Integral UBL domain proteins: a family of proteasome interacting proteins.

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Standard

Integral UBL domain proteins: a family of proteasome interacting proteins. / Hartmann-Petersen, Rasmus; Gordon, Colin.

In: Seminars in Cell and Developmental Biology, Vol. 15, No. 2, 2004, p. 247-59.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hartmann-Petersen, R & Gordon, C 2004, 'Integral UBL domain proteins: a family of proteasome interacting proteins.', Seminars in Cell and Developmental Biology, vol. 15, no. 2, pp. 247-59.

APA

Hartmann-Petersen, R., & Gordon, C. (2004). Integral UBL domain proteins: a family of proteasome interacting proteins. Seminars in Cell and Developmental Biology, 15(2), 247-59.

Vancouver

Hartmann-Petersen R, Gordon C. Integral UBL domain proteins: a family of proteasome interacting proteins. Seminars in Cell and Developmental Biology. 2004;15(2):247-59.

Author

Hartmann-Petersen, Rasmus ; Gordon, Colin. / Integral UBL domain proteins: a family of proteasome interacting proteins. In: Seminars in Cell and Developmental Biology. 2004 ; Vol. 15, No. 2. pp. 247-59.

Bibtex

@article{f3d2c15095f311dd86a6000ea68e967b,
title = "Integral UBL domain proteins: a family of proteasome interacting proteins.",
abstract = "The family of ubiquitin-like (UBL) domain proteins (UDPs) comprises a conserved group of proteins involved in a multitude of different cellular activities. However, recent studies on UBL-domain proteins indicate that these proteins appear to share a common property in their ability to interact with 26S proteasomes. The 26S proteasome is a multisubunit protease which is responsible for the majority of intracellular proteolysis in eukaryotic cells. Before degradation commences most proteins are first marked for destruction by being coupled to a chain of ubiquitin molecules. Some UBL-domain proteins catalyse the formation of ubiquitin-protein conjugates, whereas others appear to target ubiquitinated proteins for degradation and interact with chaperones. Hence, by binding to the 26S proteasome the UBL-domain proteins seem to tailor and direct the basic proteolytic functions of the particle to accommodate various cellular substrates.",
author = "Rasmus Hartmann-Petersen and Colin Gordon",
note = "Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Protein Structure, Tertiary; Ubiquitin-Protein Ligases; Ubiquitins",
year = "2004",
language = "English",
volume = "15",
pages = "247--59",
journal = "Seminars in Cell and Developmental Biology",
issn = "1084-9521",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - Integral UBL domain proteins: a family of proteasome interacting proteins.

AU - Hartmann-Petersen, Rasmus

AU - Gordon, Colin

N1 - Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Protein Structure, Tertiary; Ubiquitin-Protein Ligases; Ubiquitins

PY - 2004

Y1 - 2004

N2 - The family of ubiquitin-like (UBL) domain proteins (UDPs) comprises a conserved group of proteins involved in a multitude of different cellular activities. However, recent studies on UBL-domain proteins indicate that these proteins appear to share a common property in their ability to interact with 26S proteasomes. The 26S proteasome is a multisubunit protease which is responsible for the majority of intracellular proteolysis in eukaryotic cells. Before degradation commences most proteins are first marked for destruction by being coupled to a chain of ubiquitin molecules. Some UBL-domain proteins catalyse the formation of ubiquitin-protein conjugates, whereas others appear to target ubiquitinated proteins for degradation and interact with chaperones. Hence, by binding to the 26S proteasome the UBL-domain proteins seem to tailor and direct the basic proteolytic functions of the particle to accommodate various cellular substrates.

AB - The family of ubiquitin-like (UBL) domain proteins (UDPs) comprises a conserved group of proteins involved in a multitude of different cellular activities. However, recent studies on UBL-domain proteins indicate that these proteins appear to share a common property in their ability to interact with 26S proteasomes. The 26S proteasome is a multisubunit protease which is responsible for the majority of intracellular proteolysis in eukaryotic cells. Before degradation commences most proteins are first marked for destruction by being coupled to a chain of ubiquitin molecules. Some UBL-domain proteins catalyse the formation of ubiquitin-protein conjugates, whereas others appear to target ubiquitinated proteins for degradation and interact with chaperones. Hence, by binding to the 26S proteasome the UBL-domain proteins seem to tailor and direct the basic proteolytic functions of the particle to accommodate various cellular substrates.

M3 - Journal article

C2 - 15209385

VL - 15

SP - 247

EP - 259

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

SN - 1084-9521

IS - 2

ER -

ID: 6493154