NMR characterization of the interaction of GroEL with amyloid β as a model ligand (Q24338819)

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Maho Yagi-Utsumi

1

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Tomoko Kunihara

2

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Takashi Nakamura

3

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Yoshinori Uekusa

4

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Koki Makabe

5

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Kunihiro Kuwajima

6

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Koichi Kato

Molecular chaperones in cellular protein folding

7

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language of work or name

English

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publication date

5 June 2013

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published in

FEBS Letters

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volume

587

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page(s)

1605-9

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issue

11

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cites work

1 reference

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

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Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

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Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

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Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

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Folding of malate dehydrogenase inside the GroEL-GroES cavity

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Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

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Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.

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Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding.

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Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

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Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone

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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

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Progress towards a molecular-level structural understanding of amyloid fibrils

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Up-and-down topological mode of amyloid beta-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters

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NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid beta

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Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability.

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GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side

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

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NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution

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inferred from DOI database lookup

7 January 2021

based on heuristic

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES

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inferred from DOI database lookup

7 January 2021

based on heuristic

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

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