Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins. (Q44299975)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12562766%20AND%20SRC:MED&resulttype=core&format=json

17 December 2019

title

Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins (English)

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17 December 2019

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2

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17 December 2019

author name string

Tatiana Putilina

1

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17 December 2019

Karine Prat

3

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17 December 2019

Nicolette H Lubsen

4

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17 December 2019

Annette Tardieu

5

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17 December 2019

language of work or name

English

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publication date

31 January 2003

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Journal of Biological Chemistry

17 December 2019

published in

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17 December 2019

volume

278

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17 December 2019

issue

16

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17 December 2019

page(s)

13747-13756

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Small heat shock protein of Methanococcus jannaschii, a hyperthermophile

17 December 2019

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Lens alpha-crystallin: chaperone-like properties

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The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin

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Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro

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Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction

21 January 2018

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Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe.

21 January 2018

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Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations

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The alphaA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with alphaB-crystallin

21 January 2018

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Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii

21 January 2018

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21 January 2018

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Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature

21 January 2018

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Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily

21 January 2018

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Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions

21 January 2018

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The protein concentration gradient within eye lens might originate from constant osmotic pressure coupled to differential interactive properties of crystallins

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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

21 January 2018

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alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner

21 January 2018

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Chaperone activity in the lens

21 January 2018

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Calf lens alpha-crystallin, a molecular chaperone, builds stable complexes with beta s- and gamma-crystallins

21 January 2018

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

21 January 2018

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Lens crystallins and oxidation: the special case of γS

21 January 2018

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

21 January 2018

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

21 January 2018

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Gamma S-crystallin of bovine and human eye lens: solution structure, stability and folding of the intact two-domain protein and its separate domains

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M208157200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12562766%20AND%20SRC:MED&resulttype=core&format=json

17 December 2019

1 reference