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 tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Hartmann-Petersen, R & Gordon, C 2004, 'Proteins interacting with the 26S proteasome.', Cellular and molecular life sciences : CMLS, bind 61, nr. 13, s. 1589-95. https://doi.org/10.1007/s00018-004-4132-x

APA

Hartmann-Petersen, R., & Gordon, C. (2004). Proteins interacting with the 26S proteasome. Cellular and molecular life sciences : CMLS, 61(13), 1589-95. https://doi.org/10.1007/s00018-004-4132-x

Vancouver

Hartmann-Petersen R, Gordon C. Proteins interacting with the 26S proteasome. Cellular and molecular life sciences : CMLS. 2004;61(13):1589-95. https://doi.org/10.1007/s00018-004-4132-x

Author

Hartmann-Petersen, R ; Gordon, C. / Proteins interacting with the 26S proteasome. I: Cellular and molecular life sciences : CMLS. 2004 ; Bind 61, Nr. 13. s. 1589-95.

Bibtex

@article{8a0a4bc09e9111dd86a6000ea68e967b,
title = "Proteins interacting with the 26S proteasome.",
abstract = "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.",
author = "R Hartmann-Petersen and C Gordon",
note = "Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Substrate Specificity; Ubiquitin; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligases",
year = "2004",
doi = "10.1007/s00018-004-4132-x",
language = "English",
volume = "61",
pages = "1589--95",
journal = "EXS",
issn = "1023-294X",
publisher = "Springer Basel AG",
number = "13",

}

RIS

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