(Q71763022)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

title

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

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

author name string

K Rajaraman

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

B Raman

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

C M Rao

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

language of work or name

English

0 references

publication date

1 November 1996

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

21 October 2019

number of pages

6

1 reference

based on heuristic

inferred from page(s)

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

volume

271

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

issue

44

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

page(s)

27595-27600

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

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

21 October 2019

cites work

1 reference

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

21 January 2018

1 reference

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Expression of the murine alpha B-crystallin gene is not restricted to the lens

21 January 2018

1 reference

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Expression of alpha B-crystallin in human brain tumors.

21 January 2018

1 reference

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Expression of alpha B-crystallin in Alzheimer's disease.

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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Alpha B-crystallin is a small heat shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Hypertonic stress induces alpha B-crystallin expression

21 January 2018

1 reference

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Interaction of alpha-crystallin with lens plasma membranes. Affinity for MP26

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Alpha-crystallin can function as a molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Localization of the chaperone binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Temperature dependent chaperone-like activity of alpha-crystallin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Interaction of alpha-crystallin with spin-labeled peptides.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Carboxyl-Terminal Region of Human and Bovine Erythrocyte Carbonic Anhydrases. 1. Amino Acid Sequences of Terminal Cyanogen Bromide Fragments

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Spectrofluorimetric assessment of the surface hydrophobicity of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Hydrophobic surfaces in oligosaccharides: linear dextrims are amphiphilic chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Compact intermediate states in protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

'Molten-globule' state accumulates in carbonic anhydrase folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

The folding of hen lysozyme involves partially structured intermediates and multiple pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Refolding of denatured and denatured/reduced lysozyme at high concentrations

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Partially folded states of equine lysozyme. Structural characterization and significance for protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

A Ca(2+)-binding chimera of human lysozyme and bovine alpha-lactalbumin that can form a molten globule

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

Zinc environmental differences in carbonic anhydrase isozymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.44.27595

21 January 2018

Identifiers

DOI

10.1074/JBC.271.44.27595

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910347%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

1 reference