Journal articles on the topic 'Antithrombin'
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Izaguirre, Gonzalo, Richard Swanson, Srikumar M. Raja, Alireza R. Rezaie, and Steven T. Olson. "Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin." Journal of Biological Chemistry 282, no. 46 (September 17, 2007): 33609–22. http://dx.doi.org/10.1074/jbc.m702462200.
Full textZhou, Aiwu, James A. Huntington, and Robin W. Carrell. "Formation of the Antithrombin Heterodimer In Vivo and the Onset of Thrombosis." Blood 94, no. 10 (November 15, 1999): 3388–96. http://dx.doi.org/10.1182/blood.v94.10.3388.422k20_3388_3396.
Full textChang, Wun-Shaing W., and Paul L. Harper. "Commercial Antithrombin Concentrate Contains Inactive L-forms of Antithrombin." Thrombosis and Haemostasis 77, no. 02 (1997): 323–28. http://dx.doi.org/10.1055/s-0038-1655962.
Full textZhang, Weiqing, Yung-Jen Chuang, Richard Swanson, Juan Li, Kyunga Seo, Lawrence Leung, Lester F. Lau, and Steven T. Olson. "Antiangiogenic antithrombin down-regulates the expression of the proangiogenic heparan sulfate proteoglycan, perlecan, in endothelial cells." Blood 103, no. 4 (February 15, 2004): 1185–91. http://dx.doi.org/10.1182/blood-2003-08-2920.
Full textKaneider, Nicole C., Christina M. Reinisch, Stefan Dunzendorfer, Jürgen Römisch, and Christian J. Wiederman. "Syndecan-4 mediates antithrombin-induced chemotaxis of human peripheral blood lymphocytes and monocytes." Journal of Cell Science 115, no. 1 (January 1, 2002): 227–36. http://dx.doi.org/10.1242/jcs.115.1.227.
Full textGeorge, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.490.
Full textGeorge, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.bloodjournal732490.
Full textNavarro-Fernández, José, María Morena-Barrio, José Padilla, Antonia Miñano, Nataliya Bohdan, Sonia Águila, Irene Martínez-Martínez, et al. "Antithrombin Dublin (p.Val30Glu): a relatively common variant with moderate thrombosis risk of causing transient antithrombin deficiency." Thrombosis and Haemostasis 116, no. 07 (January 2016): 146–54. http://dx.doi.org/10.1160/th15-11-0871.
Full textKOIDE, Takehiko. "Antithrombin." Journal of Japan Atherosclerosis Society 23, no. 10 (1996): 573–79. http://dx.doi.org/10.5551/jat1973.23.10_573.
Full textRoemisch, J., E. Gray, J. N. Hoffmann, and C. J. Wiedermann. "Antithrombin." Blood Coagulation& Fibrinolysis 13, no. 8 (December 2002): 657–70. http://dx.doi.org/10.1097/00001721-200212000-00001.
Full textSakuragawa, Nobuo, Shin-ichi Kondo, Masahiko Katoh, Kaoru Takahashi, and Takehiko Koide. "Antithrombin III microheterogeneity in antithrombin III deficiency and in the antithrombin III abnormality, “antithrombin III toyama”." Thrombosis Research 47, no. 2 (July 1987): 147–53. http://dx.doi.org/10.1016/0049-3848(87)90371-9.
Full textOwen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (May 1, 1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.1275.
Full textOwen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (May 1, 1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.bloodjournal6951275.
Full textBararu-Bojan, Iris, Maria Cristina Vladeanu (Apavaloaie), Andrei Bojan, Paul-Dan Sirbu, Manuela Ciocoiu, and Oana Badulescu. "The Role of Antithrombin III in the Pathogenesis of the Thrombotic Status in Type 2 Diabetes Mellitus." Revista de Chimie 70, no. 3 (April 15, 2019): 1047–52. http://dx.doi.org/10.37358/rc.19.3.7061.
Full textKottke-Marchant, Kandice, and Alexander Duncan. "Antithrombin Deficiency." Archives of Pathology & Laboratory Medicine 126, no. 11 (November 1, 2002): 1326–36. http://dx.doi.org/10.5858/2002-126-1326-ad.
Full textCada, Dennis J., Terri L. Levien, and Danial E. Baker. "Antithrombin (Recombinant)." Hospital Pharmacy 44, no. 9 (September 2009): 785–93. http://dx.doi.org/10.1310/hpj4409-785.
Full textO'Reilly, Michael. "Antiangiogenic Antithrombin." Seminars in Thrombosis and Hemostasis 33, no. 7 (October 2007): 660–66. http://dx.doi.org/10.1055/s-2007-991533.
Full textCieśla, Marek, Ewa Wypasek, Javier Corral, Martine Alhenc-Gelas, and Anetta Undas. "Antithrombin Katowice." Blood Coagulation & Fibrinolysis 26, no. 1 (January 2015): 95–97. http://dx.doi.org/10.1097/mbc.0000000000000182.
Full textSzymańska, Magdalena, Martine Alhenc-Gelas, and Anetta Undas. "Antithrombin Rybnik." Blood Coagulation & Fibrinolysis 24, no. 5 (July 2013): 579–80. http://dx.doi.org/10.1097/mbc.0b013e32835ef7b3.
Full textBeresford, Charles H., and Maurice C. Owen. "Antithrombin III." International Journal of Biochemistry 22, no. 2 (January 1990): 121–28. http://dx.doi.org/10.1016/0020-711x(90)90172-y.
Full textMorrisette, Matthew J., Amanda Zomp-Wiebe, Katherine L. Bidwell, Steven P. Dunn, Michael G. Gelvin, Dustin T. Money, and Surabhi Palkimas. "Antithrombin supplementation in adult patients receiving extracorporeal membrane oxygenation." Perfusion 35, no. 1 (June 19, 2019): 66–72. http://dx.doi.org/10.1177/0267659119856229.
Full textBruzzese, Antonella, Cristina Santoro, Erminia Baldacci, Antonietta Ferretti, Simone Pieroni, Alessandra Serrao, Robin Foà, and Antonio Chistolini. "Antithrombin concentrate during pregnancy in congenital antithrombin deficiency." Blood Coagulation & Fibrinolysis 30, no. 6 (September 2019): 304–7. http://dx.doi.org/10.1097/mbc.0000000000000835.
Full textde Morais, Karen Batista, Carolina Okamoto Vieira, Isaura Yoshico Hirata, and Anita Mitico Tanaka-Azevedo. "Bothrops jararaca antithrombin: Isolation, characterization and comparison with other animal antithrombins." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 152, no. 2 (February 2009): 171–76. http://dx.doi.org/10.1016/j.cbpb.2008.11.002.
Full textBroman, Lars Mikael. "When antithrombin substitution strikes back." Perfusion 35, no. 1_suppl (May 2020): 34–37. http://dx.doi.org/10.1177/0267659120906770.
Full textLarsson, Helena, Peter Åkerud, Kerstin Nordling, Elke Raub-Segall, Lena Claesson-Welsh, and Ingemar Björk. "A Novel Anti-angiogenic Form of Antithrombin with Retained Proteinase Binding Ability and Heparin Affinity." Journal of Biological Chemistry 276, no. 15 (January 12, 2001): 11996–2002. http://dx.doi.org/10.1074/jbc.m010170200.
Full textSanfelippo, Michael J., Jessica M. Engel, and Adedayo A. Onitilo. "Antithrombin Levels Are Unaffected by Warfarin Use." Archives of Pathology & Laboratory Medicine 138, no. 7 (July 1, 2014): 967–68. http://dx.doi.org/10.5858/arpa.2013-0065-oa.
Full textHatton, MW, SL Moar, and M. Richardson. "On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro." Blood 67, no. 4 (April 1, 1986): 878–86. http://dx.doi.org/10.1182/blood.v67.4.878.878.
Full textHatton, MW, SL Moar, and M. Richardson. "On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro." Blood 67, no. 4 (April 1, 1986): 878–86. http://dx.doi.org/10.1182/blood.v67.4.878.bloodjournal674878.
Full textLogston, Brittany B., Emily A. Rodman, Kimberly L. Dinh, Jennifer L. Placencia, Brady S. Moffett, and Danielle R. Rios. "Effect of Exogenous Antithrombin Administration on Anti-Xa Levels in Infants Treated With Enoxaparin." Journal of Pediatric Pharmacology and Therapeutics 23, no. 4 (July 1, 2018): 315–19. http://dx.doi.org/10.5863/1551-6776-23.4.315.
Full textIba, Toshiaki, Tetsuya Sasaki, Kazutoshi Ohshima, Koichi Sato, Isao Nagaoka, and Jecko Thachil. "The Comparison of the Protective Effects of α- and β-Antithrombin against Vascular Endothelial Cell Damage Induced by Histone in Vitro." TH Open 01, no. 01 (June 2017): e3-e10. http://dx.doi.org/10.1055/s-0037-1603926.
Full textErdjument, H., D. A. Lane, H. Ireland, M. Panico, V. Di Marzo, I. Blench, and H. R. Morris. "Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin “Northwick Park”." Journal of Biological Chemistry 262, no. 28 (October 1987): 13381–84. http://dx.doi.org/10.1016/s0021-9258(19)76436-9.
Full textWeiler, J. M., and R. J. Linhardt. "Antithrombin III regulates complement activity in vitro." Journal of Immunology 146, no. 11 (June 1, 1991): 3889–94. http://dx.doi.org/10.4049/jimmunol.146.11.3889.
Full textHayakawa, Mineji, Kazuma Yamakawa, Daisuke Kudo, and Kota Ono. "Optimal Antithrombin Activity Threshold for Initiating Antithrombin Supplementation in Patients With Sepsis-Induced Disseminated Intravascular Coagulation: A Multicenter Retrospective Observational Study." Clinical and Applied Thrombosis/Hemostasis 24, no. 6 (March 8, 2018): 874–83. http://dx.doi.org/10.1177/1076029618757346.
Full textHoffmann, Johannes, Christian Wiedermann, Mathias Juers, Helmut Ostermann, Joachim Kienast, Josef Briegel, Richard Strauss, Brian Warren, and Steven Opal. "Benefit/risk profile of high-dose antithrombin in patients with severe sepsis treated with and without concomitant heparin." Thrombosis and Haemostasis 95, no. 05 (2006): 850–56. http://dx.doi.org/10.1160/th05-07-0530.
Full textDevraj-Kizuk, R., DH Chui, EV Prochownik, CJ Carter, FA Ofosu, and MA Blajchman. "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity." Blood 72, no. 5 (November 1, 1988): 1518–23. http://dx.doi.org/10.1182/blood.v72.5.1518.1518.
Full textDevraj-Kizuk, R., DH Chui, EV Prochownik, CJ Carter, FA Ofosu, and MA Blajchman. "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity." Blood 72, no. 5 (November 1, 1988): 1518–23. http://dx.doi.org/10.1182/blood.v72.5.1518.bloodjournal7251518.
Full textSorial, Mark N., Rebecca A. Greene, Andrew R. Zullo, Christine Berard-Collins, and Steve Willis. "Exogenous supplementation of antithrombin III in adult and pediatric patients receiving extracorporeal membrane oxygenation." International Journal of Artificial Organs 43, no. 5 (November 21, 2019): 315–22. http://dx.doi.org/10.1177/0391398819888932.
Full textSharpe, Christopher J., Mark A. Crowther, and Kathryn E. Webert. "Cerebral Venous Thrombosis During Pregnancy in the Setting of Type I Antithrombin Deficiency: Case Report and Literature Review." Blood 114, no. 22 (November 20, 2009): 4447. http://dx.doi.org/10.1182/blood.v114.22.4447.4447.
Full textJena, Sushanta Kumar, Minakshi Mohanty, Umesh Chandra Patra, and Sanatan Behera. "A study on demographic and clinical profile of children with extra hepatic portal venous obstruction and with special reference to thrombophilic factors." International Journal Of Community Medicine And Public Health 4, no. 3 (February 22, 2017): 640. http://dx.doi.org/10.18203/2394-6040.ijcmph20170468.
Full textKATO, Io, and Tetsuhito KOJIMA. "Antithrombin in clinic." Japanese Journal of Thrombosis and Hemostasis 25, no. 1 (2014): 33–39. http://dx.doi.org/10.2491/jjsth.25.33.
Full textMenache, Doris. "Antithrombin III Concentrates." Hematology/Oncology Clinics of North America 6, no. 5 (October 1992): 1115–20. http://dx.doi.org/10.1016/s0889-8588(18)30298-3.
Full textCarrell, Robin, Richard Skinner, Mark Wardell, and James Whisstock. "Antithrombin and heparin." Molecular Medicine Today 1, no. 5 (August 1995): 226–31. http://dx.doi.org/10.1016/s1357-4310(95)91494-3.
Full textStringer, Kathleen A., and Joann Lindenfeld. "Hirudins: Antithrombin Anticoagulants." Annals of Pharmacotherapy 26, no. 12 (December 1992): 1535–40. http://dx.doi.org/10.1177/106002809202601211.
Full textBeresford, C. H. "Antithrombin III deficiency." Blood Reviews 2, no. 4 (December 1988): 239–50. http://dx.doi.org/10.1016/0268-960x(88)90013-6.
Full textUszynski, Mieczyslaw, Andrzej Kielkowski, Waldemar Uszynski, and Ewa Zekanowska. "Thrombin-Antithrombin III Complexes and Antithrombin III in Amniotic Fluid." Gynecologic and Obstetric Investigation 43, no. 1 (1997): 29–33. http://dx.doi.org/10.1159/000291813.
Full textShiozaki, Arihiro, Takashi Arai, Rikuichi Izumi, Kenji Niiya, and Nobuo Sakuragawa. "Congenital antithrombin III deficient neonate treated with antithrombin III concentrates." Thrombosis Research 70, no. 3 (May 1993): 211–16. http://dx.doi.org/10.1016/0049-3848(93)90127-a.
Full textRodgers, George. "Role of antithrombin concentrate in treatment of hereditary antithrombin deficiency." Thrombosis and Haemostasis 101, no. 05 (2009): 806–12. http://dx.doi.org/10.1160/th08-10-0672.
Full textÁguila, Sonia, Irene Martínez-Martínez, Miriam Collado, Pilar Llamas, Ana Antón, Consuelo Martínez-Redondo, José Padilla, et al. "Compound heterozygosity involving Antithrombin Cambridge II (p.Ala416Ser) in antithrombin deficiency." Thrombosis and Haemostasis 109, no. 03 (2013): 556–58. http://dx.doi.org/10.1160/th12-09-0707.
Full textChan, Anthony K. C., Leslie R. Berry, Nethnapha Paredes, and Nagina Parmar. "Isoform composition of antithrombin in a covalent antithrombin–heparin complex." Biochemical and Biophysical Research Communications 309, no. 4 (October 2003): 986–91. http://dx.doi.org/10.1016/j.bbrc.2003.08.109.
Full textBeauchamp, N. J., R. N. Pike, M. Daly, L. Butler, M. Makris, T. R. Dafforn, A. Zhou, et al. "Antithrombins Wibble and Wobble (T85M/K): Archetypal Conformational Diseases With In Vivo Latent-Transition, Thrombosis, and Heparin Activation." Blood 92, no. 8 (October 15, 1998): 2696–706. http://dx.doi.org/10.1182/blood.v92.8.2696.
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