2017
Clonal hematopoiesis associated with TET2 deficiency accelerates atherosclerosis development in mice
Fuster JJ, MacLauchlan S, Zuriaga MA, Polackal MN, Ostriker AC, Chakraborty R, Wu CL, Sano S, Muralidharan S, Rius C, Vuong J, Jacob S, Muralidhar V, Robertson AA, Cooper MA, Andrés V, Hirschi KK, Martin KA, Walsh K. Clonal hematopoiesis associated with TET2 deficiency accelerates atherosclerosis development in mice. Science 2017, 355: 842-847. PMID: 28104796, PMCID: PMC5542057, DOI: 10.1126/science.aag1381.Peer-Reviewed Original ResearchConceptsTET2-deficient cellsLow-density lipoprotein receptor-deficient miceLipoprotein receptor-deficient miceClonal hematopoiesisBlood cellsAtherosclerotic cardiovascular diseaseAtherosclerotic plaque sizeReceptor-deficient miceBone marrow reconstitutionInterleukin-1β secretionMutant blood cellsAtherosclerosis developmentNLRP3 inhibitorAtheroprotective activityCardiovascular diseaseMarrow reconstitutionChimeric micePlaque sizeClonal expansionMiceMarked increaseCausal roleTET2 deficiencySomatic mutationsHematopoietic cells
2013
High-Level Expression, Purification and Characterization of a Constitutively Active Thromboxane A2 Receptor Polymorphic Variant
Xu B, Chakraborty R, Eilers M, Dakshinamurti S, O’Neil J, Smith S, Bhullar R, Chelikani P. High-Level Expression, Purification and Characterization of a Constitutively Active Thromboxane A2 Receptor Polymorphic Variant. PLOS ONE 2013, 8: e76481. PMID: 24086743, PMCID: PMC3781061, DOI: 10.1371/journal.pone.0076481.Peer-Reviewed Original ResearchConceptsG protein-coupled receptorsHigh-level expressionThromboxane A2 receptorSuccessful high-level expressionCell linesHigh-resolution crystal structuresProper expression systemMammalian cell linesResolution crystal structureProtein-coupled receptorsSingle-step affinity purificationStep affinity purificationCircular dichroism spectropolarimetryMembrane proteinsActive mutantAffinity purificationExpression systemBiophysical characterizationConstitutive signalingT geneSecondary structure changesT mutantGenetic variantsDiffusible ligandsHomogeneous glycosylation
2011
Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor
Arakawa M, Chakraborty R, Upadhyaya J, Eilers M, Reeves P, Smith S, Chelikani P. Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor. Biochimica Et Biophysica Acta 2011, 1808: 1170-1178. PMID: 21262196, PMCID: PMC3062665, DOI: 10.1016/j.bbamem.2011.01.012.Peer-Reviewed Original ResearchAdrenergic beta-AgonistsAdrenergic beta-AntagonistsAmino Acid SubstitutionAmino AcidsAnimalsBinding SitesChlorocebus aethiopsCOS CellsCricetinaeCyclic AMPDihydroalprenololGlycineHEK293 CellsHumansHydrogen BondingIsoproterenolModels, MolecularMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRadioligand AssayReceptors, Adrenergic, beta-2SerineStructure-Activity Relationship