| DCP1A is an unfavorable prognostic-related enhancer RNA in hepatocellular carcinoma. | DCP1A is an unfavorable prognostic-related enhancer RNA in hepatocellular carcinoma.
Wu H, Zhang J, Bai Y, Zhang S, Zhang Z, Tong W, Han P, Fu B, Zhang Y, Shen Z., Free PMC Article | 02/12/2022 |
| Expression of DCP1a in gastric cancer and its biological function and mechanism in chemotherapy resistance in gastric cancer cells. | Expression of DCP1a in gastric cancer and its biological function and mechanism in chemotherapy resistance in gastric cancer cells.
Ruan T, Zhang Y, Liu W, Li Y, Wang D, Du Z, Tao K, Wu C. | 09/4/2021 |
| Decapping enzyme 1A breaks X-chromosome symmetry by controlling Tsix elongation and RNA turnover. | Decapping enzyme 1A breaks X-chromosome symmetry by controlling Tsix elongation and RNA turnover.
Aeby E, Lee HG, Lee YW, Kriz A, Del Rosario BC, Oh HJ, Boukhali M, Haas W, Lee JT. | 10/31/2020 |
| Human MARF1 is an endoribonuclease that interacts with the DCP1:DCP2 decapping complex and degrades target mRNAs. | Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs.
Nishimura T, Fakim H, Brandmann T, Youn JY, Gingras AC, Jinek M, Fabian MR., Free PMC Article | 06/29/2019 |
| Results suggest a molecular mechanism of long non-coding RNA (MALAT1)-miR203-mRNA-decapping enzymes 1a (DCP1A) axis which is involved with the development and contributes to the malignancy of colorectal cancers. | MALAT1 promotes the colorectal cancer malignancy by increasing DCP1A expression and miR203 downregulation.
Wu C, Zhu X, Tao K, Liu W, Ruan T, Wan W, Zhang C, Zhang W. | 05/4/2019 |
| Overexpression of DCP1A is associated with malignant melanoma. | Overexpression of mRNA-decapping enzyme 1a predicts disease-specific survival in malignant melanoma.
Tang Y, Xie C, Zhang Y, Qin Y, Zhang W. | 08/18/2018 |
| The results suggest that overexpressed Dcp1a and GW182 can form different cytoplasmic aggregates and play distinct biological roles in the miRNA pathway. | Dcp1a and GW182 Induce Distinct Cellular Aggregates and Have Different Effects on microRNA Pathway.
Wang X, Chang L, Wang H, Su A, Wu Z. | 09/23/2017 |
| The E3 ligase TRAF6 binds to DCP1a and indirectly regulates DCP1a phosphorylation, expression of decapping factors, and gene-specific mRNA decay. | K63-Ubiquitylation and TRAF6 Pathways Regulate Mammalian P-Body Formation and mRNA Decapping.
Tenekeci U, Poppe M, Beuerlein K, Buro C, Müller H, Weiser H, Kettner-Buhrow D, Porada K, Newel D, Xu M, Chen ZJ, Busch J, Schmitz ML, Kracht M. | 08/26/2017 |
| DCP1A rs11551405 may have a prognostic effect on survival of CM patients. | Genetic variants in the PIWI-piRNA pathway gene DCP1A predict melanoma disease-specific survival.
Zhang W, Liu H, Yin J, Wu W, Zhu D, Amos CI, Fang S, Lee JE, Li Y, Han J, Wei Q., Free PMC Article | 04/29/2017 |
| The assembly of EDC4 and Dcp1a into processing bodies is critical for the translational regulation of IL-6. | The Assembly of EDC4 and Dcp1a into Processing Bodies Is Critical for the Translational Regulation of IL-6.
Seto E, Yoshida-Sugitani R, Kobayashi T, Toyama-Sorimachi N., Free PMC Article | 04/16/2016 |
| Phosphorylation at serine 315, serine 319, and threonine 321 of DCP1A modulates IL-8 expression during respiratory syncytial virus infection. | Decapping protein 1 phosphorylation modulates IL-8 expression during respiratory syncytial virus infection.
Dickey LL, Duncan JK, Hanley TM, Fearns R., Free PMC Article | 08/8/2015 |
| The data indicates that DCP2 activation by DCP1 occurs preferentially on the EDC4 scaffold, which may serve to couple DCP2 activation by DCP1 with 5'-to-3' mRNA degradation by XRN1 in human cells. | The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.
Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E., Free PMC Article | 07/26/2014 |
| Malin regulates the recruitment of mRNA-decapping enzyme 1A (Dcp1a) to processing bodies. | Lafora disease E3 ubiquitin ligase malin is recruited to the processing bodies and regulates the microRNA-mediated gene silencing process via the decapping enzyme Dcp1a.
Singh S, Singh PK, Bhadauriya P, Ganesh S. | 09/14/2013 |
| hDcp1a has a role in control of processing body dynamics during the cell cycle via phosphorylation | The P body protein Dcp1a is hyper-phosphorylated during mitosis.
Aizer A, Kafri P, Kalo A, Shav-Tal Y., Free PMC Article | 08/31/2013 |
| PNRC2 acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a and Dcp2. | Structural basis of the PNRC2-mediated link between mrna surveillance and decapping.
Lai T, Cho H, Liu Z, Bowler MW, Piao S, Parker R, Kim YK, Song H. | 05/18/2013 |
| Reveal DCP1a as a multifunctional regulator of mRNA expression and suggest a role for JNK kinase phosphorylation in controlling the subcellular localization of DCP1a in response to stress or inflammatory stimuli. | c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies.
Rzeczkowski K, Beuerlein K, Müller H, Dittrich-Breiholz O, Schneider H, Kettner-Buhrow D, Holtmann H, Kracht M., Free PMC Article | 10/15/2011 |
| Data show the presence of P-body-like foci in mouse oocytes, as revealed by the presence of Dcp1a and the colocalization of RNA-associated protein 55 (RAP55) and the DEAD box RNA helicase Rck/p54. | Dcp1-bodies in mouse oocytes.
Swetloff A, Conne B, Huarte J, Pitetti JL, Nef S, Vassalli JD., Free PMC Article | 03/15/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | New application of intelligent agents in sporadic amyotrophic lateral sclerosis identifies unexpected specific genetic background.
Penco S, Buscema M, Patrosso MC, Marocchi A, Grossi E., Free PMC Article | 06/11/2008 |
| These data suggest that a human decapping complex containing decapping enzymes hDcp1a and hDcp2 may be recruited to mRNAs containing premature termination codons by the hUpf proteins. | Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay.
Lykke-Andersen J., Free PMC Article | 01/21/2010 |
| Overexpression of wild-type SMIF enhanced expression of TGFbeta/BMP regulated genes, whereas a dominant-negative SMIF mutant suppressed expression. | SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling.
Bai RY, Koester C, Ouyang T, Hahn SA, Hammerschmidt M, Peschel C, Duyster J. | 01/21/2010 |