(Q47897027)

6 February 2018

title

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

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6 February 2018

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6 February 2018

author name string

Lindner RA

series ordinal

2

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6 February 2018

publication date

1 May 1998

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6 February 2018

International Journal of Biological Macromolecules

published in

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6 February 2018

volume

22

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6 February 2018

issue

3-4

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6 February 2018

page(s)

197-209

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6 February 2018

Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin

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1 H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids

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1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions

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The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin

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A 1H NMR spectroscopic comparison of gamma S- and gamma B-crystallins

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7 January 2021

Alpha-crystallin: molecular chaperone and protein surfactant

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7 January 2021

Interaction and aggregation of lens crystallins

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7 January 2021

On the interaction of alpha-crystallin with unfolded proteins

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7 January 2021

Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions

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7 January 2021

The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins

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7 January 2021

Alpha-crystallin can function as a molecular chaperone

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7 January 2021

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Identification of the major components of the high molecular weight crystallins from old human lenses

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Molecular chaperone properties of the high molecular weight aggregate from aged lens

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High-molecular-weight protein aggregates of calf and cow lens: Spectroscopic evaluation

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Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology

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Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin

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7 January 2021

On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy

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7 January 2021

Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallin

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7 January 2021

Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.

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7 January 2021

Chaperone-assisted protein folding.

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7 January 2021

On the substrate specificity of alpha-crystallin as a molecular chaperone

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7 January 2021

Temperature dependent chaperone-like activity of alpha-crystallin

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7 January 2021

Interaction of alpha-crystallin with spin-labeled peptides.

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7 January 2021

The molten globule state of alpha-lactalbumin.

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7 January 2021

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

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7 January 2021

An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure

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7 January 2021

Folding-unfolding and aggregation-dissociation of bovine alpha-crystallin subunits; evidence for unfolding intermediates of the alpha A subunits

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7 January 2021

Domain structure and evolution in alpha-crystallins and small heat-shock proteins.

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7 January 2021

Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model

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7 January 2021

A possible structure for alpha-crystallin

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7 January 2021

Possible tetramer-based quaternary structure for alpha-crystallins and small heat shock proteins

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7 January 2021

A possible chaperone-like quaternary structure for alpha-crystallin

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7 January 2021

Computer-generated model of the quaternary structure of alpha crystallin in the lens

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7 January 2021

alpha-Crystallin quaternary structure: molecular basis for its chaperone activity

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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7 January 2021

Structure of a molecular chaperone from a thermophilic archaebacterium

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7 January 2021

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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7 January 2021

The quaternary structure of bovine alpha-crystallin. Effects of variation in alkaline pH, ionic strength, temperature and calcium ion concentration

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7 January 2021

10.1016/S0141-8130(98)00017-8

Identifiers

DOI

1 reference

6 February 2018

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6 February 2018