Umesh R. Desai
Virginia Commonwealth University
17 Papers
109 Citations
Umesh R. Desai is an academic researcher from Virginia Commonwealth University. The author has contributed to research in topics: Thrombin & Allosteric regulation. The author has an hindex of 12, co-authored 17 publications.
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Papers
Factor XIa inhibitors: A review of the patent literature
Rami A. Al-Horani,Umesh R. Desai +1 more
TL;DR: Despite initial results in patients undergoing knee anthroplasty as with antisense oligonucleotides, major advances should be realized, particularly with respect to pharmacokinetics, for FXI/FXIa inhibitors to enter the clinic.
Designing Allosteric Inhibitors of Factor XIa. Lessons from the Interactions of Sulfated Pentagalloylglucopyranosides
Rami A. Al-Horani,Umesh R. Desai +1 more
TL;DR: The results indicate that SPGG may recognize more than one anion-binding, allosteric site onFXIa, and an SPGG molecule containing approximately 10 sulfate groups on positions 2 through 6 of the pentagalloylglucopyranosyl scaffold may be the optimal FXIa inhibitor for further preclinical studies.
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On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different.
TL;DR: Differences in the binding sites explain the major H/HS recognition characteristics of the two prototypic proteins, thus affording an explanation of the specificity of binding.
Allosterism-based simultaneous, dual anticoagulant and antiplatelet action: allosteric inhibitor targeting the glycoprotein Ibα-binding and heparin-binding site of thrombin.
Akul Y. Mehta,Bassem M. Mohammed,Bassem M. Mohammed,Erika J. Martin,Donald F. Brophy,David Gailani,Umesh R. Desai +6 more
TL;DR: This work presents a novel molecule exploiting a novel mechanism of anticoagulation, SbO4L, which exhibits dual antICOagulant and antiplatelet effects without increasing tail bleeding time.
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Crystal Structures of Influenza A Virus Matrix Protein M1: Variations on a Theme
TL;DR: It appears that M1 can energetically access different monomer and dimer conformations, as well as oligomeric states, with varying degree of similarities, while one of the monomers is fully defined and the N-terminal half of the second monomer shows considerable disorder that appears inherent in the protein and is potentially physiologically relevant.