Structural aspects of GroEl function (Q41633461)

5 October 2017

title

Structural aspects of GroEL function (English)

1 reference

5 October 2017

Structural aspects of GroEl function (English)

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(98)80015-8

14 December 2024

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9519301

14 December 2024

author name string

A. Horovitz

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9519301

14 December 2024

publication date

1 February 1998

1 reference

5 October 2017

February 1998

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9519301

14 December 2024

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9519301

https://api.elsevier.com/content/article/PII:S0959440X98800158?httpAccept=text/xml

14 December 2024

work available at URL

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(98)80015-8

https://api.elsevier.com/content/article/PII:S0959440X98800158?httpAccept=text/plain

14 December 2024

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(98)80015-8

Current Opinion in Structural Biology

14 December 2024

published in

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5 October 2017

volume

8

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5 October 2017

issue

1

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5 October 2017

page(s)

93-100

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publication type of scholarly work

5 October 2017

review article

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Chaperone-assisted protein folding

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Roles of molecular chaperones in protein degradation

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Structural basis of allosteric changes in the GroEL mutant Arg197→Ala

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

A structural model for GroEL-polypeptide recognition

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Nature and consequences of GroEL-protein interactions

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The hydrophobic nature of GroEL-substrate binding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL 1 1Edited by J. Karn

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

A thermodynamic coupling mechanism for GroEL-mediated unfolding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Hydrogen-exchange kinetics of reduced alpha-lactalbumin bound to the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Refolding chromatography with immobilized mini-chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Is substrate inhibition a consequence of allostery in aspartate transcarbamylase?

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Conformational changes in the GroEL oligomer during the functional cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Detection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Catalysis of protein folding by symmetric chaperone complexes

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroEL-mediated folding of structurally homologous dihydrofolate reductases

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Protein folding: how the mechanism of GroEL action is defined by kinetics

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Structural Adaptations in the Specialized Bacteriophage T4 Co-Chaperonin Gp31 Expand the Size of the Anfinsen Cage

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

GroES Promotes the T to R Transition of the GroEL Ring Distal to GroES in the GroEL−GroES Complex†

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Recombination of protein domains facilitated by co-translational folding in eukaryotes

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

The effect of macromolecular crowding on chaperonin-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980015-8

7 January 2021

Identifiers

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5 October 2017

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