G. Izaguirre

发表

Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities

S. Olson, J. Corral, V. Vicente, 2017, The Journal of Biological Chemistry.

Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin*

S. Olson, R. Swanson, S. Raja, 2007, Journal of Biological Chemistry.

The heparin-binding site of antithrombin is crucial for antiangiogenic activity.

L. Lau, S. Olson, R. Swanson, 2005, Blood.

Alcohol Treatment of Oral Streptococcus Spp . Increased the Entry of Human Papillomavirus Type 16 into NonMalignant and Oral Squamous Cell Carcinoma Cells

D. Crowe, H. Sroussi, G. Izaguirre, 2015 .

Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin.

S. Olson, R. Swanson, G. Izaguirre, 2018, Biochemistry.

Specific and Selective Inhibitors of Proprotein Convertases Engineered by Transferring Serpin B8 Reactive-Site and Exosite Determinants of Reactivity to the Serpin α1PDX.

Marcelino Arciniega, G. Izaguirre, Andrea G. Quezada, 2019, Biochemistry.

Identification of Serpin Determinants of Specificity and Selectivity for Furin Inhibition through Studies of α1PDX (α1-Protease Inhibitor Portland)-Serpin B8 and Furin Active-site Loop Chimeras*

G. Izaguirre, S. T. Olson, L. Qi, 2013, The Journal of Biological Chemistry.

The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.

Zhiyong Zhang, B. Haimovich, E. Schaefer, 2004, Molecular biology of the cell.

Characterization of the Conformational Alterations, Reduced Anticoagulant Activity, and Enhanced Antiangiogenic Activity of Prelatent Antithrombin*

S. Olson, P. Gettins, R. Swanson, 2008, Journal of Biological Chemistry.

T HE H EPARIN B INDING S ITE OF A NTITHROMBIN I S C RUCIAL FOR A NTIANGIOGENIC A CTIVITY

L. Lau, R. Swanson, G. Izaguirre, 2005 .

Kinetic Intermediates en Route to the Final Serpin-Protease Complex

P. Gettins, R. Swanson, G. Izaguirre, 2013, The Journal of Biological Chemistry.

Residues Tyr253 and Glu255 in Strand 3 of β-Sheet C of Antithrombin Are Key Determinants of an Exosite Made Accessible by Heparin Activation to Promote Rapid Inhibition of Factors Xa and IXa*

S. Olson, G. Izaguirre, S. T. Olson, 2006, Journal of Biological Chemistry.

Localization of an Antithrombin Exosite That Promotes Rapid Inhibition of Factors Xa and IXa Dependent on Heparin Activation of the Serpin*

S. Olson, R. Swanson, G. Izaguirre, 2003, Journal of Biological Chemistry.

The Cytoskeletal/Non-muscle Isoform of α-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase*

D. Schlaepfer, B. Haimovich, Yafang Hu, 2001, The Journal of Biological Chemistry.

Engineering Functional Antithrombin Exosites in α1-Proteinase Inhibitor That Specifically Promote the Inhibition of Factor Xa and Factor IXa*

S. Olson, G. Izaguirre, A. Rezaie, 2009, Journal of Biological Chemistry.

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States*♦

S. Olson, P. Gettins, R. Swanson, 2015, The Journal of Biological Chemistry.

Conformational Activation of Antithrombin by Heparin Involves an Altered Exosite Interaction with Protease*

S. Olson, P. Gettins, R. Swanson, 2014, The Journal of Biological Chemistry.

Factor Xa : IXaAntithrombin as an Inhibitor of Factor The Allosteric Mechanism of Activation of Enzymology :

Steven, P. Gettins, R. Swanson, 2013 .

The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases

G. Izaguirre, 2019, Viruses.

Tyrosine Phosphorylation of α-Actinin in Activated Platelets*

B. Haimovich, G. Izaguirre, B. Aneskievich, 1999, The Journal of Biological Chemistry.

Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.

S. Olson, P. Gettins, G. Izaguirre, 2010, Biochimie.

Metabolism of Retinaldehyde and Other Aldehydes in Soluble Extracts of Human Liver and Kidney*

G. Izaguirre, R. Pietruszko, W. Ambroziak, 1999, The Journal of Biological Chemistry.

Inhibition of EGFR Suppresses Ethyl Alcohol and Tobacco Cell Effects on Growth of Human Oral Keratinocytes and Human Papillomavirus 16 Entry as a Function of Furin

J. Schwartz, D. Crowe, G. Izaguirre, 2015 .

Methylglyoxal as substrate and inhibitor of human aldehyde dehydrogenase: comparison of kinetic properties among the three isozymes.

G. Izaguirre, A. Kikonyogo, R. Pietruszko, 1998, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin.

S. Olson, P. Gettins, R. Swanson, 2021, Biochemistry.

Conformational Activation of Antithrombin by Heparin Involves an Altered Exosite Interaction with Protease*

S. Olson, P. Gettins, R. Swanson, 2014, The Journal of Biological Chemistry.

Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.

S. Olson, P. Gettins, G. Izaguirre, 2010, Biochimie.

The Allosteric Mechanism of Activation of Antithrombin as an Inhibitor of Factor IXa and Factor Xa

S. Olson, P. Gettins, R. Swanson, 2013, The Journal of Biological Chemistry.