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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

RNA guanylyltransferase and 5'-phosphatase

HCE1, mRNA 5'-triphosphatase
Top mentioned proteins: ACID, CAN, Carboxylesterase, POLYMERASE, Alcohol Dehydrogenase
Papers on HCE1
A novel role for Cet1p mRNA 5'-triphosphatase in promoter proximal accumulation of RNA polymerase II in Saccharomyces cerevisiase.
Bhaumik et al., Carbondale, United States. In Genetics, 2014
Yeast mRNA 5'-triphosphatase, Cet1p, recognizes phosphorylated-RNA polymerase II as a component of capping machinery via Ceg1p for cotranscriptional formation of mRNA cap structure that recruits cap-binding complex (CBC) and protects mRNA from exonucleases.
Exploring the Relationship between the Inhibition Selectivity and the Apoptosis of Roscovitine-Treated Cancer Cells.
Peng et al., Beijing, China. In J Anal Methods Chem, 2012
THE ANTITUMOR ACTIVITY OF ROSCOVITINE WAS TESTED IN FOUR CERVICAL CARCINOMA CELLS: C33A, HCE-1, HeLa, and SiHa.
[Progress in the structure and function of human carboxylesterase 1].
Review
Lü et al., Changsha, China. In Sheng Wu Gong Cheng Xue Bao, 2012
Human carboxylesterase 1 (HCE1), belonging to a multigene serine hydrolase family, is a major liver carboxylesterase responsible for the hydrolysis and metabolism of various xenobiotics.
Structure of the guanylyltransferase domain of human mRNA capping enzyme.
GeneRIF
Shatkin et al., United States. In Proc Natl Acad Sci U S A, 2011
Data show that human capping enzyme residues 229-567 comprise the minimum enzymatically active human GTase (hGTase) domain and determine the structure by X-ray crystallography.
Lipopolysaccharide down-regulates carbolesterases 1 and 2 and reduces hydrolysis activity in vitro and in vivo via p38MAPK-NF-κB pathway.
Yang et al., Nanjing, China. In Toxicol Lett, 2011
In this study, we have demonstrated, in vitro and in vivo, treatment with LPS decreased the expression of HCE1 and HCE2 and the capacity of hydrolytic activity.
Effect of CD147 monoclonal antibody on paclitaxel resistance in HCE1 multicellular spheroids.
Wu et al., Changsha, China. In Zhong Nan Da Xue Xue Bao Yi Xue Ban, 2011
OBJECTIVE: To investigate the effect of CD147 monoclonal antibody (mAb) on the natural resistance to paclitaxel (TAX) in the human cervical cancer line (HCE1) multicellular spheroid (HCE1/MCS) model and if CD147 mAb can reverse the HCE1/MCS resistance to TAX.
[Effect of GM6001 on the model that cervical squamous carcinoma cell line HCE1 multicellular spheroids invade live human umbilical vein endothelium cell monolayers].
Wu et al., Changsha, China. In Zhong Nan Da Xue Xue Bao Yi Xue Ban, 2010
OBJECTIVE: To investigate the relationship between matrix matrix metalloproteinases (MMP)-9 expression in HCE1/multicellular spheroids (MCS) and invasion of cervical carcinoma, and to explore the effect of MMPs inhibitor GM6001 on the model that HCE1/MCS invade live human umbilical vein endothelium cell (HUVEC).
[Reversion of resistance to cisplatin induced by MG132 in cervical cancer line HCE1 multicellular spheroid].
Hu et al., Changsha, China. In Zhonghua Fu Chan Ke Za Zhi, 2010
OBJECTIVE: To investigate the effect of the ubiquitin-proteasome pathway inhibitor MG132 on the natural resistance to cisplatin in the human cervical cancer line (HCE1) multicellular spheroid (HCE1/MCS) model and to probe it if MG132 could reverse the HCE1/MCS resistance to cisplatin, as well as the possible mechanism of drug resistance.
Pyrethroid insecticides: isoform-dependent hydrolysis, induction of cytochrome P450 3A4 and evidence on the involvement of the pregnane X receptor.
Yan et al., United States. In Toxicol Appl Pharmacol, 2009
Some pyrethroids such as bioresmethrin were preferably hydrolyzed by carboxylesterase HCE1, whereas others such as bifenthrin preferably by HCE2.
Human carboxylesterases HCE1 and HCE2: ontogenic expression, inter-individual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin.
Yan et al., United States. In Biochem Pharmacol, 2009
The liver contains the highest carboxylesterase activity and expresses two major carboxylesterases: HCE1 and HCE2.
[Proteomic study of paclitaxel on human cervical carcinoma HCE1].
Li et al., Changsha, China. In Zhong Nan Da Xue Xue Bao Yi Xue Ban, 2008
OBJECTIVE: To explore the mechanism of paclitaxel on the protein expression of human cervical carcinoma cell line HCE1.
Interleukin-6 alters the cellular responsiveness to clopidogrel, irinotecan, and oseltamivir by suppressing the expression of carboxylesterases HCE1 and HCE2.
Yan et al., Nanjing, China. In Mol Pharmacol, 2007
In both primary hepatocytes and HepG2 cells, treatment with IL-6 decreased the expression of human carboxyl-esterases HCE1 and HCE2 by as much as 60%.
Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel.
Yan et al., United States. In J Pharmacol Exp Ther, 2006
In this study, we report that the hydrolytic activation is catalyzed by carboxylesterase human carboxylesterase (HCE) 1. Liver microsomes rapidly hydrolyzed oseltamivir, but no hydrolysis was detected with intestinal microsomes or plasma.
Antiplatelet agents aspirin and clopidogrel are hydrolyzed by distinct carboxylesterases, and clopidogrel is transesterificated in the presence of ethyl alcohol.
Yan et al., United States. In J Pharmacol Exp Ther, 2006
Consistent with the tissue distribution of two carboxylesterases human carboxylesterase (HCE) 1 and HCE2, recombinant HCE1 hydrolyzed clopidogrel, whereas recombinant HCE2 hydrolyzed aspirin.
Crystallization and preliminary X-ray analysis of HCE-1, a hatching enzyme of medaka fish, Oryzias latipes.
Tanokura et al., Tokyo, Japan. In Acta Crystallogr D Biol Crystallogr, 2004
The hatching enzyme of medaka fish, high choriolytic enzyme (HCE-1; MW = 22.7 kDa), was crystallized by the hanging-drop vapour-diffusion method using PEG 10 000 as the precipitant.
Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins.
Dubois et al., Paris, France. In J Mol Biol, 2004
The phosphorylated CTD binds to a variety of proteins including the cis/trans peptidyl-prolyl isomerase (PPIase) Pin1 and enzymes involved in processing of the primary transcript such as the capping enzyme Hce1 and CA150, a nuclear factor implicated in transcription elongation.
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