(Q47896935)

6 February 2018

review article

1 reference

title

Structural perturbation of alpha-crystallin and its chaperone-like activity. (English)

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6 February 2018

0 references

Rao CM

1

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6 February 2018

Raman B

2

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6 February 2018

Ramakrishna T

3

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6 February 2018

Rajaraman K

4

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6 February 2018

Ghosh D

5

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6 February 2018

Datta S

6

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6 February 2018

Trivedi VD

7

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6 February 2018

Sukhaswami MB

8

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6 February 2018

publication date

1 May 1998

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6 February 2018

number of pages

11

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International Journal of Biological Macromolecules

inferred from page(s)

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)

271-281

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6 February 2018

The recruitment of crystallins: new functions precede gene duplication.

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7 January 2021

Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin

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7 January 2021

Alpha-crystallin can function as a molecular chaperone

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7 January 2021

Molecular chaperone functions of heat-shock proteins

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7 January 2021

Protein folding in the cell

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7 January 2021

The role of heat-shock and chaperone proteins in protein folding: possible molecular mechanisms

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7 January 2021

Temperature dependent chaperone-like activity of alpha-crystallin

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7 January 2021

High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.

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7 January 2021

Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin

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7 January 2021

Light scattering and photocrosslinking in the calf lens crystallins gamma-II, III and IV.

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7 January 2021

Structure and stability of gamma-crystallins--IV. Aggregation and structural destabilization in photosensitized reactions

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7 January 2021

The Quaternary Structure of Bovine alpha-Crystallin. Size and Shape Studies by Sedimentation, Small-angle X-Ray Scattering and Quasi-elastic Light Scattering

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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

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

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7 January 2021

alpha m-Crystallin: the native form of the protein?

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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

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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7 January 2021

The molecular chaperone alpha-crystallin inhibits UV-induced protein aggregation

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7 January 2021

Interaction of alpha-crystallin with spin-labeled peptides.

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7 January 2021

Fractionation of oxidized insulin

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7 January 2021

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

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7 January 2021

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

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7 January 2021

The molten globular intermediate form in the folding pathway of human carbonic anhydrase B

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7 January 2021

Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation

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7 January 2021

Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)

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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

Effect of the chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease A

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7 January 2021

Refolding of denatured and denatured/reduced lysozyme at high concentrations

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7 January 2021

Defective protein folding as a basis of human disease

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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

Identification of possible regions of chaperone activity in lens alpha-crystallin

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7 January 2021

Interaction of ATP and lens alpha crystallin characterized by equilibrium binding studies and intrinsic tryptophan fluorescence spectroscopy

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7 January 2021

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

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7 January 2021

The 'molten globule' state is involved in the translocation of proteins across membranes?

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7 January 2021

A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A

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7 January 2021

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

1 reference

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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

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

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7 January 2021

Refolding of RNAse A at high concentrations: identification of non-native species

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7 January 2021

Chemical synthesis of 10 kDa chaperonin Biological activity suggests chaperonins do not require other molecular chaperones

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7 January 2021

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

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7 January 2021

The mitochondrial chaperonin hsp60 is required for its own assembly

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7 January 2021

Refolding and reassembly of active chaperonin GroEL after denaturation

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7 January 2021

10.1016/S0141-8130(98)00025-7

Identifiers

DOI

1 reference

6 February 2018

PubMed ID

9650082

1 reference

6 February 2018