2014
Calcium sensitive ring-like oligomers formed by synaptotagmin
Wang J, Bello O, Auclair SM, Wang J, Coleman J, Pincet F, Krishnakumar SS, Sindelar CV, Rothman JE. Calcium sensitive ring-like oligomers formed by synaptotagmin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 13966-13971. PMID: 25201968, PMCID: PMC4183308, DOI: 10.1073/pnas.1415849111.Peer-Reviewed Original ResearchMeSH KeywordsCalciumHumansLipid BilayersMultiprotein ComplexesProtein Structure, TertiarySNARE ProteinsSynaptotagmin IConceptsSynaptic vesicle protein Synaptotagmin 1Cytosolic domainSoluble N-ethylmaleimide-sensitive factorN-ethylmaleimide-sensitive factorMembrane fusion machineryReceptor complex assemblyRing-like oligomersFusion machineryC2 domainComplex assemblySynaptotagmin-1Helical reconstructionFusion proceedsNovel mechanismStructural mechanismsLipid monolayersNeurotransmitter releaseAbsence of calciumPhysiological concentrationsRing formationPresence of calciumFree calcium ionsSynaptotagminCalcium influxCircular arrangement
2013
Conformational Dynamics of Calcium-Triggered Activation of Fusion by Synaptotagmin
Krishnakumar SS, Kümmel D, Jones SJ, Radoff DT, Reinisch KM, Rothman JE. Conformational Dynamics of Calcium-Triggered Activation of Fusion by Synaptotagmin. Biophysical Journal 2013, 105: 2507-2516. PMID: 24314081, PMCID: PMC3853086, DOI: 10.1016/j.bpj.2013.10.029.Peer-Reviewed Original Research
2011
A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion
Krishnakumar SS, Radoff DT, Kümmel D, Giraudo CG, Li F, Khandan L, Baguley SW, Coleman J, Reinisch KM, Pincet F, Rothman JE. A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion. Nature Structural & Molecular Biology 2011, 18: 934-940. PMID: 21785412, PMCID: PMC3668341, DOI: 10.1038/nsmb.2103.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayHumansMembrane FusionModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsProtein Structure, TertiaryRatsSynaptosomal-Associated Protein 25SynaptotagminsSyntaxin 1Vesicle-Associated Membrane Protein 2Complexin cross-links prefusion SNAREs into a zigzag array
Kümmel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM. Complexin cross-links prefusion SNAREs into a zigzag array. Nature Structural & Molecular Biology 2011, 18: 927-933. PMID: 21785414, PMCID: PMC3410656, DOI: 10.1038/nsmb.2101.Peer-Reviewed Original Research
2004
Multiple‐probe analysis of folding and unfolding pathways of human serum albumin
Santra MK, Banerjee A, Krishnakumar SS, Rahaman O, Panda D. Multiple‐probe analysis of folding and unfolding pathways of human serum albumin. The FEBS Journal 2004, 271: 1789-1797. PMID: 15096218, DOI: 10.1111/j.1432-1033.2004.04096.x.Peer-Reviewed Original ResearchMeSH KeywordsBilirubinFluorescenceGuanidineHumansProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySerum Albumin
2003
Active and Inactive Orientations of the Transmembrane and Cytosolic Domains of the Erythropoietin Receptor Dimer
Seubert N, Royer Y, Staerk J, Kubatzky KF, Moucadel V, Krishnakumar S, Smith SO, Constantinescu SN. Active and Inactive Orientations of the Transmembrane and Cytosolic Domains of the Erythropoietin Receptor Dimer. Molecular Cell 2003, 12: 1239-1250. PMID: 14636581, DOI: 10.1016/s1097-2765(03)00389-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineDimerizationDNA-Binding ProteinsEnzyme ActivationErythroid Precursor CellsErythropoietinJanus Kinase 2MiceMilk ProteinsModels, MolecularMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProtein-Tyrosine KinasesProto-Oncogene ProteinsReceptors, ErythropoietinRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSequence AlignmentSignal TransductionSTAT3 Transcription FactorSTAT5 Transcription FactorTrans-ActivatorsTranscription FactorsTranscription, GeneticViral Envelope Proteins