Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. (Q44317704)

1 December 2017

Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. (English)

1 reference

1 December 2017

Galit Kafri

1

1 reference

PubMed ID

12589746

1 December 2017

Amnon Horovitz

series ordinal

2

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PubMed ID

12589746

1 December 2017

language of work or name

English

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publication date

1 February 2003

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Journal of Molecular Biology

1 December 2017

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1 December 2017

326

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1 December 2017

4

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1 December 2017

981-987

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Chaperone rings in protein folding and degradation.

1 December 2017

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Helicase structure and mechanism

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Chaperonin-mediated protein folding

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Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

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Structure and function in GroEL-mediated protein folding

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Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

7 January 2021

1 reference

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Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

7 January 2021

1 reference

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ATP-bound states of GroEL captured by cryo-electron microscopy

7 January 2021

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ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex

7 January 2021

1 reference

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Review: allostery in chaperonins

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Chaperonin function: folding by forced unfolding

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

7 January 2021

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Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

7 January 2021

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

7 January 2021

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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

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The allosteric mechanism of the chaperonin GroEL: a dynamic analysis

7 January 2021

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A dynamic model for the allosteric mechanism of GroEL

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On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins

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The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex

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Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.

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Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

7 January 2021

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3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

7 January 2021

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Review: nucleotide-dependent conformational changes of the chaperonin containing TCP-1.

7 January 2021

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Conformational rearrangements of an archaeal chaperonin upon ATPase cycling.

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Mechanisms of protein folding

7 January 2021

1 reference

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

7 January 2021

1 reference

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Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis

7 January 2021

1 reference

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Peptides derived from human C-reactive protein inhibit the enzymatic activities of human leukocyte elastase and cathepsin G: use of overlapping peptide sequences to identify a unique inhibitor

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10.1016/S0022-2836(03)00046-9

7 January 2021

Identifiers

DOI

1 reference

1 December 2017

1 reference

PubMed ID

12589746