Dipali Sinha

Temple University — United States

Medicine · Health Sciences

13h-index422citations25works0.02yr avg
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Research Topics

Coagulation, Bradykinin, Polyphosphates, and Angioedema(17), Blood Coagulation and Thrombosis Mechanisms(10), Protease and Inhibitor Mechanisms(6), Mast cells and histamine(5), Vitamin K Research Studies(4)

Publications25 total

Productive Recognition of Factor IX by Factor XIa Exosites Requires Disulfide Linkage between Heavy and Light Chains of Factor XIa
Journal of Biological Chemistry·2011· 6 citedOpen Access
The Role of Factor XIa (FXIa) Catalytic Domain Exosite Residues in Substrate Catalysis and Inhibition by the Kunitz Protease Inhibitor Domain of Protease Nexin 2
Journal of Biological Chemistry·2011· 7 citedOpen Access
Localization of Ligand-Binding Exosites In the Catalytic Domain of Factor XIa.
Blood·2010
Structural and Mutational Analysis of Canonical Loop Residues In Protease Nexin 2 Involved In Factor XIa and Trypsin Inhibition.
Blood·2010
Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with Mesotrypsin
Journal of Biological Chemistry·2010· 47 citedOpen Access
Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor
The Journal of Biochemistry·2010· 24 citedOpen Access
The Amyloid Precursor Protein/Protease Nexin 2 Kunitz Inhibitor Domain Is a Highly Specific Substrate of Mesotrypsin
Journal of Biological Chemistry·2009· 42 citedOpen Access
The Role of the P1 Residue of Protease Nexin 2 and Basic Pancreatic Trypsin Inhibitor in the Mechanism of Factor XIa Inhibition.
Blood·2008
Factor XI Homodimer Structure Is Essential for Normal Proteolytic Activation by Factor XIIa, Thrombin, and Factor XIa
Journal of Biological Chemistry·2008· 47 citedOpen Access
A Catalytic Domain Exosite (Cys<sup>527</sup>−Cys<sup>542</sup>) in Factor XIa Mediates Binding to a Site on Activated Platelets
Biochemistry·2007· 17 citedOpen Access
Factor XI Homodimer Formation Is Mediated by Electrostatic (Lys331 with Glu287) and Hydrophobic (Ile290 with Leu284 and Tyr329 with Tyr329) Interactions in the Apple 4 Domain and Is Essential for Normal Proteolytic Activation of Factor XI by Factor XIIa, Thrombin and Factor XIa.
Blood·2007
Macromolecular Substrate-Binding Exosites on Both the Heavy and Light Chains of Factor XIa Mediate the Formation of the Michaelis Complex Required for Factor IX-Activation
Biochemistry·2007· 12 cited
Factor IX Substrate Binding Exosite on the Light Chain of Factor Xia.
Blood·2005· 1 cited
Factor XIa Dimer in the Activation of Factor IX
Biochemistry·2005· 14 cited
Allosteric Modification of Factor XIa Functional Activity upon Binding to Polyanions
Biochemistry·2004· 14 cited
Molecular cloning and biochemical characterization of rabbit factor XI
Biochemical Journal·2002· 17 citedOpen Access
15-deoxy-Δ12,14 prostaglandin J2: A putative endogenous promoter of adipogenesis suppresses the ob gene
Metabolism·1999· 44 cited
Engineering DNA and Protein Chimeras Utilizing Coding Sequences of Restriction Sites
Analytical Biochemistry·1996· 3 cited
Primary Binding Domain of Bovine von Willebrand Factor Fragment Expressed in E. coli
Thrombosis and Haemostasis·1996
Ligand binding assays with recombinant proteins refolded on an affinity matrix.
PubMed·1994· 24 cited
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Frequent Co-authors

Peter N. Walsh(17), Duraiswamy Navaneetham(8), Mariola M. Marcinkiewicz(6), Meenakshi R. Bakhshi(5), Edward P. Kirby(5), James D. Lear(3), Renu K. Vora(3), Moh’d A. Salameh(2), Evette S. Radisky(2), Wenman Wu(2), Paul C. Billings(2), Tara N. Miller(2), Ya-Chi Su(2), Xiaoxin Yang(2), Andrei Z. Budzynski(2), F S Seaman(1), Alexei S. Soares(1), Sergei Shikov(1), Calvin K. Yip(1), Thomas Walz(1)