Zobrazeno 1 - 6 of 6 pro vyhledávání: '"Anuja Khan"'
1
Analytical Performance of Modified Anti-FXa Assays for Andexanet Alfa-Containing Plasma Samples on the ACL TOP/TOP 50 Coagulation Analyzers
Autor: Genmin Lu, Pamela B. Conley, Anne M. Winkler, Vy Nguyen, Krisjela Shishko, Ryan Marett, Anuja Khan, Sam Arcidiacono, Khanh Linh Bui
Publikováno v: Blood. 136:5-5
Background: Assay parameters for anti-FXa activity assays for apixaban and rivaroxaban on the ACL TOP/TOP 50 analyzers have been modified to minimize the effect of sample dilution suitable for analyzing andexanet-containing samples with drug-specific
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::818a8c8c641c17fe1cabaff688dbdf5e
https://doi.org/10.1182/blood-2020-141006
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2
Modified Anti-FXa Assays for Measuring the Residual Activity of Apixaban and Rivaroxaban in Andexanet Alfa-Containing Samples on the ACL TOP Family® Coagulation Analyzers
Autor: Anuja Khan, Pamela B. Conley, Krisjela Shishko, Sam Arcidiacono, Khanh Linh Bui, Anne M. Winkler, Genmin Lu
Publikováno v: Blood. 134:1153-1153
Background: Andexanet alfa (AnXa) is a modified human FXa protein approved in the US and EU for reversal of direct factor Xa (FXa) inhibitors (apixaban, rivaroxaban) due to life-threatening or uncontrolled bleeding. AnXa reverses the anticoagulant ef
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5fae89d9ebb8fa03cb5d26a2afbbcfab
https://doi.org/10.1182/blood-2019-126254
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3
Characterization of Medicago truncatula (barrel medic) hydroperoxide lyase (CYP74C3), a water-soluble detergent-free cytochrome P450 monomer whose biological activity is defined by monomer–micelle association
Autor: Ruth A. Ashton, Stephen Bornemann, Shirley A. Fairhurst, Richard K. Hughes, Rod Casey, Stephen E. Harding, Mylrajan Muthusamay, Eric J. Belfield, Roger N. F. Thorneley, Arthur J. Rowe, Anuja Khan
Publikováno v: Biochemical Journal. 395:641-652
We describe the detailed biochemical characterization of CYP74C3 (cytochrome P450 subfamily 74C3), a recombinant plant cytochrome P450 enzyme with HPL (hydroperoxide lyase) activity from Medicago truncatula (barrel medic). Steady-state kinetic parame
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f31c7618de8711b1e89b1b7048cb4f6
https://doi.org/10.1042/bj20051667
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4
Long-Range Allosteric Linkage Between Exosites Reciprocally Regulates the Zymogenicity of Prothrombin Derivatives
Autor: Anuja Khan, Joseph A. Micucci, Sriram Krishnaswamy, Parvathi Kamath, Paul E. Bock
Publikováno v: Blood. 126:122-122
The binding of ligands to anion binding exosite I (ABEI) and exosite II (ABEII) on prothrombin (II) derivatives plays an integral role in regulating their function. These exosites are located on opposite faces of the proteinase domain and exhibit uni
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6deb74d02fcd48dc4487453a832acd29
https://doi.org/10.1182/blood.v126.23.122.122
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6
Conformational Activation of Zymogen-Like Thrombin Variants by Tight Binding Ligands
Autor: Sriram Krishnaswamy, Paul E. Bock, Anuja Khan, Heather K Kroh, Peter Panizzi
Publikováno v: Blood. 112:3070-3070
A series of well-established structural transitions lead to proteinase formation following zymogen cleavage in the family of serine proteinases homologous to chymotrypsin. These structural changes are triggered by the formation of a salt bridge follo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2fbbea674b8a5bb48951afa7ac5144ad
https://doi.org/10.1182/blood.v112.11.3070.3070
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