PIAS proteins: pleiotropic interactors associated with SUMO

No abstract is available for this paper.

• Publication year

  2009

• Venue

  Cellular and Molecular Life Sciences

• Publication date

  2009-06-13

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1007/s00018-009-0061-zPMID 19526197PMCID PMC11115825
• 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.

• Emerging roles of desumoylating enzymes.

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  2008cited by this paper
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  2008cited by this paper
• PIASy Represses CCAAT/Enhancer-binding Protein δ (C/EBPδ) Transcriptional Activity by Sequestering C/EBPδ to the Nuclear Periphery*

  2008cited by this paper
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• Spatial Interplay between PIASy and FIP200 in the Regulation of Signal Transduction and Transcriptional Activity

  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
• Human Protein Reference Database—2009 update

  2008cited by this paper
• Small ubiquitin-related modifiers in chains.

  2007cited by this paper
• Concepts in sumoylation: a decade on

  2007influential reference
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  2007cited by this paper
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  2007cited by this paper
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  2006cited by this paper
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  2006cited by this paper
• Multiple domains in Siz SUMO ligases contribute to substrate selectivity

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  2006cited by this paper
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  2006cited by this paper
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• MINT: the Molecular INTeraction database

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• An extended consensus motif enhances the specificity of substrate modification by SUMO

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• Specification of SUMO1- and SUMO2-interacting Motifs*

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• The Interaction of Piasy with Trim32, an E3-Ubiquitin Ligase Mutated in Limb-girdle Muscular Dystrophy Type 2H, Promotes Piasy Degradation and Regulates UVB-induced Keratinocyte Apoptosis through NFκB*

  2006cited by this paper
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  2006cited by this paper
• Human protein reference database—2006 update

  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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