2022
Pathogenic Leptospira Evolved a Unique Gene Family Comprised of Ricin B-Like Lectin Domain-Containing Cytotoxins
Chaurasia R, Marroquin AS, Vinetz JM, Matthias MA. Pathogenic Leptospira Evolved a Unique Gene Family Comprised of Ricin B-Like Lectin Domain-Containing Cytotoxins. Frontiers In Microbiology 2022, 13: 859680. PMID: 35422779, PMCID: PMC9002632, DOI: 10.3389/fmicb.2022.859680.Peer-Reviewed Original ResearchVM proteinsUnique gene familiesStructural homology searchRecombinant ricin B chainΒ-trefoil domainR-type lectinsCaspase-3 activationHeLa cell surfaceBacterial plasmid DNAGene familyImportant virulence determinantN-terminal fragmentHomology searchCell surface bindingRicin B chainHuman cellsNuclear fragmentationB domainHeLa cellsCell surfaceNuclear translocationVirulence determinantsDNase activityDNase functionProtein
2016
Structural Basis for the Procofactor to Cofactor Transition in Human Factor V
Kumar S, Deng W, Stayrook S, Li R, Camire R, Krishnaswamy S. Structural Basis for the Procofactor to Cofactor Transition in Human Factor V. Blood 2016, 128: 253. DOI: 10.1182/blood.v128.22.253.253.Peer-Reviewed Original ResearchBasic regionB domainC-terminusLong standing puzzleBR bindingCrystal structureDocking studiesBr fragmentsHuman factor VCentral B domainA2 domainAmide proton exchange ratesPhosphatidylserine-containing membranesAr2Hydrogen-deuterium exchangeA1-A2-B-A3-C1-C2Adjacent regionsAmide proton exchangeComputational docking studiesProton exchange ratesDomain organizationAcid sequenceProteolytic excisionCofactor formationPrimary structure
2015
The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox
Kumar S, Stayrook S, Camire R, Krishnaswamy S. The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox. Blood 2015, 126: 121. DOI: 10.1182/blood.v126.23.121.121.Peer-Reviewed Original ResearchB domainAcid regionC-terminusCofactor functionBR bindingDiffraction quality crystalsCoagulation factor VA3 domainFactor VaCofactor activityHomologous A domainsA1-A2-B-A3-C1-C2Ca2+-dependent fashionDomain organizationMolecular replacementAcid sequenceXa bindingSingle chain antibodyPrimary sequenceProteolytic excisionDevelopment of novel strategiesBind calcium ionsProteolytic processingProteolytic cleavageStructure-based model
2014
Lack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIII
Grushin K, Miller J, Dalm D, Parker E, Healey J, Lollar P, Stoilova-McPhie S. Lack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIII. Haemophilia 2014, 20: 723-731. PMID: 24750465, PMCID: PMC4149818, DOI: 10.1111/hae.12421.Peer-Reviewed Original ResearchConceptsFVIII formsB domainFVIII-BDDPhospholipid vesicle aggregationFactor VIII B domainCryo-electron microscopyMembrane-bound statePhospholipid vesiclesMembrane-bound formSerine protease factor IXaPhysiological conditionsFVIII B domainSecondary structure distributionCryo-EMVesicle aggregationBiophysical propertiesCircular dichroismProtein therapeuticsVesiclesTenase complexPhospholipid membranesPlatelet surfaceHuman factor VIIIFactor IXaHereditary bleeding disorders
2013
Factor Xa Activation of Factor V Is of Paramount Importance in Initiating the Coagulation System
Schuijt TJ, Bakhtiari K, Daffre S, DePonte K, Wielders SJ, Marquart JA, Hovius JW, van der Poll T, Fikrig E, Bunce MW, Camire RM, Nicolaes GA, Meijers JC, van ‘t Veer C. Factor Xa Activation of Factor V Is of Paramount Importance in Initiating the Coagulation System. Circulation 2013, 128: 254-266. PMID: 23817575, PMCID: PMC3826089, DOI: 10.1161/circulationaha.113.003191.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnticoagulantsArthropod ProteinsBlood CoagulationBlood Coagulation TestsDose-Response Relationship, DrugFactor VFactor XaFactor Xa InhibitorsFeeding BehaviorFibrinogenHumansIxodesMutagenesisProtein Structure, TertiaryRabbitsRecombinant ProteinsSalivary Proteins and PeptidesSurface Plasmon ResonanceThrombin
2011
High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation
Kumar S, Stayrook S, Huntington J, Camire R, Krishnaswamy S. High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation. Blood 2011, 118: 375. DOI: 10.1182/blood.v118.21.375.375.Peer-Reviewed Original ResearchC2 domainA2 domainVenom proteinsB domainVenom of Pseudonaja textilisMembrane-dependent reactionsA1-A2-B-A3-C1-C2Absence of membranesMammalian coagulationSequence alignmentMammalian blood coagulationDomain organizationMolecular replacementRegulating blood coagulationToxin repertoireProtruding loopBinding to membranesHydrophobic residuesProteolytic processingBind membranesResolution structureMembrane bindingA-resolutionActivation of human prothrombinProteolytic activity
1984
1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes.
Prigodich R, Casas-Finet J, Williams K, Konigsberg W, Coleman J. 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes. Biochemistry 1984, 23: 522-9. PMID: 6367821, DOI: 10.1021/bi00298a019.Peer-Reviewed Original ResearchConceptsN-terminal B-domainGene 32 proteinC-terminal domainCore proteinComplex formationGene 32Bacteriophage T4Bacteriophage fdC-terminalOligonucleotide bindingChemical shift changesTyr residuesB domainAromatic residuesNucleotide basesProteinResiduesLong rotational correlation timeOligonucleotide complexesHigh affinityComplexesShift changesDomainProton resonancesRotational correlation time
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