about
Crystal structure and dynamics of Spt16N-domain of FACT complex from Cicer arietinumCrystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases.Preparation, Crystallization, and Structure Determination of Chromatin Enzyme/Nucleosome ComplexesCrystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris.Crystal structure of a novel prolidase from Deinococcus radiodurans identifies new subfamily of bacterial prolidases.Mixed-Stack Charge Transfer Crystals of Pillar[5]quinone and Tetrathiafulvalene Exhibiting Ferroelectric Features.Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.Active site gate of M32 carboxypeptidases illuminated by crystal structure and molecular dynamics simulations.Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanismsStructures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidasesA conformational switch from a closed apo- to an open holo-form equips the acyl carrier protein for acyl chain accommodationCrystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic functionStructure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognitionCorrigendum: Mixed-Stack Charge Transfer Crystals of Pillar[5]quinone and Tetrathiafulvalene Exhibiting Ferroelectric FeaturesTwo-domain aminopeptidase of M1 family: Structural features for substrate binding and gating in absence of C-terminal domainStructural basis for the unusual substrate specificity of unique two-domain M1 metallopeptidaseCrystal structures of pyrrolidone-carboxylate peptidase I from Deinococcus radiodurans reveal the mechanism of L-pyroglutamate recognitionCatalytic triad heterogeneity in S51 peptidase family: Structural basis for functional variability
P50
Q27704278-07208060-95A3-41F1-915B-DB56083C958BQ39212475-DB7F647B-8A68-433F-99EC-2FB67DF63B95Q40983368-6F5750C6-1A09-4C4D-8045-3E120ABBAC2CQ42868305-70F56587-5506-4327-B239-922139497D40Q46304080-FE6B4A4F-FDEA-42E2-B0D8-6CBE83A63614Q48203411-D754D2AD-DEFC-4A2D-8436-890897364015Q51017615-23191D2B-E5E1-4EDF-8857-2C4E769D14AEQ53094926-9E2F8CAE-089F-410A-9772-108800954B4CQ58582450-681C14CB-36CC-4A0D-A6D4-FE025FBD65A5Q90403222-2595AF15-08CB-4414-8AC1-6060F1F3BEBFQ90450439-825F48C4-B110-4563-A3AF-5EC1A7F3C5AAQ90736656-8EF3045B-0CA6-4DC6-A7B4-01AD5E44E074Q91337931-9884683C-C159-496A-8927-C525A9BF2CC1Q91731801-DE0D388C-BAEB-449F-AD72-A97020187B9CQ92223814-5321DB9F-85ED-4BE7-8052-33F67AAC0E27Q92555373-473966F4-9DA7-49E6-AE2E-B583AE21163BQ92870323-0A3BE60A-35F7-4AF7-916F-BD204F9D3702Q92995874-F66AD78A-CAF5-447D-AA62-51D651722E5C
P50
description
researcher
@en
name
Ravindra D Makde
@en
type
label
Ravindra D Makde
@en
prefLabel
Ravindra D Makde
@en
P31
P496
0000-0001-7020-0065