Eye lens alphaA- and alphaB-crystallin: complex stability versus chaperone-like activity (Q73169685)

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1 November 2019

title

Eye lens alphaA- and alphaB-crystallin: complex stability versus chaperone-like activity (English)

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1 November 2019

author name string

M A van Boekel

1

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1 November 2019

F de Lange

2

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1 November 2019

W J de Grip

3

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1 November 2019

W W de Jong

4

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1 November 2019

language of work or name

English

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publication date

1 September 1999

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Biochimica et Biophysica Acta

1 November 2019

published in

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1 November 2019

volume

1434

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1 November 2019

issue

1

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1 November 2019

page(s)

114-123

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Quaternary structure of bovine alpha-crystallin: influence of temperature.

1 November 2019

cites work

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A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits.

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The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

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The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain".

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7 January 2021

Crystal structure of a small heat-shock protein

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7 January 2021

Alpha-crystallin can function as a molecular chaperone

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7 January 2021

Interaction of alpha-crystallin with spin-labeled peptides.

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7 January 2021

Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin

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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

The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin

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7 January 2021

Chaperone-like activity and temperature-induced structural changes of alpha-crystallin

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Detection and characterization of alpha-crystallin intermediate with maximal chaperone-like activity

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7 January 2021

Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method

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7 January 2021

alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues

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7 January 2021

Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens

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7 January 2021

Acid-induced dissociation of alpha A- and alpha B-crystallin homopolymers

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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

Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin

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7 January 2021

The alternative splicing product alpha Ains-crystallin is structurally equivalent to alpha A and alpha B subunits in the rat alpha-crystallin aggregate

1 reference

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7 January 2021

Phosphorylation of alpha-crystallin in rat lenses is stimulated by H2O2 but phosphorylation has no effect on chaperone activity

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7 January 2021

The influence of some post-translational modifications on the chaperone-like activity of alpha-crystallin

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7 January 2021

Lens alpha-crystallin: chaperone-like properties

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7 January 2021

The mutation Asp69-->Ser affects the chaperone-like activity of alpha A-crystallin

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7 January 2021

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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7 January 2021

Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity

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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

Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of alpha-crystallin

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7 January 2021

The conformational stability of alpha-crystallin is rather low: calorimetric results

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7 January 2021

Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin

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7 January 2021

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

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7 January 2021

Effects of temperature and concentration on bovine lens alpha-crystallin secondary structure: a circular dichroism spectroscopic study.

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7 January 2021

Amide modes and protein conformation

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7 January 2021

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

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7 January 2021

Binding of 1-anilinonaphthalene-8-sulfonic acid to alpha-crystallin

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7 January 2021

Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin

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7 January 2021

Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins

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7 January 2021

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

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7 January 2021

Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin

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7 January 2021

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Identifiers

DOI

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1 November 2019

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