| Year |
Citation |
Score |
| 2022 |
Soule EE, Yu H, Olson L, Naqvi I, Kumar S, Krishnaswamy S, Sullenger BA. Generation of an anticoagulant aptamer that targets factor V/Va and disrupts the FVa-membrane interaction in normal and COVID-19 patient samples. Cell Chemical Biology. PMID 35114109 DOI: 10.1016/j.chembiol.2022.01.009 |
0.331 |
|
| 2020 |
Basavaraj MG, Krishnaswamy S. Exosite binding drives substrate affinity for the activation of coagulation factor X by the intrinsic Xase complex. The Journal of Biological Chemistry. PMID 32859749 DOI: 10.1074/Jbc.Ra120.015325 |
0.549 |
|
| 2020 |
Cines DB, Zaitsev S, Rauova L, Rux AH, Stepanova V, Krishnaswamy S, Sarkar A, Kowalska MA, Zhao G, Mast AE, Blumberg LJ, McCrae KR, Poncz M, Hubbard JJ, Pyzik M, et al. FcRn augments induction of tissue factor activity by IgG-containing immune complexes. Blood. PMID 32187355 DOI: 10.1182/Blood.2019001133 |
0.329 |
|
| 2018 |
Bradford HN, Krishnaswamy S. Occlusion of anion binding exosite 2 in meizothrombin explains its impaired ability to activate factor V. The Journal of Biological Chemistry. PMID 30578302 DOI: 10.1074/Jbc.Ra118.006510 |
0.45 |
|
| 2018 |
Gunaratne R, Kumar S, Frederiksen JW, Stayrook S, Lohrmann JL, Perry K, Bompiani KM, Chabata CV, Thalji NK, Ho MD, Arepally G, Camire RM, Krishnaswamy S, Sullenger BA. Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass. Nature Biotechnology. PMID 29863725 DOI: 10.1038/Nbt.4153 |
0.396 |
|
| 2018 |
Bunce M, Chintala M, Krishnaswamy S, Bradford HN. JNJ-64179375 Inhibits Exosite I-Mediated Thrombin Activity While Preserving Exosite II and Active Site Function in Vitro Blood. 132: 24-24. DOI: 10.1182/Blood-2018-99-116291 |
0.515 |
|
| 2017 |
Kamikubo Y, Mendolicchio GL, Zampolli A, Marchese P, Rothmeier AS, Nagrampa Orje J, Gale AJ, Krishnaswamy S, Gruber A, Østergaard H, Petersen LC, Ruf W, Ruggeri ZM. Selective factor VIII activation by the tissue factor-factor VIIa-factor Xa complex. Blood. PMID 28729433 DOI: 10.1182/Blood-2017-02-767079 |
0.44 |
|
| 2016 |
Bradford HN, Krishnaswamy S. The Fragment 1 Region of Prothrombin Facilitates the Favored Binding of Fragment 12 to Zymogen and Enforces Zymogen-like Character in the Proteinase. The Journal of Biological Chemistry. PMID 27013660 DOI: 10.1074/Jbc.M116.723072 |
0.387 |
|
| 2016 |
Kumar S, Deng W, Stayrook S, Li R, Camire RM, Krishnaswamy S. Structural Basis for the Procofactor to Cofactor Transition in Human Factor V Blood. 128: 253-253. DOI: 10.1182/Blood.V128.22.253.253 |
0.405 |
|
| 2015 |
Krishnaswamy S. FVIII-VWF dos-à-dos. Blood. 126: 923-4. PMID 26294711 DOI: 10.1182/Blood-2015-06-652073 |
0.315 |
|
| 2015 |
Galkin M, Bradford H, Krishnaswamy S. Assembly of Prothrombinase on Endothelial Cells: Receptor-Mediated or Phospholipid-Driven? Blood. 126: 2267-2267. DOI: 10.1182/Blood.V126.23.2267.2267 |
0.467 |
|
| 2015 |
Greene LA, Thalji NK, Bradford H, Krishnaswamy S, Camire RM. Prothrombin Membrane Binding and Gla-Dependent Function Are Not Required for Effective Hemostasis In Vivo Blood. 126: 124-124. DOI: 10.1182/Blood.V126.23.124.124 |
0.413 |
|
| 2015 |
Micucci JA, Kamath P, Khan A, Bock PE, Krishnaswamy S. Long-Range Allosteric Linkage Between Exosites Reciprocally Regulates the Zymogenicity of Prothrombin Derivatives Blood. 126: 122-122. DOI: 10.1182/Blood.V126.23.122.122 |
0.81 |
|
| 2015 |
Kumar S, Stayrook S, Camire RM, Krishnaswamy S. The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox Blood. 126: 121-121. DOI: 10.1182/Blood.V126.23.121.121 |
0.397 |
|
| 2015 |
Goolyam Basavaraj M, Krishnaswamy S. The Affinity of Factor X for the Intrinsic Xase Is Determined By Exosite Interactions Between the Substrate and the Enzyme Complex Blood. 126: 1065-1065. DOI: 10.1182/Blood.V126.23.1065.1065 |
0.561 |
|
| 2014 |
Ivanciu L, Krishnaswamy S, Camire RM. New insights into the spatiotemporal localization of prothrombinase in vivo. Blood. 124: 1705-14. PMID 24869936 DOI: 10.1182/Blood-2014-03-565010 |
0.375 |
|
| 2014 |
Kowalska MA, Zhao G, Zhai L, David G, Marcus S, Krishnaswamy S, Poncz M. Modulation of protein C activation by histones, platelet factor 4, and heparinoids: new insights into activated protein C formation. Arteriosclerosis, Thrombosis, and Vascular Biology. 34: 120-6. PMID 24177324 DOI: 10.1161/Atvbaha.113.302236 |
0.343 |
|
| 2014 |
Kumar S, Sullenger BA, Stayrook S, Krishnaswamy S. X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase Blood. 124: 4232-4232. DOI: 10.1182/Blood.V124.21.4232.4232 |
0.541 |
|
| 2014 |
Kumar S, Stayrook S, Huntington JA, Camire RM, Krishnaswamy S. New Structural Insights into High Affinity Membrane Binding By Coagulation Factor V/Va Blood. 124: 4216-4216. DOI: 10.1182/Blood.V124.21.4216.4216 |
0.426 |
|
| 2014 |
Kamikubo Y, Mendolicchio GL, Zampolli A, Marchese P, Gale AJ, Krishnaswamy S, Gruber A, Petersen LC, Ruf W, Ruggeri ZM. Distinct Mechanism of Anti-Hemophilic FVIII Activation By Nascent FXa in the Tissue Factor-FVIIa Coagulation Initiation Complex Resistant to FXa-Directed Inhibition Blood. 124: 2803-2803. DOI: 10.1182/Blood.V124.21.2803.2803 |
0.41 |
|
| 2013 |
Bunce MW, Bos MH, Krishnaswamy S, Camire RM. Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptides. The Journal of Biological Chemistry. 288: 30151-60. PMID 24014022 DOI: 10.1074/Jbc.M113.506840 |
0.361 |
|
| 2013 |
Bradford HN, Orcutt SJ, Krishnaswamy S. Membrane binding by prothrombin mediates its constrained presentation to prothrombinase for cleavage. The Journal of Biological Chemistry. 288: 27789-800. PMID 23940050 DOI: 10.1074/Jbc.M113.502005 |
0.475 |
|
| 2013 |
Lechtenberg BC, Murray-Rust TA, Johnson DJ, Adams TE, Krishnaswamy S, Camire RM, Huntington JA. Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis. Blood. 122: 2777-83. PMID 23869089 DOI: 10.1182/Blood-2013-06-511733 |
0.423 |
|
| 2013 |
Krishnaswamy S. The transition of prothrombin to thrombin. Journal of Thrombosis and Haemostasis : Jth. 11: 265-76. PMID 23809130 DOI: 10.1111/Jth.12217 |
0.443 |
|
| 2013 |
Vadivel K, Agah S, Messer AS, Cascio D, Bajaj MS, Krishnaswamy S, Esmon CT, Padmanabhan K, Bajaj SP. Structural and functional studies of γ-carboxyglutamic acid domains of factor VIIa and activated Protein C: role of magnesium at physiological calcium. Journal of Molecular Biology. 425: 1961-81. PMID 23454357 DOI: 10.1016/J.Jmb.2013.02.017 |
0.325 |
|
| 2012 |
Bradford HN, Krishnaswamy S. Meizothrombin is an unexpectedly zymogen-like variant of thrombin. The Journal of Biological Chemistry. 287: 30414-25. PMID 22815477 DOI: 10.1074/Jbc.M112.394809 |
0.479 |
|
| 2012 |
Homsher M, Zekas E, Krishnaswamy S. Conformational Dynamics of Prothrombin Dictate Its Ordered Cleavage by Prothrombinase Blood. 120: 3359-3359. DOI: 10.1182/Blood.V120.21.3359.3359 |
0.42 |
|
| 2011 |
Kowalska MA, Krishnaswamy S, Rauova L, Zhai L, Hayes V, Amirikian K, Esko JD, Bougie DW, Aster RH, Cines DB, Poncz M. Antibodies associated with heparin-induced thrombocytopenia (HIT) inhibit activated protein C generation: new insights into the prothrombotic nature of HIT. Blood. 118: 2882-8. PMID 21772054 DOI: 10.1182/Blood-2011-02-335208 |
0.367 |
|
| 2011 |
Kroh HK, Panizzi P, Tchaikovski S, Baird TR, Wei N, Krishnaswamy S, Tans G, Rosing J, Furie B, Furie BC, Bock PE. Active site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo. The Journal of Biological Chemistry. 286: 23345-56. PMID 21531712 DOI: 10.1074/Jbc.M111.230292 |
0.452 |
|
| 2011 |
Bradford H, Krishnaswamy S. Meizothrombin: Zymogen or Proteinase? Slow, Ligand-Dependent Equilibration Between Equally Populated Zymogen-Like and Proteinase-Like Forms Explains Its Selectively Anticoagulant Function Blood. 118: 533-533. DOI: 10.1182/Blood.V118.21.533.533 |
0.513 |
|
| 2011 |
Kumar S, Stayrook S, Huntington JA, Camire RM, Krishnaswamy S. High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation Blood. 118: 375-375. DOI: 10.1182/Blood.V118.21.375.375 |
0.41 |
|
| 2010 |
Kamath P, Huntington JA, Krishnaswamy S. Ligand binding shuttles thrombin along a continuum of zymogen- and proteinase-like states. The Journal of Biological Chemistry. 285: 28651-8. PMID 20639195 DOI: 10.1074/Jbc.M110.154914 |
0.814 |
|
| 2010 |
Buddai SK, Layzer JM, Lu G, Rusconi CP, Sullenger BA, Monroe DM, Krishnaswamy S. An anticoagulant RNA aptamer that inhibits proteinase-cofactor interactions within prothrombinase. The Journal of Biological Chemistry. 285: 5212-23. PMID 20022942 DOI: 10.1074/Jbc.M109.049833 |
0.785 |
|
| 2010 |
Bradford HN, Micucci JA, Krishnaswamy S. Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate. The Journal of Biological Chemistry. 285: 328-38. PMID 19858193 DOI: 10.1074/Jbc.M109.070334 |
0.459 |
|
| 2010 |
Ivanciu L, Camire RM, Krishnaswamy S. Imaging of Coagulation Reactions During Thrombus Formation In Vivo with Novel Fluorescent Protein Derivatives Blood. 116: 817-817. DOI: 10.1182/Blood.V116.21.817.817 |
0.358 |
|
| 2010 |
Kowalska MA, Rauova L, Hayes V, Cines DB, Bougie DW, Aster RH, Krishnaswamy S, Poncz M. Heparin-Induced Thrombocytopenia Antibodies Inhibit PF4-Dependent Enhancement of Activated Protein C Formation by Binding to Antigenic Complexes Formed with the Chondroitin Sulfate Side-Chain of Thrombomodulin Blood. 116: 721-721. DOI: 10.1182/Blood.V116.21.721.721 |
0.38 |
|
| 2010 |
Bradford H, Krishnaswamy S. Meizothrombin Is Unexpectedly Zymogen-Like: Its Slow Conversion to Proteinase Dominates Thrombin Production by Prothrombinase Blood. 116: 2215-2215. DOI: 10.1182/Blood.V116.21.2215.2215 |
0.471 |
|
| 2009 |
Kamath P, Krishnaswamy S. Driving Thrombin From a Protease-Like State to a Zymogen-Like State and Back. Blood. 114: 852-852. DOI: 10.1182/Blood.V114.22.852.852 |
0.809 |
|
| 2008 |
Kamath P, Krishnaswamy S. Fate of membrane-bound reactants and products during the activation of human prothrombin by prothrombinase. The Journal of Biological Chemistry. 283: 30164-73. PMID 18765660 DOI: 10.1074/Jbc.M806158200 |
0.801 |
|
| 2008 |
Cao W, Krishnaswamy S, Camire RM, Lenting PJ, Zheng XL. Factor VIII accelerates proteolytic cleavage of von Willebrand factor by ADAMTS13. Proceedings of the National Academy of Sciences of the United States of America. 105: 7416-21. PMID 18492805 DOI: 10.1073/Pnas.0801735105 |
0.401 |
|
| 2008 |
Khan A, Panizzi P, Kroh HK, Bock PE, Krishnaswamy S. Conformational Activation of Zymogen-Like Thrombin Variants by Tight Binding Ligands Blood. 112: 3070-3070. DOI: 10.1182/Blood.V112.11.3070.3070 |
0.475 |
|
| 2008 |
Bradford HN, Micucci JA, Krishnaswamy S. Effects of Substrate Geometry on Active Site Engagement Govern the Preferential Action of Prothrombinase on One of the Two Cleavage Sites in Prothrombin. Blood. 112: 2022-2022. DOI: 10.1182/Blood.V112.11.2022.2022 |
0.343 |
|
| 2008 |
Zekas E, Krishnaswamy S. Fluorescence Resonance Energy Transfer Studies of Prothrombin Recognition by Prothrombinase. Blood. 112: 2014-2014. DOI: 10.1182/Blood.V112.11.2014.2014 |
0.419 |
|
| 2008 |
Kowalska MA, Amirikian K, Mosnier LO, Weiler H, Krishnaswamy S, Poncz M. Structural and Functional Studies to Define the Molecular Basis by Which Platelet Factor 4 (PF4) Increases Survival of Mice in Lipopolysaccharide (LPS)-Induced Endotoxicity Blood. 112: 19-19. DOI: 10.1182/Blood.V112.11.19.19 |
0.313 |
|
| 2007 |
Hacisalihoglu A, Panizzi P, Bock PE, Camire RM, Krishnaswamy S. Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase. The Journal of Biological Chemistry. 282: 32974-82. PMID 17848548 DOI: 10.1074/Jbc.M706529200 |
0.454 |
|
| 2007 |
Cao W, Krishnaswamy S, Lenting P, Zheng XL. Factor VIII, a Cofactor for Accelerating Proteolytic Cleavage of von Willebrand Factor by ADAMTS13 Metalloprotease. Blood. 110: 766-766. DOI: 10.1182/Blood.V110.11.766.766 |
0.468 |
|
| 2007 |
Kamath P, Krishnaswamy S. Fate of Membrane-Bound Reactants and Products during Prothrombin Activation by Prothrombinase. Blood. 110: 2692-2692. DOI: 10.1182/Blood.V110.11.2692.2692 |
0.789 |
|
| 2007 |
Bradford HN, Shang D, Zheng XL, Krishnaswamy S. Human Platelets and Endothelial Cells Differentially Regulate the Pathway for Prothrombin Cleavage by Prothrombinase. Blood. 110: 269-269. DOI: 10.1182/Blood.V110.11.269.269 |
0.42 |
|
| 2006 |
Hacisalihoglu A, Krishnaswamy S. Ordered Cleavage of Prothrombin by Prothrombinase Results from Constrained Binding and Preferential Active Site Engagement by One of the Two Cleavage Sites in Prothrombin. Blood. 108: 335-335. DOI: 10.1182/Blood.V108.11.335.335 |
0.509 |
|
| 2005 |
Bianchini EP, Orcutt SJ, Panizzi P, Bock PE, Krishnaswamy S. Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase. Proceedings of the National Academy of Sciences of the United States of America. 102: 10099-104. PMID 16006504 DOI: 10.1073/Pnas.0504704102 |
0.421 |
|
| 2005 |
Schmidt AE, Stewart JE, Mathur A, Krishnaswamy S, Bajaj SP. Na+ site in blood coagulation factor IXa: effect on catalysis and factor VIIIa binding. Journal of Molecular Biology. 350: 78-91. PMID 15913649 DOI: 10.1016/J.Jmb.2005.04.052 |
0.418 |
|
| 2005 |
Lu G, Chhum S, Krishnaswamy S. The affinity of protein C for the thrombin.thrombomodulin complex is determined in a primary way by active site-dependent interactions. The Journal of Biological Chemistry. 280: 15471-8. PMID 15705565 DOI: 10.1074/Jbc.M500881200 |
0.492 |
|
| 2005 |
Krishnaswamy S. Exosite-driven substrate specificity and function in coagulation Journal of Thrombosis and Haemostasis. 3: 54-67. PMID 15634266 DOI: 10.1111/J.1538-7836.2004.01021.X |
0.394 |
|
| 2004 |
Orcutt SJ, Krishnaswamy S. Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin. The Journal of Biological Chemistry. 279: 54927-36. PMID 15494418 DOI: 10.1074/Jbc.M410866200 |
0.406 |
|
| 2004 |
Boskovic DS, Troxler T, Krishnaswamy S. Active site-independent recognition of substrates and product by bovine prothrombinase: a fluorescence resonance energy transfer study. The Journal of Biological Chemistry. 279: 20786-93. PMID 14988397 DOI: 10.1074/Jbc.M400469200 |
0.776 |
|
| 2004 |
Lu G, Broze GJ, Krishnaswamy S. Formation of factors IXa and Xa by the extrinsic pathway: differential regulation by tissue factor pathway inhibitor and antithrombin III. The Journal of Biological Chemistry. 279: 17241-9. PMID 14963035 DOI: 10.1074/Jbc.M312827200 |
0.453 |
|
| 2004 |
Bianchini E, Orcutt SJ, Krishnaswamy S. Ratcheting between Two Distinct Conformations of Substrate Drives the Sequential Cleavage of Prothrombin by Prothrombinase. Blood. 104: 1717-1717. DOI: 10.1182/Blood.V104.11.1717.1717 |
0.353 |
|
| 2004 |
Orcutt SJ, Krishnaswamy S. The Substrate -Membrane Interaction Constrains Bond Presentation and Cleavage in the Action of Prothrombinase on Prothrombin. Blood. 104: 1712-1712. DOI: 10.1182/Blood.V104.11.1712.1712 |
0.484 |
|
| 2004 |
Lu G, Chhum S, Krishnaswamy S. Active Site-Dependent Substrate Recognition Plays a Primary Role in Determining the Affinity of the Thrombin-Thrombomodulin Complex for Protein C. Blood. 104: 125-125. DOI: 10.1182/Blood.V104.11.125.125 |
0.445 |
|
| 2002 |
Venkateswarlu D, Krishnaswamy S, Darden TA, Pedersen LG. Three-dimensional solution structure of Tropidechis carinatus venom extract trocarin: a structural homologue of Xa and prothrombin activator. Journal of Molecular Modeling. 8: 302-13. PMID 12483230 DOI: 10.1007/S00894-002-0099-4 |
0.359 |
|
| 2002 |
Orcutt SJ, Pietropaolo C, Krishnaswamy S. Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate. The Journal of Biological Chemistry. 277: 46191-6. PMID 12370181 DOI: 10.1074/Jbc.M208677200 |
0.461 |
|
| 2002 |
Buddai SK, Toulokhonova L, Bergum PW, Vlasuk GP, Krishnaswamy S. Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase. The Journal of Biological Chemistry. 277: 26689-98. PMID 12011050 DOI: 10.1074/Jbc.M202507200 |
0.802 |
|
| 2002 |
Wilkens M, Krishnaswamy S. The contribution of factor Xa to exosite-dependent substrate recognition by prothrombinase. The Journal of Biological Chemistry. 277: 9366-74. PMID 11782479 DOI: 10.1074/Jbc.M110848200 |
0.702 |
|
| 2000 |
Boskovic DS, Krishnaswamy S. Exosite binding tethers the macromolecular substrate to the prothrombinase complex and directs cleavage at two spatially distinct sites. The Journal of Biological Chemistry. 275: 38561-70. PMID 10984491 DOI: 10.1074/Jbc.M006637200 |
0.78 |
|
| 2000 |
Baugh RJ, Dickinson CD, Ruf W, Krishnaswamy S. Exosite interactions determine the affinity of factor X for the extrinsic Xase complex. The Journal of Biological Chemistry. 275: 28826-33. PMID 10889208 DOI: 10.1074/Jbc.M005266200 |
0.84 |
|
| 1998 |
Betz A, Krishnaswamy S. Regions remote from the site of cleavage determine macromolecular substrate recognition by the prothrombinase complex Journal of Biological Chemistry. 273: 10709-10718. PMID 9553135 DOI: 10.1074/Jbc.273.17.10709 |
0.729 |
|
| 1998 |
Baugh RJ, Broze GJ, Krishnaswamy S. Regulation of extrinsic pathway factor Xa formation by tissue factor pathway inhibitor. The Journal of Biological Chemistry. 273: 4378-86. PMID 9468488 DOI: 10.1074/Jbc.273.8.4378 |
0.802 |
|
| 1998 |
Baugh RJ, Pickinson C, Ruf W, Krishnaswamy S. The affinity of factor X for VIIaTF is determined by interactions at exoshes Faseb Journal. 12: A1414. |
0.793 |
|
| 1997 |
Krishnaswamy S, Betz A. Exosites determine macromolecular substrate recognition by prothrombinase Biochemistry. 36: 12080-12086. PMID 9315846 DOI: 10.1021/Bi970979+ |
0.786 |
|
| 1997 |
Krishnaswamy S, Walker RK. Contribution of the prothrombin fragment 2 domain to the function of factor Va in the prothrombinase complex. Biochemistry. 36: 3319-30. PMID 9116010 DOI: 10.1021/Bi9623993 |
0.755 |
|
| 1997 |
Betz A, Vlasuk GP, Bergum PW, Krishnaswamy S. Selective inhibition of the prothrombinase complex: Factor Va alters macromolecular recognition of a tick anticoagulant peptide mutant by factor Xa Biochemistry. 36: 181-191. PMID 8993332 DOI: 10.1021/Bi962060G |
0.735 |
|
| 1996 |
Cutsforth GA, Koppaka V, Krishnaswamy S, Wu JR, Mann KG, Lentz BR. Insights into the complex association of bovine factor Va with acidic-lipid-containing synthetic membranes. Biophysical Journal. 70: 2938-49. PMID 8744332 DOI: 10.1016/S0006-3495(96)79864-8 |
0.583 |
|
| 1996 |
Baugh RJ, Krishnaswamy S. Role of the activation peptide domain in human factor X activation by the extrinsic Xase complex. The Journal of Biological Chemistry. 271: 16126-34. PMID 8663201 DOI: 10.1074/Jbc.271.27.16126 |
0.805 |
|
| 1994 |
Krishnaswamy S, Vlasuk GP, Bergum PW. Assembly of the prothrombinase complex enhances the inhibition of bovine factor Xa by tick anticoagulant peptide Biochemistry. 33: 7897-7907. PMID 8011652 DOI: 10.1021/Bi00191A017 |
0.546 |
|
| 1994 |
Walker RK, Krishnaswamy S. The activation of prothrombin by the prothrombinase complex. The contribution of the substrate-membrane interaction to catalysis. The Journal of Biological Chemistry. 269: 27441-50. PMID 7961657 |
0.724 |
|
| 1994 |
Barrow RT, Parker ET, Krishnaswamy S, Lollar P. Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator Journal of Biological Chemistry. 269: 26796-26800. PMID 7929416 |
0.311 |
|
| 1993 |
Krishnaswamy S, Nesheim ME, Pryzdial EL, Mann KG. Assembly of prothrombinase complex. Methods in Enzymology. 222: 260-80. PMID 8412798 DOI: 10.1016/0076-6879(93)22018-B |
0.505 |
|
| 1993 |
Kalafatis M, Krishnaswamy S, Rand MD, Mann KG. Factor V. Methods in Enzymology. 222: 224-36. PMID 8412796 DOI: 10.1016/0076-6879(93)22016-9 |
0.633 |
|
| 1993 |
Lawson JH, Krishnaswamy S, Butenas S, Mann KG. Extrinsic pathway proteolytic activity. Methods in Enzymology. 222: 177-95. PMID 8412793 DOI: 10.1016/0076-6879(93)22013-6 |
0.616 |
|
| 1993 |
Walker RK, Krishnaswamy S. The influence of factor Va on the active site of factor Xa. The Journal of Biological Chemistry. 268: 13920-9. PMID 8314758 |
0.755 |
|
| 1992 |
Mann KG, Krishnaswamy S, Lawson JH. Surface-dependent hemostasis. Seminars in Hematology. 29: 213-26. PMID 1641667 |
0.363 |
|
| 1992 |
Krishnaswamy S, Field KA, Edgington TS, Morrissey JH, Mann KG. Role of the membrane surface in the activation of human coagulation factor X. The Journal of Biological Chemistry. 267: 26110-20. PMID 1464622 |
0.79 |
|
| 1992 |
Krishnaswamy S. The interaction of human factor VIIa with tissue factor Journal of Biological Chemistry. 267: 23696-23706. PMID 1429710 |
0.421 |
|
| 1991 |
Mann KG, Bovill EG, Krishnaswamy S. Surface-dependent reactions in the propagation phase of blood coagulation. Annals of the New York Academy of Sciences. 614: 63-75. PMID 2024894 DOI: 10.1111/J.1749-6632.1991.Tb43692.X |
0.458 |
|
| 1990 |
Mosesson MW, Church WR, DiOrio JP, Krishnaswamy S, Mann KG, Hainfeld JF, Wall JS. Structural model of factors V and Va based on scanning transmission electron microscope images and mass analysis. The Journal of Biological Chemistry. 265: 8863-8. PMID 2341407 |
0.412 |
|
| 1990 |
Krishnaswamy S. Prothrombinase complex assembly: Contributions of protein-protein and protein-membrane interactions toward complex formation Journal of Biological Chemistry. 265: 3708-3718. PMID 2303476 |
0.337 |
|
| 1990 |
Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood. 76: 1-16. PMID 2194585 DOI: 10.1182/Blood.V76.1.1.1 |
0.638 |
|
| 1990 |
Mann KG, Williams EB, Krishnaswamy S, Church W, Giles A, Tracy RP. Active site-specific immunoassays. Blood. 76: 755-66. PMID 2116928 DOI: 10.1182/Blood.V76.4.755.Bloodjournal764755 |
0.624 |
|
| 1989 |
Krishnaswamy S, Russell GD, Mann KG. The reassociation of factor Va from its isolated subunits. The Journal of Biological Chemistry. 264: 3160-8. PMID 2914947 |
0.744 |
|
| 1989 |
Gendreau MA, Krishnaswamy S, Mann KG. The interaction of bone Gla protein (osteocalcin) with phospholipid vesicles. The Journal of Biological Chemistry. 264: 6972-8. PMID 2785110 |
0.557 |
|
| 1989 |
Williams EB, Krishnaswamy S, Mann KG. Zymogen/enzyme discrimination using peptide chloromethyl ketones. The Journal of Biological Chemistry. 264: 7536-45. PMID 2708377 |
0.575 |
|
| 1988 |
Krishnaswamy S, Jones KC, Mann KG. Prothrombinase complex assembly. Kinetic mechanism of enzyme assembly on phospholipid vesicles. The Journal of Biological Chemistry. 263: 3823-34. PMID 3346225 |
0.512 |
|
| 1988 |
Krishnaswamy S, Mann KG. The binding of factor Va to phospholipid vesicles. The Journal of Biological Chemistry. 263: 5714-23. PMID 3162734 |
0.578 |
|
| 1988 |
Mann KG, Jenny RJ, Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annual Review of Biochemistry. 57: 915-56. PMID 3052293 DOI: 10.1146/Annurev.Bi.57.070188.004411 |
0.514 |
|
| 1987 |
Krishnaswamy S, Church WR, Nesheim ME, Mann KG. Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism. The Journal of Biological Chemistry. 262: 3291-9. PMID 3818642 |
0.503 |
|
| 1987 |
Lecompte MF, Krishnaswamy S, Mann KG, Nesheim ME, Gitler C. Membrane penetration of bovine factor V and Va detected by labeling with 5-iodonaphthalene-1-azide. The Journal of Biological Chemistry. 262: 1935-7. PMID 3818583 |
0.528 |
|
| 1986 |
Krishnaswamy S, Williams EB, Mann KG. The binding of activated protein C to factors V and Va. The Journal of Biological Chemistry. 261: 9684-93. PMID 3755431 |
0.587 |
|
| 1986 |
Krishnaswamy S, Mann KG, Nesheim ME. The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction. The Journal of Biological Chemistry. 261: 8977-84. PMID 3755135 |
0.516 |
|
| 1986 |
Krishnaswamy S, Bryan JK. Use of monoclonal antibodies for the purification and characterization of the threonine-sensitive isozyme of maize homoserine dehydrogenase. Archives of Biochemistry and Biophysics. 246: 250-62. PMID 3083775 DOI: 10.1016/0003-9861(86)90471-6 |
0.691 |
|
| 1983 |
Krishnaswamy S, Bryan JK. Ligand-induced interconversions of maize homoserine dehydrogenase among different states. Archives of Biochemistry and Biophysics. 222: 449-63. PMID 6405698 DOI: 10.1016/0003-9861(83)90544-1 |
0.689 |
|
| 1983 |
Krishnaswamy S, Bryan JK. Characterization of ligand-induced states of maize homoserine dehydrogenase. Archives of Biochemistry and Biophysics. 227: 210-24. PMID 6357097 DOI: 10.1016/0003-9861(83)90364-8 |
0.68 |
|
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