2021
Evolving A RIG-I Antagonist: A Modified DNA Aptamer Mimics Viral RNA
Ren X, Gelinas AD, Linehan M, Iwasaki A, Wang W, Janjic N, Pyle A. Evolving A RIG-I Antagonist: A Modified DNA Aptamer Mimics Viral RNA. Journal Of Molecular Biology 2021, 433: 167227. PMID: 34487794, DOI: 10.1016/j.jmb.2021.167227.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, ViralAptamers, NucleotideBinding SitesCloning, MolecularCrystallography, X-RayDEAD Box Protein 58Escherichia coliGene ExpressionGenetic VectorsHumansImmunologic FactorsKineticsModels, MolecularMolecular MimicryMutationNucleic Acid ConformationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsReceptors, ImmunologicRecombinant ProteinsRNA, ViralSELEX Aptamer TechniqueConceptsHigh-resolution crystal structuresResolution crystal structureRIG-I receptorResult of mutationsSame amino acidsVertebrate organismsProtein receptorsInnate immune receptorsRNA virusesImmune receptorsAmino acidsTool compoundsViral ligandsViral RNAImportant receptorPathogenic moleculesGeneralizable strategyDNA aptamersMolecular mimicryCentral roleDisease statesReceptorsTerminusRNAOrganisms
2020
Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1
Travis SM, DAmico K, Yu IM, McMahon C, Hamid S, Ramirez-Arellano G, Jeffrey PD, Hughson FM. Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1. Journal Of Biological Chemistry 2020, 295: 10125-10135. PMID: 32409579, PMCID: PMC7383367, DOI: 10.1074/jbc.ra120.013654.Peer-Reviewed Original ResearchConceptsCoat protein ITarget membraneDsl1 complexSNARE motifEndoplasmic reticulumSNARE complexMembrane-bridging SNARE complexesSensitive factor attachment protein receptorsFactor attachment protein receptorsAttachment protein receptorsN-terminal domainHabc domainMacromolecular machinesCOPI coatVesicle dockingFusion machineryStructural basisMembrane fusionOpen conformationProtein IProtein receptorsDsl1X-ray crystallographySnareCentral hinge
2018
Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly
Ma L, Jiao J, Zhang Y. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly. Methods In Molecular Biology 2018, 1860: 95-114. PMID: 30317500, PMCID: PMC6441361, DOI: 10.1007/978-1-4939-8760-3_6.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE assemblyHigh-resolution optical tweezersN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsOptical tweezers studiesNeuronal SNARE assemblyIntracellular membrane fusionAttachment protein receptorsOptical tweezersΑ-SNAPDetailed experimental protocolCellular compartmentsRegulatory proteinsProtein receptorsDifferent cellsSpatiotemporal resolutionProteinAssemblyFusion processManipulation approachTweezersExperimental approachFusion
2017
Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers
Zhang Y. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers. Protein Science 2017, 26: 1252-1265. PMID: 28097727, PMCID: PMC5477538, DOI: 10.1002/pro.3116.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorSNARE assemblyMembrane fusionSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsFast calcium-triggered fusionAttachment protein receptorsHigh-resolution optical tweezersCalcium-triggered fusionC-terminal domainFour-helix bundleNeurotransmitter-containing vesiclesLinker domainPlasma membraneDomain associationProtein receptorsMolecular engineDifferent functionsPathwayAssemblyMembraneOptical tweezersSynaptic transmission
2016
Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex
Zhang X, Rebane AA, Ma L, Li F, Jiao J, Qu H, Pincet F, Rothman JE, Zhang Y. Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e8031-e8040. PMID: 27911771, PMCID: PMC5167175, DOI: 10.1073/pnas.1605748113.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsMembrane FusionMiceMicroscopy, Atomic ForceMolecular Dynamics SimulationMunc18 ProteinsOptical TweezersProtein ConformationProtein DomainsProtein FoldingProtein StabilityQa-SNARE ProteinsSNARE ProteinsSynaptic TransmissionSynaptosomal-Associated Protein 25Vesicle-Associated Membrane Protein 2ConceptsSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorT-SNARE complexC-terminal domainN-terminal domainSNARE zipperingPlasma membraneN-ethylmaleimide-sensitive factor attachment protein receptorsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsTarget plasma membraneAttachment protein receptorsFour-helix bundleThree-helix bundleSynaptic vesicle fusionSingle-molecule force spectroscopyV-SNARESNARE assemblySNARE complexHelical bundleConformational switchC-terminusMembrane fusionVesicle fusionProtein receptorsZipperingα-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
Ma L, Kang Y, Jiao J, Rebane AA, Keun HK, Xi Z, Qu H, Zhang Y. α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle. Cell Reports 2016, 15: 531-539. PMID: 27068468, PMCID: PMC4838522, DOI: 10.1016/j.celrep.2016.03.050.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsC-terminal domainN-terminal domainMembrane fusionLinker domainΑ-SNAPSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsIntracellular membrane fusionAttachment protein receptorsConformational selection mechanismFour-helix bundleSNARE assemblySNARE complexProtein receptorsDynamic assemblyStepwise assemblyAssemblyDomainFusionZipperingOptical tweezersRecent experimentsReceptors
2014
Altered Genome-Wide Methylation in Endometriosis
Naqvi H, Ilagan Y, Krikun G, Taylor HS. Altered Genome-Wide Methylation in Endometriosis. Reproductive Sciences 2014, 21: 1237-1243. PMID: 24784717, PMCID: PMC5933183, DOI: 10.1177/1933719114532841.Peer-Reviewed Original ResearchConceptsGene expressionBone morphogenetic protein receptorGenome-wide methylationDual specificity phosphatase 22Morphogenetic protein receptorTumor protein 73Genome-wide methylation arrayAberrant DNA methylationInhibitor of DNADNA methylationCandidate genesBinding protein 7Member 21Methylation arraysProtein receptorsQuantitative real-time polymerase chain reactionGenesImmunoglobulin SuperfamilyAberrant methylationMethylation statusProtein 7MethylationCell proliferationAbnormal regulationReceptor 1BCommon intermediates and kinetics, but different energetics, in the assembly of SNARE proteins
Zorman S, Rebane AA, Ma L, Yang G, Molski MA, Coleman J, Pincet F, Rothman JE, Zhang Y. Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins. ELife 2014, 3: e03348. PMID: 25180101, PMCID: PMC4166003, DOI: 10.7554/elife.03348.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEnergy TransferHumansKineticsModels, MolecularMolecular Sequence DataMultiprotein ComplexesOptical TweezersProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryQa-SNARE ProteinsRatsSequence Homology, Amino AcidSNARE ProteinsThermodynamicsVesicle-Associated Membrane Protein 2Vesicular Transport ProteinsConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE complexN-ethylmaleimide-sensitive factor attachment protein receptorsMembrane fusionFactor attachment protein receptorsAttachment protein receptorsHigh-resolution optical tweezersNeuronal SNARE complexFolding/assemblyEnergy releaseSNARE proteinsSingle-molecule levelProtein receptorsDomain associationOptical tweezersTerminal partZippering mechanismFusion kineticsZipperingComplexesAssemblyDifferent energeticsEnergyYeastTweezers
2013
Live-cell imaging of exocyst links its spatiotemporal dynamics to various stages of vesicle fusion
Rivera-Molina F, Toomre D. Live-cell imaging of exocyst links its spatiotemporal dynamics to various stages of vesicle fusion. Journal Of Cell Biology 2013, 201: 673-680. PMID: 23690179, PMCID: PMC3664709, DOI: 10.1083/jcb.201212103.Peer-Reviewed Original ResearchConceptsLive-cell imagingVesicle fusionEndocytic recycling compartmentAttachment protein receptorsSNARE fusion machineryExocyst complexMembrane traffickingFusion machineryRecycling compartmentCell cortexSec8Cell protrusionsPlasma membraneVesicle attachmentFusion poreMembrane expansionProtein receptorsCell polarizationFluorescence recoverySpatiotemporal dynamicsExocystUbiquitous roleVesiclesTraffickingMorphological criteria
2011
Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex
Shi L, Kümmel D, Coleman J, Melia TJ, Giraudo CG. Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex. Molecular Biology Of The Cell 2011, 22: 4150-4160. PMID: 21900493, PMCID: PMC3204075, DOI: 10.1091/mbc.e11-02-0150.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalorimetryCell MembraneHeLa CellsHuman Growth HormoneHumansLiposomesMiceMicroscopy, FluorescenceMolecular ChaperonesMunc18 ProteinsNeuroendocrine CellsPC12 CellsProtein BindingProtein Interaction Domains and MotifsProtein TransportRatsRecombinant ProteinsSNARE ProteinsSyntaxin 1ThermodynamicsTitrimetryConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSyntaxin 1AMunc18-1N-ethylmaleimide-sensitive factor attachment protein receptorsSec1/Munc18 (SM) proteinsFactor attachment protein receptorsCentral cavitySNARE complex assemblyIntracellular membrane traffickingAttachment protein receptorsMunc18-1 mutantsLiposome fusionPrecise molecular mechanismsMunc18 proteinsMembrane traffickingSNARE complexChaperone functionH3 domainDistinct binding modesMembrane fusionMolecular mechanismsProtein receptorsDual functionNeuroendocrine cellsBinding modes
2010
Protein Determinants of SNARE-Mediated Lipid Mixing
Ji H, Coleman J, Yang R, Melia TJ, Rothman JE, Tareste D. Protein Determinants of SNARE-Mediated Lipid Mixing. Biophysical Journal 2010, 99: 553-560. PMID: 20643074, PMCID: PMC2905075, DOI: 10.1016/j.bpj.2010.04.060.Peer-Reviewed Original ResearchConceptsSNARE proteinsN-ethylmaleimide-sensitive factor attachment protein receptorsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSensitive factor attachment protein receptorsFactor attachment protein receptorsT-SNARE complexMembrane SNARE proteinsT-SNARE proteinsAttachment protein receptorsLipid mixingMembrane SNAREsProtein receptorsProtein determinantsReconstitution conditionsReconstitution protocolsSnareLiposome fusionProteinLiposome populationsSpecific activityLipidsOptimal lipidProteoliposomesPhysiologyRecent work
2001
Absence of Functional Type 1 Parathyroid Hormone (PTH)/PTH-Related Protein Receptors in Humans Is Associated with Abnormal Breast Development and Tooth Impaction
Wysolmerski J. Absence of Functional Type 1 Parathyroid Hormone (PTH)/PTH-Related Protein Receptors in Humans Is Associated with Abnormal Breast Development and Tooth Impaction. The Journal Of Clinical Endocrinology & Metabolism 2001, 86: 1788-1794. DOI: 10.1210/jc.86.4.1788.Peer-Reviewed Original Research
1980
Identification of functional domains of human erythrocyte spectrin.
Morrow J, Speicher D, Knowles W, Hsu C, Marchesi V. Identification of functional domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 6592-6596. PMID: 6935670, PMCID: PMC350332, DOI: 10.1073/pnas.77.11.6592.Peer-Reviewed Original ResearchConceptsHuman erythrocyte spectrinErythrocyte membrane vesiclesMembrane vesiclesBinding of spectrinErythrocyte spectrinHigh-affinity membraneCleavage of spectrinFunctional domainsCytoplasmic surfaceDimeric spectrinProtein receptorsPolypeptide chainTerminal regionSpectrinTemperature-dependent associationUnique polypeptide chainsNoncovalent associationTerminal portionAlpha chainBeta chain
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply