Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry
about
The DEAD-box helicase DDX3 supports the assembly of functional 80S ribosomesMass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3Functional analysis of novel phosphorylation sites of CREB-binding protein using mass spectrometry and mammalian two-hybrid assaysControl of Paip1-eukayrotic translation initiation factor 3 interaction by amino acids through S6 kinaseThe translational factor eIF3f: the ambivalent eIF3 subunitStructural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteinsNovel insights into the architecture and protein interaction network of yeast eIF3What Is the Impact of mRNA 5' TL Heterogeneity on Translational Start Site Selection and the Mammalian Cellular Phenotype?eIF3 targets cell-proliferation messenger RNAs for translational activation or repressionHuman eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosomeTwo RNA-binding motifs in eIF3 direct HCV IRES-dependent translationEukaryotic translation initiation factor 3, subunit a, regulates the extracellular signal-regulated kinase pathwayAn oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3Knowledge based identification of essential signaling from genome-scale siRNA experiments.Getting a grip on complexes.HSV usurps eukaryotic initiation factor 3 subunit M for viral protein translation: novel prevention target.A conserved structure within the HIV gag open reading frame that controls translation initiation directly recruits the 40S subunit and eIF3.Phosphorylation stoichiometries of human eukaryotic initiation factorsNovel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tagsFunctional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit.Human-like eukaryotic translation initiation factor 3 from Neurospora crassaIdentification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.The ISG56/IFIT1 gene family.N-myc downstream regulated 1 (NDRG1) is regulated by eukaryotic initiation factor 3a (eIF3a) during cellular stress caused by iron depletion.Novel RNA-binding protein P311 binds eukaryotic translation initiation factor 3 subunit b (eIF3b) to promote translation of transforming growth factor β1-3 (TGF-β1-3).The eukaryotic translation initiation factor 3 subunit L protein interacts with Flavivirus NS5 and may modulate yellow fever virus replication.Topological models of heteromeric protein assemblies from mass spectrometry: application to the yeast eIF3:eIF5 complexPhosphorylation of human eukaryotic initiation factor 2γ: novel site identification and targeted PKC involvement.The translation initiation complex eIF3 in trypanosomatids and other pathogenic excavates--identification of conserved and divergent features based on orthologue analysis.The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit.Joining forces: integrating proteomics and cross-linking with the mass spectrometry of intact complexes.MiR-488 inhibits proliferation and cisplatin sensibility in non-small-cell lung cancer (NSCLC) cells by activating the eIF3a-mediated NER signaling pathway.Noncovalent protein tetramers and pentamers with "n" charges yield monomers with n/4 and n/5 chargeseIF3a improve cisplatin sensitivity in ovarian cancer by regulating XPC and p27Kip1 translation.The Rice Eukaryotic Translation Initiation Factor 3 Subunit f (OseIF3f) Is Involved in Microgametogenesis.Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation.The potential impact of recent developments in three-dimensional quantitative interaction proteomics on structural biology.Assembly of eIF3 Mediated by Mutually Dependent Subunit Insertion.Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components.
P2860
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
P248
Q24305010-6CBE0FF4-B46D-483B-9CA8-27C9F9A6EFC5Q24309617-F7C9AF9A-196C-440F-9533-DF99D1FB556AQ24313470-91F1346C-CABC-409F-9829-E748C7720B3AQ24317685-5C724775-E42F-4D14-9196-DDA8D6212D68Q27016102-FB1768C4-1EDC-4AD6-BD8A-1956A86292B6Q27678819-C998B2AC-A771-4080-8434-8D717404E21FQ27939840-2F059304-3DF8-4D31-9B9C-D23098CAC6DFQ28072703-87692A72-2A92-44C4-BC0C-31B1CBFAFD80Q28115960-7769CF61-F13F-46F1-99CE-54E2FEAD6D3EQ28117731-3BB55052-85DB-4967-BCD3-69D67417EAB7Q28118899-0E231771-5705-4CAF-97B7-06752B243A4DQ28580284-BE46CA92-3C57-4746-A577-14B51CB9AB15Q30438861-ACEDA833-65BC-47F7-ACCC-1FC48E3935CAQ33490280-C6F6CFEB-A6DB-405E-B5B1-CEC739D66745Q33635370-1092FB9E-DD37-4853-AC41-8CAA8391BC10Q33646802-B0F80AB8-B90E-43DD-9686-B0FBAFA49FB7Q34024695-15AD3F53-AA2C-46E3-AFC2-2E164107E2FDQ34072222-04F4A4A1-D9F4-4BD8-A2ED-DFC2310CF1C1Q34150462-77C81424-A7CC-4175-9380-0B1A46FDA262Q34237617-6B2BAAC4-424F-4374-8CD2-0905B231E26DQ34284595-63A2F347-85E8-46FD-8DF6-99AE167AE7FEQ34386187-B1D57F8A-375E-4F86-8BE9-BC1BBA35D65DQ34399983-C191A56D-04D1-413F-B0D0-15537E555B87Q34492459-128D9DDF-8C5B-4394-BF26-A939A9AF0061Q34600331-EFB00B09-8B69-4115-8CCE-991FBBC11A5EQ34634172-53407D8B-C858-45AD-B76E-AD35CFD7655EQ34783090-2088998C-9FD8-47DD-8893-161840E94E06Q35013562-0FB4B12A-20ED-4AAE-8C0F-280E13BD1577Q35533479-ED452A77-0022-4A14-83B1-E1D1822AE8D2Q35533889-B0A96C69-1122-49EF-8602-361F712E6389Q35672266-37F3F016-90B7-4936-8E49-902BBA9742E8Q35863308-274C3B02-0466-48C4-BA3B-256A5BB30330Q36246037-4AFC665E-E558-4230-8723-DAB659363BB7Q36335649-885AFA4C-B80E-4846-8764-46048AD92CECQ36413207-5525F7FD-67C6-4C7B-8C00-4D2B06A2B6AAQ36834419-E06D74EF-916A-42C3-AE6D-DF088D60A01AQ36949719-3BC75EEC-B738-4479-9E84-5A161018C45CQ37078577-46A5CFE6-F126-40F6-A4D9-023EE4364EFBQ37078817-69693A0D-6301-4989-859A-C049247248BFQ37343983-85CD768A-7B19-4944-8CA5-226316A1F269
P2860
Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Structural characterization of ...... n complex by mass spectrometry
@ast
Structural characterization of ...... n complex by mass spectrometry
@en
Structural characterization of ...... n complex by mass spectrometry
@en-gb
Structural characterization of ...... n complex by mass spectrometry
@nl
type
label
Structural characterization of ...... n complex by mass spectrometry
@ast
Structural characterization of ...... n complex by mass spectrometry
@en
Structural characterization of ...... n complex by mass spectrometry
@en-gb
Structural characterization of ...... n complex by mass spectrometry
@nl
prefLabel
Structural characterization of ...... n complex by mass spectrometry
@ast
Structural characterization of ...... n complex by mass spectrometry
@en
Structural characterization of ...... n complex by mass spectrometry
@en-gb
Structural characterization of ...... n complex by mass spectrometry
@nl
P2093
P2860
P50
P921
P3181
P1476
Structural characterization of ...... n complex by mass spectrometry
@en
P2093
Christopher S Fraser
Eugen Damoc
Greg L Mayeur
John W B Hershey
Julie A Leary
P2860
P304
P3181
P356
10.1074/MCP.M600399-MCP200
P407
P577
2007-07-01T00:00:00Z