gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Serine carboxypeptidase 1

RISC, serine carboxypeptidase
may act as a serine carboxypeptidase [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, Cdc4, carboxypeptidase, Dicer, ACID
Papers using RISC antibodies
Antiapoptotic function of RNA-binding protein HuR effected through prothymosin alpha.
Preiss Thomas, In PLoS ONE, 2004
... transfected (2 µg per plate) to study the association of miR-24 with mRNAs in the RISC complex.HeLa Tet-off cells (Clontech) were transfected with the ...
Papers on RISC
All-Trans Retinoic Acid Attenuates Hypoxia-Induced Injury in NRK52E Cells via Inhibiting NF-x03BA;B/VEGF and TGF-β2/VEGF Pathway.
Zheng et al., Xuzhou, China. In Cell Physiol Biochem, Feb 2016
The cell viability, expression of VEGF, p65, transforming growth factor-β2 (TGF-β2) and serine carboxypeptidase 1 (Scpep1), and nuclear factor of kappaB (NF-x03BA;B) activities after ATRA treatment were determined by MTT, western blot and electrophoretic mobility shift assay.
RISC assembly: Coordination between small RNAs and Argonaute proteins.
Tomari et al., Tokyo, Japan. In Biochim Biophys Acta, Jan 2016
Small RNAs, including microRNAs, small interfering RNAs, and PIWI-interacting RNAs, assemble with Argonaute (Ago) family proteins into the effector complex called RNA-induced silencing complex (RISC), which mediates sequence-specific target gene silencing.
TP53 regulates miRNA association with AGO2 to remodel the miRNA-mRNA interaction network.
Castellano et al., London, United Kingdom. In Genome Res, Jan 2016
Using AGO2 RIP-seq and PAR-CLIP-seq we show that the DNA-damage-induced increase in binding of let-7 family members to the RISC complex is functional.
Cell-type and Tissue Context-dependent Nuclear Distribution of Human Ago2.
Zheng et al., United States. In J Biol Chem, Jan 2016
UNASSIGNED: Argonaute-2 protein (Ago2), a major component of RISC, has been viewed as a cytoplasmic protein.
Exosome mediated communication within the tumor microenvironment.
Amiji et al., Boston, United States. In J Control Release, Jan 2016
An illustrative distinction is that exosomes derived from cancer cells contain more microRNA than healthy cells and unlike exosomes released from healthy cells, this microRNA can be associated with the RNA-induced silencing complex (RISC) which is required for processing mature and biologically active microRNA.
Recombinant hTRBP and hPACT Modulate hAgo2-Catalyzed siRNA-Mediated Target RNA Cleavage In Vitro.
Restle et al., Regensburg, Germany. In Plos One, Dec 2015
Together with hArgonaute2 (hAgo2) and hDicer they have been reported to form the RISC-loading complex (RLC).
MiRNA-Target Interaction Reveals Cell-Specific Post-Transcriptional Regulation in Mammalian Cell Lines.
Nares et al., Chicago, United States. In Int J Mol Sci, Dec 2015
Ago-2 immunoprecipitation show that miRNA repressed renilla mRNA are associated with functional mi-RISC (miRNA-RNA induced silencing complex).
Single-Molecule Imaging Reveals that Argonaute Reshapes the Binding Properties of Its Nucleic Acid Guides.
Serebrov et al., Worcester, United States. In Cell, Aug 2015
We have developed single-molecule methods to analyze target binding and cleavage mediated by the Argonaute:guide complex, RISC.
[MicroRNAs: what cardiologists should know about them?].
Mericskay, Paris, France. In Presse Med, Jul 2015
MiRNAs are small 21-22 nucleotides long RNAs transcribed from non coding genes or introns of coding genes that are involved the repression of cellular messenger RNAs by the RISC complex.
Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex.
Tomari et al., Tokyo, Japan. In Nature, Jun 2015
Although loading of siRNA duplexes into Drosophila Ago2 requires the Dicer-2-R2D2 heterodimer and the Hsc70/Hsp90 (Hsp90 also known as Hsp83) chaperone machinery, the details of RISC assembly remain unclear.
[Acyltransferases involved in plant secondary metabolism: classification, structure, reaction mechanism].
Jakubowska et al., In Postepy Biochem, 2014
Plant acyltransferases can be divided into two families: serine carboxypeptidase-like acyltransferases (SCPL) and BAHD acyltransferases (named after its first four characterized enzymes).
MicroRNA Processing and Human Cancer.
Calin et al., Houston, United States. In J Clin Med, 2014
As previous studies have shown, the sequential miRNA processing can be divided into three steps: processing by RNAse in the nucleus; transportation by Exportin-5 (XPO5) from the nucleus; and processing by the RNA-induced silencing complex (RISC) in the cytoplasm.
Epigenetic regulation of the DLK1-MEG3 microRNA cluster in human type 2 diabetic islets.
Kaestner et al., Philadelphia, United States. In Cell Metab, 2014
Using HITS-CLIP for the essential RISC-component Argonaute, we identified disease-relevant targets of the chromosome 14q32 microRNAs, such as IAPP and TP53INP1, that cause increased β cell apoptosis upon overexpression in human islets.
Mapping the human miRNA interactome by CLASH reveals frequent noncanonical binding.
Tollervey et al., Edinburgh, United Kingdom. In Cell, 2013
We speculate that these affect the response of RISC to miRNA-target binding.
The structure of human argonaute-2 in complex with miR-20a.
Joshua-Tor et al., United States. In Cell, 2012
Argonaute proteins lie at the heart of the RNA-induced silencing complex (RISC), wherein they use small RNA guides to recognize targets.
Aberrant brain microRNA target and miRISC gene expression in the anx/anx anorexia mouse model.
Estivill et al., Barcelona, Spain. In Gene, 2012
A closer look to the mRNA transcriptome allowed authors to identify upregulation of five miRISC genes, including Dgcr8 and Fmr1, and Ago2, which were later confirmed by real time PCR.
Receptor for activated protein kinase C: requirement for efficient microRNA function and reduced expression in hepatocellular carcinoma.
Koike et al., Tokyo, Japan. In Plos One, 2010
RACK1 binds to KH-type splicing regulatory protein (KSRP), a member of the Dicer complex, and is required for the recruitment of mature miRNAs to the RNA-induced silencing complex (RISC).
Functional characterization of a putative serine carboxypeptidase in vascular smooth muscle cells.
Miano et al., Rochester, United States. In Circ Res, 2009
SCPEP1 promotes smooth muscle cell proliferation and migration in a catalytic triad-dependent, cleavage-independent manner.
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1.
Lübke et al., Göttingen, Germany. In Febs J, 2009
Scpep1-deficient mice were viable and fertile, and did not exhibit either lysosomal storage or reduced lysosomal SC activity under any tested condition.
share on facebooktweetadd +1mail to friends