2021
Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome
Sztacho M, Šalovská B, Červenka J, Balaban C, Hoboth P, Hozák P. Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome. Cells 2021, 10: 68. PMID: 33406800, PMCID: PMC7824793, DOI: 10.3390/cells10010068.Peer-Reviewed Original ResearchConceptsGene expressionHuman nuclear proteomeLimited proteolysisLabel-free quantitative mass spectrometryNuclear pore complexGene ontology analysisCell cycle regulationQuantitative mass spectrometryNuclear proteomeProtein effectorsPore complexPol IIRNA splicingOntology analysisMRNA splicingCycle regulationPIP2 bindingProtein interactionsDNA repairBioinformatics analysisNuclear envelopeFunctional domainsMass spectrometry identifiesSpecific proteinsCell cycle
2020
Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding
Park D, Chetrit D, Hu B, Roy CR, Liu J. Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding. MBio 2020, 11: 10.1128/mbio.03328-19. PMID: 32071271, PMCID: PMC7029142, DOI: 10.1128/mbio.03328-19.Peer-Reviewed Original ResearchConceptsType IV secretion systemSecretion systemCryoelectron tomographyInner membraneDot/Icm apparatusConformational changesDot/IcmEukaryotic host cellsBacterial inner membraneWild-type cellsHost cell membraneWhole-cell contextMultiprotein nanomachineSubtomogram analysisSophisticated nanomachinesCytoplasmic substratesProtein effectorsCell polesDNA substratesSubtomogram averagingATPase complexDNA transferHost infectionStructural basisHost cells
2012
Riboswitch control of Rho-dependent transcription termination
Hollands K, Proshkin S, Sklyarova S, Epshtein V, Mironov A, Nudler E, Groisman EA. Riboswitch control of Rho-dependent transcription termination. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 5376-5381. PMID: 22431636, PMCID: PMC3325659, DOI: 10.1073/pnas.1112211109.Peer-Reviewed Original ResearchConceptsRho-dependent transcription terminationTranscription terminationRiboswitch ligandsGene expressionControl gene expressionRho-specific inhibitorIntrinsic transcription terminationATPase activityActivity of RhoSalmonella enterica serovar TyphimuriumRiboswitch actionRiboswitch controlTranscription machineryProtein effectorsGene regulationRho ATPase activityEnterica serovar TyphimuriumTranslation initiationThird general mechanismRiboswitchTranscriptionEscherichia coliRNA sensorsWidespread modeSerovar Typhimurium
2004
RGS-7 Completes a Receptor-Independent Heterotrimeric G Protein Cycle to Asymmetrically Regulate Mitotic Spindle Positioning in C. elegans
Hess HA, Röper JC, Grill SW, Koelle MR. RGS-7 Completes a Receptor-Independent Heterotrimeric G Protein Cycle to Asymmetrically Regulate Mitotic Spindle Positioning in C. elegans. Cell 2004, 119: 209-218. PMID: 15479638, DOI: 10.1016/j.cell.2004.09.025.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell DivisionCentrosomeEmbryo, NonmammalianGTP-Binding Protein alpha SubunitsGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHeterotrimeric GTP-Binding ProteinsMutationNuclear ProteinsProtein BindingRecombinant Fusion ProteinsRGS ProteinsRNA InterferenceSpindle ApparatusConceptsG protein functionRIC-8G proteinsProtein functionC. elegans embryosAsymmetric cell divisionG protein effectorsHeterotrimeric G proteinsMitotic spindle positioningG protein signalingG-protein cycleSeven-transmembrane receptorsGPR-1/2RGS domainElegans embryosGTPase activatorProtein effectorsProtein cycleMicrotubule forcesSpindle positioningProtein signalingCell cortexCell divisionGTP hydrolysisMitotic spindle
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