Proteins interacting with the 26S proteasome.
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Proteins interacting with the 26S proteasome. / Hartmann-Petersen, R; Gordon, C.
I: Cellular and molecular life sciences : CMLS, Bind 61, Nr. 13, 2004, s. 1589-95.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Proteins interacting with the 26S proteasome.
AU - Hartmann-Petersen, R
AU - Gordon, C
N1 - Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Substrate Specificity; Ubiquitin; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligases
PY - 2004
Y1 - 2004
N2 - The 26S proteasome is the multi-protein protease that recognizes and degrades ubiquitinylated substrates targeted for destruction by the ubiquitin pathway. In addition to the well-documented subunit organization of the 26S holoenzyme, it is clear that a number of other proteins transiently associate with the 26S complex. These transiently associated proteins confer a number of different roles such as substrate presentation, cleavage of the multi-ubiquitin chain from the protein substrate and turnover of misfolded proteins. Such activities are essential for the 26S proteasome to efficiently fulfill its intracellular function in protein degradation.
AB - The 26S proteasome is the multi-protein protease that recognizes and degrades ubiquitinylated substrates targeted for destruction by the ubiquitin pathway. In addition to the well-documented subunit organization of the 26S holoenzyme, it is clear that a number of other proteins transiently associate with the 26S complex. These transiently associated proteins confer a number of different roles such as substrate presentation, cleavage of the multi-ubiquitin chain from the protein substrate and turnover of misfolded proteins. Such activities are essential for the 26S proteasome to efficiently fulfill its intracellular function in protein degradation.
U2 - 10.1007/s00018-004-4132-x
DO - 10.1007/s00018-004-4132-x
M3 - Journal article
C2 - 15224183
VL - 61
SP - 1589
EP - 1595
JO - EXS
JF - EXS
SN - 1023-294X
IS - 13
ER -
ID: 6708789