about
Structural, kinetic and chemical mechanism of isocitrate dehydrogenase-1 from Mycobacterium tuberculosisThe sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analoguesPost-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and releaseStructural basis for activation of the therapeutic L-nucleoside analogs 3TC and troxacitabine by human deoxycytidine kinaseNXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosisStructure of MurNAc 6-Phosphate Hydrolase (MurQ) from Haemophilus influenzae with a Bound InhibitorTebipenem, a New Carbapenem Antibiotic, Is a Slow Substrate That Inhibits the β-Lactamase from Mycobacterium tuberculosisAngiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular SystemInhibiting the β-Lactamase ofMycobacterium tuberculosis(Mtb) with Novel Boronic Acid Transition-State Inhibitors (BATSIs)Understanding the role of structural integrity and differential expression of integrin profiling to identify potential therapeutic targets in breast cancer.Cadherin profiling for therapeutic interventions in Epithelial Mesenchymal Transition (EMT) and tumorigenesis.Novel mutation in exon 14 of the sarcomere gene MYH7 in familial left ventricular noncompaction with bicuspid aortic valveIdentification of differentially expressed microRNAs in Sahiwal (Bos indicus) breed of cattle during thermal stressUnderstanding structure-based dynamic interactions of antihypertensive peptides extracted from food sourcesInsights into the role of d-amino acid oxidase mutations in amyotrophic lateral sclerosisU32 collagenase from Pseudoalteromonas agarivorans NW4327: Activity, structure, substrate interactions and molecular dynamics simulations
P50
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P50
description
researcher ORCID ID = 0000-0002-3074-1534
@en
name
Saugata Hazra
@ast
Saugata Hazra
@en
Saugata Hazra
@es
Saugata Hazra
@nl
type
label
Saugata Hazra
@ast
Saugata Hazra
@en
Saugata Hazra
@es
Saugata Hazra
@nl
prefLabel
Saugata Hazra
@ast
Saugata Hazra
@en
Saugata Hazra
@es
Saugata Hazra
@nl
P1153
15837197000
P31
P496
0000-0002-3074-1534