E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme (Q28213786)

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J Y Choi

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Y M Sung

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H Park

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H Rhim

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S Kang

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902689-8

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language of work or name

English

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publication date

10 August 2001

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published in

FEBS Letters

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volume

503

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issue

1

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page(s)

61-4

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1 reference

Basic Medical Research Award. The ubiquitin system.

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Protein degradation or regulation: Ub the judge

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The ubiquitin-conjugation system

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RING finger proteins: mediators of ubiquitin ligase activity

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Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme

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A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4

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The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1

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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

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The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase

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The APC11 RING-H2 finger mediates E2-dependent ubiquitination

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The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain

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Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

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RING for destruction?

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Proteolysis and the cell cycle: with this RING I do thee destroy

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The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases

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Biochemistry. Ubiquitination--more than two to tango

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Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain.

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The Bmi-1 oncoprotein interacts with dinG and MPh2: the role of RING finger domains

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Identification and analysis of a third mouse Polycomb gene, MPc3

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Production of monoclonal antibodies against mammalian Ring1B proteins

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