Dynamic complex formation during the yeast cell cycle

Research output: Contribution to journalJournal articlepeer-review

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Dynamic complex formation during the yeast cell cycle. / de Lichtenberg, Ulrik; Jensen, Lars Juhl; Brunak, Søren; Bork, Peer.

In: Science (New York, N.Y.), Vol. 307, No. 5710, 2005, p. 724-7.

Research output: Contribution to journalJournal articlepeer-review

Harvard

de Lichtenberg, U, Jensen, LJ, Brunak, S & Bork, P 2005, 'Dynamic complex formation during the yeast cell cycle', Science (New York, N.Y.), vol. 307, no. 5710, pp. 724-7. https://doi.org/10.1126/science.1105103

APA

de Lichtenberg, U., Jensen, L. J., Brunak, S., & Bork, P. (2005). Dynamic complex formation during the yeast cell cycle. Science (New York, N.Y.), 307(5710), 724-7. https://doi.org/10.1126/science.1105103

Vancouver

de Lichtenberg U, Jensen LJ, Brunak S, Bork P. Dynamic complex formation during the yeast cell cycle. Science (New York, N.Y.). 2005;307(5710):724-7. https://doi.org/10.1126/science.1105103

Author

de Lichtenberg, Ulrik ; Jensen, Lars Juhl ; Brunak, Søren ; Bork, Peer. / Dynamic complex formation during the yeast cell cycle. In: Science (New York, N.Y.). 2005 ; Vol. 307, No. 5710. pp. 724-7.

Bibtex

@article{2c49764ce12242958adb241cebbfbd15,
title = "Dynamic complex formation during the yeast cell cycle",
abstract = "To analyze the dynamics of protein complexes during the yeast cell cycle, we integrated data on protein interactions and gene expression. The resulting time-dependent interaction network places both periodically and constitutively expressed proteins in a temporal cell cycle context, thereby revealing previously unknown components and modules. We discovered that most complexes consist of both periodically and constitutively expressed subunits, which suggests that the former control complex activity by a mechanism of just-in-time assembly. Consistent with this, we show that additional regulation through targeted degradation and phosphorylation by Cdc28p (Cdk1) specifically affects the periodically expressed proteins.",
author = "{de Lichtenberg}, Ulrik and Jensen, {Lars Juhl} and S{\o}ren Brunak and Peer Bork",
year = "2005",
doi = "10.1126/science.1105103",
language = "English",
volume = "307",
pages = "724--7",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5710",

}

RIS

TY - JOUR

T1 - Dynamic complex formation during the yeast cell cycle

AU - de Lichtenberg, Ulrik

AU - Jensen, Lars Juhl

AU - Brunak, Søren

AU - Bork, Peer

PY - 2005

Y1 - 2005

N2 - To analyze the dynamics of protein complexes during the yeast cell cycle, we integrated data on protein interactions and gene expression. The resulting time-dependent interaction network places both periodically and constitutively expressed proteins in a temporal cell cycle context, thereby revealing previously unknown components and modules. We discovered that most complexes consist of both periodically and constitutively expressed subunits, which suggests that the former control complex activity by a mechanism of just-in-time assembly. Consistent with this, we show that additional regulation through targeted degradation and phosphorylation by Cdc28p (Cdk1) specifically affects the periodically expressed proteins.

AB - To analyze the dynamics of protein complexes during the yeast cell cycle, we integrated data on protein interactions and gene expression. The resulting time-dependent interaction network places both periodically and constitutively expressed proteins in a temporal cell cycle context, thereby revealing previously unknown components and modules. We discovered that most complexes consist of both periodically and constitutively expressed subunits, which suggests that the former control complex activity by a mechanism of just-in-time assembly. Consistent with this, we show that additional regulation through targeted degradation and phosphorylation by Cdc28p (Cdk1) specifically affects the periodically expressed proteins.

U2 - 10.1126/science.1105103

DO - 10.1126/science.1105103

M3 - Journal article

C2 - 15692050

VL - 307

SP - 724

EP - 727

JO - Science

JF - Science

SN - 0036-8075

IS - 5710

ER -

ID: 40740621