| Year |
Citation |
Score |
| 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 |
0.752 |
|
| 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 |
0.641 |
|
| 2017 |
Gupta P, Zhang Z, Sugiman-Marangos SN, Tam J, Raman S, Julien JP, Kroh HK, Lacy DB, Murgolo N, Bekkari K, Therien AG, Hernandez LD, Melnyk RA. Functional defects in Clostridium difficile TcdB toxin uptake identify CSPG4 receptor binding determinants. The Journal of Biological Chemistry. PMID 28842504 DOI: 10.1074/Jbc.M117.806687 |
0.39 |
|
| 2017 |
Kroh HK, Chandrasekaran R, Rosenthal K, Woods R, Jin X, Ohi MD, Nyborg AC, Rainey GJ, Warrener P, Spiller BW, Lacy DB. Use of a neutralizing antibody helps identify structural features critical for binding of Clostridium difficile toxin TcdA to the host cell surface. The Journal of Biological Chemistry. PMID 28705932 DOI: 10.1074/Jbc.M117.781112 |
0.408 |
|
| 2017 |
Hernandez LD, Kroh HK, Hsieh E, Yang X, Beaumont M, Sheth PR, DiNunzio E, Rutherford SA, Ohi MD, Ermakov G, Xiao L, Secore S, Karczewski J, Racine F, Mayhood T, et al. Epitopes and Mechanism of Action of the Clostridium Difficile Toxin A-Neutralizing Antibody Actoxumab. Journal of Molecular Biology. PMID 28232034 DOI: 10.1016/J.Jmb.2017.02.010 |
0.422 |
|
| 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 |
0.769 |
|
| 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, 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 |
0.663 |
|
| 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 |
0.732 |
|
| 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 |
0.76 |
|
| 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 |
0.776 |
|
| 2008 |
Khan A, Panizzi P, Kroh HK, Bock PE, Krishnaswamy S. Conformational Activation of Zymogen-Like Thrombin Variants by Tight Binding Ligands Blood. 112: 3070-3070. DOI: 10.1182/Blood.V112.11.3070.3070 |
0.729 |
|
| 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 |
0.688 |
|
| 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 |
0.762 |
|
| 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 |
0.721 |
|
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