{"id":407,"date":"2018-09-13T16:22:14","date_gmt":"2018-09-13T16:22:14","guid":{"rendered":"http:\/\/komiveslab.ucsd.edu\/?page_id=407"},"modified":"2023-02-08T05:00:21","modified_gmt":"2023-02-08T05:00:21","slug":"thrombin-publications","status":"publish","type":"page","link":"https:\/\/komiveslab.ucsd.edu\/?page_id=407","title":{"rendered":"Thrombin Publications"},"content":{"rendered":"<p><a name=\"Thrombin\"><\/a><br \/>\n<strong><a href=\"http:\/\/localhost:8888\/wordpressprojects\/#Thrombin\">Thrombin-Thrombomodulin<\/a><\/strong><\/p>\n<p class=\"heading-title\">Peacock RB, McGrann T, Zaragoza S, Komives EA. (2022) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/34978431\/\">How Thrombomodulin Enables W215A\/E217A Thrombin to Cleave Protein C but Not Fibrinogen.<\/a> Biochemistry. 61(2):77-84<\/p>\n<p class=\"heading-title\">Peacock RB, Komives EA. (2021) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/34159782\/\">Hydrogen\/Deuterium Exchange and Nuclear Magnetic Resonance Spectroscopy Reveal Dynamic Allostery on Multiple Time Scales in the Serine Protease Thrombin.<\/a> Biochemistry 60(46):3441-3448<\/p>\n<p>Peacock RB, McGrann T, Tonelli M, Komives EA. (2021) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/33931701\/\">Serine protease dynamics revealed by NMR analysis of the thrombin-thrombomodulin complex.\u00a0<\/a>Sci Rep. 11(1):9354<\/p>\n<p>Markwick PRL, Peacock RB, Komives EA. (2019) <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/30558884\/\">Accurate Prediction of Amide Exchange in the Fast Limit Reveals Thromobin Allostery.<\/a> Biophys J. 116(1):49-56<\/p>\n<p>Peacock RB, Davis JR, Markwick PRL, Komives EA. (2018) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29634247\" target=\"_blank\" rel=\"noopener\">Dynamic Consequences of Mutation of Tryptophan 215 in Thrombin.<\/a> Biochemistry. 2018;57(18):2694-2703.<\/p>\n<p>Handley, LD, Fuglestad, B, Stearns, K, Tonelli, M, Fenwick, RB, Markwick, PRL, and Komives, EA (2017) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28059082\" target=\"_blank\" rel=\"noopener\">NMR reveals a dynamic allosteric pathway in thrombin. <\/a> Scientific Reports 7:39575. PMC5216386<\/p>\n<p>Handley LD, Treuheit NA, Venkatesh VJ, Komives EA. (2015)<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/26468766\" target=\"_blank\" rel=\"noopener\">Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin <\/a>Biochemistry 54(43):6650-8. PMC4697735<\/p>\n<p>Boechi L, Pierce L, Komives EA, McCammon JA. (2014)<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25131668\" target=\"_blank\" rel=\"noopener\">Trypsinogen activation as observed in accelerated molecular dynamics simulations.<\/a>Protein Sci. 2014 Nov;23(11):1550-8. PMC4241106<\/p>\n<p>Fuglestad B, Gasper PM, McCammon JA, Markwick PR, Komives EA. (2013) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23621631\" target=\"_blank\" rel=\"noopener\">Correlated Motions and Residual Frustration in Thrombin. <\/a>J Phys Chem B. 117(42):12857-63 PMC3808083<\/p>\n<p>Gasper, PM, Fuglestad, B., Komives, EA, Markwick, PRL, McCammon, JA. (2012) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23197839\" target=\"_blank\" rel=\"noopener\">Allosteric networks in thrombin distinguish procoagulant and anticoagulant activities. <\/a>Proc Natl Acad Sci USA 109(52):21216-22. PMC3535651<\/p>\n<p>Fuglestad B, Gasper PM, Tonelli M, McCammon JA, Markwick PR, Komives EA. (2012) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22828334\" target=\"_blank\" rel=\"noopener\">The dynamic structure of thrombin in solution. <\/a>Biophys J. 103(1):79-88. PMC3388214<\/p>\n<p>Treuheit, NA, Beach, MA. and Komives, EA. (2011) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21526769\" target=\"_blank\" rel=\"noopener\">Thermodynamic compensation upon binding to exosite 1 and the active site of thrombin. <\/a>Biochemistry 50, 4590-6. PMC3107735<\/p>\n<p>Koeppe, J. R., Beach, M.S. and Komives, E. A. (2008) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/18803401\" target=\"_blank\" rel=\"noopener\">Mutations in the fourth EGF-like domain affect thrombomodulin-induced changes in the active site of thrombin.<\/a>&#8221; Biochemistry 47, 10933-39.<\/p>\n<p>Koeppe, J. R. and Komives, E. A. (2006) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16784223\" target=\"_blank\" rel=\"noopener\">Amide H\/2H Exchange Reveals a Mechanism of Thrombin Activation.<\/a>&#8221; Biochemistry 45, 7724-32.<\/p>\n<p>Wood, M. J., Prieto, J. H. &amp; Komives, E. A. (2005) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15680222\" target=\"_blank\" rel=\"noopener\">Structural and functional consequences of methionine oxidation in thrombomodulin<\/a> Biochim. Biophys. Acta 1703, 141-147.<\/p>\n<p>Koeppe, J. R., Seitova, A., Mather, T., Komives, E. A. (2005) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16274226\" target=\"_blank\" rel=\"noopener\">Thrombomodulin tightens the thrombin active site loops to promote protein C activation.<\/a>&#8221; Biochemistry 44, 14784-91.<\/p>\n<p>Prieto, J. H., Sampoli Benitez, B., Melacini, G., Johnson, D. A., Wood, M. J., &amp; Komives, E. A. (2005) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15667216\" target=\"_blank\" rel=\"noopener\">Dynamics of the Fragment of Thrombomodulin Containing the Fourth and Fifth EGF-Like Domains Correlate with Function<\/a>Biochemistry 44, 1225-1235.<\/p>\n<p>Croy, C.H., Koeppe, J.R., Bergqvist, S., Komives, E.A.(2004) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15122890\" target=\"_blank\" rel=\"noopener\">Allosteric changes in solvent accessibility observed in thrombin upon active site occupation.<\/a>&#8221; Biochemistry 43, 5246-55.<\/p>\n<p>Baerga-Ortiz, A., Bergqvist, S. P., Mandell, J. G. &amp; Komives, E. A. (2004) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/14691232\" target=\"_blank\" rel=\"noopener\">Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles<\/a>&#8221; Protein Science 13, 166-176.<\/p>\n<p>Wood, M. J., Becvar, L. A., Prieto, J. H., Melacini, G., &amp; Komives, E. A. (2003) <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/14556624\" target=\"_blank\" rel=\"noopener\">NMR Structures Reveal How Oxidation Inactivates Thrombomodulin<\/a> Biochemistry 42, 11932-42.<\/p>\n<p>Baerga-Ortiz, A., Hughes, C. A., Mandell, J. G. &amp; Komives, E. A. (2002) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/12021429\" target=\"_blank\" rel=\"noopener\">Epitope Mapping of a monoclonal antibody against human thrombin by H\/D exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein<\/a>&#8221; Protein Science 11, 1300-1308.<\/p>\n<p>Mandell, J. G. Baerga-Ortiz, A., Akashi, S., Takio, K. &amp; Komives, E. A. (2001) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11178915\" target=\"_blank\" rel=\"noopener\">Solvent Accessibility of the Thrombin-Thrombomodulin Interface<\/a>&#8221; J. Mol. Biol. 306, 575-589.<\/p>\n<p>Baerga-Ortiz, A. J., Rezaie, A. R. &amp; Komives, E. A. (2000) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10669614\" target=\"_blank\" rel=\"noopener\">Electrostatic Dependence of the Thrombin-Thrombomodulin interaction<\/a>&#8221; J. Mol. Biol. 296: 651 &#8211; 658.<\/p>\n<p>Sampoli Benitez, B.&amp; Komives, E. A. (2000) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10813841\" target=\"_blank\" rel=\"noopener\">Disulfide bond plasticity in EGF<\/a>&#8221; Proteins, Structure, Function and Genetics 40, 168 &#8211; 174.<\/p>\n<p>Wood, M. J., Sampoli Benitez, B., Komives, E. A. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10700277\" target=\"_blank\" rel=\"noopener\">Solution structure of the smallest cofactor-active fragment of thrombomodulin.<\/a> Nature Structural Biology, 2000 Mar, 7(3):200-4.<\/p>\n<p>Sampoli Benitez, BA; Hunter, MJ; Meininger, DP; Komives, EA. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/9367781\" target=\"_blank\" rel=\"noopener\">Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern.<\/a>&#8221; Journal of Molecular Biology, 1997 Nov 7, 273(4):913-26.<\/p>\n<p>White, CE; Hunter, MJ; Meininger, DP; Garrod, S; Komives, EA. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8816772\" target=\"_blank\" rel=\"noopener\">The fifth epidermal growth factor-like domain of thrombomodulin does not have an epidermal growth factor-like disulfide bonding pattern.<\/a> Proceedings of the National Academy of Sciences of the United States of America, 1996 Sep 17, 93(19):10177-82.<\/p>\n<p>White, C. E., Hunter, M. J., Meininger, D. P., White, L. R. &amp; Komives, E. A. (1995) &#8220;<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8819984\" target=\"_blank\" rel=\"noopener\">&#8220;Large Scale Expression, Purification and Characterization of the Smallest Active Fragment of Thrombomodulin: The Roles of the Sixth Domain and of Methionine-388<\/a>&#8221; Protein Engineering 8, 1177 &#8211; 1187.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Thrombin-Thrombomodulin Peacock RB, McGrann T, Zaragoza S, Komives EA. (2022) How Thrombomodulin Enables W215A\/E217A Thrombin to Cleave Protein C but Not Fibrinogen. Biochemistry. 61(2):77-84 Peacock RB, Komives EA. (2021) Hydrogen\/Deuterium Exchange and Nuclear Magnetic Resonance Spectroscopy Reveal Dynamic Allostery on Multiple Time Scales in the Serine Protease Thrombin. Biochemistry 60(46):3441-3448 Peacock RB, McGrann T, Tonelli M, Komives EA. (2021) Serine<\/p>\n<div class=\"clearfix\"><\/div>\n<div class=\"pull-left padding-top-25\"><a href=\"https:\/\/komiveslab.ucsd.edu\/?page_id=407\" class=\"btn btn-theme\">Continue reading<span class=\"screen-reader-text\"> &#8220;Thrombin Publications&#8221;<\/span> <i class=\"fa fa-fw fa-long-arrow-right\"><\/i> <\/a>  <\/div>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"spay_email":"","footnotes":""},"class_list":["post-407","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/pages\/407","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=407"}],"version-history":[{"count":6,"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/pages\/407\/revisions"}],"predecessor-version":[{"id":764,"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=\/wp\/v2\/pages\/407\/revisions\/764"}],"wp:attachment":[{"href":"https:\/\/komiveslab.ucsd.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=407"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}