(Q43028887)

12 November 2017

title

Characterization of a novel complex from halophilic archaebacteria, which displays chaperone-like activities in vitro (English)

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12 November 2017

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2

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12 November 2017

4

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12 November 2017

Franzetti B

1

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12 November 2017

Ebel C

series ordinal

3

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12 November 2017

Ruigrok RW

series ordinal

5

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12 November 2017

Zaccai G

series ordinal

6

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12 November 2017

language of work or name

English

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publication date

6 June 2001

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Journal of Biological Chemistry

12 November 2017

published in

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12 November 2017

volume

276

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12 November 2017

issue

32

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12 November 2017

page(s)

29906-29914

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Ion metabolism in a Halobacterium. I. Influence of age of culture on intracellular concentrations

12 November 2017

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Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions.

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Molecular chaperones in cellular protein folding

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The Hsp70 and Hsp60 chaperone machines

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Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.

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The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome.

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

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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

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Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro

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A molecular chaperone, ClpA, functions like DnaK and DnaJ.

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An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes

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Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome

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21 January 2018

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Osmotically induced response in representatives of halophilic prokaryotes: the bacterium Halomonas elongata and the archaeon Haloferax volcanii

21 January 2018

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Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization

21 January 2018

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Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

21 January 2018

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Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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Biochemical and serological evidence for an RNase E-like activity in halophilic Archaea

21 January 2018

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The protein sequence of an archaeal catalase-peroxidase

21 January 2018

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21 January 2018

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21 January 2018

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Solution studies of elongation factor Tu from the extreme halophile Halobacterium marismortui

21 January 2018

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

21 January 2018

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Stabilization of halophilic malate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

Genome sequence of Halobacterium species NRC-1

21 January 2018

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

21 January 2018

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Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase.

21 January 2018

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Hsp90 & Co. - a holding for folding

21 January 2018

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Denaturation of a halophilic enzyme monitored by small-angle neutron scattering

21 January 2018

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Halophilic enzymes: proteins with a grain of salt

21 January 2018

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The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M102098200

The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro

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

1 reference

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Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102098200

21 January 2018

Identifiers

DOI

10.1074/JBC.M102098200

1 reference

12 November 2017

1 reference