Domain Motions in GroEL upon Binding of an Oligopeptide (Q27642561)

https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

3 April 2024

author name string

Jimin Wang

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Lingling Chen

full work available at URL

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language of work or name

English

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publication date

28 November 2003

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https://api.elsevier.com/content/article/PII:S0022283603012361?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

https://api.elsevier.com/content/article/PII:S0022283603012361?httpAccept=text/plain

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Journal of Molecular Biology

3 April 2024

published in

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volume

334

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issue

3

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page(s)

489-99

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cites work

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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20 May 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

Structure and function in GroEL-mediated protein folding

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Chaperonin-mediated protein folding

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

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3

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Identification of in vivo substrates of the chaperonin GroEL

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Mechanism of substrate recognition by the chaperonin GroEL.

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Residues in chaperonin GroEL required for polypeptide binding and release

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

A structural model for GroEL-polypeptide recognition

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10

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

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11

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Stabilization of GroEL minichaperones by core and surface mutations

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12

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperones.

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13

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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14

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

3 April 2024

15

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

3 April 2024

16

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Symmetric complexes of GroE chaperonins as part of the functional cycle

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Catalysis of protein folding by symmetric chaperone complexes

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Catalysis, commitment and encapsulation during GroE-mediated folding.

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Review: allostery in chaperonins

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23

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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

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33

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Molecular structure of a new family of ribonucleases

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Shape complementarity at protein/protein interfaces

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

3 April 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

GroEL/GroES-mediated folding of a protein too large to be encapsulated

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

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https://api.crossref.org/works/10.1016/J.JMB.2003.09.074

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