about
Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino terminiCloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motifPACT, a protein activator of the interferon-induced protein kinase, PKR.Nuclear localization and regulation of erk- and rsk-encoded protein kinasesMechanism and regulation of eukaryotic protein synthesisAn analysis of vertebrate mRNA sequences: intimations of translational controlInteraction of Staufen1 with the 5' end of mRNA facilitates translation of these RNAsLigand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunitGCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae.Dioxin-dependent activation of murine Cyp1a-1 gene transcription requires protein kinase C-dependent phosphorylationMissense mutation in the second RNA binding domain reveals a role for Prkra (PACT/RAX) during skull developmentTranslation of viral mRNA without active eIF2: the case of picornavirusesSuppression of ribosomal function triggers innate immune signaling through activation of the NLRP3 inflammasomeMycobacterium tuberculosis protein kinase K enables growth adaptation through translation controlZfp206 regulates ES cell gene expression and differentiationDeficient signaling in mice devoid of double-stranded RNA-dependent protein kinaseAn oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3Cloning of the mitogen-activated S6 kinase from rat liver reveals an enzyme of the second messenger subfamily.Mechanism of interferon action: identification of essential positions within the novel 15-base-pair KCS element required for transcriptional activation of the RNA-dependent protein kinase pkr geneIdentical Mr 70,000 S6 kinase is activated biphasically by epidermal growth factor: a phosphopeptide that characterizes the late phaseAdenovirus inhibition of cellular protein synthesis is prevented by the drug 2-aminopurine.Identifying the right stop: determining how the surveillance complex recognizes and degrades an aberrant mRNA.Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2.mRNAs containing extensive secondary structure in their 5' non-coding region translate efficiently in cells overexpressing initiation factor eIF-4EDouble-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53The yeast translational allosuppressor, SAL6: a new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension.Glucose-dependent turnover of the mRNAs encoding succinate dehydrogenase peptides in Saccharomyces cerevisiae: sequence elements in the 5' untranslated region of the Ip mRNA play a dominant role.Identification of GCD14 and GCD15, novel genes required for translational repression of GCN4 mRNA in Saccharomyces cerevisiae.Phosphorylation of tobacco eukaryotic translation initiation factor 4A upon pollen tube germinationStructural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI.The role of Misshapen NCK-related kinase (MINK), a novel Ste20 family kinase, in the IRES-mediated protein translation of human enterovirus 71.Mechanism of interferon action: structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinaseUnfolded Protein Response and PERK Kinase as a New Therapeutic Target in the Pathogenesis of Alzheimer's DiseaseMechanism of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase.Activation of the double-stranded RNA (dsRNA)-activated human protein kinase in vivo in the absence of its dsRNA binding domain.Induction of CD4 expression and human immunodeficiency virus type 1 replication by mutants of the interferon-inducible protein kinase PKR.Attenuating mutations in the poliovirus 5' untranslated region alter its interaction with polypyrimidine tract-binding protein.Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase.Beta-actin mRNA localization is regulated by signal transduction mechanisms.The protein activator of protein kinase R, PACT/RAX, negatively regulates protein kinase R during mouse anterior pituitary development.
P2860
Q24311546-00F7CDFB-DFE5-4DAE-8E28-DCD251845787Q24313807-31CF3C80-4AEE-4D55-BCF1-9B83D4AED20EQ24319677-E5C694E1-ECB2-4F44-A648-82A9AF0F9BA4Q24606980-3491BC58-2B9F-468D-81FB-E4BFB8DB328CQ24634693-187FF43E-DECF-45CB-8BCC-E5BE0E14E6A2Q24642530-7491036C-AC39-4DBC-AA02-B125A7C548ADQ24816776-CD430915-94A1-41F0-A3C0-300B35DA7DB9Q27935210-FD3EDBCA-57B8-4606-8022-261EADC831DCQ27939500-2C9E7C75-C36A-4227-9D64-3DDB91213FB2Q28343069-AF9BBEDF-B0C4-4C5C-A902-751BDB1B2835Q28478412-F68266DE-86DD-4030-8828-AD03F9699013Q28479039-2322CDBB-8A40-48AE-9026-F7C66F296DBBQ28483673-19A34FAE-9FED-47CC-A727-E3FEB74AF74AQ28487634-CDE3C79B-207F-43D0-AFE5-8832F630C01BQ28594679-0D3A4430-3FCB-4C50-B54E-B46141DB4FA0Q29620280-D841CEE4-CA17-440D-BEA9-B6F406DB35B9Q30438861-40845D73-F826-4670-9BA6-A5C30A09E07BQ30824759-4FFE55A8-92B4-40C8-ABF7-21E39D0B5966Q33786084-E1A3BF80-CC7F-4018-8E51-4EBC169DEBCAQ33788073-BF56B42E-5511-42F3-9ED3-EF2EF15D56C3Q33792872-EE87A2B6-BB58-4B39-8965-A526DB039E5DQ33888137-855928A3-409A-423C-9F28-DBA01E5FAB64Q33937662-619EFDB8-2E23-4625-B571-938FC024775DQ33938526-CD19EEC5-6C52-408D-9D29-4C469512825BQ33957610-21625500-4BC6-485E-9101-AA8756C1362DQ33963825-E27D5DD2-4C44-403C-8D14-BB84A347C59BQ34451316-F8ABBB53-697A-4C95-91A0-F9AA9DB73E06Q34603714-3A658CA4-F480-4621-8464-8870B56A5EF4Q34663936-E18F898E-9858-46E1-9937-E8AED1B78DBAQ34888248-55324B91-5AC1-4632-8831-11BCAE56A3D1Q35154777-9C3FB6D5-F0BE-4828-858E-D24E283C2524Q35676576-53F98519-41D4-41E6-8487-43E9B08DDB11Q35748263-34EFFC8F-D08F-49B8-96F8-EB754E19BC41Q35845342-7D41A53D-699E-4996-B31B-C081908FC249Q35861821-1D8C7C36-53D6-4564-9A83-52C1BB42A410Q35877650-12CF1A81-F4D6-4492-86F4-B3EB208125FBQ35883492-4B4995A3-3936-4131-AED1-F50CF1BA24C6Q36039597-0915F97B-F06B-47B5-BB1C-4CEA20C75E8DQ36234607-12B1C6B7-A8A5-4F93-954A-0BCF1334D7ADQ36469830-0D18F1CA-7918-4019-BE0D-5920B6B2CD7E
P2860
description
1989 nî lūn-bûn
@nan
1989 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Protein phosphorylation controls translation rates.
@ast
Protein phosphorylation controls translation rates.
@en
Protein phosphorylation controls translation rates.
@nl
type
label
Protein phosphorylation controls translation rates.
@ast
Protein phosphorylation controls translation rates.
@en
Protein phosphorylation controls translation rates.
@nl
prefLabel
Protein phosphorylation controls translation rates.
@ast
Protein phosphorylation controls translation rates.
@en
Protein phosphorylation controls translation rates.
@nl
P1476
Protein phosphorylation controls translation rates.
@en
P2093
Hershey JW
P304
20823-20826
P407
P577
1989-12-01T00:00:00Z