2023
The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidence
2012
Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2
Copps K, White M. Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2. Diabetologia 2012, 55: 2565-2582. PMID: 22869320, PMCID: PMC4011499, DOI: 10.1007/s00125-012-2644-8.Peer-Reviewed Original ResearchConceptsInsulin receptor substrateT phosphorylationReceptor substrateSerine/threonine residuesSerine/threonine phosphorylationInsulin receptor tyrosine kinaseInsulin-stimulated kinasesReceptor tyrosine kinasesThreonine phosphorylationThreonine residuesNegative regulationTyrosine kinasePhosphorylationCultured cellsKinaseMetabolic diseasesIRS2IRS1Hormonal controlKey targetAltered patternTail regionComplex mechanismsRegulationDysregulation
2009
Detecting essential and removable interactions in genome-wide association studies.
Dewan A, Dubrow R, Hoh J, Liu X, Wu C, Yang Y, Ying Z, Zhang H. Detecting essential and removable interactions in genome-wide association studies. Statistics And Its Interface 2009, 2: 161-170. PMID: 21165165, PMCID: PMC3002050, DOI: 10.4310/sii.2009.v2.n2.a6.Peer-Reviewed Original Research
2007
Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatssrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBinds
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