ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation

scientific article published in January 2003

ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/S1097-2765(02)00775-X
P698PubMed publication ID12535522
P5875ResearchGate publication ID10943135

P50authorNadia BenaroudjQ100457219
P2093author name stringWolfgang Baumeister
Alfred L Goldberg
Peter Zwickl
Erika Seemüller
P2860cites workPAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperoneQ73135763
Structure and functions of the 20S and 26S proteasomesQ24328777
A gated channel into the proteasome core particleQ27627907
Structural basis for the activation of 20S proteasomes by 11S regulatorsQ27628418
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolutionQ27730197
Structure of 20S proteasome from yeast at 2.4 A resolutionQ27735081
The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product releaseQ27933726
The regulatory particle of the Saccharomyces cerevisiae proteasome.Q27936746
Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasomeQ27937064
AAA+ superfamily ATPases: common structure--diverse functionQ28208908
Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machineQ28366801
The proteasome: paradigm of a self-compartmentalizing proteaseQ29615187
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.Q30322959
Proteasomes and other self-compartmentalizing proteases in prokaryotesQ33542295
An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomesQ33873082
A proteasomal ATPase subunit recognizes the polyubiquitin degradation signalQ33958676
Conformational constraints in protein degradation by the 20S proteasomeQ34058982
Proteasome from Thermoplasma acidophilum: a threonine proteaseQ34309062
The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinaseQ34742836
Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.Q35190125
Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.Q35190292
The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzymeQ36342543
The mechanism and functions of ATP-dependent proteases in bacterial and animal cellsQ36736334
Structural features of 26S and 20S proteasomes.Q40494212
Proteins are unfolded on the surface of the ATPase ring before transport into the proteasomeQ43846790
Dynamics of substrate denaturation and translocation by the ClpXP degradation machineQ47235359
Renaturation of Aequorea green-fluorescent proteinQ52735030
Chaperonin-mediated folding of green fluorescent protein.Q54566046
Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli.Q54668957
Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured proteinQ56135899
Secondary structure of bovine αS1- and β-casein in solutionQ70994728
Critical elements in proteasome assemblyQ71955022
P433issue1
P304page(s)69-78
P577publication date2003-01-01
P1433published inMolecular CellQ3319468
P1476titleATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
P478volume11

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cites work (P2860)
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