P. Gettins

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Serpin structure, mechanism, and function.

P. Gettins, 2002, Chemical reviews.

Specificity of Binding of the Low Density Lipoprotein Receptor-related Protein to Different Conformational States of the Clade E Serpins Plasminogen Activator Inhibitor-1 and Proteinase Nexin-1*

P. Gettins, J. Jensen, K. Dolmer, 2009, The Journal of Biological Chemistry.

The F‐helix of serpins plays an essential, active role in the proteinase inhibition mechanism

P. Gettins, 2002, FEBS letters.

Properties of thrombin- and elastase-modified human antithrombin III.

P. Gettins, B. Harten, 1988, Biochemistry.

Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding.

J. Huntington, S. Olson, P. Gettins, 1996, Biochemistry.

Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways.

J. Huntington, P. Gettins, D. B. Hood, 1994, Biochemistry.

The role of conformational change in serpin structure and function

P. Gettins, P. Patston, M. Schapira, 1993, BioEssays : news and reviews in molecular, cellular and developmental biology.

Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa.

P. Gettins, A. Futamura, A. Futamura, 2000, The Journal of biological chemistry.

Mapping the Serpin-Proteinase Complex Using Single Cysteine Variants of α1-Proteinase Inhibitor Pittsburgh*

P. Gettins, E. Stratikos, 1998, The Journal of Biological Chemistry.

A Database of Recombinant Wild-type and Mutant Serpins

P. Gettins, P. Patston, P. Patston, 1994, Thrombosis and Haemostasis.

Active Site Distortion Is Sufficient for Proteinase Inhibition by Serpins

J. Dobó, P. Gettins, A. Dementiev, 2006, Journal of Biological Chemistry.

α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition*

J. Dobó, P. Gettins, 2004, Journal of Biological Chemistry.

The ternary complex of antithrombin–anhydrothrombin–heparin reveals the basis of inhibitor specificity

J. Herbert, P. Gettins, M. Petitou, 2004, Nature Structural &Molecular Biology.

Characterization of the calcium site in two complement-like domains from the low-density lipoprotein receptor-related protein (LRP) and comparison with a repeat from the low-density lipoprotein receptor.

W. Huang, P. Gettins, K. Dolmer, 1998, Biochemistry.

NMR Solution Structure of Complement-like Repeat CR3 from the Low Density Lipoprotein Receptor-related Protein

W. Huang, P. Gettins, K. Dolmer, 2000, The Journal of Biological Chemistry.

Role of Calcium in Protein Folding and Function of Tva, the Receptor of Subgroup A Avian Sarcoma and Leukosis Virus

Lijun Rong, Qing-yin Wang, P. Gettins, 2001, Journal of Virology.

Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP. Comparison with related domains from the LRP and the LDL receptor.

K. Volz, D. Strickland, W. Huang, 2001, Biochemistry.

Cytokine Response Modifier A Inhibition of Initiator Caspases Results in Covalent Complex Formation and Dissociation of the Caspase Tetramer*

G. Salvesen, S. Olson, J. Dobó, 2006, Journal of Biological Chemistry.

On the structural changes of native human alpha2-macroglobulin upon proteinase entrapment. Three-dimensional structure of the half-transformed molecule.

P. Gettins, J. K. Stoops, U. Qazi, 1998, The Journal of biological chemistry.

Structural Details of Proteinase Entrapment by Human α2-Macroglobulin Emerge from Three-dimensional Reconstructions of Fab labeled Native, Half-transformed, and Transformed Molecules*

D. Strickland, P. Gettins, J. K. Stoops, 1999, The Journal of Biological Chemistry.

Quantitative Dissection of the Binding Contributions of Ligand Lysines of the Receptor-associated Protein (RAP) to the Low Density Lipoprotein Receptor-related Protein (LRP1)*

P. Gettins, K. Dolmer, A. Campos, 2013, The Journal of Biological Chemistry.

1H-N.m.r. spectral assignments for two series of heparin-derived oligosaccharides.

P. Gettins, A. Horne, Angela Horne, 1992, Carbohydrate research.

Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP

P. Gettins, J. Jensen, K. Dolmer, 2009, The Biochemical journal.

High‐resolution structure of the stable plasminogen activator inhibitor type‐1 variant 14‐1B in its proteinase‐cleaved form: A new tool for detailed interaction studies and modeling

P. Gettins, J. Jensen, 2008, Protein science : a publication of the Protein Society.

Molecular basis for group B beta-hemolytic streptococcal disease.

C. Hellerqvist, P. Gettins, H. Sundell, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Interaction of saccharide haptens with myeloma proteins. A 270-MHz proton nuclear magnetic resonance study.

R. Dwek, J. Boyd, P. Gettins, 1981, Biochemistry.

Recombinant human pigment epithelium‐derived factor (PEDF): Characterization of PEDF overexpressed and secreted by eukaryotic cells

E. Alberdi, P. Gettins, E. Stratikos, 1996, Protein science : a publication of the Protein Society.

On the domain structure of antithrombin III. Tentative localization of the heparin binding region using 1H NMR spectroscopy.

E. W. Wooten, P. Gettins, 1987, Biochemistry.

Lysine-heparin interactions in antithrombin. Properties of K125M and K290M,K294M,K297M variants.

I. Turko, P. Gettins, B. Fan, 1994, Biochemistry.

Complement-Like Repeats in Proteins of the Complement System

P. Gettins, K. Dolmer, 2005 .

Kinetic Analysis of Binding Interaction between the Subgroup A Rous Sarcoma Virus Glycoprotein SU and Its Cognate Receptor Tva: Calcium Is Not Required for Ligand Binding

J. Young, Qing-yin Wang, P. Gettins, 2003, Journal of Virology.

Characterization of the LDL‐A module mutants of Tva, the subgroup A Rous sarcoma virus receptor, and the implications in protein folding

Qing-yin Wang, P. Gettins, K. Dolmer, 2002, Protein science : a publication of the Protein Society.

Pigment Epithelium-Derived Factor (PEDF), a Serpin with Potent Anti-Angiogenic and Neurite Outgrowth-promoting Properties

K. Volz, P. Gettins, M. Simonović, 2002, Biological chemistry.

Lack of involvement of strand s1'A of the viral serpin CrmA in anti-apoptotic or caspase-inhibitory functions.

G. Salvesen, K. Volz, J. Denault, 2005, Archives of biochemistry and biophysics.

Linkage between the hormone binding site and the reactive center loop of thyroxine binding globulin.

P. Gettins, P. Patston, S. Suda, 2000, Archives of biochemistry and biophysics.

Canonical Inhibitor-like Interactions Explain Reactivity of α1-Proteinase Inhibitor Pittsburgh and Antithrombin with Proteinases*

K. Volz, P. Gettins, A. Dementiev, 2003, Journal of Biological Chemistry.

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.

Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin.

J. Huntington, P. Gettins, James A. Huntington, 1998, Biochemistry.

Pigment epithelium-derived factor as a multifunctional regulator of wound healing.

L. DiPietro, P. Gettins, M. Wietecha, 2015, American journal of physiology. Heart and circulatory physiology.

Structure and mechanism of action of serpins.

P. Gettins, P. Patston, M. Schapira, 1992, Hematology/oncology clinics of North America.

Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage*

D. Lomas, T. Dafforn, P. Gettins, 2000, The Journal of Biological Chemistry.

Use of fluorescence resonance energy transfer to study serpin-proteinase interactions.

P. Gettins, S. T. Olson, 2004, Methods.

Kinetic Intermediates en Route to the Final Serpin-Protease Complex

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

77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase.

P. Gettins, B. Crews, 1991, The Journal of biological chemistry.

NMR relaxation properties of 77Se-labeled proteins.

P. Gettins, S. A. Wardlaw, 1991, The Journal of biological chemistry.

A unique pair of zinc binding sites in the human alpha 2-macroglobulin tetramer. A 35Cl and 37Cl NMR study.

P. Gettins, L. Cunningham, 1986, Biochemistry.

Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155.

J. Huntington, T. Edmunds, P. Gettins, 1996, Biochemistry.

Serpins: Structure, Function and Biology

S. Olson, P. Gettins, S. T. Olson, 1996 .

The Mechanism by Which Serpins Inhibit Thrombin and Other Serine Proteinases a

P. Gettins, P. Patston, M. Schapira, 1994, Annals of the New York Academy of Sciences.

Specificity and reactive loop length requirements for crmA inhibition of serine proteases

P. Gettins, S. T. Olson, M. P. Raghavendra, 2005, Protein science : a publication of the Protein Society.

The gross architecture of an antibody-combining site as determined by spin-label mapping.

R. Dwek, S. Wain-Hobson, D. Givol, 1977, The Biochemical journal.

Serpin conformational change in ovalbumin. Enhanced reactive center loop insertion through hinge region mutations.

D. Lawrence, J. Huntington, P. Gettins, 1997, Biochemistry.

Crystal Structure of Human Maspin, a Serpin with Antitumor Properties

K. Volz, P. Gettins, M. Alayyoubi, 2004, Journal of Biological Chemistry.

Crystallization and preliminary X-ray diffraction analysis of a recombinant cysteine-free mutant of crmA.

K. Volz, P. Gettins, M. Simonović, 2000, Acta crystallographica. Section D, Biological crystallography.

Serine and Cysteine Proteases Are Translocated to Similar Extents upon Formation of Covalent Complexes with Serpins

S. Olson, P. Gettins, R. Swanson, 2007, Journal of Biological Chemistry.

Dissection of RAP-LRP interactions: binding of RAP and RAP fragments to complement-like repeats 7 and 8 from ligand binding cluster II of LRP.

D. Strickland, A. Lazić, P. Gettins, 2006, Archives of biochemistry and biophysics.

Critical Role of Asparagine 1065 of Human α2-Macroglobulin in Formation and Reactivity of the Thiol Ester*

P. Gettins, K. Dolmer, S. Suda, 1997, The Journal of Biological Chemistry.

Bait region‐thiol ester mapping in human α 2‐macroglobulin

K. Hideg, A. Beth, P. Gettins, 1995 .

Alpha 2-macroglobulin bait region variants. A role for the bait region in tetramer formation.

P. Gettins, K. Hahn, B. Crews, 1995, The Journal of biological chemistry.

Binding of Epidermal Growth Factor to Human α2‐Macroglobulin

P. Gettins, B. Crews, 1994 .

Binding of epidermal growth factor to human alpha 2-macroglobulin. Significance for cytokine alpha 2-macroglobulin interactions.

P. Gettins, B. Crews, 1994, Annals of the New York Academy of Sciences.

Thiol ester role in correct folding and conformation of human alpha 2-macroglobulin. Properties of recombinant C949S variant.

E. Boel, P. Gettins, B. Crews, 1994, FEBS letters.

Human α2‐macroglobulin structure

P. Gettins, B. Crews, 1993 .

Epidermal growth factor binding to human alpha 2-macroglobulin. Implications for alpha 2-macroglobulin-growth factor interactions.

P. Gettins, B. Crews, 1993, Biochemistry.

Separation and localization of the four cysteine-949 residues in human alpha 2-macroglobulin using fluorescence energy transfer.

J. Beechem, P. Gettins, L. Cunningham, 1990, Biochemistry.

Inhibition and partial reversal of the methylamine-induced conversion of "slow" to "fast" electrophoretic forms of human alpha 2-macroglobulin by modification of the thiols.

P. Gettins, L. Cunningham, B. Crews, 1990, Biochemistry.

Preparation and initial characterization of an intermediate, half-cleaved form of human alpha 2-macroglobulin.

P. Gettins, L. Cunningham, B. Crews, 1989, Biochemistry.

In support of the trap hypothesis. Chymotrypsin is not rigidly held in its complex with human alpha 2-macroglobulin.

A. Beth, P. Gettins, L. Cunningham, 1987, Biochemistry.

A 1H NMR probe for mobility in the reactive center loops of serpins: spin-echo studies of native and modified forms of ovalbumin and alpha 1-proteinase inhibitor.

P. Gettins, D. B. Hood, 1991, Biochemistry.

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.

One- and two-dimensional 13C-n.m.r. characterization of two series of oligosaccharides derived from porcine intestinal mucosal heparin by degradation with heparinase.

P. Gettins, A. Horne, Angela Horne, 1992, Carbohydrate research.

Crystal Structure of Plasminogen Activator Inhibitor-1 in an Active Conformation with Normal Thermodynamic Stability*

P. Nissen, J. P. Morth, P. Andreasen, 2011, The Journal of Biological Chemistry.

Importance of lysine 125 for heparin binding and activation of antithrombin.

U. Desai, S. Olson, P. Gettins, 2002, Biochemistry.

Critical Role of the Linker Region between Helix D and Strand 2A in Heparin Activation of Antithrombin*

S. Olson, J. Meagher, P. Gettins, 2000, The Journal of Biological Chemistry.

Deconvolution of the Fluorescence Emission Spectrum of Human Antithrombin and Identification of the Tryptophan Residues That Are Responsive to Heparin Binding*

J. Beechem, S. Olson, J. Meagher, 1998, The Journal of Biological Chemistry.

Role of Arginine 132 and Lysine 133 in Heparin Binding to and Activation of Antithrombin*

J. Huntington, J. Meagher, P. Gettins, 1996, 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.

Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement

P. Gettins, S. T. Olson, 2009, FEBS letters.

ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE

P. Gettins, M. Petitou, A. Dementiev, 2004 .

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

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

Conformational equilibrium of the reactive center loop of antithrombin examined by steady state and time-resolved fluorescence measurements: consequences for the mechanism of factor Xa inhibition by antithrombin-heparin complexes.

J. Beechem, P. Gettins, A. Futamura, 2001, Biochemistry.

Role of tryptophan 49 in the heparin cofactor activity of human antithrombin III.

P. Gettins, J. Choay, B. Crews, 1992, The Journal of biological chemistry.

1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.

P. Gettins, A. Horne, 1992, Biochemistry.

Exosite Determinants of Serpin Specificity*

S. Olson, P. Gettins, S. T. Olson, 2009, The Journal of Biological Chemistry.

Thiol ester cleavage-dependent conformational change in human alpha 2-macroglobulin. Influence of attacking nucleophile and of Cys949 modification.

P. Gettins, 1995, Biochemistry.

Zn(II)-113Cd(II) and Zn(II)-Mg(II) hybrids of alkaline phosphatase. 31P and 113Cd NMR.

P. Gettins, J. Coleman, 1984, The Journal of biological chemistry.

Transmission of conformational change from the heparin binding site to the reactive center of antithrombin.

I. Turko, P. Gettins, B. Fan, 1993, Biochemistry.

Nitrogen‐15 nuclear magnetic resonance spectroscopy as a probe of hapten—antibody interactions

R. Dwek, P. Gettins, I. Stenhouse, 1980, FEBS letters.

Model compounds for the active site selenocysteine of glutathione peroxidase: A 77Se NMR study

P. Gettins, D. Dowd, 1988 .

Alkaline phosphatase, solution structure, and mechanism.

P. Gettins, J. Coleman, 2006, Advances in enzymology and related areas of molecular biology.

Solution Structure of the Viral Receptor Domain of Tva and Its Implications in Viral Entry

Qing-yin Wang, P. Gettins, K. Dolmer, 2002, Journal of Virology.

Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor

P. Gettins, M. Simonović, K. Volz, 2001, Proceedings of the National Academy of Sciences of the United States of America.

A physico-chemical study of heparin. Evidence for a calcium-induced co-operative conformational transition.

F. B. Williamson, P. Gettins, J. Boyd, 1980, Journal of molecular biology.

Synthesis in vitro of 5,6-dihydroxyindole-2-carboxylic acid by dopachrome conversion factor from Cloudman S91 melanoma cells.

P. Gettins, A. Korner, 1985, The Journal of investigative dermatology.

31P nuclear magnetic resonance of phosphoenzyme intermediates of alkaline phosphatase.

P. Gettins, J. Coleman, 1983, The Journal of biological chemistry.

The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins

J. Whisstock, J. Irving, D. Lomas, 2001, The Journal of Biological Chemistry.

Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.

P. Gettins, E. Stratikos, 1999, Proceedings of the National Academy of Sciences of the United States of America.

1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.

P. Gettins, 1994, International journal of biological macromolecules.

Localization of basic residues required for receptor binding to the single α‐helix of the receptor binding domain of human α2‐macroglobulin

P. Gettins, K. Dolmer, W. Huang, 1998 .

Antithrombin histidine variants 1H NMR resonance assignments and functional properties

I. Turko, P. Gettins, B. Fan, 1994, FEBS letters.

Antithrombin III and its interaction with heparin. Comparison of the human, bovine, and porcine proteins by 1H NMR spectroscopy.

P. Gettins, 1987, Biochemistry.

Mechanism of Acceleration of Antithrombin-Proteinase Reactions by Low Affinity Heparin

S. Olson, P. Gettins, I. Björk, 1995, The Journal of Biological Chemistry.

Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities

I. Turko, P. Gettins, B. Fan, 1993, FEBS letters.

Heterogeneity of recombinant human antithrombin III expressed in baby hamster kidney cells. Effect of glycosylation differences on heparin binding and structure.

I. Turko, P. Gettins, J. Choay, 1993, The Journal of biological chemistry.

Examination, by 1H-n.m.r. spectroscopy, of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III.

P. Gettins, J. Choay, 1989, Carbohydrate research.

113Cd nuclear magnetic resonance of Cd(II) alkaline phosphatases.

P. Gettins, J. Coleman, 1983, The Journal of biological chemistry.

Alkaline phosphatase. 31P NMR probes of the mechanism.

M. Metzler, P. Gettins, J. Coleman, 1985, The Journal of biological chemistry.

Chloride binding to alkaline phosphatase. 113Cd and 35Cl NMR.

P. Gettins, J. Coleman, 1984, The Journal of biological chemistry.

Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.

S. Olson, P. Gettins, S. T. Olson, 2016, The Biochemical journal.

Significance of secondary structure predictions on the reactive center loop region of seprins: a model for the folding of serpins into a metastable state

P. Gettins, P. Patston, P. Patston, 1996, FEBS letters.

Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate.

J. Beechem, P. Gettins, P. Patston, 1991, Biochemistry.

The High Affinity Binding Site on Plasminogen Activator Inhibitor-1 (PAI-1) for the Low Density Lipoprotein Receptor-related Protein (LRP1) Is Composed of Four Basic Residues*

P. Gettins, K. Dolmer, 2015, The Journal of Biological Chemistry.

Identification of 1H resonances from the bait region of human alpha 2-macroglobulin and effects of proteases and methylamine.

P. Gettins, L. Cunningham, 1986, Biochemistry.

The P6-P2 region of serpins is critical for proteinase inhibition and complex stability.

J. Huntington, P. Gettins, P. Patston, 1997, Biochemistry.

Significance of secondary structure predictions on the reactive center loop region of serpins: a model for the folding of serpins into a metastable state

P. Gettins, Philip A. Patson, 2022 .

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.

Serpins Are Suicide Substrates: Implications for the Regulation of Proteolytic Pathways

P. Gettins, P. Patston, M. Schapira, 1994, Seminars in thrombosis and hemostasis.

alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli.

P. Gettins, N. Doan, 2008, The Journal of biological chemistry.

Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3.

P. Gettins, N. Doan, 2007, The Biochemical journal.

Human α 2-macroglobulin is composed of multiple domains , as predicted by homology with complement component C 3 Ninh

P. Gettins, Doan, 2007 .

Major proteinase movement upon stable serpin-proteinase complex formation.

P. Gettins, E. Stratikos, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Regulation of proteases by protein inhibitors of the serpin superfamily.

S. Olson, P. Gettins, 2011, Progress in molecular biology and translational science.

Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition

K. Volz, P. Gettins, M. Simonović, 2000, Protein science : a publication of the Protein Society.

Maspin Binds to Urokinase-type and Tissue-type Plasminogen Activator through Exosite-Exosite Interactions*

B. Schwartz, P. Gettins, M. Alayyoubi, 2007, Journal of Biological Chemistry.

S‐ovalbumin, an ovalbumin conformer with properties analogous to those of loop‐inserted serpins

J. Huntington, P. Gettins, P. Patston, 1995, Protein science : a publication of the Protein Society.

A combined proton and phosphorus-31 nuclear magnetic resonance investigation of the combining site of M603, a phosphocholine-binding myeloma protein.

R. Dwek, R. Leatherbarrow, P. Gettins, 1982, Biochemistry.

NMR Solution Structure of Complement-like Repeat CR8 from the Low Density Lipoprotein Receptor-related Protein*

P. Gettins, K. Dolmer, W. Huang, 1999, The Journal of Biological Chemistry.

Proximity of thiol esters and bait region in human alpha 2-macroglobulin: paramagnetic mapping.

A. Beth, P. Gettins, L. Cunningham, 1988, Biochemistry.

Structure of an antibody combining site by magnetic resonance

R. Dwek, S. Wain-Hobson, S. Dower, 1977, Nature.

High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.

N. Gordon, F. Peterson, P. Gettins, 2001, Biochemistry.

Use of NMR to study serpin function.

F. Peterson, M. Backovic, P. Gettins, 2004, Methods.

The binding of 2,4,6-trinitrophenyl derivatives to the mouse myeloma immunoglobulin A protein MOPC 315.

R. Dwek, S. Dower, D. Givol, 1978, The Biochemical journal.

D. Lawrence, M. Backovic, P. Gettins, 2002, Protein science : a publication of the Protein Society.

Keeping the serpin machine running smoothly.

P. Gettins, 2000, Genome research.

Basis for the Specificity and Activation of the Serpin Protein Z-dependent Proteinase Inhibitor (ZPI) as an Inhibitor of Membrane-associated Factor Xa*

S. Olson, P. Gettins, A. Dementiev, 2010, The Journal of Biological Chemistry.

A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein)

P. Gettins, K. Dolmer, 2011, The Biochemical journal.

Three Complement-like Repeats Compose the Complete α2-Macroglobulin Binding Site in the Second Ligand Binding Cluster of the Low Density Lipoprotein Receptor-related Protein*

P. Gettins, K. Dolmer, 2006, Journal of Biological Chemistry.

Insight into the mechanism of serpin-proteinase inhibition from 2D [1H-15N] NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex.

F. Peterson, P. Gettins, 2001, Biochemistry.

NMR Solution Structure of the Receptor Binding Domain of Human α2-Macroglobulin*

P. Gettins, K. Dolmer, W. Huang, 2000, The Journal of Biological Chemistry.

NMR Solution Structure of Complement-like Repeat CR3 from the Low Density Lipoprotein Receptor-related Protein EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN a 2 -MACROGLOBULIN*

P. Gettins, K. Dolmer, W. Huang, 2000 .

Investigation of hapten—antibody interactions in McPC603 by 1H and 31P NMR spectroscopy

R. Dwek, S. Rudikoff, P. Gettins, 1977, FEBS letters.

Importance of the P2 Glycine of Antithrombin in Target Proteinase Specificity, Heparin Activation, and the Efficiency of Proteinase Trapping as Revealed by a P2 Gly → Pro Mutation*

S. Olson, Y. Chuang, P. Gettins, 1999, The Journal of Biological Chemistry.

Structural basis of recognition in the immune response.

R. Dwek, P. Závodszky, P. Gettins, 1978, Biochemical Society transactions.

Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin-proteinase complex.

S. Olson, P. Gettins, A. Futamura, 1998, Biochemistry.

The Conformational Activation of Antithrombin

R. Carrell, X. Pei, J. Huntington, 2000, The Journal of Biological Chemistry.

Structural organization of the receptor associated protein.

D. Strickland, P. Gettins, K. Dolmer, 2003, Biochemistry.

Selenium-dependent glutathione peroxidases from ovine and bovine erythrocytes occur as longer chain forms than previously recognized.

P. Gettins, B. Crews, D. Dyal, 1992, Archives of biochemistry and biophysics.

Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin.

P. Gettins, 1989, The Journal of biological chemistry.

Helix D Elongation and Allosteric Activation of Antithrombin*

Aiwu Zhou, R. Carrell, J. Huntington, 2002, The Journal of Biological Chemistry.

How the Serpin α1-Proteinase Inhibitor Folds

P. Gettins, K. Dolmer, 2012, The Journal of Biological Chemistry.

The structure of the C949S mutant human alpha(2)-macroglobulin demonstrates the critical role of the internal thiol esters in its proteinase-entrapping structural transformation.

P. Gettins, J. K. Stoops, S. Kolodziej, 2000, Journal of structural biology.

Pathogenic alpha(1)-antitrypsin polymers are formed by reactive loop-beta-sheet A linkage

Pasupathy Sivasothy, Timothy R. Dafforn, Peter G. W. Gettins, 1999 .

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

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

113Cd NMR. Arsenate binding to Cd(II) alkaline phosphatase.

P. Gettins, J. Coleman, 1984, Journal of Biological Chemistry.

Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.

S. Olson, P. Gettins, 2016, The Biochemical journal.

Serine and Cysteine Proteases Are Translocated to Similar Extents upon Formation of Covalent Complexes with Serpins

S. Olson, P. Gettins, R. Swanson, 2007, Journal of Biological Chemistry.

Regulation of proteases by protein inhibitors of the serpin superfamily.

S. Olson, P. Gettins, 2011, Progress in molecular biology and translational science.

α-Macroglobulins Are Present in Some Gram-negative Bacteria

P. Gettins, N. Doan, 2008, Journal of Biological Chemistry.

Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement

S. Olson, P. Gettins, 2009, FEBS letters.

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.

Insight into residues critical for antithrombin function from analysis of an expanded database of sequences that includes frog, turtle, and ostrich antithrombins.

M. Backovic, P. Gettins, 2002, Journal of proteome research.

Thermolysin-inhibitor complexes examined by 31P and 113Cd NMR spectroscopy.

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