(Q24337796)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

title

N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

Amyloid beta precursor protein

27 February 2020

main subject

molecular chaperones

0 references

1 reference

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Bishwajit Kundu

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

author name string

Rachana Tomar

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

Dushyant K Garg

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

Rahul Mishra

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

Ashwani K Thakur

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

language of work or name

English

0 references

publication date

29 April 2013

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

volume

280

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

issue

11

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

27 February 2020

page(s)

2688-2699

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23551356%20AND%20SRC:MED&resulttype=core&format=json

Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.

27 February 2020

cites work

1 reference

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Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins

21 January 2018

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21 January 2018

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Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein

21 January 2018

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Alpha crystallin: the quest for a homogeneous quaternary structure

21 January 2018

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Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies

21 January 2018

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Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin

21 January 2018

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HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: structural and functional aspects

21 January 2018

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Alpha-crystallin can function as a molecular chaperone

21 January 2018

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

21 January 2018

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Chaperone-like activity of tubulin. binding and reactivation of unfolded substrate enzymes.

21 January 2018

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Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2.

21 January 2018

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Small heat shock protein of Methanococcus jannaschii, a hyperthermophile

21 January 2018

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Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus.

21 January 2018

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Large potentials of small heat shock proteins

21 January 2018

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Small heat shock proteins and protein-misfolding diseases

21 January 2018

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Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions

21 January 2018

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The intramolecular chaperone-mediated protein folding

21 January 2018

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Some like it hot: the structure and function of small heat-shock proteins.

21 January 2018

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The small heat shock proteins and their clients

21 January 2018

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Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones

21 January 2018

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Stability of domain structures in multi-domain proteins

21 January 2018

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Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin

21 January 2018

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

21 January 2018

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Translationally controlled tumor protein is a novel heat shock protein with chaperone-like activity

21 January 2018

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Interaction of chaperone alpha-crystallin with unfolded state of alpha-amylase: Implications for reconstitution of the active enzyme.

21 January 2018

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

21 January 2018

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Refolding of recombinant proteins

21 January 2018

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Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.

21 January 2018

1 reference

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AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12271

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation

21 January 2018

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Mutational analysis of the structural organization of polyglutamine aggregates

21 January 2018

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Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins

21 January 2018

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Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins

21 January 2018

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Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding

21 January 2018

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7 January 2021

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

1 reference

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7 January 2021

Artemin as an efficient molecular chaperone

1 reference

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7 January 2021

Temperature dependent chaperone-like activity of alpha-crystallin

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7 January 2021

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

1 reference

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7 January 2021

Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway

1 reference

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7 January 2021

The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12271

7 January 2021

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

1 reference

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7 January 2021

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

1 reference

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7 January 2021

Avoiding the oligomeric state: αB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils

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7 January 2021