Abdul Basit
8 Papers
Abdul Basit is an academic researcher. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 1, co-authored 7 publications.
Chat about Author
Papers
Quantitative Characterization of Clinically Relevant Drug-Metabolizing Enzymes and Transporters in Rat Liver and Intestinal Segments for Applications in PBPK Modeling.
Sheena Sharma,Dilip K. Singh,Vijaya Saradhi Mettu,Guihua Yue,Deepak Ahire,Abdul Basit,Scott Heyward,Bhagwat Prasad +7 more
TL;DR: In this paper , the levels of DMET proteins in rats were quantified using the global proteomics-based total protein approach (TPA) and targeted proteomics, and the abundance of the major DMET protein was largely comparable using quantitative global and localized proteomics.
6
Dimethandrolone, a Potential Male Contraceptive Pill, is Primarily Metabolized by the Highly Polymorphic UDP-Glucuronosyltransferase 2B17 Enzyme in Human Intestine and Liver
Sheena Sharma,Deepak Ahire,Abdul Basit,Maria Lajoie,Christina Wang,Min S Lee,Diana L. Blithe,John K. Amory,Dilip K. Singh,Scott Heyward,Bhagwat Prasad +10 more
TL;DR: This study found that UGT2B17-mediated high intestinal first-pass metabolism is the key mechanism of variable DMA bioavailability and could be used as a clinical probe of UGT 2B17 activity.
4
Characterization of Gla proteoforms and non-Gla peptides of gamma carboxylated proteins: Application to quantification of prothrombin proteoforms in human plasma
Dilip Kumar Singh,Abdul Basit,Allan E. Rettie,Nathan Alade,Kenneth Thummel,Bhagwat Prasad +5 more
TL;DR: An alkaline mobile phase in combination with polarity switching to simultaneously identify and quantify γ-carboxylated VKDPs was applied to compare Gla proteomics of prothrombin (FII) in 10 μL plasma samples of healthy control and warfarin-treated adults.
1
Multi-functional regulation of cGAS by the nuclear localization signal2 (NLS2) motif: Nuclear localization, enzyme activity and protein degradation.
TL;DR: In this article , the role of NLS2 motifs in cyclic GMP-AMP synthase (cGAS) was investigated by mutating known NLS motifs and assessing its functionality by monitoring the downstream target, interferon regulatory factor-3 (IRF3).
1