2024
The RNA-dependent association of phosphatidylinositol 4,5-bisphosphate with intrinsically disordered proteins contribute to nuclear compartmentalization
Sztacho M, Červenka J, Šalovská B, Antiga L, Hoboth P, Hozák P. The RNA-dependent association of phosphatidylinositol 4,5-bisphosphate with intrinsically disordered proteins contribute to nuclear compartmentalization. PLOS Genetics 2024, 20: e1011462. PMID: 39621780, PMCID: PMC11668513, DOI: 10.1371/journal.pgen.1011462.Peer-Reviewed Original ResearchPhosphatidylinositol 4,5-bisphosphateBromodomain-containing protein 4Nuclear specklesNuclear architectureRNA-dependent associationRNA-dependent mannerAssociated with RNAFunctional nuclear architectureRNA-dependentUbiquitination sitesNuclear compartmentalizationNuclear localizationNuclear fociNuclear compartmentDisordered proteinsPIP2 levelsDisordered regionsGene expressionHuman cellsPIP2RNANuclear processesBRD4 proteinProteinRNA content
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
2017
Non-apoptotic functions of BCL-2 family proteins
Gross A, Katz SG. Non-apoptotic functions of BCL-2 family proteins. Cell Death & Differentiation 2017, 24: 1348-1358. PMID: 28234359, PMCID: PMC5520452, DOI: 10.1038/cdd.2017.22.Peer-Reviewed Original ResearchConceptsNon-apoptotic rolesBcl-2 family proteinsFamily proteinsApoptotic roleNon-apoptotic functionsWhole-cell metabolismCellular survival pathwaysMitochondrial physiologyCellular survivalSurvival pathwaysMajor regulatorNuclear processesApoptosis processProteinMechanism of actionPhysiologyImportant cluesRoleAutophagyRegulatorFascinating fieldRegulationPathwayMechanismMetabolism
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
2012
Large-scale molecular dynamics simulations of dense plasmas: The Cimarron Project
Graziani F, Batista V, Benedict L, Castor J, Chen H, Chen S, Fichtl C, Glosli J, Grabowski P, Graf A, Hau-Riege S, Hazi A, Khairallah S, Krauss L, Langdon A, London R, Markmann A, Murillo M, Richards D, Scott H, Shepherd R, Stanton L, Streitz F, Surh M, Weisheit J, Whitley H. Large-scale molecular dynamics simulations of dense plasmas: The Cimarron Project. High Energy Density Physics 2012, 8: 105-131. DOI: 10.1016/j.hedp.2011.06.010.Peer-Reviewed Original ResearchDense plasmaNon-Maxwellian particle distributionsInertial confinement fusion experimentsQuantum statistical potentialsNew experimental effortsLawrence Livermore National LaboratoryLivermore National LaboratoryFusion plasmasElectron trajectoriesQuantum effectsStellar interiorsParallel molecular dynamics codePlasma conditionsDynamical timescaleSignificant electromagnetic fieldQuantum eventsFusion experimentsMolecular dynamics codeDynamical methodsElectromagnetic fieldNational LaboratoryEffective interactionStatistical potentialsNuclear processesExperimental efforts
2006
Regulation of Cell Adhesion Responses by Abl Family Kinases
Tanis K, Schwartz M. Regulation of Cell Adhesion Responses by Abl Family Kinases. Molecular Biology Intelligence Unit 2006, 16-25. DOI: 10.1007/978-0-387-68744-5_3.Peer-Reviewed Original ResearchAbl family kinasesFamily kinasesAbl familyMultiple focal adhesion proteinsFocal adhesion proteinsCytoskeletal regulatory proteinsNonreceptor tyrosine kinaseCell cycle progressionCell surface receptorsCell adhesive responsesInteraction of cellsIntegrin engagementRegulatory proteinsAdhesion proteinsGene expressionCell adhesion responsesCycle progressionCell spreadingTyrosine kinaseCellular responsesHuman diseasesCell survivalNuclear processesKinaseExtracellular matrix
1979
Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus
Lerner M, Steitz J. Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1979, 76: 5495-5499. PMID: 316537, PMCID: PMC411675, DOI: 10.1073/pnas.76.11.5495.Peer-Reviewed Original ResearchConceptsSmall nuclear RNA moleculesNuclear extractsMouse Ehrlich ascites cellsSmall nuclear RNANuclear RNA moleculesSmall nuclear ribonucleoproteinNuclear RNP particlesMammalian nucleiVertebrate speciesNuclear RNANuclear ribonucleoproteinRNA moleculesSystemic lupus erythematosusDifferent polypeptidesEhrlich ascites cellsIdentical complementSpecific proteinsMajor polypeptidesRNP particlesMolecular identityPossible functionsNuclear processesNuclear RNPAnti-Sm seraVirtue of association
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply