Autoantigen Ro52 is an E3 ubiquitin ligase (Q24296239)

protein monoubiquitination

GOA release 2020-03-11

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Biochemical and Biophysical Research Communications

GOA release 2020-03-11

author name string

Keiji Wada

series ordinal

1

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Tetsu Kamitani

series ordinal

2

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language of work or name

English

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publication date

6 January 2006

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published in

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volume

339

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page(s)

415-21

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issue

1

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cites work

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TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase

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Ubiquitination of Ro52 autoantigen

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pVHL-independent ubiquitination of HIF1alpha and its stabilization by cobalt ion.

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Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain

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Does this have a familiar RING?

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RING finger ubiquitin protein ligases: implications for tumorigenesis, metastasis and for molecular targets in cancer

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Interaction between 52 kDa SSA/Ro and deubiquitinating enzyme UnpEL: a clue to function

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Enhanced Mdm2 activity inhibits pRB function via ubiquitin-dependent degradation

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Association of stress proteins with autoantigens: a possible mechanism for triggering autoimmunity?

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Two B or not two B? Overview of the rapidly expanding B-box family of proteins

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The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate.

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E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

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Covalent modification of PML by the sentrin family of ubiquitin-like proteins

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Ubiquitin ligases and the immune response

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Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes

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SS-A/Ro52, an autoantigen involved in CD28-mediated IL-2 production.

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

4681540

4681540

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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