about
Mutations in the RNA granule component TDRD7 cause cataract and glaucomaRNA-binding proteins in eye development and disease: implication of conserved RNA granule componentsEffects of stress and aging on ribonucleoprotein assembly and function in the germ lineThe Structure and Enzymatic Properties of a Novel RNase II Family Enzyme from Deinococcus radioduransRoquin binding to target mRNAs involves a winged helix-turn-helix motifMeiosis arrest female 1 (MARF1) has nuage-like function in mammalian oocytesTDRD5 is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis in miceMARF1 regulates essential oogenic processes in miceThe RNA-binding protein MARF1 promotes cortical neurogenesis through its RNase activity domainThe LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuageNew perspectives on the diversification of the RNA interference system: insights from comparative genomics and small RNA sequencing.Comprehensive classification of the PIN domain-like superfamilyThe phylogenetic origin of oskar coincided with the origin of maternally provisioned germ plasm and pole cells at the base of the HolometabolaEvolution of the deaminase fold and multiple origins of eukaryotic editing and mutagenic nucleic acid deaminases from bacterial toxin systems.RNA granule component TDRD7 gene polymorphisms in a Han Chinese population with age-related cataract.The Tudor domain protein Tapas, a homolog of the vertebrate Tdrd7, functions in the piRNA pathway to regulate retrotransposons in germline of Drosophila melanogasterComprehensive analysis of the HEPN superfamily: identification of novel roles in intra-genomic conflicts, defense, pathogenesis and RNA processing.LMKB/MARF1 localizes to mRNA processing bodies, interacts with Ge-1, and regulates IFI44L gene expression.Divergent RNA Localisation Patterns of Maternal Genes Regulating Embryonic Patterning in the Butterfly Pararge aegeria.Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectorsStructure of Drosophila Oskar reveals a novel RNA binding protein.(1)H, (15)N and (13)C resonance assignments for the three LOTUS RNA binding domains of Tudor domain-containing protein TDRD7.The evolution of insect germline specification strategies.Solution structure of a C-terminal fragment (175-257) of CV_0373 protein from Chromobacterium violaceum adopts a winged helix-turn-helix (wHTH) fold.Two NYN domain containing putative nucleases are involved in transcript maturation in Arabidopsis mitochondria.Patterns of molecular evolution of the germ line specification gene oskar suggest that a novel domain may contribute to functional divergence in Drosophila.TDRD5 binds piRNA precursors and selectively enhances pachytene piRNA processing in mice.Interference with the C-terminal structure of MARF1 causes defective oocyte meiotic division and female infertility in mice.Biased Duplications and Loss of Members in Tdrd Family in Teleost Fish.LOTUS domain protein MARF1 binds CCR4-NOT deadenylase complex to post-transcriptionally regulate gene expression in oocytesRibonuclease activity of MARF1 controls oocyte RNA homeostasis and genome integrity in mice
P2860
Q24298044-92580DB4-B4D8-499E-839E-C820236DE869Q26748745-34CB3CE5-9904-4DB9-AAAA-CEE6488F7369Q27003381-8AE244AB-589E-4EC8-A82A-A6386733A7C8Q27675907-0C4FB26F-004D-42AA-944E-A375A361628AQ27696852-17AFFD4E-5E72-4138-9E3B-5117A5DF683DQ28511020-9BFBBAFC-F415-4407-80B9-9A26E84D74A0Q28588119-DF279F5B-1FBD-4770-9BD5-45268A19CC46Q28594981-0D076287-DB4F-46AD-B0D0-A34889698057Q33682478-EEF5DA95-6E08-4BEA-9542-D61DBBEDAD4EQ33763607-802DF4C4-C32A-4953-9AE9-3547EF54CC8DQ33791621-BAD682EF-C511-45FB-883D-D5D14D3DF26FQ33878209-69F36F38-05C6-448D-84B2-D3D009A74BEBQ33892343-14935126-D6A7-42F3-8AEC-E31A9272BD89Q34010890-BF5720F0-2FA4-4049-BF5B-D2FA23DC65FCQ34398458-AF0D1C00-1A7E-41D6-BBF3-945390227267Q34410063-8735BC08-E9C8-49B7-BF0F-CE0D2D214205Q34773696-577D7E59-1BAC-4CE4-A16E-840A07F79A6EQ35155260-2D348881-E32A-4EA4-93C4-C9138E0A21BCQ35859884-B36F53E5-E709-416C-804D-14F8C646CB79Q35984251-B4BDC583-3CF9-4BEB-A5D7-587184D14E6DQ36079094-2364071F-16FC-4FD8-B511-D568647DC7C6Q36101123-8A018CF8-6E0D-4593-B284-84DDAD1D1D52Q36785985-D62B3D13-649E-4C07-9CB9-B5D5A3ED72E1Q37055461-FA345C60-868E-4617-95FA-58C13FC37C41Q46617783-9423A325-8EDE-462D-8468-F77BE536C9C1Q46948466-5351D6EB-DEBB-4B0A-89C7-FBF6505C2484Q47215644-5269A4A0-5FFD-4F70-A4F3-829F74252BD4Q47550946-4C43831E-4942-4D7B-B223-492F99F65A48Q48203882-647CEB20-B02C-45AC-9DD7-2977BEAC1FCBQ57048736-495891E5-C28C-4739-96FE-285EF0322F57Q58594605-641823EA-B807-4E79-AF5E-EA38239A3C58
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
OST-HTH: a novel predicted RNA-binding domain.
@ast
OST-HTH: a novel predicted RNA-binding domain.
@en
OST-HTH: a novel predicted RNA-binding domain.
@nl
type
label
OST-HTH: a novel predicted RNA-binding domain.
@ast
OST-HTH: a novel predicted RNA-binding domain.
@en
OST-HTH: a novel predicted RNA-binding domain.
@nl
prefLabel
OST-HTH: a novel predicted RNA-binding domain.
@ast
OST-HTH: a novel predicted RNA-binding domain.
@en
OST-HTH: a novel predicted RNA-binding domain.
@nl
P2860
P50
P356
P1433
P1476
OST-HTH: a novel predicted RNA-binding domain.
@en
P2860
P2888
P356
10.1186/1745-6150-5-13
P577
2010-03-19T00:00:00Z
P5875
P6179
1035652165