Crystal structure of human eIF3k, the first structure of eIF3 subunits
about
Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3Prediction of a common structural scaffold for proteasome lid, COP9-signalosome and eIF3 complexes.C. elegans EIF-3.K promotes programmed cell death through CED-3 caspaseThe Arabidopsis COP9 Signalosome Subunit 7 Is a Model PCI Domain Protein with Subdomains Involved in COP9 Signalosome AssemblyStructural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporationThe proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes togetherStructural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complexStructural integrity of the PCI domain of eIF3a/TIF32 is required for mRNA recruitment to the 43S pre-initiation complexesStructure characterization of the 26S proteasome.Crystal structure of the human COP9 signalosomeMolecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complexNovel insights into the architecture and protein interaction network of yeast eIF3Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75Structural and biochemical characterization of the Cop9 signalosome CSN5/CSN6 heterodimerSolution structure of yeast Rpn9: insights into proteasome lid assemblyIsolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a structure-function study of the proteasome-COP9-initiation factor domainStructure of mammalian eIF3 in the context of the 43S preinitiation complex.The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes.Tackling the crystallographic structure determination of the COP9 signalosome.Architecture of human translation initiation factor 3.Structural biology of the PCI-protein fold.Interaction of PABPC1 with the translation initiation complex is critical to the NMD resistance of AUG-proximal nonsense mutations.Methodology for measuring conformation of solvent-disrupted protein subunits using T-WAVE ion mobility MS: an investigation into eukaryotic initiation factors.A novel plant-specific family gene, ROOT PRIMORDIUM DEFECTIVE 1, is required for the maintenance of active cell proliferation.eIF3: a factor for human health and disease.
P2860
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P2860
Crystal structure of human eIF3k, the first structure of eIF3 subunits
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին 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
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@ast
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@en
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@nl
type
label
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@ast
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@en
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@nl
prefLabel
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@ast
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@en
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@nl
P2093
P2860
P356
P1476
Crystal structure of human eIF3k, the first structure of eIF3 subunits
@en
P2093
Ping Zhang
Weimin Gong
Zhaocai Zhou
Zhongjun Cheng
P2860
P304
34983-34990
P356
10.1074/JBC.M405158200
P407
P50
P577
2004-06-04T00:00:00Z