about
An RNA trapping mechanism in Alphavirus mRNA promotes ribosome stalling and translation initiationHepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunitStructural integrity of the PCI domain of eIF3a/TIF32 is required for mRNA recruitment to the 43S pre-initiation complexesCrystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11Crystal structure of the human COP9 signalosomeStructure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complexMolecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complexTwo RNA-binding motifs in eIF3 direct HCV IRES-dependent translationTranslation initiation factors eIF3 and HCR1 control translation termination and stop codon read-through in yeast cellsStructural and biochemical characterization of the Cop9 signalosome CSN5/CSN6 heterodimerFunctional and biochemical characterization of human eukaryotic translation initiation factor 3 in living cells.Human-like eukaryotic translation initiation factor 3 from Neurospora crassaStructure of mammalian eIF3 in the context of the 43S preinitiation complex.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 translation initiation complex eIF3 in trypanosomatids and other pathogenic excavates--identification of conserved and divergent features based on orthologue analysis.Mechanism of cytoplasmic mRNA translation.The eIF3 complex of Leishmania-subunit composition and mode of recruitment to different cap-binding complexes.Heterogeneity of the translational machinery: Variations on a common theme.Assembly of eIF3 Mediated by Mutually Dependent Subunit Insertion.Eukaryotic translation initiation factor 3 subunit D overexpression is associated with the occurrence and development of ovarian cancerHuman eIF3: from 'blobology' to biological insight.Coupling 40S ribosome recruitment to modification of a cap-binding initiation factor by eIF3 subunit e.The eIF3 complex of Trypanosoma brucei: composition conservation does not imply the conservation of structural assembly and subunits function.Unveiling Contacts within Macromolecular Assemblies by Solving Minimum Weight Connectivity Inference (MWC) Problems.A Transcript-Specific eIF3 Complex Mediates Global Translational Control of Energy Metabolism.Purification of mRNA-programmed translation initiation complexes suitable for mass spectrometry analysis.Human eIF3b and eIF3a serve as the nucleation core for the assembly of eIF3 into two interconnected modules: the yeast-like core and the octamer.Interaction of p190A RhoGAP with eIF3A and Other Translation Preinitiation Factors Suggests a Role in Protein Biosynthesis.Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Fluorescently-tagged human eIF3 for single-molecule spectroscopy.eIF3: a factor for human health and disease.
P2860
50eab427bd52e78749bbbfbd03c1534635a5950072368078cbd48f653fe165faa713623d21d0ffda72abd8bd108d9eb703acbbd9f65474f55a60182f82fd0f47ecd02c058528589bda99b174b01248929bee7f4740cd521e7b21d640051ced55a8988237a778cd3e651a5f629fd7f87b96ed3af00bcc0d95b009e3c8e5e747719974041cb03b8a6bee029b37d9d80e6172b16d053d2ff3cd1156e995cbbce31cf05f0202a589ac33ee195a501345fd46b43dd181f3c9d7d0cacc26899980ebc36a810514b96a1e5effc58f308c3810289bd02ea402aec3b73bfc9460
P248
Q24701801-BE310644-96EE-436B-B8D2-1BDDF4C37848Q27680505-06EF2CEA-0977-4171-BEE4-C20FA7FBD94DQ27681329-579E5702-05B6-4D55-BD3B-3A1023F83C82Q27681666-4EED5221-8D42-4154-AD1F-A828BE3FDC6DQ27694578-2CBE3CE9-0096-4A94-954E-7B08BB69958AQ27697933-44A2C117-316B-431A-8F6A-9C2C67DE07BCQ27934341-2DAD6EC5-607C-4CD4-9450-708E0F223DB5Q28118899-7ECF9886-5041-4351-BC97-15D548334D2DQ28535333-AA5F6655-C28C-4D62-9A91-C9BCB08558B2Q28542494-EE7C0680-8ADD-4BA9-B215-A55F5FAB3F2BQ34056518-726C6C73-9A28-49EA-A45A-24D14C66C213Q34386187-BB57B894-FCED-4065-BA13-57B9962ACD94Q34492793-70C903FB-1261-4091-9BD5-762AD6256B0CQ34634172-9F05F861-FB73-470F-93C7-EF22C0C26F75Q35533889-A8203D66-1A36-42A6-9417-0CBC811ED1DEQ35636275-55E0B9C0-1DA4-4D42-831A-A6E8F8B5ABFDQ35885901-AC38E1E0-DA86-4C89-B848-1ADE551242CEQ36972906-3235E79E-F0C8-403B-90EC-EBB57C95D2D1Q37078817-944CFF33-090E-468F-BF03-1EC5F495FFFCQ37635646-DA0947DF-90BD-4D35-B405-1A383F8757AFQ37644283-93AC252A-BE5B-48A0-9065-8AAD569717E5Q37729759-8D7DB06B-882B-40B6-930E-13A59EC53A39Q39175805-3865205D-6CAB-43C8-8841-9D13055D7DDBQ41605726-8D7AAB49-6619-4088-AD34-088A8809DDA2Q41698817-B99F3494-1F9D-4C0D-976F-E047544B5BBCQ42145681-256B7CB6-53D0-4272-AE07-2DB75BFE426CQ42351633-E29F4002-6F62-4143-A2F0-7997574DF9E3Q42804398-B0ADC343-AD09-4FC9-99B0-8C440112BB22Q47234689-D4BAC3EA-CA3F-47A4-A99E-29FD2F53310DQ48518399-1E3C10F0-E66D-461A-BB0F-23DBAE6FBFAAQ52445969-8DAE69C1-6E94-43DD-A50A-6915F0256F6A
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 25 April 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Architecture of human translation initiation factor 3.
@en
Architecture of human translation initiation factor 3.
@nl
type
label
Architecture of human translation initiation factor 3.
@en
Architecture of human translation initiation factor 3.
@nl
prefLabel
Architecture of human translation initiation factor 3.
@en
Architecture of human translation initiation factor 3.
@nl
P2093
P2860
P1433
P1476
Architecture of human translation initiation factor 3.
@en
P2093
Chaomin Sun
Jacob M Vogan
Jamie H D Cate
Jordi Querol-Audi
M Duane Smith
P2860
P304
P356
10.1016/J.STR.2013.04.002
P50
P577
2013-04-25T00:00:00Z