Protein degradation: recognition of ubiquitinylated substrates.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Protein degradation: recognition of ubiquitinylated substrates. / Hartmann-Petersen, Rasmus; Gordon, Colin.

I: Current Biology, Bind 14, Nr. 18, 2004, s. R754-6.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Hartmann-Petersen, R & Gordon, C 2004, 'Protein degradation: recognition of ubiquitinylated substrates.', Current Biology, bind 14, nr. 18, s. R754-6. https://doi.org/10.1016/j.cub.2004.09.012

APA

Hartmann-Petersen, R., & Gordon, C. (2004). Protein degradation: recognition of ubiquitinylated substrates. Current Biology, 14(18), R754-6. https://doi.org/10.1016/j.cub.2004.09.012

Vancouver

Hartmann-Petersen R, Gordon C. Protein degradation: recognition of ubiquitinylated substrates. Current Biology. 2004;14(18):R754-6. https://doi.org/10.1016/j.cub.2004.09.012

Author

Hartmann-Petersen, Rasmus ; Gordon, Colin. / Protein degradation: recognition of ubiquitinylated substrates. I: Current Biology. 2004 ; Bind 14, Nr. 18. s. R754-6.

Bibtex

@article{1b231b2095f311dd86a6000ea68e967b,
title = "Protein degradation: recognition of ubiquitinylated substrates.",
abstract = "A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.",
author = "Rasmus Hartmann-Petersen and Colin Gordon",
note = "Keywords: Carrier Proteins; Cell Cycle Proteins; DNA-Binding Proteins; Models, Biological; Proteasome Endopeptidase Complex; Protein Binding; Proteins; Saccharomyces cerevisiae Proteins; Schizosaccharomyces pombe Proteins; Ubiquitins; Yeasts",
year = "2004",
doi = "10.1016/j.cub.2004.09.012",
language = "English",
volume = "14",
pages = "R754--6",
journal = "Current Biology",
issn = "0960-9822",
publisher = "Cell Press",
number = "18",

}

RIS

TY - JOUR

T1 - Protein degradation: recognition of ubiquitinylated substrates.

AU - Hartmann-Petersen, Rasmus

AU - Gordon, Colin

N1 - Keywords: Carrier Proteins; Cell Cycle Proteins; DNA-Binding Proteins; Models, Biological; Proteasome Endopeptidase Complex; Protein Binding; Proteins; Saccharomyces cerevisiae Proteins; Schizosaccharomyces pombe Proteins; Ubiquitins; Yeasts

PY - 2004

Y1 - 2004

N2 - A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.

AB - A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.

U2 - 10.1016/j.cub.2004.09.012

DO - 10.1016/j.cub.2004.09.012

M3 - Journal article

C2 - 15380085

VL - 14

SP - R754-6

JO - Current Biology

JF - Current Biology

SN - 0960-9822

IS - 18

ER -

ID: 6493136