Interaction of alpha-lactalbumin with mini-alphaA-crystallin (Q43742400)

26 November 2017

Interaction of alpha-lactalbumin with mini-alphaA-crystallin (English)

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26 November 2017

Sreelakshmi Y

1

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PubMed ID

11563692

26 November 2017

Sharma KK

series ordinal

2

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26 November 2017

1 February 2001

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26 November 2017

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20

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2

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26 November 2017

123-130

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https://scigraph.springernature.com/pub.10.1023/a:1011077307262

26 November 2017

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cites work

Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein

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12 December 2020

Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function

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12 December 2020

Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study

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Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin

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S-nitrosoglutathione photolysis as a novel therapy for antifibrosis in filtration surgery

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Chaperone-like activity of a synthetic peptide toward oxidized gamma-crystallin

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12 December 2020

Increased exposure of hydrophobic surface in molten globule state of alpha-lactalbumin. Fluorescence and hydrophobic photolabeling studies

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12 December 2020

Alpha-crystallin can function as a molecular chaperone

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12 December 2020

Quantitative analysis of cystine, methionine, lysine, and nine other amino acids by a single oxidation--4 hour hydrolysis method

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12 December 2020

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

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12 December 2020

The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐Crystallin

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12 December 2020

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

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12 December 2020

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

1 reference

12 December 2020

The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states.

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12 December 2020

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

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12 December 2020

Chaperone-like activity and quaternary structure of alpha-crystallin

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12 December 2020

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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12 December 2020

Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones

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12 December 2020

Thermal unfolding of bovine alpha-lactalbumin. Comparison of circular dichroism with hydrophobicity measurements

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12 December 2020

The C-terminal region of alpha-crystallin: involvement in protection against heat-induced denaturation

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12 December 2020

Effect of cross-linking on the chaperone-like function of alpha crystallin

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12 December 2020

The molten globule state of alpha-lactalbumin.

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Cloning, expression, and chaperone-like activity of human alphaA-crystallin

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Lens alpha-crystallin: chaperone-like properties

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1023/A:1011077307262

1 reference

PubMed ID

11563692

Dimensions Publication ID

26 November 2017

0 references

1 reference

PubMed ID

11563692