about
Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodiesTranslation repression in human cells by microRNA-induced gene silencing requires RCK/p54hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNAMultiple mRNA decapping enzymes in mammalian cellsMetal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)Phosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fateEvolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzymeUpf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decayMechanistic and kinetic analysis of the DcpS scavenger decapping enzymeYeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decayKinetic signatures of microRNA modes of actionC. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesisA role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decayDevelopmentally regulated instability of the GPI-PLC mRNA is dependent on a short-lived protein factorStructure-function analysis of yeast RNA debranching enzyme (Dbr1), a manganese-dependent phosphodiesterase.Human miR-221/222 in Physiological and Atherosclerotic Vascular RemodelingMechanisms of deadenylation-dependent decayProteins involved in the degradation of cytoplasmic mRNA in the major eukaryotic model systemsEvolutionary conservation and expression of human RNA-binding proteins and their role in human genetic diseaseTranslation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fatesStructural Basis of Dcp2 Recognition and Activation by Dcp1The RRM domain of poly(A)-specific ribonuclease has a noncanonical binding site for mRNA cap analog recognitionStructural and biochemical studies of the 5′→3′ exoribonuclease Xrn1Coupled 5′ Nucleotide Recognition and Processivity in Xrn1-Mediated mRNA DecayDxo1 is a new type of eukaryotic enzyme with both decapping and 5′-3′ exoribonuclease activityLsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activationIn Vitro Reconstitution of a Cellular Phase-Transition Process that Involves the mRNA Decapping MachineryMammalian microRNAs predominantly act to decrease target mRNA levelsNutrients and the Pkh1/2 and Pkc1 protein kinases control mRNA decay and P-body assembly in yeastRpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies.Yeast Edc3 targets RPS28B mRNA for decapping by binding to a 3' untranslated region decay-inducing regulatory element.Saccharomyces cerevisiae Ebs1p is a putative ortholog of human Smg7 and promotes nonsense-mediated mRNA decay.Multiple Nudix family proteins possess mRNA decapping activityDecapping activators in Saccharomyces cerevisiae act by multiple mechanisms.Scavenger decapping activity facilitates 5' to 3' mRNA decayCrystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation.An interaction between two RNA binding proteins, Nab2 and Pub1, links mRNA processing/export and mRNA stability.The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs.The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics
P2860
Q21090536-3580E1BA-2A02-4464-9848-2B16D4C01407Q21146051-F0A8020D-82F7-420D-BFC5-965808DC2DB5Q24293616-912A79C6-8063-4B52-97DF-EC17F4C35FD9Q24306739-C4A17537-2DA7-4065-B4AE-F0165E8A9192Q24310271-C5EA9F30-DA2E-4D5E-84CA-63A74D29942DQ24310482-81036221-6EBF-4DFC-85E9-557F3946C7A6Q24316889-B3482614-D159-4650-890B-CA0CFC5A49DFQ24323275-97ED6533-30E0-4BFB-9DBF-065A60C5A6ADQ24336105-B9275FEB-0A13-4404-BF3D-1EF1688641AEQ24548790-C8E60221-20EF-4BCC-90D0-F98E7C499695Q24613847-5F8E2EAF-1B0B-424E-BEC3-3AE08399DEB5Q24649055-4B2048AD-80C6-4F5C-8462-C34A19C30767Q24679242-20A45AEE-FF83-4212-93D5-399B7698E6C3Q24795700-1C8CBBD5-34EC-4A09-BF43-8E725B7F8416Q24815032-8C3D1930-C5E7-44F9-9DF6-B85B9142362FQ26801898-5A5DEADE-58C0-4126-9954-6EA2CDC6CDA6Q26829435-110B8E17-730D-40E3-B5BD-D28B687F93BAQ26864165-AFD6BB05-0622-40B7-AB7A-A06A03154469Q26991754-DD8807EF-0A6A-4156-931D-46F0D92C292CQ27488970-0CAA00F5-17D0-403D-B073-B5FF85895DF7Q27649872-5C7CD9CE-BDE7-42CB-A0C0-FFC6FF876F81Q27651271-D81CE4ED-B2B1-4F87-BE56-ADB7D3DB8F65Q27666866-4ED56E0F-26E4-410C-A08C-AE95B4F4D5A6Q27667115-A50812E2-F3E2-4983-88A7-DDA7BF04C6F4Q27672794-0685496F-BF4A-468A-8555-23326593CBACQ27680627-B0CDFFDE-874E-4AD6-BD7D-66FFABDC3D6EQ27683953-5DDEB8A3-6613-4DBF-9E45-324E2F6315F5Q27860535-ABDC0D80-D1B8-416A-A23A-E18B360CB800Q27930050-998E0A55-A403-47C9-9593-2A31078654E8Q27930127-E9901716-CD83-4A53-B457-EBE70FEA9799Q27930271-76A76AF5-1E8E-443A-8C51-F7C83A09644AQ27930308-30CB9019-470A-4F03-BAB9-9F04C623F2D4Q27930396-552A39B9-64CD-4F6A-9229-76127C7BD3DCQ27931642-DF900848-3F21-4277-804C-3394D91AA655Q27931807-B8D43D66-7860-4BE8-8A50-778794D2DD74Q27932261-4C310F03-F40F-4A5E-983B-0D2E2A7B33E1Q27932697-9426D99E-0B77-48C9-8792-2845E2B16C35Q27932841-16A1DA9E-7FB5-4D5F-B57B-0751CEF02A20Q27933345-C536D5F6-DBC8-4C42-8D7D-0F0991262E11Q27935227-BE8ABFDB-2BD6-4C58-8BF8-7C63FDEC95A7
P2860
description
2004 nî lūn-bûn
@nan
2004 թուականին հրատարակուած գիտական յօդուած
@hyw
2004 թվականին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Eukaryotic mRNA decapping
@ast
Eukaryotic mRNA decapping
@en
type
label
Eukaryotic mRNA decapping
@ast
Eukaryotic mRNA decapping
@en
prefLabel
Eukaryotic mRNA decapping
@ast
Eukaryotic mRNA decapping
@en
P3181
P1476
Eukaryotic mRNA decapping
@en
P2093
P304
P3181
P356
10.1146/ANNUREV.BIOCHEM.73.011303.074032
P407
P577
2004-01-01T00:00:00Z