GroEL-mediated protein folding: making the impossible, possible.Use of monoclonal antibodies to facilitate identification, cloning, and purification of Chlamydia trachomatis hsp10.The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.GroEL-mediated protein folding.Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10.Immune profiling of leprosy and tuberculosis patients to 15-mer peptides of Mycobacterium leprae and M. tuberculosis GroES in a BCG vaccinated area: implications for development of vaccine and diagnostic reagents.A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein FoldingLeprosy patients with lepromatous disease recognize cross-reactive T cell epitopes in the Mycobacterium leprae 10-kD antigen
P2860
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P2860
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@ast
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@en
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@nl
type
label
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@ast
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@en
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@nl
prefLabel
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@ast
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@en
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@nl
P2093
P1433
P1476
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
@en
P2093
P356
10.1126/SCIENCE.271.5246.203
P407
P577
1996-01-12T00:00:00Z