N Benaroudj
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Explore the profile of N Benaroudj including associated specialties, affiliations and a list of published articles.
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8
Citations
352
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Recent Articles
1.
Benaroudj N, Lee D, GOLDBERG A
J Biol Chem
. 2001 Apr;
276(26):24261-7.
PMID: 11301331
The disaccharide trehalose, which accumulates dramatically during heat shock and stationary phase in many organisms, enhances thermotolerance and reduces aggregation of denatured proteins. Here we report a new role for...
2.
Benaroudj N, Tarcsa E, Cascio P, GOLDBERG A
Biochimie
. 2001 Apr;
83(3-4):311-8.
PMID: 11295491
26S proteasomes are composed of a 20S proteolytic core and two ATPase-containing 19S regulatory particles. To clarify the role of these ATPases in proteolysis, we studied the PAN complex, the...
3.
Benaroudj N, GOLDBERG A
Nat Cell Biol
. 2000 Nov;
2(11):833-9.
PMID: 11056539
The proteasome-activating nucleotidase (PAN) from Methanococcus jannaschii is a complex of relative molecular mass 650,000 that is homologous to the ATPases in the eukaryotic 26S proteasome. When mixed with 20S...
4.
Fouchaq B, Benaroudj N, Ebel C, Ladjimi M
Eur J Biochem
. 1999 Jan;
259(1-2):379-84.
PMID: 9914517
Crystallographic and biochemical studies have indicated that the peptide-binding site of the molecular chaperone HSC70 is located in a small subdomain comprising a beta-sheet motif followed by a helical region,...
5.
Benaroudj N, Fouchaq B, Ladjimi M
J Biol Chem
. 1997 Mar;
272(13):8744-51.
PMID: 9079709
We have previously shown that the molecular chaperone HSC70 self-associates in solution into dimers, trimers, and probably high order oligomers, according to a slow temperature- and concentration-dependent equilibrium that is...
6.
Benaroudj N, Triniolles F, Ladjimi M
J Biol Chem
. 1996 Aug;
271(31):18471-6.
PMID: 8702492
In a previous study, we showed that the molecular chaperone HSC70 self-associates in solution in a reversible and likely unlimited fashion. Here, we examine the influence of nucleotides, nucleotide analogs,...
7.
Benaroudj N, Batelier G, Triniolles F, Ladjimi M
Biochemistry
. 1995 Nov;
34(46):15282-90.
PMID: 7578144
The self-association properties of the molecular chaperone HSC70 have been analyzed by a wide range of biochemical and biophysical techniques. Nondenaturing gel electrophoresis and cross-linking studies show the presence of...
8.
Benaroudj N, Fang B, Triniolles F, Ghelis C, Ladjimi M
Eur J Biochem
. 1994 Apr;
221(1):121-8.
PMID: 8168501
The 70-kDa heat-shock cognate protein (HSC70), a constitutively expressed protein in mammalian cells, plays a major role in several cellular processes such as protein folding and assembly, uncoating of clathrin-coated...