Identification and characterization of a mitogen-activated S6 kinase.
about
Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino terminiPhosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinasesmTOR: from growth signal integration to cancer, diabetes and ageingDual requirement for a newly identified phosphorylation site in p70s6kUp-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's diseaseThe role and regulation of mTOR in T-lymphocyte functionThe human histamine H(2) receptor regulates c-jun and c-fos in a differential mannerRibosomal protein S6 phosphorylation and function during late gestation liver development in the ratTarget of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progressionCloning of the mitogen-activated S6 kinase from rat liver reveals an enzyme of the second messenger subfamily.A single gene encodes two isoforms of the p70 S6 kinase: activation upon mitogenic stimulation.Differential regulation of S6 phosphorylation by insulin and epidermal growth factor in Swiss mouse 3T3 cells: insulin activation of type 1 phosphatase.mRNA-selective translation induced by FSH in primary Sertoli cellsS6 kinase in quiescent Swiss mouse 3T3 cells is activated by phosphorylation in response to serum treatmentIdentical Mr 70,000 S6 kinase is activated biphasically by epidermal growth factor: a phosphopeptide that characterizes the late phaseInsulin activates a 70-kDa S6 kinase through serine/threonine-specific phosphorylation of the enzyme polypeptide.Luteinizing hormone stimulates mammalian target of rapamycin signaling in bovine luteal cells via pathways independent of AKT and mitogen-activated protein kinase: modulation of glycogen synthase kinase 3 and AMP-activated protein kinaseMolecular structure of a major insulin/mitogen-activated 70-kDa S6 protein kinase.Disruption of the p70(s6k)/p85(s6k) gene reveals a small mouse phenotype and a new functional S6 kinase.Abnormal regulation of ribosomal protein S6 kinase by insulin in skeletal muscle of insulin-resistant humans.Identification and early activation of a Xenopus laevis p70s6k following progesterone-induced meiotic maturation.The complexes of mammalian target of rapamycin.The modular phosphorylation and activation of p70s6k.Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism: implications for a direct activation of mTOR by phosphatidic acid.Ciliary transport regulates PDGF-AA/αα signaling via elevated mammalian target of rapamycin signaling and diminished PP2A activity.Targeted disruption of p70(s6k) defines its role in protein synthesis and rapamycin sensitivity.Development of monoclonal antibodies specific to ribosomal protein S6 kinase 2.Dissociation of inositol trisphosphate from diacylglycerol production in Rous sarcoma virus-transformed fibroblastsThe role of S6K1 in ER-positive breast cancer.Epidermal growth factor (EGF) stimulates association and kinase activity of Raf-1 with the EGF receptor.Regulation of pp90rsk phosphorylation and S6 phosphotransferase activity in Swiss 3T3 cells by growth factor-, phorbol ester-, and cyclic AMP-mediated signal transduction.Identification of mitogen-responsive ribosomal protein S6 kinase pp90rsk, a homolog of Xenopus S6 kinase II, in chicken embryo fibroblastsTwo distinct enzymes contribute to biphasic S6 phosphorylation in serum-stimulated chicken embryo fibroblastsIdentification of Xenopus S6 protein kinase homologs (pp90rsk) in somatic cells: phosphorylation and activation during initiation of cell proliferation.A Novel Mechanism of PPARgamma Regulation of TGFbeta1: Implication in Cancer BiologySequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinasePolyomavirus middle T antigen induces ribosomal protein S6 phosphorylation through pp60c-src-dependent and -independent pathways.Tuberous sclerosis complex, implication from a rare genetic disease to common cancer treatment.Activation of p70s6k is associated with phosphorylation of four clustered sites displaying Ser/Thr-Pro motifsmTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin
P2860
Q24311546-BD7D628E-456F-4279-BD1F-DBE2C902CD24Q24599204-A7C07618-6073-44F6-911F-E72A71263F3AQ24633662-A6B2EE44-E4A9-4498-9C6E-9059A3C90057Q24644595-DF7FEA23-6E6B-4A07-99DD-A77511E384DDQ24685592-311ED629-24D0-4C40-811E-41DA5DD6C177Q26830161-520E62C6-A72F-4760-A1CD-D78789206640Q28145670-B806FB4B-D8C8-4571-9C2E-588291556643Q28568255-CC090BE5-2734-4E45-8764-419BCA9F7515Q29617473-BF397614-22DD-4752-8984-3C4958A0D8ABQ30824759-052CC0CD-416B-4DB7-969E-EEA57BDAD650Q30846613-F2701AF1-5E88-4818-B507-44FABFEF9B7AQ33584931-2A8775F5-92D7-4A23-9D03-9A3B74545292Q33636672-C9D3B402-FAC0-4735-894E-CF8B2B413D8CQ33650875-35B3CA01-96C1-437C-9596-E0D34DA8355AQ33788073-6AE592BF-B39D-43B5-9346-DD97BBC9C18BQ33841430-234388E0-387D-463B-8E39-A5DD80D7C207Q33874422-952467E1-73DE-404D-97A1-445F9E7C2EA0Q33877880-06354DAA-6EB4-49D0-B467-78EEC9D8C269Q33890035-8EC2BFFE-85CE-4D76-8B3D-F66D2BB86439Q33890133-EC7E45AD-72D3-46F1-B004-E59E31957248Q33937723-4809471F-8BE5-4205-A482-223EEE170680Q34116818-E0260340-3EC6-48BD-A70E-5C51A4D722FEQ34434557-0907BCFC-A7DE-4458-9DC6-373074777D61Q34450669-1E3A8CF6-B448-4980-8758-FA5C6889F192Q34960781-C7406340-72C0-4B1F-8C39-6CD6BE95D001Q36063511-9057DCB3-46C1-446D-95CC-753E65597451Q36168887-2FB7F58F-167D-47C7-B170-4B8BC221F985Q36220044-4CDD706E-2A8F-4B59-AE38-A5CBC5FEC09DQ36304094-19C6D820-BC9D-4EC8-BD42-3872D105E32DQ36684473-D09E62E6-3E3B-4C5E-BF15-73939FCDFD2FQ36687724-099099B9-2950-405C-B487-45925A9D2002Q36709337-C43665D2-4A6A-4AF1-BC34-9B96A6A17B39Q36710538-DBD4A25E-6797-4723-B8B9-D0097A706446Q36711986-FF493462-7A92-4064-99E4-732E57FB65E2Q36743890-FB05A5AF-E1E0-4BDC-80EB-CF0384DE3D8EQ36760407-A0ED71F4-6F1F-4C2C-877D-F7633723EEDFQ36789817-479FE1C0-9F0F-42CB-85F1-BBCBC0D198D4Q37134137-94D23DAF-6A95-461A-A6CA-0EC978511C3BQ37143272-63D0413E-F023-440D-82A6-7AF05CD7580AQ37166913-8A59C2F7-D44A-4804-A3F8-D961C5384B97
P2860
Identification and characterization of a mitogen-activated S6 kinase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1988
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Identification and characterization of a mitogen-activated S6 kinase.
@en
Identification and characterization of a mitogen-activated S6 kinase.
@nl
type
label
Identification and characterization of a mitogen-activated S6 kinase.
@en
Identification and characterization of a mitogen-activated S6 kinase.
@nl
prefLabel
Identification and characterization of a mitogen-activated S6 kinase.
@en
Identification and characterization of a mitogen-activated S6 kinase.
@nl
P2093
P2860
P356
P1476
Identification and characterization of a mitogen-activated S6 kinase.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.2.406
P407
P577
1988-01-01T00:00:00Z