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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Anaphase promoting complex subunit 11

APC11, ANAPC11, Apc11p
Top mentioned proteins: Ubiquitin, APC, APC2, Cullin, PCNA
Papers on APC11
RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex.
Schulman et al., Vienna, Austria. In Proc Natl Acad Sci U S A, May 2015
On the opposite side of the APC, the dynamic catalytic core contains the cullin-like subunit APC2 and its RING partner APC11, which collaborates with the E2 UBCH10 (UBE2C) to ubiquitinate substrates.
A single-nucleotide exon found in Arabidopsis.
Liu et al., Beijing, China. In Sci Rep, 2014
Here we report that the Anaphase Promoting Complex subunit 11 (APC11) gene in Arabidopsis thaliana carries a constitutive single-nucleotide exon.
Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly.
Schulman et al., Memphis, United States. In Mol Cell, 2014
During chain assembly, a distinct APC11 RING surface helps deliver a substrate-linked ubiquitin to accept another ubiquitin from UBE2S.
The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation.
Yokoyama et al., Yokohama, Japan. In Febs Open Bio, 2013
Furthermore, we revealed that the ZBR fragment of Emi2 inhibits in vitro ubiquitin chain elongation catalyzed by the APC/C cullin-RING ligase module, the ANAPC2-ANAPC11 subcomplex, in combination with the ubiquitin chain-initiating E2, E2C/UBE2C/UbcH10.
Transcription-independent function of Polycomb group protein PSC in cell cycle control.
Verrijzer et al., Rotterdam, Netherlands. In Science, 2012
Cell-based experiments and reconstituted reactions established that PSC and Lemming (LMG, also called APC11) associate and ubiquitylate CYC-B cooperatively, marking it for proteosomal degradation.
lemmingA encodes the Apc11 subunit of the APC/C in Drosophila melanogaster that forms a ternary complex with the E2-C type ubiquitin conjugating enzyme, Vihar and Morula/Apc2.
Deák et al., Szeged, Hungary. In Cell Div, 2011
Here, lemming (lmg) mutants were used to study the APC/C subunit, Apc11, and its interaction partners in Drosophila melanogaster.
Knockdown expression of Apc11 leads to cell-cycle distribution reduction in G2/M phase.
Huo et al., Shanghai, China. In Genet Mol Res, 2011
In this study, 4 synthesized small interfering RNAs (siRNAs) were transfected into HEK293T cells to suppress messenger RNA (mRNA) of Apc11; 2 of these reduced the amount of Apc11 mRNA by over 50%.
Structural basis for the subunit assembly of the anaphase-promoting complex.
Barford et al., London, United Kingdom. In Nature, 2011
Our structure explains how this TPR sub-complex, together with additional scaffolding subunits (Apc1, Apc4 and Apc5), coordinate the juxtaposition of the catalytic and substrate recognition module (Apc2, Apc11 and Apc10 (also known as Doc1)), and TPR-phosphorylation sites, relative to co-activator, regulatory proteins and substrates.
Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.
Peters et al., Vienna, Austria. In Nat Struct Mol Biol, 2011
We show that Doc1 interacts with Cdc27, Cdc16 and Apc1 and is located in the vicinity of the cullin-RING module Apc2-Apc11 in the inner cavity of the APC/C.
Orf virus cell cycle regulator, PACR, competes with subunit 11 of the anaphase promoting complex for incorporation into the complex.
Mercer et al., Dunedin, New Zealand. In J Gen Virol, 2010
The authors showed, in vitro, a direct interaction between Orf virus anaphase promoting complex regulator and APC2 and its interference with interactions between APC11 and APC2.
Molecular structure of the N-terminal domain of the APC/C subunit Cdc27 reveals a homo-dimeric tetratricopeptide repeat architecture.
Barford et al., London, United Kingdom. In J Mol Biol, 2010
Biochemical and genetic studies are consistent with the notion that subunits of APC/C are organised into two distinct sub-complexes; a catalytic sub-complex including the cullin domain and RING finger subunits Apc2 and Apc11, respectively, and a tetratricopeptide repeat (TPR) sub-complex composed of the TPR subunits Cdc16, Cdc23 and Cdc27 (Apc3).
The emerging role of APC/CCdh1 in controlling differentiation, genomic stability and tumor suppression.
Cross et al., Freiburg, Germany. In Oncogene, 2010
Studies indicate that APC/C(Cdh1) is required to maintain genomic stability.
Cell cycle deregulation by a poxvirus partial mimic of anaphase-promoting complex subunit 11.
Mercer et al., Dunedin, New Zealand. In Proc Natl Acad Sci U S A, 2009
APC consists of at least 12 subunits with the catalytic core formed by a scaffold protein, APC2, and a RING-H2 protein, APC11.
Molecular cloning of cDNA encoding APC11, a catalytic component of anaphase-promoting-complex (APC/C), from goldfish (Carassius auratus), and establishment of in vitro ubiquitinating system.
Tokumoto et al., Shizuoka, Japan. In Zoolog Sci, 2006
Here we present the cloning, sequencing, and expression analysis of goldfish (Carassius auratus) APC11, which encodes the catalytic component of APC/C from goldfish ovary.
Methods to measure ubiquitin-dependent proteolysis mediated by the anaphase-promoting complex.
Peters et al., Vienna, Austria. In Methods, 2006
In vitro, APC's RING finger subunit Apc11 alone can also function as a ubiquitin ligase.
The RING-H2-finger protein APC11 as a target of hydrogen peroxide.
Rhee et al., Bethesda, United States. In Free Radic Biol Med, 2004
Inhibition of APC11 function by H(2)O(2) contributes to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress
APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.
Yu et al., Dallas, United States. In Mol Biol Cell, 2001
APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.
Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins.
Nasmyth et al., Vienna, Austria. In Science, 1998
Apc2p, Apc5p, and the RING-finger protein Apc11p are conserved from yeast to humans.
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