Biomaterial Database

Decapper comes into focus. 2006

Vincent Shen, and Megerditch Kiledjian

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D011755	Pyrophosphatases	A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.	Pyrophosphatase
D000096964	Nudix Hydrolases	A group of Mg2+/Mn2+-dependent mainly pyrophosphohydrolases that hydrolyzes structures of NUcleoside DIphosphate linked to another moiety X to nucleoside monophosphate and X-Phosphate. Nudix hydrolases share conserved Nudix box (GX5EX7REUXEEXGU) and degrade variety of substrates including oxidized nucleotides (e.g., MutT) and metabolic intermediates (e.g., THIAMINE PYROPHOSPHATASE). In humans, Nudix superfamily proteins such as MutT proteins participate in DNA damage repairs. Mutations on a nudix hydrolase (NUDT15) are associated with a PURINE-PYRIMIDINE METABOLISM, INBORN ERRORS disorder called THPM2, and mutations in nudix hydrolase (NUDT2) are associated with IDDPN, a developmental intellectual disorder.	Nucleoside Diphosphates-Linked to Moiety-X Hydrolases,Nudix Hydrolase,Nudix Proteins,Hydrolase, Nudix,Nucleoside Diphosphates Linked to Moiety X Hydrolases
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012315	RNA Caps	Nucleic acid structures found on the 5' end of eukaryotic cellular and viral messenger RNA and some heterogeneous nuclear RNAs. These structures, which are positively charged, protect the above specified RNAs at their termini against attack by phosphatases and other nucleases and promote mRNA function at the level of initiation of translation. Analogs of the RNA caps (RNA CAP ANALOGS), which lack the positive charge, inhibit the initiation of protein synthesis.	RNA Cap,5' Capped RNA,5' mRNA Cap Structure,Cap, RNA,Caps, RNA,RNA, 5' Capped
D020537	RNA, Small Nucleolar	Small nuclear RNAs that are involved in the processing of pre-ribosomal RNA in the nucleolus. Box C/D containing snoRNAs (U14, U15, U16, U20, U21 and U24-U63) direct site-specific methylation of various ribose moieties. Box H/ACA containing snoRNAs (E2, E3, U19, U23, and U64-U72) direct the conversion of specific uridines to pseudouridine. Site-specific cleavages resulting in the mature ribosomal RNAs are directed by snoRNAs U3, U8, U14, U22 and the snoRNA components of RNase MRP and RNase P.	Small Nucleolar RNA,snoRNA
D029867	Xenopus Proteins	Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.	Xenopus laevis Proteins
D039381	RNA Cap-Binding Proteins	Proteins that specifically bind to RNA CAPS and form nuclear cap binding protein complexes. In addition to stabilizing the 5' end of mRNAs, they serve a diverse array of functions such as enhancing mRNA transport out of the CELL NUCLEUS and regulating MRNA TRANSLATION in the CYTOPLASM.	Cap Binding Protein,Cap Binding Proteins,Cap-Binding Protein Complex,RNA Cap Binding Proteins,mRNA Cap Binding Proteins,Binding Protein, Cap,Binding Proteins, Cap,Cap Binding Protein Complex,Cap-Binding Proteins, RNA