Identification and Herc5-mediated ISGylation of novel target proteins.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Biochemical and Biophysical Research Communications - BBRC

• Publication date

  2006-09-22

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/J.BBRC.2006.07.076PMID 16884686
• 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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• Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.

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• Identification of Interferon-Stimulated Gene 15 as an Antiviral Molecule during Sindbis Virus Infection In Vivo

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• ISG15: a ubiquitin-like enigma.

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• The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-α/β-induced ubiquitin-like protein

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• Interferon-Inducible Ubiquitin E2, Ubc8, Is a Conjugating Enzyme for Protein ISGylation

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• HERC5, a HECT E3 ubiquitin ligase tightly regulated in LPS activated endothelial cells

  2004cited by this paper
• The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein.

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• Alternate interferon signaling pathways.

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• Tom1, a VHS Domain-containing Protein, Interacts with Tollip, Ubiquitin, and Clathrin*

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• UBP43 (USP18) Specifically Removes ISG15 from Conjugated Proteins*

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• Mechanisms underlying ubiquitination.

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• ISG15: It's Complicated

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• Covalent ISG15 conjugation to CHIP promotes its ubiquitin E3 ligase activity and inhibits lung cancer cell growth in response to type I interferon

  2018cites this paper
• SUMO‐specific protease 2 (SENP2) suppresses keratinocyte migration by targeting NDR1 for de‐SUMOylation

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