Chaperone-assisted protein folding: the path to discovery from a personal perspective (Q48297216)

10 February 2018

title

Chaperone-assisted protein folding: the path to discovery from a personal perspective (English)

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10 February 2018

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1

F Ulrich Hartl

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10 February 2018

language of work or name

English

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publication date

11 October 2011

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published in

Nature Medicine

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volume

17

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issue

10

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page(s)

1206-1210

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Principles that govern the folding of protein chains

cites work

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Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.

21 January 2018

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70K heat shock related proteins stimulate protein translocation into microsomes

21 January 2018

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A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

21 January 2018

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Speculations on the functions of the major heat shock and glucose-regulated proteins

21 January 2018

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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

21 January 2018

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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

21 January 2018

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

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Proteins as molecular chaperones.

21 January 2018

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Host participation in bacteriophage lambda head assembly

21 January 2018

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Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). II. The propagation of phage lambda

21 January 2018

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Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

21 January 2018

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

21 January 2018

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

21 January 2018

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

21 January 2018

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

21 January 2018

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

21 January 2018

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Protein folding in the cell: molecular chaperones pave the way.

21 January 2018

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Molecular chaperones. Opening and closing the Anfinsen cage.

21 January 2018

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

21 January 2018

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

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GroEL structure: a new chapter on assisted folding

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

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In vivo observation of polypeptide flux through the bacterial chaperonin system.

21 January 2018

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A systematic survey of in vivo obligate chaperonin-dependent substrates

21 January 2018

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Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

21 January 2018

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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

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Molecular chaperones in cellular protein folding

21 January 2018

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The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

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

21 January 2018

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Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

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Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

21 January 2018

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Molecular chaperones in protein folding and proteostasis

21 January 2018

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Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

21 January 2018

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Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

21 January 2018

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Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

21 January 2018

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Unfolding protein folding

21 January 2018

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Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

21 January 2018

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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

21 January 2018

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12 December 2020

Lord of the rings: GroES structure

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12 December 2020

Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes

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12 December 2020

The processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related.

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12 December 2020

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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12 December 2020

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

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12 December 2020

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

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12 December 2020

Abortive bacteriophage T4 head assembly in mutants of Escherichia coli

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12 December 2020

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

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12 December 2020

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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12 December 2020

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

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12 December 2020

Peptide binding and release by proteins implicated as catalysts of protein assembly

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12 December 2020

Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs

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12 December 2020

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

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12 December 2020

Identifiers

DOI

10.1038/NM.2467

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10 February 2018

Dimensions Publication ID

1011803139

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10 February 2018