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Biochemistry|May 7, 2008
Factor Va alters the conformation of the Na+-binding loop of factor Xa in the prothrombinase complexLikui Yang, Chandrashekhara Manithody, Shabir H Qureshi, et al.
The Journal of Biological Chemistry|July 15, 2010
Role of the residues of the 39-loop in determining the substrate and inhibitor specificity of factor IXaLikui Yang, Chandrashekhara Manithody, Shabir H Qureshi, et al.
Blood|September 8, 2007
The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cellsJong-Sup Bae, Likui Yang, Chandrashekhara Manithody, et al.
Biochemistry|April 22, 2009
Membrane-dependent interaction of factor Xa and prothrombin with factor Va in the prothrombinase complexShabir H Qureshi, Likui Yang, Chandrashekhara Manithody, et al.
The Journal of Biological Chemistry|July 15, 2004
The cofactor function of the N-terminal domain of tissue factorFarooqahmed S Kittur, Chandrashekhara Manithody, James H Morrissey, et al.
Biochemistry|May 30, 2015
Expression and Characterization of Gly-317 Variants of Factor IX Causing Variable Bleeding in Hemophilia B PatientsQiuya Lu, Likui Yang, Chandrashekhara Manithody, et al.
Thrombosis Research|September 3, 2014
Molecular basis of the clotting defect in a bleeding patient missing the Asp-185 codon in the factor X geneQiuya Lu, Likui Yang, Chandrashekhara Manithody, et al.
Biochimica Et Biophysica Acta|June 25, 2014
Characterization of the protein Z-dependent protease inhibitor interactive-sites of protein ZShabir H Qureshi, Qiuya Lu, Chandrashekhara Manithody, et al.
Biochemistry|July 31, 2009
Mutagenesis studies toward understanding allostery in thrombinShabir H Qureshi, Likui Yang, Chandrashekhara Manithody, et al.
Biochemistry|March 14, 2013
Variable contributions of basic residues forming an APC exosite in the binding and inactivation of factor VIIIaMasahiro Takeyama, Jennifer M Wintermute, Chandrashekhara Manithody, et al.
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