Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.
about
Pharmacological brake-release of mRNA translation enhances cognitive memoryPancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stressEukaryotic initiation factor 2B: identification of multiple phosphorylation sites in the epsilon-subunit and their functions in vivoMutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse waysA mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alphaIdentification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formationMutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activityCrystal structure of eukaryotic translation initiation factor 2BeIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.eIF5 has GDI activity necessary for translational control by eIF2 phosphorylationeIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core.Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiationThe yeast eukaryotic translation initiation factor 2B translation initiation complex interacts with the fatty acid synthesis enzyme YBR159W and endoplasmic reticulum membranesPosttranscriptional control of gene expression in yeast.A ribosomal protein is required for translational regulation of GCN4 mRNA. Evidence for involvement of the ribosome in eIF2 recycling.Biochemical analysis of the eIF2beta gamma complex reveals a structural function for eIF2alpha in catalyzed nucleotide exchangeA yeast purification system for human translation initiation factors eIF2 and eIF2Bε and their use in the diagnosis of CACH/VWM diseaseIdentification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complexeIF2 interactions with initiator tRNA and eIF2B are regulated by post-translational modifications and conformational dynamicsGCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and Lhp1p in the maturation of initiator methionyl-tRNA in Saccharomyces cerevisiae.Insights into the architecture of the eIF2Bα/β/δ regulatory subcomplexPKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alphaInhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain.Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.Fusel alcohols regulate translation initiation by inhibiting eIF2B to reduce ternary complex in a mechanism that may involve altering the integrity and dynamics of the eIF2B body.Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase.Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation.Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2Archaeal aIF2B interacts with eukaryotic translation initiation factors eIF2alpha and eIF2Balpha: Implications for aIF2B function and eIF2B regulation.Regulation of the unfolded protein response by eif2Bdelta isoforms.The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivoThe small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assemblyMinimum requirements for the function of eukaryotic translation initiation factor 2.Fifteen novel EIF2B1-5 mutations identified in Chinese children with leukoencephalopathy with vanishing white matter and a long term follow-up.Pharmacological dimerization and activation of the exchange factor eIF2B antagonizes the integrated stress response.Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.Archaeal translation initiation revisited: the initiation factor 2 and eukaryotic initiation factor 2B alpha-beta-delta subunit families.Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivoMechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2.
P2860
57c1718ed557df725710c2ced2be20749d72649c5910a9693c2382ada871850f5d2853758381845d7f452b730d2bccf8d921ec67f7538e42c657f2f4a004a51e707f9380b3141708a011ff841752cd65b9c1840841dd62f8200842642e6fc41b39b2e9bec91a1f770058a4737f4732881d56ac9d0d9afe8be428e917f6c40007e3b0adc7efa50443fe309066f252fe835299e4b6d4bac86891ad554762786e59
P248
Q21128794-29735DF5-68FF-4D3F-A43F-8C4E197C86F4Q22253195-7B37A055-4284-4BD5-9154-7223DFC048A8Q24291550-3E60F91C-3CE2-41DE-9C75-C3968DE95489Q24323177-4F385848-119B-4C38-89BC-3987704285CAQ24548092-D54B74A6-AC55-4786-AF13-B177DB4C8054Q24554201-A60EB010-93A0-452F-8AD6-0CD104E34867Q24629691-C131B212-8101-49DF-B9C3-EF3762D5D0D2Q27704065-2CF8D9F2-4F8A-43EA-B0B9-2F769C70B98FQ27930296-CC27B8F3-FB1D-471C-BEAF-C5910ED8DC8EQ27931061-6DED7C35-6AF2-48A8-863B-CD0AB001F9DBQ27933768-8D719613-378B-4F5E-9C98-215F5A8D6341Q27934320-4643E5EC-8D0D-477F-8891-27CE91DF4241Q27936706-9211160A-368F-4289-9458-254503642BE4Q27937074-9691D9D1-BBFE-460C-9BD0-7DF751227375Q27939864-2776F2BF-6FAC-4FC5-943F-18D7BE9D769EQ28141855-AD3BF331-20E7-4988-B4E8-73E6A3C9A62BQ28485114-A360EDF3-B72B-498C-ABA6-02F853A2BC24Q28730770-F8B02212-A703-47D3-B3B2-B4E55D71C583Q28833240-4739ACE0-823C-4B6E-8606-93CC426B5AC4Q33652039-76E5FBBD-263A-4E2A-8CAC-EF5599440863Q33710467-2A8C02DA-56F2-41FA-9D79-82A26DA64C48Q33724522-842A02AC-FA18-4C95-A7AF-E28417326795Q33781751-342AE214-DEEE-4055-8E93-E9EBBF60F5D7Q33890632-2FC7EF7D-2DE6-4D4D-8FBE-153C9B290EA8Q33948525-0EF4644E-29A3-4363-AD68-EB8AB365B42EQ33962759-AC5CB9C8-F5E6-48D2-A77E-2C7560A4A93BQ33969048-6C61EEE8-9C6D-42DE-B019-D6230B682FA1Q33996300-16926423-2A54-4A6F-AD4C-4858395ADB84Q34118639-8A532641-07FA-4D5B-A0DD-4BC4428FDAD5Q34186326-7B0669A6-CB78-4046-A102-315EFC2F0810Q34190226-81A0B796-0080-4B0C-A15C-557E5A1E1A0FQ34464670-9962BD98-4CB1-4D01-B23D-406A9E08BE2BQ34612559-A1826A15-FD2B-4ABC-9122-9C8129EFE194Q35168282-C5AF6265-87F1-4DA7-B4E7-9085D4D5BD27Q35590995-F6E449DC-83D3-4D0F-8F8B-E1575FD84B4FQ35776884-14F02004-4CE4-4370-B069-2295BE269F25Q36009255-D262467E-8F39-4329-9C87-A7F11F10522CQ36092079-B9E668A4-69CA-499B-99E6-C4D384793BEDQ36875727-8D21683A-7AA0-4128-9401-E4BF6DF2F271Q37110590-B8286BE6-99BA-4809-AC12-321A444E9840
P2860
Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.
description
1997 nî lūn-bûn
@nan
1997 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մարտին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Homologous segments in three s ...... on by phosphorylation of eIF2.
@ast
Homologous segments in three s ...... on by phosphorylation of eIF2.
@en
Homologous segments in three s ...... on by phosphorylation of eIF2.
@nl
type
label
Homologous segments in three s ...... on by phosphorylation of eIF2.
@ast
Homologous segments in three s ...... on by phosphorylation of eIF2.
@en
Homologous segments in three s ...... on by phosphorylation of eIF2.
@nl
prefLabel
Homologous segments in three s ...... on by phosphorylation of eIF2.
@ast
Homologous segments in three s ...... on by phosphorylation of eIF2.
@en
Homologous segments in three s ...... on by phosphorylation of eIF2.
@nl
P2860
P3181
P356
P1476
Homologous segments in three s ...... ion by phosphorylation of eIF2
@en
P2093
A G Hinnebusch
P2860
P304
P3181
P356
10.1128/MCB.17.3.1298
P407
P577
1997-03-01T00:00:00Z