• proteins
  • RNA in cells is always associated with RNA-binding proteins that regulate all aspects of RNA metabolism including RNA splicing, export from the nucleus, RNA localization, mRNA turn-over as well as translation. (mdpi.com)
  • Given their diverse functions, cells express a variety of RNA-binding proteins, which play important roles in the pathologies of a number of diseases. (mdpi.com)
  • In this review we focus on the effect of alcohol on different RNA-binding proteins and their possible contribution to alcohol-related disorders, and discuss the role of these proteins in the development of neurological diseases and cancer. (mdpi.com)
  • We further discuss the conventional methods and newer techniques that are employed to identify RNA-binding proteins. (mdpi.com)
  • In this review we provide a succinct overview of the role of RNA-binding proteins (RBPs) in regulating gene expression. (mdpi.com)
  • We have divided the review into subheadings under which we discuss the effect of alcohol on RNA-binding proteins, RNA-binding proteins in neurological diseases and cancer, and finally the methods employed to identify RBPs and/or ligands of a RBP. (mdpi.com)
  • For this process the RNA is associated with nuclear proteins that aid in splicing and nuclear export [ 1 ]. (mdpi.com)
  • As mRNA molecules emerge from the nucleus, bound nuclear proteins are often replaced with a new set of RNA-binding proteins (RBPs). (mdpi.com)
  • RNA-binding proteins and their role in RNA metabolism: Genomic DNA is transcribed in the nucleus resulting in generation of hnRNA. (mdpi.com)
  • RNA-binding proteins (RBP) are involved in ( 1 ) splicing and alternative splicing of hnRNA, resulting in the formation of mRNAs. (mdpi.com)
  • mRNA
  • In fact RBPs are involved in every step of the RNA lifecycle, e.g., transport of mRNA to the site of translation, storage and mRNA degradation ( Figure 1 ) [ 1 ]. (mdpi.com)
  • Morpholinos are synthetic oligonucleotides that can be used to inhibit nuclear RNA splicing or mRNA translation and are the common gene inhibition reagent in Xenopus as neither siRNA or miRNA have yet been shown to reproducibly function in frog embryos. (wikipedia.org)
  • enzyme
  • The results indicate that productive formation of an enzyme-RNA-MgATP complex is pH independent over a broad pH range, but that formation of an active enzyme-RNA-MgPP i complex is strongly pH dependent, consistent with the production of a proton on the enzyme in the forward reaction. (biochemj.org)
  • whereas
  • Strong overexpression of Cga1 produces dark green, semidwarf plants with reduced tillering, whereas RNA interference knockdown results in reduced chlorophyll and increased tillering. (plantphysiol.org)
  • electron
  • Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. (wikipedia.org)
  • extensive
  • Before this information can be relayed to the cytoplasm, the nascent RNA undergoes extensive post-transcriptional processing before arriving at its final destination in cells. (mdpi.com)
  • cells
  • RNA was isolated from Z210R.1 cells, oligo-dT-primed cDNA was synthesized and cloned into the pDC406 vector, pools of clones were generated, and transfections into CV-1/EBNA cells were performed, all as described ( 8 ). (rupress.org)
  • This process (transfer of nuclei from cloned cells) is referred to as serial transplantation. (wikipedia.org)
  • cell
  • The transcribed RNA now represents information required to direct cellular function to maintain cell homeostasis. (mdpi.com)
  • Entry
  • Now EC 3.4.11.2, membrane alanyl aminopeptidase EC 3.4.13.7: Glu-Glu dipeptidase EC 3.4.13.8: Transferred entry: Pro-X dipeptidase. (wikipedia.org)
  • Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.9: X-Pro dipeptidase EC 3.4.13.10: Transferred entry: β-aspartyldipeptidase. (wikipedia.org)
  • Now EC 3.4.19.5, β-aspartyl-peptidase EC 3.4.13.11: Transferred entry: dipeptidase. (wikipedia.org)
  • Now EC 3.4.13.19, membrane dipeptidase EC 3.4.13.12: Met-X dipeptidase EC 3.4.13.13: Transferred entry: homocarnosinase. (wikipedia.org)
  • Now EC 3.4.13.3, X-His dipeptidase EC 3.4.13.14: Deleted entry: γ-glutamyldipeptidase EC 3.4.13.15: Transferred entry: N2-β-alanylarginine dipeptidase. (wikipedia.org)
  • Now EC 3.4.19.1, acylaminoacyl-peptidase EC 3.4.14.4: dipeptidyl-peptidase III EC 3.4.14.5: dipeptidyl-peptidase IV EC 3.4.14.6: dipeptidyl-dipeptidase EC 3.4.14.7: Deleted entry: tetralysine endopeptidase EC 3.4.14.8: Transferred entry: tripeptidyl peptidase. (wikipedia.org)
  • Now EC 3.4.14.10, tripeptidyl-peptidase II EC 3.4.14.9: tripeptidyl-peptidase I EC 3.4.14.10: tripeptidyl-peptidase II EC 3.4.14.11: Xaa-Pro dipeptidyl-peptidase EC 3.4.14.12: Xaa-Xaa-Pro tripeptidyl-peptidase EC 3.4.15.1: peptidyl-dipeptidase A EC 3.4.15.2: Transferred entry: pepdidyl carboxyamidase. (wikipedia.org)
  • Now EC 3.4.19.2, peptidyl-glycinamidase EC 3.4.15.3: Transferred entry: dipeptidyl carboxypeptidase. (wikipedia.org)
  • Now EC 3.4.15.5, peptidyl-dipeptidase Dcp EC 3.4.15.4: Peptidyl-dipeptidase B EC 3.4.15.5: Peptidyl-dipeptidase Dcp EC 3.4.15.6: cyanophycinase EC 3.4.16.1: Transferred entry: serine carboxypeptidase. (wikipedia.org)
  • Now included with EC 3.4.16.5, carboxypeptidase C EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase EC 3.4.16.5: carboxypeptidase c EC 3.4.16.6: carboxypeptidase D EC 3.4.17.1: carboxypeptidase A EC 3.4.17.2: carboxypeptidase B EC 3.4.17.3: lysine carboxypeptidase EC 3.4.17.4: Gly-X carboxypeptidase EC 3.4.17.5: Deleted entry: aspartate carboxypeptidase EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Transferred entry: acylmuramoyl-alanine carboxypeptidase. (wikipedia.org)
  • Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) EC 3.4.21.9: enteropeptidase EC 3.4.21.10: acrosin EC 3.4.21.11: Transferred entry: elastase. (wikipedia.org)
  • Now EC 3.4.21.37, leukocyte elastase EC 3.4.21.12: alpha-lytic endopeptidase EC 3.4.21.13: Transferred entry: Phaseolus proteinase. (wikipedia.org)
  • Now EC 3.4.16.6, carboxypeptidase D EC 3.4.21.14: Transferred entry: now EC 3.4.21.67 endopeptidase So EC 3.4.21.15: Transferred entry: Aspergillus alkaline proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.29: Transferred entry: Bothrops atrox serine proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.30: Transferred entry: Crotalus adamanteus serine proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.31: Transferred entry: urokinase. (wikipedia.org)