2023
Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery
Sundaram R, Chatterjee A, Bera M, Grushin K, Panda A, Li F, Coleman J, Lee S, Ramakrishnan S, Ernst A, Gupta K, Rothman J, Krishnakumar S. Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2309516120. PMID: 37590407, PMCID: PMC10450444, DOI: 10.1073/pnas.2309516120.Peer-Reviewed Original ResearchConceptsCore protein machineryRelease-ready vesiclesSynaptic vesicle primingVesicle primingProtein machinerySingle-molecule imagingSNAREpin assemblyFunctional intermediatesFunctional reconstitutionMunc13DiacylglycerolCoordinated actionMunc18VesiclesMachineryComplete reconstitutionNew roleSelective effectDetailed characterizationChaperonesRate of caReconstitutionVAMP2ComplexinMutations
2020
Nuclear filaments: role in chromosomal positioning and gene expression
Bera M, Sengupta K. Nuclear filaments: role in chromosomal positioning and gene expression. Nucleus 2020, 11: 99-110. PMID: 32453974, PMCID: PMC7529408, DOI: 10.1080/19491034.2020.1769445.Peer-Reviewed Original ResearchConceptsChromosomal contactsGene expressionLMNA mutationsInner nuclear membraneDNA damage repairGene expression profilesIntrachromosomal contactsChromosomal positioningChromosome positioningNuclear actinNuclear laminsEpigenetic modificationsLamin networkChromosomal loopsDamage repairExpression profilesNuclear membraneNuclear processesKey playersLaminsLaminopathiesMutationsElastic meshworkMuscle tissueMechanical rigidity
2016
Significance of 1B and 2B domains in modulating elastic properties of lamin A
Bera M, Ainavarapu S, Sengupta K. Significance of 1B and 2B domains in modulating elastic properties of lamin A. Scientific Reports 2016, 6: 27879. PMID: 27301336, PMCID: PMC4908593, DOI: 10.1038/srep27879.Peer-Reviewed Original ResearchConceptsLamin ASingle-molecule force spectroscopyRod domainType V intermediate filament proteinsLamin rod domainsSingle molecular levelInner nuclear membraneC-terminal domainIntermediate filament proteinsForce spectroscopyNuclear laminsLaminsNuclear membraneFilament proteinsElastic meshworkNuclear shapeMutationsComparable mechanical propertiesDomainViscoelastic behaviorSpectroscopyLaminopathiesProperties
2014
Characterization of Unfolding Mechanism of Human Lamin A Ig Fold by Single-Molecule Force SpectroscopyImplications in EDMD
Bera M, Kotamarthi H, Dutta S, Ray A, Ghosh S, Bhattacharyya D, Ainavarapu S, Sengupta K. Characterization of Unfolding Mechanism of Human Lamin A Ig Fold by Single-Molecule Force SpectroscopyImplications in EDMD. Biochemistry 2014, 53: 7247-7258. PMID: 25343322, DOI: 10.1021/bi500726f.Peer-Reviewed Original ResearchConceptsIg domainsBasic nuclear processesB-type laminsC-terminal domainHelical rod domainAutosomal dominant Emery-Dreifuss muscular dystrophySingle-molecule force spectroscopyEmery-Dreifuss muscular dystrophyIntermediate filament proteinsHuman laminLamin proteinsNuclear laminaLamin ALamin A.Nuclear envelopeRod domainNuclear processesUnfolding mechanismFilament proteinsMisshapen nucleiCausative mutationsKey playersR453WLaminsMutations