2023
Human TRPV1 structure and inhibition by the analgesic SB-366791
Neuberger A, Oda M, Nikolaev Y, Nadezhdin K, Gracheva E, Bagriantsev S, Sobolevsky A. Human TRPV1 structure and inhibition by the analgesic SB-366791. Nature Communications 2023, 14: 2451. PMID: 37117175, PMCID: PMC10147690, DOI: 10.1038/s41467-023-38162-9.Peer-Reviewed Original ResearchConceptsSB-366791Transient receptor potential (TRP) ion channelsPotential ion channelsPain pathwaysPain therapyPain treatmentPsychiatric disordersOpioid crisisTherapy targetTRPV1 inhibitorElectrophysiological recordingsHuman TRPV1TRP channelsTRPV1New drugsDisease conditionsVanilloid subfamilyIon channelsTreatmentInhibitorsOpioidsPainTherapyDiseaseCryo-electron microscopy structure
2021
Extracellular cap domain is an essential component of the TRPV1 gating mechanism
Nadezhdin KD, Neuberger A, Nikolaev YA, Murphy LA, Gracheva EO, Bagriantsev SN, Sobolevsky AI. Extracellular cap domain is an essential component of the TRPV1 gating mechanism. Nature Communications 2021, 12: 2154. PMID: 33846324, PMCID: PMC8041747, DOI: 10.1038/s41467-021-22507-3.Peer-Reviewed Original ResearchConceptsCap domainC-terminusIon conductance pathwaysNumerous physiological processesTransient receptor potential channelsTRP channel familyCryo-EMPhysiological processesChannel familyExtracellular entranceHuman diseasesGating mechanismÎ’-sheetConductance pathwayCritical determinantMolecular sensorsOpen probabilityPotential channelsIon selectivityEssential componentTRPV1 functionDomainTerminusProteinDeletion
2019
Mammalian TRP ion channels are insensitive to membrane stretch
Nikolaev YA, Cox CD, Ridone P, Rohde PR, Cordero-Morales JF, Vásquez V, Laver DR, Martinac B. Mammalian TRP ion channels are insensitive to membrane stretch. Journal Of Cell Science 2019, 132: jcs238360. PMID: 31722978, PMCID: PMC6918743, DOI: 10.1242/jcs.238360.Peer-Reviewed Original ResearchConceptsTRP channelsTouch-insensitive mutantsMembrane stretchIon channelsTRP ion channel familyIon channel familyTransient receptor potential (TRP) ion channelsTRP ion channelsMammalian subfamiliesMammalian membersPotential ion channelsArtificial bilayer systemInsensitive mutantsCytoplasmic tethersDownstream componentsMechanosensory processesSignaling cascadesChannel familyCellular componentsBlood pressure regulationCell membraneCerebrospinal fluid flowMechanical forcesStretch activationPressure regulationPiezo2 integrates mechanical and thermal cues in vertebrate mechanoreceptors
Zheng W, Nikolaev YA, Gracheva EO, Bagriantsev SN. Piezo2 integrates mechanical and thermal cues in vertebrate mechanoreceptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 17547-17555. PMID: 31413193, PMCID: PMC6717272, DOI: 10.1073/pnas.1910213116.Peer-Reviewed Original Research
2017
Adding dimension to cellular mechanotransduction: Advances in biomedical engineering of multiaxial cell-stretch systems and their application to cardiovascular biomechanics and mechano-signaling
Friedrich O, Schneidereit D, Nikolaev Y, Nikolova-Krstevski V, Schürmann S, Wirth-Hücking A, Merten A, Fatkin D, Martinac B. Adding dimension to cellular mechanotransduction: Advances in biomedical engineering of multiaxial cell-stretch systems and their application to cardiovascular biomechanics and mechano-signaling. Progress In Biophysics And Molecular Biology 2017, 130: 170-191. PMID: 28647645, DOI: 10.1016/j.pbiomolbio.2017.06.011.Peer-Reviewed Original ResearchConceptsFocal adhesion complexesCell-substrate junctionLive-cell imagingMechanosensitive ion channelsDirect mechanistic studiesAdhesion complexesCellular mechanotransductionMembrane junctionsIntracellular signalingMechanotransduction researchCellular stretchCellular modelIon channelsCellular levelCell membraneMechanotransductionIndividual cardiomyocytesBiomedical engineeringMechanical wall stressMembraneMechanistic studiesCellsStretch deviceCardiomyocytesElastomeric membrane
2015
Lipid–protein interactions: Lessons learned from stress
Battle A, Ridone P, Bavi N, Nakayama Y, Nikolaev Y, Martinac B. Lipid–protein interactions: Lessons learned from stress. Biochimica Et Biophysica Acta 2015, 1848: 1744-1756. PMID: 25922225, DOI: 10.1016/j.bbamem.2015.04.012.Peer-Reviewed Original ResearchConceptsLipid-protein interactionsMS channelsLipid bilayersRegulation of cellMechanosensitive membrane channelsMechanosensitive proteinsMembrane proteinsCellular compartmentsTransmembrane portionProkaryotic systemIntracellular signalsPhysical barrierPhysiological processesHypoosmotic shockMembrane channelsMS proteinBiological membranesProteinVariety of rolesCell lysisNormal functionIntracellular spaceEukaryotesCardiac hypertrophyMuscular dystrophy
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