about
Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin.Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159pFunctional organization of the yeast proteome by systematic analysis of protein complexesConservation of the deadenylase activity of proteins of the Caf1 family in humanC2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complexThe BTG2 protein is a general activator of mRNA deadenylationProteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicingThe splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5' splice sites.Complexes between the nonsense-mediated mRNA decay pathway factor human upf1 (up-frameshift protein 1) and essential nonsense-mediated mRNA decay factors in HeLa cellsPartial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assemblyRNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.Positive feedback in eukaryotic gene networks: cell differentiation by graded to binary response conversionThe DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription.The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodiesHuman Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structuresA Sm-like protein complex that participates in mRNA degradationRNA channelling by the archaeal exosomeCytoplasmic foci are sites of mRNA decay in human cellsThe U1 snRNP-associated factor Luc7p affects 5' splice site selection in yeast and humanDcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathwayA Novel Protein-Protein Interaction in the RES (REtention and Splicing) ComplexX-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complexStructure of the yeast Pml1 splicing factor and its integration into the RES complexDissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathwaysStructural and functional analysis of Nro1/Ett1: a protein involved in translation termination in S. cerevisiae and in O2-mediated gene control in S. pombeRbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitmentThe Elongator subcomplex Elp456 is a hexameric RecA-like ATPaseArchitecture of the nuclease module of the yeast Ccr4-not complex: the Not1-Caf1-Ccr4 interactionThe C-Terminal Domain from S. cerevisiae Pat1 Displays Two Conserved Regions Involved in Decapping Factor RecruitmentStructure and RNA-binding properties of the Not1-Not2-Not5 module of the yeast Ccr4-Not complexStructure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modificationStructure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activatorA generic protein purification method for protein complex characterization and proteome explorationEndonucleolytic RNA cleavage by a eukaryotic exosome.The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program.RRP20, a component of the 90S preribosome, is required for pre-18S rRNA processing in Saccharomyces cerevisiaeCryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase.The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants.The yeast U2A'/U2B complex is required for pre-spliceosome formation.
P50
Q22009995-3347856A-A05B-4633-A11A-24AA5EFF8548Q22010452-8EFC101F-FF18-4BB4-89DD-3B0A69A62090Q24292209-8A399290-CF22-47F0-9251-06E556D0168EQ24298094-F61BB4A6-85A2-4D47-9F2E-801A407C062EQ24305555-682DDACA-5744-4794-87AE-701A512C6F14Q24310741-D6929845-0294-436A-9A28-51F6633CA537Q24317157-2C21C277-97BC-4ED7-A92F-8B4539B5E2FDQ24337164-B7BD666C-FF3A-4CE4-8D23-596B2EF545B0Q24530107-74BEC694-6A78-40FB-9218-91EE98B0EE89Q24534180-9BF82223-2388-4ADD-BEC8-C10E3E1FB1C8Q24534404-3601814F-0C35-4FF3-B75E-FE316EDF6C0CQ24535235-4E9CE1B4-4FB3-4738-8FEB-E098C055E580Q24536154-7C8BD450-BE85-4A09-A8A8-689373205853Q24540223-8A51420A-150D-4C60-9DE3-CBB0663F6B1DQ24543188-F2F18D45-1421-4EA8-852C-288E6CF82730Q24630673-35655DB9-8122-4A75-AE75-670191B4161CQ24671892-96D295E3-BD79-4082-AA08-4D7131452260Q24677437-49125DC5-329A-4352-B65A-661A6E647027Q24678283-7676705F-ED27-491F-A7DA-C1272F4465C8Q24683331-886F95C9-E80D-48CF-900E-88EA0379C9B7Q27640535-16376AB3-DA4F-4883-9189-DCC801A84F55Q27642540-95DC92B0-98BF-41F0-9CE4-B6C5627F382FQ27652991-2A852918-D3FB-4571-A51E-95B76811046AQ27666043-D9973F00-6ECA-473B-9B71-8E3A7B1D160FQ27667987-89E363DA-9A3A-4773-8207-992EDB8B7EC9Q27673562-87618490-CD68-44E2-8D76-3E723A6429B7Q27677343-33759499-F806-49DA-A462-D38A1160DC7EQ27682188-413F323F-9EA8-4D3F-ABB5-593026CD2744Q27683791-365C775E-8D7E-4F35-85BF-03C2AA53574EQ27687142-5F1B26A9-C6C3-4685-B18C-73CC70C64DB5Q27697604-F1586910-EFBF-46D3-9B71-18D03E9E4014Q27728161-A2241DF3-70E1-4E02-ABE0-ADF13F0B1D56Q27861087-04AA0C0B-4FC4-4F5E-876E-E5B982DCDD01Q27930673-017F2E31-D224-4E55-A4D6-3B5859E2F632Q27931213-771FAC17-D5D6-44B6-BE5E-75DE6B86217EQ27932054-9180D10F-E067-4983-A6DE-FB2792194D1EQ27932117-A582E761-F69C-42FB-B928-B23621BF38EEQ27932287-78D9107C-DD61-4025-B507-778D4505D871Q27932830-D9C2FEF2-1F3D-4E5E-B619-319CEA24949EQ27933005-73337555-7F20-4D12-9C0F-DDB4C0747CE7
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Bertrand Séraphin
@ast
Bertrand Séraphin
@en
Bertrand Séraphin
@es
Bertrand Séraphin
@fr
Bertrand Séraphin
@nl
Bertrand Séraphin
@sl
type
label
Bertrand Séraphin
@ast
Bertrand Séraphin
@en
Bertrand Séraphin
@es
Bertrand Séraphin
@fr
Bertrand Séraphin
@nl
Bertrand Séraphin
@sl
prefLabel
Bertrand Séraphin
@ast
Bertrand Séraphin
@en
Bertrand Séraphin
@es
Bertrand Séraphin
@fr
Bertrand Séraphin
@nl
Bertrand Séraphin
@sl
P106
P21
P31
P496
0000-0002-5168-1921