(Q53913822)

22 May 2018

title

Unfolding and refolding of bovine alpha-crystallin in urea and its chaperone activity. (English)

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22 May 2018

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S Saha

1

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22 May 2018

K P Das

series ordinal

2

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22 May 2018

publication date

1 August 2007

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22 May 2018

published in

The Protein Journal

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22 May 2018

volume

26

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22 May 2018

issue

5

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22 May 2018

page(s)

315-326

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22 May 2018

The nature of protein folding pathways: the classical versus the new view

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Spectrofluorimetric assessment of the surface hydrophobicity of proteins

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https://api.crossref.org/works/10.1007%2FS10930-007-9074-3

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

21 January 2018

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https://api.crossref.org/works/10.1007%2FS10930-007-9074-3

Conformational stability of bovine alpha-crystallin. Evidence for a destabilizing effect of ascorbate

21 January 2018

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Lens alpha-crystallin: chaperone-like properties

21 January 2018

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12 December 2020

Alpha-crystallin does not require temperature activation for its chaperone-like activity

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

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Cooperative multiple binding of bisANS and daunomycin to tubulin

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Intermediates in the folding reactions of small proteins

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

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Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

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Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin.

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Energy Transfer Studies of the Distances between the Colchicine, Ruthenium red, and BisANS Binding Sites on Calf Brain Tubulin

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Bis(1,8-anilinonaphthalenesulfonate). A novel and potent inhibitor of microtubule assembly

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12 December 2020

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

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12 December 2020

Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin

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12 December 2020

On the structure of alpha m-crystallin. The reversibility of urea dissociation

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12 December 2020

alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease

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Chaperone-like activity and quaternary structure of alpha-crystallin

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Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

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Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain

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Relationship between chaperone activity and oligomeric size of recombinant human alphaA- and alphaB-crystallin: a tryptic digestion study

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12 December 2020

Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function

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12 December 2020

Alpha A-crystallin confers cellular thermoresistance

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Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin

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12 December 2020

The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

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

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Small heat shock proteins are molecular chaperones.

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Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences

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From Levinthal to pathways to funnels

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A differential scanning calorimetric study of the bovine lens crystallins

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12 December 2020

Alpha-crystallin can function as a molecular chaperone

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12 December 2020

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

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12 December 2020

Experimental studies of protein folding and unfolding

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Principles that govern the folding of protein chains

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Theory for the folding and stability of globular proteins

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Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor

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Fluorescence quenching studies with proteins

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12 December 2020

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

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Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study

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alpha-Crystallin acting as a molecular chaperonin against photodamage by UV irradiation

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SDS induced structural changes in alpha-crystallin and it's effect on refolding

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Thermal unfolding and refolding of beta-lactoglobulin. An intrinsic andextrinsic fluorescence study.

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Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins

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Thermodynamic stability of human lens recombinant alphaA- and alphaB-crystallins

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Identification of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid binding sequences in alpha-crystallin

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12 December 2020

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

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12 December 2020

alpha A-crystallin is expressed in non-ocular tissues

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Proctor Lecture. The function of alpha-crystallin

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12 December 2020

Circular dichroism and optical rotatory dispersion of the aggregates of purified polypeptides of alpha-crystallin.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

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12 December 2020

The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

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12 December 2020

Some properties of the low molecular weight alpha-crystallin from normal human lens: comparison with bovine lens

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12 December 2020

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

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12 December 2020

Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli

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12 December 2020

Matching speed and stability

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12 December 2020

Kinetics versus thermodynamics in protein folding

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12 December 2020

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

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12 December 2020

10.1007/S10930-007-9074-3

Identifiers

DOI

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22 May 2018

1 reference

22 May 2018