The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study (Q44021096)

29 November 2017

The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study (English)

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29 November 2017

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7

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29 November 2017

6

Christopher M Dobson

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29 November 2017

Robyn A Lindner

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29 November 2017

Charles Lyon

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29 November 2017

Denis Canet

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4

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29 November 2017

Helena Hernandez

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5

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29 November 2017

language of work or name

English

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publication date

1 May 2002

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Journal of Molecular Biology

29 November 2017

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29 November 2017

318

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29 November 2017

3

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29 November 2017

815-827

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From computer simulations to human disease: emerging themes in protein folding

29 November 2017

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The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

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Protein misfolding, evolution and disease

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Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease

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The second decade--into the third millenium

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NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.

7 January 2021

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Probing the structure and interactions of crystallin proteins by NMR spectroscopy.

7 January 2021

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Principles of protein folding in the cellular environment

7 January 2021

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Moledular chaperones ten years. Introduction

7 January 2021

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The function of alpha-crystallin in vision

7 January 2021

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Equilibrium NMR studies of unfolded and partially folded proteins

7 January 2021

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Kinetic studies of protein folding using NMR spectroscopy

7 January 2021

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The molten globule state of alpha-lactalbumin.

7 January 2021

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Refined structure of baboon α-lactalbumin at 1.7 Å resolution

7 January 2021

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Crystal structure of human α-lactalbumin at 1·7 Å resolution

7 January 2021

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Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase

7 January 2021

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

7 January 2021

1 reference

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The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin

7 January 2021

2 references

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7 January 2021

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900144-4

inferred from DOI database lookup

7 January 2021

based on heuristic

Structural alterations of alpha-crystallin during its chaperone action

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https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900144-4

Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond

7 January 2021

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Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin

7 January 2021

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Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin 1 1Edited by P. E. Wright

7 January 2021

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Following protein folding in real time using NMR spectroscopy

7 January 2021

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Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin

7 January 2021

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The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin

7 January 2021

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Interaction of alpha-crystallin with spin-labeled peptides.

7 January 2021

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Disulfide determinants of calcium-induced packing in alpha-lactalbumin

7 January 2021

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The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

7 January 2021

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

7 January 2021

1 reference

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A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein

7 January 2021

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

7 January 2021

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On the interaction of alpha-crystallin with unfolded proteins

7 January 2021

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Subunit exchange of alphaA-crystallin

7 January 2021

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Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations

7 January 2021

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Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling.

7 January 2021

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Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin

7 January 2021

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Temperature dependent chaperone-like activity of alpha-crystallin

7 January 2021

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The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

7 January 2021

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The mode of chaperoning of dithiothreitol-denatured alpha-lactalbumin by alpha-crystallin

7 January 2021

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Rapid separation of bovine beta-crystallin subunits beta B1, beta B2, beta B3, beta A3 and beta A4.

7 January 2021

1 reference

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10.1016/S0022-2836(02)00144-4

7 January 2021

Identifiers

DOI

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29 November 2017

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