Year |
Citation |
Score |
2021 |
Maddur AA, Voehler M, Panizzi P, Meiler J, Bock PE, Verhamme IM. Mapping of the fibrinogen-binding site on the staphylocoagulase C-terminal repeat region. The Journal of Biological Chemistry. 101493. PMID 34915025 DOI: 10.1016/j.jbc.2021.101493 |
0.681 |
|
2020 |
Panizzi P, Krohn-Grimberghe M, Keliher E, Ye YX, Grune J, Frodermann V, Sun Y, Muse CG, Bushey K, Iwamoto Y, van Leent MMT, Meerwaldt A, Toner YC, Munitz J, Maier A, ... ... Bock PE, et al. Multimodal imaging of bacterial-host interface in mice and piglets with endocarditis. Science Translational Medicine. 12. PMID 33148623 DOI: 10.1126/scitranslmed.aay2104 |
0.719 |
|
2020 |
Maddur AA, Kroh HK, Aschenbrenner ME, Gibson BH, Panizzi P, Sheehan JH, Meiler J, Bock PE, Verhamme IM. Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin. The Journal of Biological Chemistry. PMID 32156702 DOI: 10.1074/Jbc.Ra120.012588 |
0.814 |
|
2019 |
Huang X, Swanson R, Kroh HK, Bock PE. Protein Z-dependent protease inhibitor (ZPI) is a physiologically significant inhibitor of prothrombinase function. The Journal of Biological Chemistry. PMID 30918026 DOI: 10.1074/jbc.RA118.006787 |
0.757 |
|
2018 |
Baaten CCFMJ, Swieringa F, Misztal T, Mastenbroek TG, Feijge MAH, Bock PE, Donners MMPC, Collins PW, Li R, van der Meijden PEJ, Heemskerk JWM. Platelet heterogeneity in activation-induced glycoprotein shedding: functional effects. Blood Advances. 2: 2320-2331. PMID 30232085 DOI: 10.1182/Bloodadvances.2017011544 |
0.376 |
|
2016 |
Davis RW, Brannen AD, Hossain MJ, Monsma S, Bock PE, Nahrendorf M, Mead D, Lodes M, Liles MR, Panizzi P. Complete genome of Staphylococcus aureus Tager 104 provides evidence of its relation to modern systemic hospital-acquired strains. Bmc Genomics. 17: 179. PMID 26940863 DOI: 10.1186/S12864-016-2433-8 |
0.733 |
|
2015 |
Verhamme IM, Panizzi PR, Bock PE. Pathogen activators of plasminogen. Journal of Thrombosis and Haemostasis : Jth. 13: S106-14. PMID 26149011 DOI: 10.1111/Jth.12939 |
0.719 |
|
2015 |
Davis RW, Eggleston H, Johnson F, Nahrendorf M, Bock PE, Peterson T, Panizzi P. In Vivo Tracking of Streptococcal Infections of Subcutaneous Origin in a Murine Model. Molecular Imaging and Biology : Mib : the Official Publication of the Academy of Molecular Imaging. PMID 25921659 DOI: 10.1007/S11307-015-0856-2 |
0.694 |
|
2015 |
Micucci JA, Kamath P, Khan A, Bock PE, Krishnaswamy S. Long-Range Allosteric Linkage Between Exosites Reciprocally Regulates the Zymogenicity of Prothrombin Derivatives Blood. 126: 122-122. DOI: 10.1182/Blood.V126.23.122.122 |
0.474 |
|
2014 |
Verhamme IM, Bock PE. Rapid binding of plasminogen to streptokinase in a catalytic complex reveals a three-step mechanism. The Journal of Biological Chemistry. 289: 28006-18. PMID 25138220 DOI: 10.1074/Jbc.M114.589077 |
0.494 |
|
2013 |
Nolan M, Bouldin SD, Bock PE. Full time course kinetics of the streptokinase-plasminogen activation pathway. The Journal of Biological Chemistry. 288: 29482-93. PMID 23970549 DOI: 10.1074/Jbc.M113.477935 |
0.496 |
|
2012 |
Kroh HK, Bock PE. Effect of zymogen domains and active site occupation on activation of prothrombin by von Willebrand factor-binding protein. The Journal of Biological Chemistry. 287: 39149-57. PMID 23012355 DOI: 10.1074/Jbc.M112.415562 |
0.82 |
|
2011 |
Newell-Caito JL, Laha M, Tharp AC, Creamer JI, Xu H, Maddur AA, Tans G, Bock PE. Notecarin D binds human factor V and factor Va with high affinity in the absence of membranes. The Journal of Biological Chemistry. 286: 38286-97. PMID 21911491 DOI: 10.1074/Jbc.M111.247122 |
0.512 |
|
2011 |
Panizzi P, Nahrendorf M, Figueiredo JL, Panizzi J, Marinelli B, Iwamoto Y, Keliher E, Maddur AA, Waterman P, Kroh HK, Leuschner F, Aikawa E, Swirski FK, Pittet MJ, Hackeng TM, ... ... Bock PE, et al. In vivo detection of Staphylococcus aureus endocarditis by targeting pathogen-specific prothrombin activation. Nature Medicine. 17: 1142-6. PMID 21857652 DOI: 10.1038/Nm.2423 |
0.775 |
|
2011 |
Laha M, Panizzi P, Nahrendorf M, Bock PE. Engineering streptokinase for generation of active site-labeled plasminogen analogs. Analytical Biochemistry. 415: 105-15. PMID 21570944 DOI: 10.1016/J.Ab.2011.04.025 |
0.71 |
|
2011 |
Corral-Rodríguez MÁ, Bock PE, Hernández-Carvajal E, Gutiérrez-Gallego R, Fuentes-Prior P. Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction. Blood. 117: 7164-73. PMID 21555742 DOI: 10.1182/Blood-2010-10-315309 |
0.464 |
|
2011 |
Kroh HK, Panizzi P, Tchaikovski S, Baird TR, Wei N, Krishnaswamy S, Tans G, Rosing J, Furie B, Furie BC, Bock PE. Active site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo. The Journal of Biological Chemistry. 286: 23345-56. PMID 21531712 DOI: 10.1074/Jbc.M111.230292 |
0.803 |
|
2010 |
Nicolaes GA, Bock PE, Segers K, Wildhagen KC, Dahlbäck B, Rosing J. Inhibition of thrombin formation by active site mutated (S360A) activated protein C. The Journal of Biological Chemistry. 285: 22890-900. PMID 20484050 DOI: 10.1074/Jbc.M110.131029 |
0.555 |
|
2010 |
Berny MA, Munnix IC, Auger JM, Schols SE, Cosemans JM, Panizzi P, Bock PE, Watson SP, McCarty OJ, Heemskerk JW. Spatial distribution of factor Xa, thrombin, and fibrin(ogen) on thrombi at venous shear. Plos One. 5: e10415. PMID 20454680 DOI: 10.1371/Journal.Pone.0010415 |
0.679 |
|
2010 |
Wiles KG, Panizzi P, Kroh HK, Bock PE. Skizzle is a novel plasminogen- and plasmin-binding protein from Streptococcus agalactiae that targets proteins of human fibrinolysis to promote plasmin generation. The Journal of Biological Chemistry. 285: 21153-64. PMID 20435890 DOI: 10.1074/Jbc.M110.107730 |
0.819 |
|
2009 |
Tharp AC, Laha M, Panizzi P, Thompson MW, Fuentes-Prior P, Bock PE. Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase beta-domain and kringle 5 of the substrate. The Journal of Biological Chemistry. 284: 19511-21. PMID 19473980 DOI: 10.1074/Jbc.M109.005512 |
0.732 |
|
2009 |
Kroh HK, Panizzi P, Bock PE. Von Willebrand factor-binding protein is a hysteretic conformational activator of prothrombin. Proceedings of the National Academy of Sciences of the United States of America. 106: 7786-91. PMID 19416890 DOI: 10.1073/Pnas.0811750106 |
0.832 |
|
2008 |
Verhamme IM, Bock PE. Rapid-reaction kinetic characterization of the pathway of streptokinase-plasmin catalytic complex formation. The Journal of Biological Chemistry. 283: 26137-47. PMID 18658146 DOI: 10.1074/Jbc.M804038200 |
0.461 |
|
2008 |
Smith SB, Verhamme IM, Sun MF, Bock PE, Gailani D. Characterization of Novel Forms of Coagulation Factor XIa: independence of factor XIa subunits in factor IX activation. The Journal of Biological Chemistry. 283: 6696-705. PMID 18192270 DOI: 10.1074/Jbc.M707234200 |
0.398 |
|
2007 |
Segers K, Dahlbäck B, Bock PE, Tans G, Rosing J, Nicolaes GA. The role of thrombin exosites I and II in the activation of human coagulation factor V. The Journal of Biological Chemistry. 282: 33915-24. PMID 17878169 DOI: 10.1074/Jbc.M701123200 |
0.463 |
|
2007 |
Hacisalihoglu A, Panizzi P, Bock PE, Camire RM, Krishnaswamy S. Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase. The Journal of Biological Chemistry. 282: 32974-82. PMID 17848548 DOI: 10.1074/Jbc.M706529200 |
0.711 |
|
2007 |
Henry BL, Monien BH, Bock PE, Desai UR. A novel allosteric pathway of thrombin inhibition: Exosite II mediated potent inhibition of thrombin by chemo-enzymatic, sulfated dehydropolymers of 4-hydroxycinnamic acids. The Journal of Biological Chemistry. 282: 31891-9. PMID 17804413 DOI: 10.1074/Jbc.M704257200 |
0.445 |
|
2007 |
Munnix IC, Kuijpers MJ, Auger J, Thomassen CM, Panizzi P, van Zandvoort MA, Rosing J, Bock PE, Watson SP, Heemskerk JW. Segregation of platelet aggregatory and procoagulant microdomains in thrombus formation: regulation by transient integrin activation. Arteriosclerosis, Thrombosis, and Vascular Biology. 27: 2484-90. PMID 17761939 DOI: 10.1161/Atvbaha.107.151100 |
0.643 |
|
2007 |
Bock PE, Panizzi P, Verhamme IM. Exosites in the substrate specificity of blood coagulation reactions. Journal of Thrombosis and Haemostasis : Jth. 81-94. PMID 17635714 DOI: 10.1111/J.1538-7836.2007.02496.X |
0.74 |
|
2007 |
Kroh HK, Tans G, Nicolaes GA, Rosing J, Bock PE. Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation. The Journal of Biological Chemistry. 282: 16095-104. PMID 17430903 DOI: 10.1074/Jbc.M610577200 |
0.785 |
|
2006 |
Panizzi P, Boxrud PD, Verhamme IM, Bock PE. Binding of the COOH-terminal lysine residue of streptokinase to plasmin(ogen) kringles enhances formation of the streptokinase.plasmin(ogen) catalytic complexes. The Journal of Biological Chemistry. 281: 26774-8. PMID 16857686 DOI: 10.1074/Jbc.C600171200 |
0.752 |
|
2006 |
Panizzi P, Friedrich R, Fuentes-Prior P, Kroh HK, Briggs J, Tans G, Bode W, Bock PE. Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions. The Journal of Biological Chemistry. 281: 1169-78. PMID 16230340 DOI: 10.1074/Jbc.M507955200 |
0.819 |
|
2006 |
Panizzi P, Friedrich R, Fuentes-Prior P, Richter K, Bock PE, Bode W. Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes. The Journal of Biological Chemistry. 281: 1179-87. PMID 16230339 DOI: 10.1074/Jbc.M507956200 |
0.744 |
|
2006 |
Friedrich R, Panizzi P, Kawabata S, Bode W, Bock PE, Fuentes-Prior P. Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation. The Journal of Biological Chemistry. 281: 1188-95. PMID 16230338 DOI: 10.1074/Jbc.M507957200 |
0.725 |
|
2006 |
Smith SB, Sun M, Bock PE, Gailani D. Independence of Factor XIa Subunits in Factor IX Activation. Blood. 108: 334-334. DOI: 10.1182/Blood.V108.11.334.334 |
0.528 |
|
2006 |
Panizzi PR, Bock PE. Identification and Characterization of a Sodium Ion Binding Site on the Staphylocoagulase-Prothrombin Complex. Blood. 108: 1700-1700. DOI: 10.1182/Blood.V108.11.1700.1700 |
0.727 |
|
2006 |
Creamer JI, Panizzi PR, Bock PE. Streptococcus pyogenes Fibronectin-Binding Protein Is a Novel Prothrombin Activator. Blood. 108: 1691-1691. DOI: 10.1182/Blood.V108.11.1691.1691 |
0.775 |
|
2006 |
Bock P, Panizzi P, Kroh H. ID: 334 von Willebrand Factor Binding Protein is a Novel Conformational Activator of Prothrombin that Functions Through a Substrate-assisted Molecular Sexuality Mechanism Journal of Thrombosis and Haemostasis. 4: 117-117. DOI: 10.1111/J.1538-7836.2006.00334.X |
0.794 |
|
2005 |
Bianchini EP, Orcutt SJ, Panizzi P, Bock PE, Krishnaswamy S. Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase. Proceedings of the National Academy of Sciences of the United States of America. 102: 10099-104. PMID 16006504 DOI: 10.1073/Pnas.0504704102 |
0.694 |
|
2005 |
Ogawa T, Verhamme IM, Sun MF, Bock PE, Gailani D. Exosite-mediated substrate recognition of factor IX by factor XIa. The factor XIa heavy chain is required for initial recognition of factor IX. The Journal of Biological Chemistry. 280: 23523-30. PMID 15829482 DOI: 10.1074/Jbc.M500894200 |
0.469 |
|
2005 |
Bean RR, Verhamme IM, Bock PE. Role of the streptokinase alpha-domain in the interactions of streptokinase with plasminogen and plasmin. The Journal of Biological Chemistry. 280: 7504-10. PMID 15623524 DOI: 10.1074/Jbc.M411637200 |
0.373 |
|
2004 |
Panizzi P, Friedrich R, Fuentes-Prior P, Bode W, Bock PE. The staphylocoagulase family of zymogen activator and adhesion proteins. Cellular and Molecular Life Sciences : Cmls. 61: 2793-8. PMID 15558209 DOI: 10.1007/S00018-004-4285-7 |
0.717 |
|
2004 |
Boxrud PD, Verhamme IM, Bock PE. Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase. The Journal of Biological Chemistry. 279: 36633-41. PMID 15215240 DOI: 10.1074/Jbc.M405264200 |
0.524 |
|
2004 |
Boxrud PD, Bock PE. Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase. The Journal of Biological Chemistry. 279: 36642-9. PMID 15215239 DOI: 10.1074/Jbc.M405265200 |
0.47 |
|
2004 |
Verhamme IM, Bock PE, Jackson CM. The preferred pathway of glycosaminoglycan-accelerated inactivation of thrombin by heparin cofactor II. The Journal of Biological Chemistry. 279: 9785-95. PMID 14701814 DOI: 10.1074/Jbc.M313962200 |
0.423 |
|
2003 |
Friedrich R, Panizzi P, Fuentes-Prior P, Richter K, Verhamme I, Anderson PJ, Kawabata S, Huber R, Bode W, Bock PE. Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature. 425: 535-9. PMID 14523451 DOI: 10.1038/Nature01962 |
0.758 |
|
2003 |
Anderson PJ, Bock PE. Role of prothrombin fragment 1 in the pathway of regulatory exosite I formation during conversion of human prothrombin to thrombin. The Journal of Biological Chemistry. 278: 44489-95. PMID 12939270 DOI: 10.1074/Jbc.M306916200 |
0.396 |
|
2003 |
Anderson PJ, Nesset A, Bock PE. Effects of activation peptide bond cleavage and fragment 2 interactions on the pathway of exosite I expression during activation of human prethrombin 1 to thrombin. The Journal of Biological Chemistry. 278: 44482-8. PMID 12939269 DOI: 10.1074/Jbc.M306917200 |
0.479 |
|
2003 |
Bedsted T, Swanson R, Chuang YJ, Bock PE, Björk I, Olson ST. Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites. Biochemistry. 42: 8143-52. PMID 12846563 DOI: 10.1021/Bi034363Y |
0.419 |
|
2003 |
Flanagan JJ, Chen JC, Miao Y, Shao Y, Lin J, Bock PE, Johnson AE. Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens. The Journal of Biological Chemistry. 278: 18628-37. PMID 12621052 DOI: 10.1074/Jbc.M300173200 |
0.334 |
|
2002 |
Verhamme IM, Olson ST, Tollefsen DM, Bock PE. Binding of exosite ligands to human thrombin. Re-evaluation of allosteric linkage between thrombin exosites I and II. The Journal of Biological Chemistry. 277: 6788-98. PMID 11724802 DOI: 10.1074/Jbc.M110257200 |
0.444 |
|
2001 |
Anderson PJ, Bock PE. Biotin Derivatives of d-Phe-Pro-Arg-CH2Cl for Active-Site-Specific Labeling of Thrombin and Other Serine Proteinases Analytical Biochemistry. 296: 254-261. PMID 11554721 DOI: 10.1006/Abio.2001.5302 |
0.43 |
|
2001 |
Monteiro RQ, Bock PE, Bianconi ML, Zingali RB. Characterization of bothrojaracin interaction with human prothrombin. Protein Science. 10: 1897-1904. PMID 11514680 DOI: 10.1110/Ps.09001 |
0.455 |
|
2001 |
Boxrud PD, Verhamme IMA, Fay WP, Bock PE. Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. Journal of Biological Chemistry. 276: 26084-26089. PMID 11369771 DOI: 10.1074/Jbc.M101966200 |
0.529 |
|
2001 |
Pekovich SR, Bock PE, Hoover RL. Thrombin–thrombomodulin activation of protein C facilitates the activation of progelatinase A Febs Letters. 494: 129-132. PMID 11297749 DOI: 10.1016/S0014-5793(01)02296-7 |
0.371 |
|
2000 |
Boxrud PD, Bock PE. Streptokinase Binds Preferentially to the Extended Conformation of Plasminogen through Lysine Binding Site and Catalytic Domain Interactions Biochemistry. 39: 13974-13981. PMID 11076540 DOI: 10.1021/Bi000594I |
0.499 |
|
2000 |
Boxrud PD, Fay WP, Bock PE. Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen. Journal of Biological Chemistry. 275: 14579-14589. PMID 10799544 DOI: 10.1074/Jbc.275.19.14579 |
0.502 |
|
2000 |
Anderson PJ, Nesset A, Dharmawardana KR, Bock PE. Role of Proexosite I in Factor Va-dependent Substrate Interactions of Prothrombin Activation Journal of Biological Chemistry. 275: 16435-16442. PMID 10748008 DOI: 10.1074/Jbc.M001255200 |
0.437 |
|
2000 |
Anderson PJ, Nesset A, Dharmawardana KR, Bock PE. Characterization of Proexosite I on Prothrombin Journal of Biological Chemistry. 275: 16428-16434. PMID 10748007 DOI: 10.1074/Jbc.M001254200 |
0.45 |
|
1999 |
Dharmawardana KR, Olson ST, Bock PE. Role of regulatory exosite I in binding of thrombin to human factor V, factor Va, factor Va subunits, and activation fragments. Journal of Biological Chemistry. 274: 18635-18643. PMID 10373475 DOI: 10.1074/Jbc.274.26.18635 |
0.463 |
|
1998 |
Colwell NS, Blinder MA, Tsiang M, Gibbs CS, Bock PE, Tollefsen DM. Allosteric effects of a monoclonal antibody against thrombin exosite II Biochemistry. 37: 15057-15065. PMID 9790668 DOI: 10.1021/Bi980925F |
0.381 |
|
1998 |
Dharmawardana KR, Bock PE. Demonstration of exosite I-dependent interactions of thrombin with human factor V and factor Va involving the factor Va heavy chain: analysis by affinity chromatography employing a novel method for active-site-selective immobilization of serine proteinases. Biochemistry. 37: 13143-13152. PMID 9748321 DOI: 10.1021/Bi9812165 |
0.471 |
|
1997 |
Bock PE, Olson ST, Björk I. Inactivation of Thrombin by Antithrombin Is Accompanied by Inactivation of Regulatory Exosite I Journal of Biological Chemistry. 272: 19837-19845. PMID 9242645 DOI: 10.1074/Jbc.272.32.19837 |
0.501 |
|
1997 |
Hogg PJ, Bock PE. Modulation of thrombin and heparin activities by fibrin. Thrombosis and Haemostasis. 77: 424-433. DOI: 10.1055/S-0038-1655982 |
0.374 |
|
1996 |
Hogg PJ, Jackson CM, Labanowski JK, Bock PE. Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen. The Journal of Biological Chemistry. 271: 26088-95. PMID 8824251 DOI: 10.1074/Jbc.271.42.26088 |
0.511 |
|
1996 |
Bock PE, Day DE, Verhamme IM, Bernardo MM, Olson ST, Shore JD. Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinase. The Journal of Biological Chemistry. 271: 1072-80. PMID 8557633 DOI: 10.1074/Jbc.271.2.1072 |
0.443 |
|
1996 |
Olson ST, Bock PE, Kvassman J, Shore JD, Lawrence DA, Ginsburg D, Björk I. Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes. The Journal of Biological Chemistry. 270: 30007-17. PMID 8530403 DOI: 10.1074/Jbc.270.50.30007 |
0.466 |
|
1995 |
Olson ST, Stephens AW, Hirs CH, Bock PE, Björk I. Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation. The Journal of Biological Chemistry. 270: 9717-24. PMID 7730349 DOI: 10.1074/Jbc.270.17.9717 |
0.438 |
|
1993 |
Bock PE. Thioester peptide chloromethyl ketones: reagents for active site-selective labeling of serine proteinases with spectroscopic probes. Methods in Enzymology. 222: 478-503. PMID 8412811 DOI: 10.1016/0076-6879(93)22030-J |
0.332 |
|
1991 |
Olson ST, Bock PE, Sheffer R. Quantitative evaluation of solution equilibrium binding interactions by affinity partitioning: application to specific and nonspecific protein-heparin interactions. Archives of Biochemistry and Biophysics. 286: 533-545. PMID 1897976 DOI: 10.1016/0003-9861(91)90076-U |
0.374 |
|
1989 |
Bock PE, Craig PA, Olson ST, Singh P. Isolation of human blood coagulation α-factor Xa by soybean trypsin inhibitor-Sepharose chromatography and its active-site titration with fluorescein mono-p-guanidinobenzoate☆ Archives of Biochemistry and Biophysics. 273: 375-388. PMID 2774557 DOI: 10.1016/0003-9861(89)90496-7 |
0.38 |
|
1988 |
Bock PE. Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2Cl. Biochemistry. 27: 6633-6639. PMID 3219359 DOI: 10.1021/Bi00417A063 |
0.423 |
|
1987 |
Shore JD, Day DE, Bock PE, Olson ST. Acceleration of surface-dependent autocatalytic activation of blood coagulation factor XII by divalent metal ions. Biochemistry. 26: 2250-8. PMID 3113477 DOI: 10.1021/Bi00382A027 |
0.331 |
|
1980 |
Bock PE, Luscombe M, Marshall SE, Pepper DS, Holbrook JJ. The multiple complexes formed by the interaction of platelet factor 4 with heparin. The Biochemical Journal. 191: 769-76. PMID 7283972 DOI: 10.1042/Bj1910769 |
0.365 |
|
1978 |
Holbrook JJ, Lewis BA, Freyssinet JM, Bock PE, Shore JD. Factor XIII: a study using polarization of fluorescence of the activation of the enzyme by calcium and by substrate [proceedings]. Biochemical Society Transactions. 5: 1247-51. PMID 923904 DOI: 10.1042/Bst0051247A |
0.33 |
|
1978 |
Bock PE, Frieden C. Another look at the cold lability of enzymes Trends in Biochemical Sciences. 3: 100-103. DOI: 10.1016/S0968-0004(78)80013-9 |
0.509 |
|
1975 |
Bock PE, Gilbert HR, Frieden C. Analysis of the cold lability behavior of rabbit muscle phosphofructokinase Biochemical and Biophysical Research Communications. 66: 564-569. PMID 241341 DOI: 10.1016/0006-291X(75)90547-1 |
0.552 |
|
1974 |
Bock PE, Frieden C. pH-induced cold lability of rabbit skeletal muscle phosphofructokinase Biochemistry. 13: 4191-4196. PMID 4277765 DOI: 10.1021/Bi00717A020 |
0.469 |
|
Show low-probability matches. |