| Year |
Citation |
Score |
| 2016 |
Gettins PG, Olson ST. Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance. The Biochemical Journal. 473: 2273-93. PMID 27470592 DOI: 10.1042/Bcj20160014 |
0.401 |
|
| 2015 |
Gettins PG, Dolmer K. 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. The Journal of Biological Chemistry. PMID 26555266 DOI: 10.1074/Jbc.M115.688820 |
0.434 |
|
| 2015 |
Roth R, Swanson R, Izaguirre G, Bock SC, Gettins PG, Olson ST. Saturation mutagenesis of the antithrombin reactive center loop P14 residue supports a 3-step mechanism of heparin allosteric activation involving intermediate and fully-activated states. The Journal of Biological Chemistry. PMID 26359493 DOI: 10.1074/Jbc.M115.678839 |
0.35 |
|
| 2014 |
Izaguirre G, Aguila S, Qi L, Swanson R, Roth R, Rezaie AR, Gettins PG, Olson ST. Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease. The Journal of Biological Chemistry. 289: 34049-64. PMID 25331949 DOI: 10.1074/Jbc.M114.611707 |
0.396 |
|
| 2013 |
Dementiev A, Swanson R, Roth R, Isetti G, Izaguirre G, Olson ST, Gettins PG. The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. The Journal of Biological Chemistry. 288: 33611-9. PMID 24068708 DOI: 10.1074/Jbc.M113.510727 |
0.434 |
|
| 2013 |
Maddur AA, Swanson R, Izaguirre G, Gettins PG, Olson ST. Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of α1-protease inhibitor with trypsin. The Journal of Biological Chemistry. 288: 32020-35. PMID 24047901 DOI: 10.1074/Jbc.M113.510990 |
0.403 |
|
| 2013 |
Dolmer K, Campos A, Gettins PG. Quantitative dissection of the binding contributions of ligand lysines of the receptor-associated protein (RAP) to the low density lipoprotein receptor-related protein (LRP1). The Journal of Biological Chemistry. 288: 24081-90. PMID 23798683 DOI: 10.1074/Jbc.M113.473728 |
0.426 |
|
| 2012 |
Dolmer K, Gettins PG. How the serpin α1-proteinase inhibitor folds. The Journal of Biological Chemistry. 287: 12425-32. PMID 22334651 DOI: 10.1074/Jbc.M111.315465 |
0.359 |
|
| 2012 |
Gettins PG, Dolmer K. 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). The Biochemical Journal. 443: 65-73. PMID 22181833 DOI: 10.1042/Bj20111867 |
0.427 |
|
| 2011 |
Jensen JK, Thompson LC, Bucci JC, Nissen P, Gettins PG, Peterson CB, Andreasen PA, Morth JP. Crystal structure of plasminogen activator inhibitor-1 in an active conformation with normal thermodynamic stability. The Journal of Biological Chemistry. 286: 29709-17. PMID 21697084 DOI: 10.1074/Jbc.M111.236554 |
0.413 |
|
| 2011 |
Olson ST, Gettins PG. Regulation of proteases by protein inhibitors of the serpin superfamily. Progress in Molecular Biology and Translational Science. 99: 185-240. PMID 21238937 DOI: 10.1016/B978-0-12-385504-6.00005-1 |
0.385 |
|
| 2010 |
Olson ST, Richard B, Izaguirre G, Schedin-Weiss S, Gettins PG. Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors. Biochimie. 92: 1587-96. PMID 20685328 DOI: 10.1016/J.Biochi.2010.05.011 |
0.4 |
|
| 2010 |
Huang X, Dementiev A, Olson ST, Gettins PG. Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa. The Journal of Biological Chemistry. 285: 20399-409. PMID 20427285 DOI: 10.1074/Jbc.M110.112748 |
0.425 |
|
| 2009 |
Gettins PG, Olson ST. Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement. Febs Letters. 583: 3397-400. PMID 19818773 DOI: 10.1016/J.Febslet.2009.10.005 |
0.39 |
|
| 2009 |
Jensen JK, Dolmer K, Gettins PG. 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. The Journal of Biological Chemistry. 284: 17989-97. PMID 19439404 DOI: 10.1074/Jbc.M109.009530 |
0.435 |
|
| 2009 |
Gettins PG, Olson ST. Exosite determinants of serpin specificity. The Journal of Biological Chemistry. 284: 20441-5. PMID 19401470 DOI: 10.1074/Jbc.R800064200 |
0.367 |
|
| 2009 |
Jensen JK, Dolmer K, Schar C, Gettins PG. 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. The Biochemical Journal. 421: 273-82. PMID 19397492 DOI: 10.1042/Bj20090175 |
0.423 |
|
| 2008 |
Jensen JK, Gettins PG. 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. Protein Science : a Publication of the Protein Society. 17: 1844-9. PMID 18725454 DOI: 10.1110/Ps.036707.108 |
0.374 |
|
| 2008 |
Doan N, Gettins PG. alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli. The Journal of Biological Chemistry. 283: 28747-56. PMID 18697741 DOI: 10.1074/Jbc.M803127200 |
0.567 |
|
| 2008 |
Richard B, Swanson R, Schedin-Weiss S, Ramirez B, Izaguirre G, Gettins PG, Olson ST. Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombin. The Journal of Biological Chemistry. 283: 14417-29. PMID 18375953 DOI: 10.1074/Jbc.M710327200 |
0.399 |
|
| 2007 |
Doan N, Gettins PG. Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3. The Biochemical Journal. 407: 23-30. PMID 17608619 DOI: 10.1042/Bj20070764 |
0.598 |
|
| 2007 |
Al-Ayyoubi M, Schwartz BS, Gettins PG. Maspin binds to urokinase-type and tissue-type plasminogen activator through exosite-exosite interactions. The Journal of Biological Chemistry. 282: 19502-9. PMID 17510061 DOI: 10.1074/Jbc.M702445200 |
0.455 |
|
| 2007 |
Swanson R, Raghavendra MP, Zhang W, Froelich C, Gettins PG, Olson ST. Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins. Fluorescence perturbation and fluorescence resonance energy transfer mapping of the protease binding site in CrmA complexes with granzyme B and caspase-1. The Journal of Biological Chemistry. 282: 2305-13. PMID 17142451 DOI: 10.1074/Jbc.M609546200 |
0.393 |
|
| 2006 |
Dobó J, Swanson R, Salvesen GS, Olson ST, Gettins PG. Cytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramer. The Journal of Biological Chemistry. 281: 38781-90. PMID 17052983 DOI: 10.1074/Jbc.M605151200 |
0.304 |
|
| 2006 |
Dolmer K, Gettins PG. Three complement-like repeats compose the complete alpha2-macroglobulin binding site in the second ligand binding cluster of the low density lipoprotein receptor-related protein. The Journal of Biological Chemistry. 281: 34189-96. PMID 16982616 DOI: 10.1074/Jbc.M604389200 |
0.43 |
|
| 2006 |
Lazic A, Dolmer K, Strickland DK, Gettins PG. 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. Archives of Biochemistry and Biophysics. 450: 167-75. PMID 16723114 DOI: 10.1016/J.Abb.2006.04.007 |
0.772 |
|
| 2006 |
Dementiev A, Dobó J, Gettins PG. Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase. The Journal of Biological Chemistry. 281: 3452-7. PMID 16321984 DOI: 10.1074/Jbc.M510564200 |
0.364 |
|
| 2005 |
Simonovic M, Denault JB, Salvesen GS, Volz K, Gettins PG. Lack of involvement of strand s1'A of the viral serpin CrmA in anti-apoptotic or caspase-inhibitory functions. Archives of Biochemistry and Biophysics. 440: 1-9. PMID 15993378 DOI: 10.1016/J.Abb.2005.05.018 |
0.62 |
|
| 2005 |
Tesch LD, Raghavendra MP, Bedsted-Faarvang T, Gettins PG, Olson ST. Specificity and reactive loop length requirements for crmA inhibition of serine proteases. Protein Science : a Publication of the Protein Society. 14: 533-42. PMID 15632287 DOI: 10.1110/Ps.041104905 |
0.372 |
|
| 2004 |
Al-Ayyoubi M, Gettins PG, Volz K. Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained. The Journal of Biological Chemistry. 279: 55540-4. PMID 15501821 DOI: 10.1074/Jbc.M409957200 |
0.316 |
|
| 2004 |
Dementiev A, Petitou M, Herbert JM, Gettins PG. The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity. Nature Structural & Molecular Biology. 11: 863-7. PMID 15311268 DOI: 10.1038/Nsmb810 |
0.45 |
|
| 2004 |
Gettins PG, Backovic M, Peterson FC. Use of NMR to study serpin function. Methods (San Diego, Calif.). 32: 120-9. PMID 14698624 DOI: 10.1016/S1046-2023(03)00203-2 |
0.684 |
|
| 2004 |
Gettins PG, Olson ST. Use of fluorescence resonance energy transfer to study serpin-proteinase interactions. Methods (San Diego, Calif.). 32: 110-9. PMID 14698623 DOI: 10.1016/S1046-2023(03)00202-0 |
0.375 |
|
| 2004 |
Dobó J, Gettins PG. alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibition. The Journal of Biological Chemistry. 279: 9264-9. PMID 14593107 DOI: 10.1074/Jbc.M311731200 |
0.396 |
|
| 2003 |
Lazic A, Dolmer K, Strickland DK, Gettins PG. Structural organization of the receptor associated protein. Biochemistry. 42: 14913-20. PMID 14674767 DOI: 10.1021/Bi035779E |
0.755 |
|
| 2003 |
Dementiev A, Simonovic M, Volz K, Gettins PG. Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases. The Journal of Biological Chemistry. 278: 37881-7. PMID 12860985 DOI: 10.1074/Jbc.M305195200 |
0.674 |
|
| 2003 |
Yu X, Wang QY, Guo Y, Dolmer K, Young JA, Gettins PG, Rong L. 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. Journal of Virology. 77: 7517-26. PMID 12805452 DOI: 10.1128/Jvi.77.13.7517-7526.2003 |
0.393 |
|
| 2002 |
Backovic M, Gettins PG. Insight into residues critical for antithrombin function from analysis of an expanded database of sequences that includes frog, turtle, and ostrich antithrombins. Journal of Proteome Research. 1: 367-73. PMID 12645893 DOI: 10.1021/Pr025515Z |
0.681 |
|
| 2002 |
Gettins PG, Simonovic M, Volz K. Pigment epithelium-derived factor (PEDF), a serpin with potent anti-angiogenic and neurite outgrowth-promoting properties. Biological Chemistry. 383: 1677-82. PMID 12530532 DOI: 10.1515/Bc.2002.188 |
0.599 |
|
| 2002 |
Wang QY, Manicassamy B, Yu X, Dolmer K, Gettins PG, Rong L. Characterization of the LDL-A module mutants of Tva, the subgroup A Rous sarcoma virus receptor, and the implications in protein folding. Protein Science : a Publication of the Protein Society. 11: 2596-605. PMID 12381843 DOI: 10.1110/Ps.0219802 |
0.383 |
|
| 2002 |
Backovic M, Stratikos E, Lawrence DA, Gettins PG. Structural similarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use of site-specific fluorescent probes of local environment. Protein Science : a Publication of the Protein Society. 11: 1182-91. PMID 11967374 DOI: 10.1110/Ps.4320102 |
0.761 |
|
| 2002 |
Schedin-Weiss S, Desai UR, Bock SC, Gettins PG, Olson ST, Björk I. Importance of lysine 125 for heparin binding and activation of antithrombin. Biochemistry. 41: 4779-88. PMID 11939772 DOI: 10.1021/Bi012163L |
0.439 |
|
| 2002 |
Wang QY, Huang W, Dolmer K, Gettins PG, Rong L. Solution structure of the viral receptor domain of Tva and its implications in viral entry. Journal of Virology. 76: 2848-56. PMID 11861852 DOI: 10.1128/Jvi.76.6.2848-2856.2002 |
0.376 |
|
| 2002 |
Belzar KJ, Zhou A, Carrell RW, Gettins PG, Huntington JA. Helix D elongation and allosteric activation of antithrombin. The Journal of Biological Chemistry. 277: 8551-8. PMID 11741963 DOI: 10.1074/Jbc.M110807200 |
0.432 |
|
| 2001 |
Simonovic M, Dolmer K, Huang W, Strickland DK, Volz K, Gettins PG. 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. Biochemistry. 40: 15127-34. PMID 11735395 DOI: 10.1021/Bi015688M |
0.63 |
|
| 2001 |
Simonovic M, Gettins PG, Volz K. Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor. Proceedings of the National Academy of Sciences of the United States of America. 98: 11131-5. PMID 11562499 DOI: 10.1073/Pnas.211268598 |
0.633 |
|
| 2001 |
Futamura A, Beechem JM, Gettins PG. 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. Biochemistry. 40: 6680-7. PMID 11380263 DOI: 10.1021/Bi0029346 |
0.664 |
|
| 2001 |
Peterson FC, Gettins PG. 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. Biochemistry. 40: 6284-92. PMID 11371190 DOI: 10.1021/Bi010100X |
0.42 |
|
| 2001 |
Peterson FC, Gordon NC, Gettins PG. 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. Biochemistry. 40: 6275-83. PMID 11371189 DOI: 10.1021/Bi0100992 |
0.419 |
|
| 2001 |
Wang QY, Dolmer K, Huang W, Gettins PG, Rong L. Role of calcium in protein folding and function of Tva, the receptor of subgroup A avian sarcoma and leukosis virus. Journal of Virology. 75: 2051-8. PMID 11160709 DOI: 10.1128/Jvi.75.5.2051-2058.2001 |
0.354 |
|
| 2000 |
Suda SA, Gettins PG, Patston PA. Linkage between the hormone binding site and the reactive center loop of thyroxine binding globulin. Archives of Biochemistry and Biophysics. 384: 31-6. PMID 11147833 DOI: 10.1006/Abbi.2000.2110 |
0.408 |
|
| 2000 |
Gettins PG. Keeping the serpin machine running smoothly. Genome Research. 10: 1833-5. PMID 11116079 DOI: 10.1101/Gr.168900 |
0.371 |
|
| 2000 |
Simonovic M, Gettins PG, Volz K. Crystallization and preliminary X-ray diffraction analysis of a recombinant cysteine-free mutant of crmA. Acta Crystallographica. Section D, Biological Crystallography. 56: 1440-2. PMID 11053845 DOI: 10.1107/S0907444900009884 |
0.616 |
|
| 2000 |
Peterson FC, Gordon NC, Gettins PG. Formation of a noncovalent serpin-proteinase complex involves no conformational change in the serpin. Use of 1H-15N HSQC NMR as a sensitive nonperturbing monitor of conformation. Biochemistry. 39: 11884-92. PMID 11009600 DOI: 10.1021/Bi001152+ |
0.433 |
|
| 2000 |
Qazi U, Kolodziej SJ, Gettins PG, Stoops JK. 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. Journal of Structural Biology. 131: 19-26. PMID 10945966 DOI: 10.1006/Jsbi.2000.4269 |
0.408 |
|
| 2000 |
Sivasothy P, Dafforn TR, Gettins PG, Lomas DA. Pathogenic alpha 1-antitrypsin polymers are formed by reactive loop-beta-sheet A linkage. The Journal of Biological Chemistry. 275: 33663-8. PMID 10924508 DOI: 10.1074/Jbc.M004054200 |
0.311 |
|
| 2000 |
Huntington JA, McCoy A, Belzar KJ, Pei XY, Gettins PG, Carrell RW. The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions. The Journal of Biological Chemistry. 275: 15377-83. PMID 10809774 DOI: 10.1074/Jbc.275.20.15377 |
0.448 |
|
| 2000 |
Futamura A, Gettins PG. Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa. The Journal of Biological Chemistry. 275: 4092-8. PMID 10660568 DOI: 10.1074/Jbc.275.6.4092 |
0.66 |
|
| 2000 |
Dolmer K, Huang W, Gettins PG. 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 alpha(2)-macroglobulin. The Journal of Biological Chemistry. 275: 3264-9. PMID 10652313 DOI: 10.1074/Jbc.275.5.3264 |
0.451 |
|
| 2000 |
Meagher JL, Olson ST, Gettins PG. Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin. The Journal of Biological Chemistry. 275: 2698-704. PMID 10644732 DOI: 10.1074/Jbc.275.4.2698 |
0.452 |
|
| 2000 |
Huang W, Dolmer K, Liao X, Gettins PG. NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin. The Journal of Biological Chemistry. 275: 1089-94. PMID 10625650 DOI: 10.1074/Jbc.275.2.1089 |
0.435 |
|
| 1999 |
Chuang YJ, Gettins PG, Olson ST. 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. The Journal of Biological Chemistry. 274: 28142-9. PMID 10497166 DOI: 10.1074/Jbc.274.40.28142 |
0.377 |
|
| 1999 |
Huang W, Dolmer K, Gettins PG. NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein. The Journal of Biological Chemistry. 274: 14130-6. PMID 10318830 DOI: 10.1074/Jbc.274.20.14130 |
0.409 |
|
| 1999 |
Stratikos E, Gettins PG. 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. Proceedings of the National Academy of Sciences of the United States of America. 96: 4808-13. PMID 10220375 DOI: 10.1073/Pnas.96.9.4808 |
0.402 |
|
| 1999 |
Qazi U, Gettins PG, Strickland DK, Stoops JK. Structural details of proteinase entrapment by human alpha2-macroglobulin emerge from three-dimensional reconstructions of Fab labeled native, half-transformed, and transformed molecules. The Journal of Biological Chemistry. 274: 8137-42. PMID 10075716 DOI: 10.1074/Jbc.274.12.8137 |
0.366 |
|
| 1998 |
Huang W, Dolmer K, Liao X, Gettins PG. Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin. Protein Science : a Publication of the Protein Society. 7: 2602-12. PMID 9865955 DOI: 10.1002/Pro.5560071214 |
0.424 |
|
| 1998 |
Dolmer K, Huang W, Gettins PG. 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. Biochemistry. 37: 17016-23. PMID 9836596 DOI: 10.1021/Bi982022S |
0.406 |
|
| 1998 |
Futamura A, Stratikos E, Olson ST, Gettins PG. Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin-proteinase complex. Biochemistry. 37: 13110-9. PMID 9748317 DOI: 10.1021/Bi981234M |
0.647 |
|
| 1998 |
Meagher JL, Beechem JM, Olson ST, Gettins PG. Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding. The Journal of Biological Chemistry. 273: 23283-9. PMID 9722560 DOI: 10.1074/Jbc.273.36.23283 |
0.393 |
|
| 1998 |
Stratikos E, Gettins PG. Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh. The Journal of Biological Chemistry. 273: 15582-9. PMID 9624149 DOI: 10.1074/Jbc.273.25.15582 |
0.386 |
|
| 1998 |
Qazi U, Gettins PG, Stoops JK. On the structural changes of native human alpha2-macroglobulin upon proteinase entrapment. Three-dimensional structure of the half-transformed molecule. The Journal of Biological Chemistry. 273: 8987-93. PMID 9535885 DOI: 10.1074/Jbc.273.15.8987 |
0.35 |
|
| 1998 |
Huntington JA, Gettins PG. Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin. Biochemistry. 37: 3272-7. PMID 9521646 DOI: 10.1021/Bi972182O |
0.383 |
|
| 1998 |
Bowen ME, Gettins PG. Bait region involvement in the dimer-dimer interface of human alpha 2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides. The Journal of Biological Chemistry. 273: 1825-31. PMID 9430734 DOI: 10.1074/Jbc.273.3.1825 |
0.639 |
|
| 1997 |
Suda SA, Dolmer K, Gettins PG. Critical role of asparagine 1065 of human alpha2-macroglobulin in formation and reactivity of the thiol ester. The Journal of Biological Chemistry. 272: 31107-12. PMID 9388263 DOI: 10.1074/Jbc.272.49.31107 |
0.397 |
|
| 1997 |
Chaillan-Huntington CE, Gettins PG, Huntington JA, Patston PA. The P6-P2 region of serpins is critical for proteinase inhibition and complex stability. Biochemistry. 36: 9562-70. PMID 9236002 DOI: 10.1021/Bi970651G |
0.323 |
|
| 1997 |
Huntington JA, Fan B, Karlsson KE, Deinum J, Lawrence DA, Gettins PG. Serpin conformational change in ovalbumin. Enhanced reactive center loop insertion through hinge region mutations. Biochemistry. 36: 5432-40. PMID 9154925 DOI: 10.1021/Bi9702142 |
0.335 |
|
| 1997 |
Bowen ME, Armstrong PB, Quigley JP, Gettins PG. Comparison of Limulus alpha-macroglobulin with human alpha2-macroglobulin: thiol ester characterization, subunit organization, and conformational change. Archives of Biochemistry and Biophysics. 337: 191-201. PMID 9016813 DOI: 10.1006/Abbi.1996.9760 |
0.64 |
|
| 1997 |
Stratikos E, Gettins PG. Major proteinase movement upon stable serpin-proteinase complex formation. Proceedings of the National Academy of Sciences of the United States of America. 94: 453-8. PMID 9012804 DOI: 10.1073/Pnas.94.2.453 |
0.333 |
|
| 1996 |
Stratikos E, Alberdi E, Gettins PG, Becerra SP. Recombinant human pigment epithelium-derived factor (PEDF): characterization of PEDF overexpressed and secreted by eukaryotic cells. Protein Science : a Publication of the Protein Society. 5: 2575-82. PMID 8976566 DOI: 10.1002/Pro.5560051220 |
0.327 |
|
| 1996 |
Meagher JL, Huntington JA, Fan B, Gettins PG. Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. The Journal of Biological Chemistry. 271: 29353-8. PMID 8910598 DOI: 10.1074/Jbc.271.46.29353 |
0.443 |
|
| 1996 |
Garone L, Edmunds T, Hanson E, Bernasconi R, Huntington JA, Meagher JL, Fan B, Gettins PG. Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155. Biochemistry. 35: 8881-9. PMID 8688424 DOI: 10.1021/Bi960542M |
0.425 |
|
| 1996 |
Huntington JA, Olson ST, Fan B, Gettins PG. Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding. Biochemistry. 35: 8495-503. PMID 8679610 DOI: 10.1021/Bi9604643 |
0.425 |
|
| 1996 |
Patston PA, Gettins PG. Significance of secondary structure predictions on the reactive center loop region of serpins: a model for the folding of serpins into a metastable state. Febs Letters. 383: 87-92. PMID 8612799 DOI: 10.1016/0014-5793(96)00231-1 |
0.35 |
|
| 1995 |
Streusand VJ, Björk I, Gettins PG, Petitou M, Olson ST. Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement. The Journal of Biological Chemistry. 270: 9043-51. PMID 7721817 DOI: 10.1074/Jbc.270.16.9043 |
0.444 |
|
| 1995 |
Huntington JA, Patston PA, Gettins PG. S-ovalbumin, an ovalbumin conformer with properties analogous to those of loop-inserted serpins. Protein Science : a Publication of the Protein Society. 4: 613-21. PMID 7613461 DOI: 10.1002/Pro.5560040403 |
0.414 |
|
| 1995 |
Gettins PG. Thiol ester cleavage-dependent conformational change in human alpha 2-macroglobulin. Influence of attacking nucleophile and of Cys949 modification. Biochemistry. 34: 12233-40. PMID 7547965 DOI: 10.1021/Bi00038A018 |
0.359 |
|
| 1995 |
Gettins PG, Crews B, Beth AH, Hideg K. Bait region-thiol ester mapping in human alpha 2-macroglobulin. Febs Letters. 367: 137-40. PMID 7540989 DOI: 10.1016/0014-5793(95)00530-M |
0.324 |
|
| 1995 |
Gettins PG, Hahn KH, Crews BC. Alpha 2-macroglobulin bait region variants. A role for the bait region in tetramer formation. The Journal of Biological Chemistry. 270: 14160-7. PMID 7539801 DOI: 10.1074/Jbc.270.23.14160 |
0.405 |
|
| 1994 |
Hood DB, Huntington JA, Gettins PG. Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry. 33: 8538-47. PMID 8031789 DOI: 10.1021/Bi00194A020 |
0.372 |
|
| 1994 |
Fan B, Turko IV, Gettins PG. Antithrombin histidine variants 1H NMR resonance assignments and functional properties. Febs Letters. 354: 84-8. PMID 7957907 DOI: 10.1016/0014-5793(94)01083-8 |
0.39 |
|
| 1994 |
Fan B, Turko IV, Gettins PG. Lysine-heparin interactions in antithrombin. Properties of K125M and K290M,K294M,K297M variants. Biochemistry. 33: 14156-61. PMID 7947827 DOI: 10.1021/Bi00251A026 |
0.419 |
|
| 1994 |
Gettins PG. 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa. International Journal of Biological Macromolecules. 16: 227-35. PMID 7893627 DOI: 10.1016/0141-8130(94)90027-2 |
0.372 |
|
| 1994 |
Gettins PG, Crews BC. Binding of epidermal growth factor to human alpha 2-macroglobulin. Significance for cytokine alpha 2-macroglobulin interactions. Annals of the New York Academy of Sciences. 737: 383-98. PMID 7524409 DOI: 10.1111/J.1749-6632.1994.Tb44325.X |
0.316 |
|
| 1994 |
Gettins PG, Boel E, Crews BC. Thiol ester role in correct folding and conformation of human alpha 2-macroglobulin. Properties of recombinant C949S variant. Febs Letters. 339: 276-80. PMID 7509297 DOI: 10.1016/0014-5793(94)80430-3 |
0.424 |
|
| 1993 |
Gettins P, Patston PA, Schapira M. The role of conformational change in serpin structure and function. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 15: 461-7. PMID 8379949 DOI: 10.1002/Bies.950150705 |
0.44 |
|
| 1993 |
Gettins PG, Fan B, Crews BC, Turko IV, Olson ST, Streusand VJ. Transmission of conformational change from the heparin binding site to the reactive center of antithrombin. Biochemistry. 32: 8385-9. PMID 8357789 DOI: 10.1021/Bi00084A001 |
0.41 |
|
| 1993 |
Turko IV, Fan B, Gettins PG. Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities. Febs Letters. 335: 9-12. PMID 8243674 DOI: 10.1016/0014-5793(93)80429-X |
0.376 |
|
| 1993 |
Gettins PG, Crews BC. Human alpha 2-macroglobulin structure. Location of Cys-949 residues within a half-molecule measured by fluorescence energy transfer. Febs Letters. 332: 211-4. PMID 7691661 DOI: 10.1016/0014-5793(93)80633-6 |
0.331 |
|
| 1993 |
Gettins PG, Crews BC. Epidermal growth factor binding to human alpha 2-macroglobulin. Implications for alpha 2-macroglobulin-growth factor interactions. Biochemistry. 32: 7916-21. PMID 7688570 DOI: 10.1021/Bi00082A012 |
0.356 |
|
| 1992 |
Horne A, Gettins P. 1H-N.m.r. spectral assignments for two series of heparin-derived oligosaccharides. Carbohydrate Research. 225: 43-57. PMID 1633604 DOI: 10.1016/0008-6215(92)80038-3 |
0.323 |
|
| 1992 |
Gettins P, Horne AP. One- and two-dimensional 13C-n.m.r. characterization of two series of oligosaccharides derived from porcine intestinal mucosal heparin by degradation with heparinase. Carbohydrate Research. 223: 81-98. PMID 1596934 DOI: 10.1016/0008-6215(92)80008-O |
0.329 |
|
| 1992 |
Gettins P, Dyal D, Crews B. Selenium-dependent glutathione peroxidases from ovine and bovine erythrocytes occur as longer chain forms than previously recognized. Archives of Biochemistry and Biophysics. 294: 511-8. PMID 1567207 DOI: 10.1016/0003-9861(92)90718-C |
0.371 |
|
| 1992 |
Horne A, Gettins P. 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Biochemistry. 31: 2286-94. PMID 1311598 DOI: 10.1021/Bi00123A011 |
0.439 |
|
| 1991 |
Hood DB, Gettins P. 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. Biochemistry. 30: 9054-60. PMID 1892818 DOI: 10.1021/Bi00101A021 |
0.362 |
|
| 1991 |
Patston PA, Gettins P, Beechem J, Schapira M. Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate. Biochemistry. 30: 8876-82. PMID 1888745 DOI: 10.1021/Bi00100A022 |
0.336 |
|
| 1990 |
Gettins P, Beechem JM, Crews BC, Cunningham LW. Separation and localization of the four cysteine-949 residues in human α2-macroglobulin using fluorescence energy transfer Biochemistry. 29: 7747-7753. PMID 1702992 DOI: 10.1021/Bi00485A025 |
0.345 |
|
| 1990 |
Cunningham LW, Crews BC, Gettins P. 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. Biochemistry. 29: 1638-43. PMID 1692242 DOI: 10.1021/Bi00458A040 |
0.312 |
|
| 1989 |
Gettins P, Choay J. Examination, by 1H-n.m.r. spectroscopy, of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III. Carbohydrate Research. 185: 69-76. PMID 2713873 DOI: 10.1016/0008-6215(89)84022-4 |
0.434 |
|
| 1989 |
Gettins P, Crews BC, Cunningham LW. Preparation and initial characterization of an intermediate, half-cleaved form of human alpha 2-macroglobulin. Biochemistry. 28: 5613-8. PMID 2476174 DOI: 10.1021/Bi00439A041 |
0.313 |
|
| 1988 |
Gettins P, Harten B. Properties of thrombin- and elastase-modified human antithrombin III. Biochemistry. 27: 3634-9. PMID 3408716 DOI: 10.1021/Bi00410A017 |
0.417 |
|
| 1988 |
Gettins P, Beth AH, Cunningham LW. Proximity of thiol esters and bait region in human alpha 2-macroglobulin: paramagnetic mapping. Biochemistry. 27: 2905-11. PMID 2456780 DOI: 10.1021/Bi00408A036 |
0.339 |
|
| 1987 |
Gettins P, Wooten EW. On the domain structure of antithrombin III. Tentative localization of the heparin binding region using 1H NMR spectroscopy. Biochemistry. 26: 4403-8. PMID 3663595 DOI: 10.1021/Bi00388A032 |
0.434 |
|
| 1987 |
Gettins P. Antithrombin III and its interaction with heparin. Comparison of the human, bovine, and porcine proteins by 1H NMR spectroscopy. Biochemistry. 26: 1391-8. PMID 3567176 DOI: 10.1021/Bi00379A027 |
0.387 |
|
| 1987 |
Crews BC, James MW, Beth AH, Gettins P, Cunningham LW. In support of the trap hypothesis. Chymotrypsin is not rigidly held in its complex with human alpha 2-macroglobulin. Biochemistry. 26: 5963-7. PMID 2446656 DOI: 10.1021/Bi00393A003 |
0.344 |
|
| 1986 |
Gettins P, Cunningham LW. Identification of 1H resonances from the bait region of human alpha 2-macroglobulin and effects of proteases and methylamine. Biochemistry. 25: 5011-7. PMID 2429692 DOI: 10.1021/Bi00366A007 |
0.35 |
|
| 1986 |
Gettins P, Cunningham LW. A unique pair of zinc binding sites in the human alpha 2-macroglobulin tetramer. A 35Cl and 37Cl NMR study. Biochemistry. 25: 5004-10. PMID 2429691 DOI: 10.1021/Bi00366A006 |
0.386 |
|
| 1983 |
Coleman JE, Gettins P. Alkaline phosphatase, solution structure, and mechanism. Advances in Enzymology and Related Areas of Molecular Biology. 55: 381-452. PMID 6312783 |
0.429 |
|
| 1982 |
Gettins P, Pótter M, Leatherbarrow RJ, Dwek RA. A combined proton and phosphorus-31 nuclear magnetic resonance investigation of the combining site of M603, a phosphocholine-binding myeloma protein. Biochemistry. 21: 4927-31. PMID 6291593 DOI: 10.1021/Bi00263A015 |
0.662 |
|
| 1982 |
Gettins P, Boyd J, Glaudemans CP, Potter M, Dwek RA. Interaction of saccharide haptens with myeloma proteins. A 270-MHz proton nuclear magnetic resonance study. Biochemistry. 20: 7463-9. PMID 6275881 DOI: 10.1021/Bi00529A021 |
0.368 |
|
| 1981 |
Gettins P, Dwek RA, Perutz RN. The variability of nitro group--protein interaction in the 2,4-dinitrophenyl-binding antibodies M315, M460 and X25 investigated by resonance Raman spectroscopy. The Biochemical Journal. 197: 119-25. PMID 7317024 DOI: 10.1042/bj1970119 |
0.433 |
|
| 1981 |
Gettins P, Dwek RA. Strategies for spectral assignment in the 1H NMR spectra of a 25 000 Mr murine antibody fragment: (i) in vivo deuteration and (ii) use of a denaturant. Febs Letters. 124: 248-52. PMID 7227530 DOI: 10.1016/0014-5793(81)80148-2 |
0.369 |
|
| 1979 |
Easterbrook-Smith SB, Závodszky P, Willan KJ, Gettins P, Dwek RA. Structural basis of recognition in the immune response. Biochemical Society Transactions. 6: 1126-31. PMID 744370 DOI: 10.1042/Bst0061126 |
0.471 |
|
| 1978 |
Gettins P, Givol D, Dwek RA. The role of nitro groups in the binding of nitroaromatics to protein MOPC 315 Biochemical Journal. 173: 713-722. PMID 708369 DOI: 10.1042/Bj1730713 |
0.449 |
|
| 1978 |
Dower SK, Gettins P, Jackson R, Dwek RA, Givol D. The binding of 2,4,6-trinitrophenyl derivatives to the mouse myeloma immunoglobulin A protein MOPC 315 Biochemical Journal. 169: 179-188. PMID 629744 DOI: 10.1042/Bj1690179 |
0.47 |
|
| 1978 |
Gettins P, Potter M, Rudikoff S, Dwek RA. Investigation of hapten-antibody interactions in McPC603 by 1 H and 31 P NMR spectroscopy. Febs Letters. 84: 87-91. PMID 590531 DOI: 10.1016/0014-5793(77)81063-6 |
0.382 |
|
| 1977 |
Wain-Hobson S, Dower SK, Gettins P, Givol D, McLaughlin AC, Pecht I, Sunderland CA, Dwek RA. Specificity of interactions of hapten side chains with the combining site of the myeloma protein MOPC 315. The Biochemical Journal. 165: 227-35. PMID 921746 DOI: 10.1042/Bj1650227 |
0.455 |
|
| 1977 |
Perkins SJ, Dower SK, Gettins P, Wain-Hobson S, Dwek RA. Application of ring-current theory based on the Johnson-Bovey equation to the aromatic amino acids. The Biochemical Journal. 165: 223-5. PMID 921745 DOI: 10.1042/Bj1650223 |
0.313 |
|
| 1977 |
Sutton BJ, Gettins P, Givol D, Marsh D, Wain-Hobson S, Willan KJ, Dwek RA. The gross architecture of an antibody-combining site as determined by spin-label mapping. The Biochemical Journal. 165: 177-97. PMID 200219 DOI: 10.1042/Bj1650177 |
0.426 |
|
| 1977 |
Dwek RA, Wain-Hobson S, Dower S, Gettins P, Sutton B, Perkins SJ, Givol D. Structure of an antibody combining site by magnetic resonance. Nature. 266: 31-7. PMID 190543 DOI: 10.1038/266031A0 |
0.428 |
|
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