GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side. - Wikidata - awgldk - TriplyDB

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

http://www.wikidata.org/entity/Q42123947

about

Heterozygous yeast deletion collection screens reveal essential targets of Hsp90 NMR characterization of the interaction of GroEL with amyloid β as a model ligand Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a Chaperonin Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR How do chaperonins fold protein?The synthetic and biological studies of discorhabdins and related compounds.Forces Driving Chaperone Action Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Formation of the chaperonin complex studied by 2D NMR spectroscopy.Sequence features governing aggregation or degradation of prion-like proteins

P2860

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P2860

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

http://www.wikidata.org/entity/Q42123947

description

2008 nî lūn-bûn

@nan

2008年の論文

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2008年論文

@yue

2008年論文

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2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@en

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@nl

type

label

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@en

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@nl

prefLabel

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@en

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@nl

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P1433

Journal of Biological Chemistry

P1476

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

@en

P2093

Lingling Chen

http://www.w3.org/2001/XMLSchema#string

Xinfeng Gao

http://www.w3.org/2001/XMLSchema#string

Yali Li

http://www.w3.org/2001/XMLSchema#string

P2860

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

Domain motions in GroEL upon binding of an oligopeptide

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

A structural model for GroEL-polypeptide recognition

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

MOLMOL: a program for display and analysis of macromolecular structures

P304

4324-4331

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scholarly article

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10.1074/JBC.M804818200

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7

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284

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2008-12-12T00:00:00Z

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19074438

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2640968

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