2021
A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase
Chen E, Reiss K, Shah D, Manjula R, Allen B, Murphy EL, Murphy JW, Batista VS, Bhandari V, Lolis EJ, Lisi GP. A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase. Journal Of Biological Chemistry 2021, 297: 101061. PMID: 34384784, PMCID: PMC8405996, DOI: 10.1016/j.jbc.2021.101061.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric SiteAmino Acid SequenceAntigens, Differentiation, B-LymphocyteBinding SitesCatalytic DomainCrystallography, X-RayCytokinesHistocompatibility Antigens Class IIHumansIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsProtein BindingStructure-Activity RelationshipConceptsAllosteric siteDopachrome tautomeraseDynamic regulatory networksEnzymatic activityLow sequence identityLigand-binding siteMultiple ligand-binding sitesNonoverlapping functionsRegulatory networksAllosteric couplingMacrophage migration inhibitory factor (MIF) familyFactor familySequence identityHomolog DStructural basisPrimary sequenceCD74 activationFunctional similarityConformational changesSolution NMRMIF-2X-ray crystallographyCatalytic siteStructural consequencesSolvent channelsA structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase
Chen, E., Reiss, K., Shah, D., Manjula, R., Allen, B., Murphy, E.L., Murphy, J.W., Batista, V.S., Bhandari, V., Lolis, E.J., and Lisi, G.P. (2021).Peer-Reviewed Original Research
2020
SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases.
Manjula R, Anuja K, Alcain FJ. SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases. Frontiers In Pharmacology 2020, 11: 585821. PMID: 33597872, PMCID: PMC7883599, DOI: 10.3389/fphar.2020.585821.Peer-Reviewed Original Research
2019
Design, synthesis, in-vitro evaluation and molecular docking studies of novel indole derivatives as inhibitors of SIRT1 and SIRT2.
Manjula R, Gokhale N, Unni S, Deshmukh P, Reddyrajula R, Srinivas Bharath MM, Dalimba U, Padmanabhan B. Design, synthesis, in-vitro evaluation and molecular docking studies of novel indole derivatives as inhibitors of SIRT1 and SIRT2. Bioorganic Chemistry 2019, 92: 103281. PMID: 31561106, DOI: 10.1016/j.bioorg.2019.103281.Peer-Reviewed Original ResearchRational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis.
Manjula R, Unni S, Wright GSA, Bharath M M S, Padmanabhan B. Rational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis. Journal Of Biomolecular Structure & Dynamics 2019, 37: 3936-3946. PMID: 30286701, DOI: 10.1080/07391102.2018.1531787.Peer-Reviewed Original Research
2018
Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation.
Manjula R, Wright GSA, Strange RW, Padmanabhan B. Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation. FEBS Letters 2018, 592: 1725-1737. PMID: 29679384, DOI: 10.1002/1873-3468.13055.Peer-Reviewed Original Research
2016
Bromodomain and extra-terminal (BET) family proteins: New therapeutic targets in major diseases.
Padmanabhan B, Mathur S, Manjula R, Tripathi S. Bromodomain and extra-terminal (BET) family proteins: New therapeutic targets in major diseases. Journal Of Biosciences 2016, 41: 295-311. PMID: 27240990, DOI: 10.1007/s12038-016-9600-6.Peer-Reviewed Original ResearchIdentification of New Inhibitors for Human SIRT1: An in-silico Approach.
Padmanabhan B, Ramu M, Mathur S, Unni S, Thiyagarajan S. Identification of New Inhibitors for Human SIRT1: An in-silico Approach. Medicinal Chemistry 2016, 12: 347-61. PMID: 26740209, DOI: 10.2174/1573406412666160107111612.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsDynamics simulationsNew chemical librariesInhibitor compoundsChemical librariesCrystal structureStructure-based methodsUseful scaffoldsVirtual screeningChemical classesAutoDock VinaCompoundsNew inhibitorsDiphenylNew classSilico approachInhibitory activityTreatment of cancerComplex structureStructureDerivativesVinaScaffoldsAvailable drugsHuman SIRT1A Novel Phenanthridionone Based Scaffold As a Potential Inhibitor of the BRD2 Bromodomain: Crystal Structure of the Complex.
Tripathi S, Mathur S, Deshmukh P, Manjula R, Padmanabhan B. A Novel Phenanthridionone Based Scaffold As a Potential Inhibitor of the BRD2 Bromodomain: Crystal Structure of the Complex. PloS One 2016, 11: e0156344. PMID: 27243809, PMCID: PMC4886958, DOI: 10.1371/journal.pone.0156344.Peer-Reviewed Original ResearchIdentification of New Inhibitors for Human SIRT1: An in-silico Approach
Padmanabhan Balasundaram, Ramu Manjula, Mathur Shruti, Unni Sruthi and Thiyagarajan Saravanamuthu, Identification of New Inhibitors for Human SIRT1: An in-silico Approach, Medicinal Chemistry 2016; 12(4) . https://dx.doi.org/10.2174/1573406412666160107111612Peer-Reviewed Original Research