2003
Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*
Suenaga A, Kiyatkin AB, Hatakeyama M, Futatsugi N, Okimoto N, Hirano Y, Narumi T, Kawai A, Susukita R, Koishi T, Furusawa H, Yasuoka K, Takada N, Ohno Y, Taiji M, Ebisuzaki T, Hoek JB, Konagaya A, Kholodenko BN. Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*. Journal Of Biological Chemistry 2003, 279: 4657-4662. PMID: 14613932, DOI: 10.1074/jbc.m310598200.Peer-Reviewed Original ResearchConceptsPhosphotyrosine bindingTyr-317Shc phosphorylationSH2 domainC-terminal Src homology 2 domainSrc homology 2 domainRas/Raf/MEK/ERK pathwayShc adaptor proteinRaf/MEK/ERK pathwayMEK/ERK pathwayReceptor tyrosine kinasesShc functionPhosphorylated ShcPhosphorylation sitesAdaptor proteinLinker regionShcTyrosine kinaseERK pathwayMembrane receptorsPhosphorylationDomain motionMolecular dynamics simulationsNumerous partnersDomain coupling
1996
Prostaglandin E2 Stimulates a Ca2+-dependent K+ Channel in Human Erythrocytes and Alters Cell Volume and Filterability*
Li Q, Jungmann V, Kiyatkin A, Low P. Prostaglandin E2 Stimulates a Ca2+-dependent K+ Channel in Human Erythrocytes and Alters Cell Volume and Filterability*. Journal Of Biological Chemistry 1996, 271: 18651-18656. PMID: 8702518, DOI: 10.1074/jbc.271.31.18651.Peer-Reviewed Original ResearchConceptsProstaglandin E2Red blood cellsRelease of PGE2Efflux pathwayGardos channel inhibitorGardos channel activationM. Prostaglandin E2PGE2 treatmentIntact red blood cellsHuman erythrocytesMean cell volumeChannel inhibitorsClot formationEffects of metabolitesCell shrinkageGardos channelHuman red blood cellsNa/K/2Cl cotransportBlood cellsOsmotic fragilityChannel activationRed cellsPossible involvementPlateletsCell volume