The Doc1 subunit is a processivity factor for the anaphase-promoting complex

No abstract is available for this paper.

• Publication year

  2002

• Venue

  Nature Cell Biology

• Publication date

  2002-11-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/ncb871PMID 12402045
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2001cited by this paper
• Mechanisms underlying ubiquitination.

  2001cited by this paper
• Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex.

  2001cited by this paper
• Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC

  2001cited by this paper
• Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex

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• The tandem affinity purification (TAP) method: a general procedure of protein complex purification.

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• APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.

  2001cited by this paper
• Sliding clamps: a (tail)ored fit.

  2000cited by this paper
• The APC11 RING-H2 finger mediates E2-dependent ubiquitination.

  2000cited by this paper
• The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex.

  2000cited by this paper
• Ubiquitin in chains.

  2000cited by this paper
• A generic protein purification method for protein complex characterization and proteome exploration

  1999cited by this paper
• Characterization of the DOC1/APC10 Subunit of the Yeast and the Human Anaphase-promoting Complex*

  1999cited by this paper
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  1999cited by this paper
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  1998cited by this paper
• The ubiquitin system.

  1998cited by this paper
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• Activation of the APC/C ubiquitin ligase by enhanced E2 efficiency.

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