Contents 1 History 2 Physiology 2.1 Synthesis 2.2 Mechanism of action 2.3 Negative feedback 3 Structure 4 Gene 5 Role in disease 6 Applications 6.1 Research tool 6.2 Medicine and surgery 6.3 Food production 7 See also 8 References 9 Further reading 10 External links


History[edit] After the description of fibrinogen and fibrin, Alexander Schmidt hypothesised the existence of an enzyme that converts fibrinogen into fibrin in 1872.[7]


Physiology[edit] Synthesis[edit] Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). The activity of factor Xa is greatly enhanced by binding to activated Factor V (Va), termed the prothrombinase complex. Prothrombin is produced in the liver and is co-translationally modified in a vitamin K-dependent reaction that converts 10-12 glutamic acids in the N terminus of the molecule to gamma-carboxyglutamic acid (Gla).[8] In the presence of calcium, the Gla residues promote the binding of prothrombin to phospholipid bilayers. Deficiency of vitamin K or administration of the anticoagulant warfarin inhibits the production of gamma-carboxyglutamic acid residues, slowing the activation of the coagulation cascade. In human adults, the normal blood level of antithrombin activity has been measured to be around 1.1 units/mL. Newborn levels of thrombin steadily increase after birth to reach normal adult levels, from a level of around 0.5 units/mL 1 day after birth, to a level of around 0.9 units/mL after 6 months of life.[9] Mechanism of action[edit] In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa. Factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between lysine and glutamine residues in fibrin. The covalent bonds increase the stability of the fibrin clot. Thrombin interacts with thrombomodulin.[10][11] As part of its activity in the coagulation cascade, thrombin also promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet. Negative feedback[edit] Thrombin bound to thrombomodulin activates protein C, an inhibitor of the coagulation cascade. The activation of protein C is greatly enhanced following the binding of thrombin to thrombomodulin, an integral membrane protein expressed by endothelial cells. Activated protein C inactivates factors Va and VIIIa. Binding of activated protein C to protein S leads to a modest increase in its activity. Thrombin is also inactivated by antithrombin, a serine protease inhibitor.


Structure[edit] Anchoring of bovine prothrombin to the membrane through its Gla domain.[12] The molecular weight of prothrombin is approximately 72,000 Da. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36,000 Da. Structurally, it is a member of the large PA clan of proteases. Prothrombin is composed of four domains; an N-terminal Gla domain, two kringle domains and a C-terminal trypsin-like serine protease domain. Factor Xa with factor V as a cofactor leads to cleavage of the Gla and two Kringle domains (forming together a fragment called fragment 1.2) and leave thrombin, consisting solely of the serine protease domain.[13] As is the case for all serine proteases, prothrombin is converted to active thrombin by proteolysis of an internal peptide bond, exposing a new N-terminal Ile-NH3. The historic model of activation of serine proteases involves insertion of this newly formed N-terminus of the heavy chain into the β-barrel promoting the correct conformation of the catalytic residues.[14] Contrary to crystal structures of active thrombin, hydrogen-deuterium exchange mass spectrometry studies indicate that this N-terminal Ile-NH3 does not become inserted into the β-barrel in the apo form of thrombin. However, binding of the active fragment of thrombomodulin appears to allosterically promote the active conformation of thrombin by inserting this N-terminal region.[15]


Gene[edit] The thrombin (prothrombin) gene is located on the eleventh chromosome (11p11-q12).[5] There are an estimated 30 people in the world that have been diagnosed with the congenital form of Factor II deficiency,[16] which should not be confused with the prothrombin G20210A mutation, which is also called the factor II mutation. Prothrombin G20210A is congenital.[17] Prothrombin G20210A is not usually accompanied by other factor mutations (i.e., the most common is factor V Leiden). The gene may be inherited heterozygous (1 pair), or much more rarely, homozygous (2 pairs), and is not related to gender or blood type. Homozygous mutations increase the risk of thrombosis more than heterozygous mutations, but the relative increased risk is not well documented. Other potential risks for thrombosis, such as oral contraceptives may be additive. The previously reported relationship of inflammatory bowel disease (i.e., Crohn's disease or ulcerative colitis) and prothrombin G20210A or factor V Leiden mutation have been contradicted by research.[18]


Role in disease[edit] Activation of prothrombin is crucial in physiological and pathological coagulation. Various rare diseases involving prothrombin have been described (e.g., hypoprothrombinemia). Anti-prothrombin antibodies in autoimmune disease may be a factor in the formation of the lupus anticoagulant also known as (antiphospholipid syndrome). Hyperprothrombinemia can be caused by the G20210A mutation. Thrombin, a potent vasoconstrictor and mitogen, is implicated as a major factor in vasospasm following subarachnoid hemorrhage. Blood from a ruptured cerebral aneurysm clots around a cerebral artery, releasing thrombin. This can induce an acute and prolonged narrowing of the blood vessel, potentially resulting in cerebral ischemia and infarction (stroke). Beyond its key role in the dynamic process of thrombus formation, thrombin has a pronounced pro-inflammatory character, which may influence the onset and progression of atherosclerosis. Acting via its specific cell membrane receptors (protease activated receptors: PAR-1, PAR-3 and PAR-4), which are abundantly expressed in all arterial vessel wall constituents, thrombin has the potential to exert pro-atherogenic actions such as inflammation, leukocyte recruitment into the atherosclerotic plaque, enhanced oxidative stress, migration and proliferation of vascular smooth muscle cells, apoptosis and angiogenesis.[19][20][21] Thrombin is implicated in the physiology of blood clots. Its presence indicates the existence of a clot. In 2013 a system for detecting the presence of thrombin was developed in mice. It combines peptide-coated iron oxide attached to "reporter chemicals". When a peptide binds to a thrombin molecule, the report is released and appears in the urine where it can be detected. Human testing has not been conducted.[22]


Applications[edit] Research tool[edit] Due to its high proteolytic specificity, thrombin is a valuable biochemical tool. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is commonly included in linker regions of recombinant fusion protein constructs. Following purification of the fusion protein, thrombin can be used to selectively cleave between the Arginine and Glycine residues of the cleavage site, effectively removing the purification tag from the protein of interest with a high degree of specificity. Medicine and surgery[edit] Prothrombin complex concentrate and fresh frozen plasma are prothrombin-rich coagulation factor preparations that can be used to correct deficiencies (usually due to medication) of prothrombin. Indications include intractable bleeding due to warfarin. Manipulation of prothrombin is central to the mode of action of most anticoagulants. Warfarin and related drugs inhibit vitamin K-dependent carboxylation of several coagulation factors, including prothrombin. Heparin increases the affinity of antithrombin to thrombin (as well as factor Xa). The direct thrombin inhibitors, a newer class of medication, directly inhibit thrombin by binding to its active site. Recombinant thrombin is available as a powder for reconstitution into aqueous solution. It can be applied topically during surgery, as an aid to hemostasis. It can be useful for controlling minor bleeding from capillaries and small venules, but ineffective and not indicated for massive or brisk arterial bleeding.[23][24][25] Food production[edit] Thrombin is sold under the brand name Fibrimex for use as a binding agent for meat. The thrombin in Fibrimex derives from porcine or bovine blood.[26] According to the manufacturer it can be used to produce new kinds of mixed meats (for example combining beef and fish seamlessly). The manufacturer also states that it can be used to combine whole muscle meat, form and portion these thus cutting down on production costs without a loss in quality.[27] General secretary Jan Bertoft of Swedish Consumers' Association has stated that "there is danger of misleading the consumers since there is no way to tell this reconstituted meat from real meat"[26]


See also[edit] Cerastocytin Fibrin glue Fibrinogen PA clan of proteases The Proteolysis Map


References[edit] ^ a b c GRCh38: Ensembl release 89: ENSG00000180210 - Ensembl, May 2017 ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027249 - Ensembl, May 2017 ^ "Human PubMed Reference:".  ^ "Mouse PubMed Reference:".  ^ a b Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular Genetics. 13 (3): 285–92. doi:10.1007/BF01535211. PMID 3474786.  ^ Degen SJ, Davie EW (September 1987). "Nucleotide sequence of the gene for human prothrombin". Biochemistry. 26 (19): 6165–77. doi:10.1021/bi00393a033. PMID 2825773.  ^ Schmidt A (1872). "Neue Untersuchungen ueber die Fasserstoffesgerinnung". Pflüger's Archiv für die gesamte Physiologie. 6: 413–538. doi:10.1007/BF01612263.  ^ Knorre, DG; Kudryashova, NV; Godovikova, TS (October 2009). "Chemical and Functional Aspects of Posttranslational Modification of Proteins". Acta Nature. 1 (3): 29-51.  |access-date= requires |url= (help) ^ Andrew M, Paes B, Milner R, Johnston M, Mitchell L, Tollefsen DM, Powers P (July 1987). "Development of the human coagulation system in the full-term infant". Blood. 70 (1): 165–72. PMID 3593964.  ^ Bajzar L, Morser J, Nesheim M (July 1996). "TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex". The Journal of Biological Chemistry. 271 (28): 16603–8. doi:10.1074/jbc.271.28.16603. PMID 8663147.  ^ Jakubowski HV, Owen WG (July 1989). "Macromolecular specificity determinants on thrombin for fibrinogen and thrombomodulin". The Journal of Biological Chemistry. 264 (19): 11117–21. PMID 2544585.  ^ PDB: 1nl2​; Huang M, Rigby AC, Morelli X, Grant MA, Huang G, Furie B, Seaton B, Furie BC (September 2003). "Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins". Nature Structural Biology. 10 (9): 751–6. doi:10.1038/nsb971. PMID 12923575.  ^ Davie EW, Kulman JD (April 2006). "An overview of the structure and function of thrombin". Seminars in Thrombosis and Hemostasis. 32 Suppl 1: 3–15. doi:10.1055/s-2006-939550. PMID 16673262.  ^ Huber, Robert; Bode, Wolfram (1978-03-01). "Structural basis of the activation and action of trypsin". Accounts of Chemical Research. 11 (3): 114–122. doi:10.1021/ar50123a006. ISSN 0001-4842.  ^ Handley LD, Treuheit NA, Venkatesh VJ, Komives EA (November 2015). "Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin". Biochemistry. 54 (43): 6650–8. doi:10.1021/acs.biochem.5b00825. PMC 4697735 . PMID 26468766.  ^ Degen SJ, McDowell SA, Sparks LM, Scharrer I (February 1995). "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala". Thrombosis and Haemostasis. 73 (2): 203–9. PMID 7792730.  ^ Varga EA, Moll S (July 2004). "Cardiology patient pages. Prothrombin 20210 mutation (factor II mutation)". Circulation. 110 (3): e15–8. doi:10.1161/01.CIR.0000135582.53444.87. PMID 15262854.  ^ Bernstein CN, Sargent M, Vos HL, Rosendaal FR (February 2007). "Mutations in clotting factors and inflammatory bowel disease". The American Journal of Gastroenterology. 102 (2): 338–43. doi:10.1111/j.1572-0241.2006.00974.x. PMID 17156138.  ^ Borissoff JI, Spronk HM, Heeneman S, ten Cate H (June 2009). "Is thrombin a key player in the 'coagulation-atherogenesis' maze?". Cardiovascular Research. 82 (3): 392–403. doi:10.1093/cvr/cvp066. PMID 19228706.  ^ Borissoff JI, Heeneman S, Kilinç E, Kassák P, Van Oerle R, Winckers K, Govers-Riemslag JW, Hamulyák K, Hackeng TM, Daemen MJ, ten Cate H, Spronk HM (August 2010). "Early atherosclerosis exhibits an enhanced procoagulant state". Circulation. 122 (8): 821–30. doi:10.1161/CIRCULATIONAHA.109.907121. PMID 20697022.  ^ Borissoff JI, Spronk HM, ten Cate H (May 2011). "The hemostatic system as a modulator of atherosclerosis". The New England Journal of Medicine. 364 (18): 1746–60. doi:10.1056/NEJMra1011670. PMID 21542745.  ^ Economist (2013-11-05). "Nanomedicine: Particle physiology". The Economist. Retrieved 2013-12-15.  ^ Chapman WC, Singla N, Genyk Y, McNeil JW, Renkens KL, Reynolds TC, Murphy A, Weaver FA (August 2007). "A phase 3, randomized, double-blind comparative study of the efficacy and safety of topical recombinant human thrombin and bovine thrombin in surgical hemostasis". Journal of the American College of Surgeons. 205 (2): 256–65. doi:10.1016/j.jamcollsurg.2007.03.020. PMID 17660072.  ^ Singla NK, Ballard JL, Moneta G, Randleman CD, Renkens KL, Alexander WA (July 2009). "A phase 3b, open-label, single-group immunogenicity and safety study of topical recombinant thrombin in surgical hemostasis". Journal of the American College of Surgeons. 209 (1): 68–74. doi:10.1016/j.jamcollsurg.2009.03.016. PMID 19651065.  ^ Greenhalgh DG, Gamelli RL, Collins J, Sood R, Mozingo DW, Gray TE, Alexander WA (2009). "Recombinant thrombin: safety and immunogenicity in burn wound excision and grafting". Journal of Burn Care & Research. 30 (3): 371–9. doi:10.1097/BCR.0b013e3181a28979. PMID 19349898.  ^ a b "Sverige röstade ja till köttklister" [Sweden voted in favor of the meat paste] (in Swedish). Dagens Nyheter. 2010-02-09. Retrieved 2010-10-17.  ^ "Welcome to Fibrimex". Fibrimex website. FX Technology. Retrieved 2010-10-17. 


Further reading[edit] Esmon CT (July 1995). "Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface". FASEB Journal. 9 (10): 946–55. PMID 7615164.  Wu H, Zhang Z, Li Y, Zhao R, Li H, Song Y, Qi J, Wang J (October 2010). "Time course of upregulation of inflammatory mediators in the hemorrhagic brain in rats: correlation with brain edema". Neurochemistry International. 57 (3): 248–53. doi:10.1016/j.neuint.2010.06.002. PMC 2910823 . PMID 20541575.  Lenting PJ, van Mourik JA, Mertens K (December 1998). "The life cycle of coagulation factor VIII in view of its structure and function". Blood. 92 (11): 3983–96. PMID 9834200.  Plow EF, Cierniewski CS, Xiao Z, Haas TA, Byzova TV (July 2001). "AlphaIIbbeta3 and its antagonism at the new millennium". Thrombosis and Haemostasis. 86 (1): 34–40. PMID 11487023.  Maragoudakis ME, Tsopanoglou NE, Andriopoulou P (April 2002). "Mechanism of thrombin-induced angiogenesis". Biochemical Society Transactions. 30 (2): 173–7. doi:10.1042/BST0300173. PMID 12023846.  Han X, Lan X, Li Q, Gao Y, Zhu W, Cheng T, Maruyama T, Wang J (June 2016). "Inhibition of prostaglandin E2 receptor EP3 mitigates thrombin-induced brain injury". Journal of Cerebral Blood Flow and Metabolism. 36 (6): 1059–74. doi:10.1177/0271678X15606462. PMID 26661165.  Howell DC, Laurent GJ, Chambers RC (April 2002). "Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis". Biochemical Society Transactions. 30 (2): 211–6. doi:10.1042/BST0300211. PMID 12023853.  Firth SM, Baxter RC (December 2002). "Cellular actions of the insulin-like growth factor binding proteins". Endocrine Reviews. 23 (6): 824–54. doi:10.1210/er.2001-0033. PMID 12466191.  Minami T, Sugiyama A, Wu SQ, Abid R, Kodama T, Aird WC (January 2004). "Thrombin and phenotypic modulation of the endothelium". Arteriosclerosis, Thrombosis, and Vascular Biology. 24 (1): 41–53. doi:10.1161/01.ATV.0000099880.09014.7D. PMID 14551154.  De Cristofaro R, De Candia E (June 2003). "Thrombin domains: structure, function and interaction with platelet receptors". Journal of Thrombosis and Thrombolysis. 15 (3): 151–63. doi:10.1023/B:THRO.0000011370.80989.7b. PMID 14739624.  Tsopanoglou NE, Maragoudakis ME (February 2004). "Role of thrombin in angiogenesis and tumor progression". Seminars in Thrombosis and Hemostasis. 30 (1): 63–9. doi:10.1055/s-2004-822971. PMID 15034798.  Bode W (2007). "Structure and interaction modes of thrombin". Blood Cells, Molecules & Diseases. 36 (2): 122–30. doi:10.1016/j.bcmd.2005.12.027. PMID 16480903.  Wolberg AS (May 2007). "Thrombin generation and fibrin clot structure". Blood Reviews. 21 (3): 131–42. doi:10.1016/j.blre.2006.11.001. PMID 17208341.  Degen S: Prothrombin. In: High K, Roberts H, eds. Molecular Basis of Thrombosis and Hemostasis. New York, NY: Marcel Dekker; 1995:75.


External links[edit] The MEROPS online database for peptidases and their inhibitors: S01.217 GeneReviews/NCBI/NIH/UW entry on Prothrombin Thrombophilia Anti-coagulation & proteases on YouTube by The Proteolysis Map-animation [1] PMAP: The Proteolysis Map/Thrombin Thrombin: RCSB PDB Molecule of the Month Prothrombin Structure v t e PDB gallery 1a2c: STRUCTURE OF THROMBIN INHIBITED BY AERUGINOSIN298-A FROM A BLUE-GREEN ALGA  1a3b: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG1  1a3e: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG2  1a46: THROMBIN COMPLEXED WITH HIRUGEN AND A BETA-STRAND MIMETIC INHIBITOR  1a4w: CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1' BINDING SITE  1a5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN  1a61: THROMBIN COMPLEXED WITH A BETA-MIMETIC THIAZOLE-CONTAINING INHIBITOR  1abi: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS  1abj: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS  1ad8: COMPLEX OF THROMBIN WITH AND INHIBITOR CONTAINING A NOVEL P1 MOIETY  1ae8: HUMAN ALPHA-THROMBIN INHIBITION BY EOC-D-PHE-PRO-AZALYS-ONP  1aht: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND P-AMIDINOPHENYLPYRUVATE) AT 1.6 ANGSTROMS RESOLUTION  1ai8: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG  1aix: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL  1awf: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT  1awh: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT  1ay6: THROMBIN INHIBITOR FROM THEONALLA, CYCLOTHEANAMIDE-BASED MACROCYCLIC TRIPEPTIDE MOTIF  1b5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN  1b7x: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225I MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE  1ba8: THROMBIN INHIBITOR WITH A RIGID TRIPEPTIDYL ALDEHYDES  1bb0: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES  1bbr: THE STRUCTURE OF RESIDUES 7-16 OF THE A ALPHA CHAIN OF HUMAN FIBRINOGEN BOUND TO BOVINE THROMBIN AT 2.3 ANGSTROMS RESOLUTION  1bcu: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN  1bhx: X-RAY STRUCTURE OF THE COMPLEX OF HUMAN ALPHA THROMBIN WITH THE INHIBITOR SDZ 229-357  1bth: STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR  1c1u: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES  1c1v: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES  1c1w: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES  1c4u: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.  1c4v: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.  1c4y: SELECTIVE NON-ELECTROPHILIC THROMBIN INHIBITORS  1c5l: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR  1c5n: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR  1c5o: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR  1ca8: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES  1d3d: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZOTHIOPHENE INHIBITOR 4  1d3p: CRYSTAL STRUCTURE OF HUMAN APLHA-THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 3  1d3q: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 2  1d3t: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 1  1d4p: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH 5-AMIDINOINDOLE-4-BENZYLPIPERIDINE INHIBITOR  1d6w: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTROPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1  1d9i: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTOPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1  1de7: INTERACTION OF FACTOR XIII ACTIVATION PEPTIDE WITH ALPHA-THROMBIN: CRYSTAL STRUCTURE OF THE ENZYME-SUBSTRATE COMPLEX  1dit: COMPLEX OF A DIVALENT INHIBITOR WITH THROMBIN  1dm4: SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)  1doj: Crystal structure of human alpha-thrombin*RWJ-51438 complex at 1.7 A  1dwb: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS  1dwc: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS  1dwd: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS  1dwe: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS  1dx5: CRYSTAL STRUCTURE OF THE THROMBIN-THROMBOMODULIN COMPLEX  1e0f: CRYSTAL STRUCTURE OF THE HUMAN ALPHA-THROMBIN-HAEMADIN COMPLEX: AN EXOSITE II-BINDING INHIBITOR  1eb1: COMPLEX STRUCTURE OF HUMAN THROMBIN WITH N-METHYL-ARGININE INHIBITOR  1eoj: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES  1eol: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES  1fpc: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN  1fph: THE INTERACTION OF THROMBIN WITH FIBRINOGEN: A STRUCTURAL BASIS FOR ITS SPECIFICITY  1g30: THROMBIN INHIBITOR COMPLEX  1g32: THROMBIN INHIBITOR COMPLEX  1g37: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH-10556 AND EXOSITE-DIRECTED PEPTIDE  1ghv: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE  1ghw: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE  1ghx: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE  1ghy: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE  1gj4: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN  1gj5: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN  1h8d: X-RAY STRUCTURE OF THE HUMAN ALPHA-THROMBIN COMPLEX WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.  1h8i: X-RAY CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.  1hag: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN  1hah: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN  1hai: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN  1hao: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON NMR MODEL OF DNA  1hap: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON X-RAY MODEL OF DNA)  1hbt: HUMAN ALPHA-THROMBIN COMPLEXED WITH A PEPTIDYL PYRIDINIUM METHYL KETONE CONTAINING BIVALENT INHIBITOR  1hdt: STRUCTURE OF A RETRO-BINDING PEPTIDE INHIBITOR COMPLEXED WITH HUMAN ALPHA-THROMBIN  1hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN  1hlt: THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN  1hut: THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER  1hxe: SERINE PROTEASE  1hxf: HUMAN THROMBIN COMPLEX WITH HIRUDIN VARIANT  1ihs: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-6  1iht: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-6  1jmo: Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex  1jou: Crystal Structure of Native S195A Thrombin with an Unoccupied Active Site  1jwt: CRYSTAL STRUCTURE OF THROMBIN IN COMPLEX WITH A NOVEL BICYCLIC LACTAM INHIBITOR  1k21: HUMAN THROMBIN-INHIBITOR COMPLEX  1k22: HUMAN THROMBIN-INHIBITOR COMPLEX  1kts: Thrombin Inhibitor Complex  1ktt: Thrombin inhibitor complex  1lhc: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROARG-OH  1lhd: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH  1lhe: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-N-BUTYL-AMIDINO-GLYCINE-OH  1lhf: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-HOMOLYS-OH  1lhg: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROORNITHINE-OH  1mh0: Crystal structure of the anticoagulant slow form of thrombin  1mu6: Crystal Structure of Thrombin in Complex with L-378,622  1mu8: thrombin-hirugen_l-378,650  1mue: Thrombin-Hirugen-L405,426  1nm6: thrombin in complex with selective macrocyclic inhibitor at 1.8A  1no9: Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: molecular and X-ray crystallographic studies.  1nrn: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nro: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nrp: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nrq: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nrr: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nrs: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES  1nt1: thrombin in complex with selective macrocyclic inhibitor  1nu7: Staphylocoagulase-Thrombin Complex  1nu9: Staphylocoagulase-Prethrombin-2 complex  1ny2: Human alpha thrombin inhibited by RPPGF and hirugen  1nzq: D-Phe-Pro-Arg-Type Thrombin Inhibitor  1o0d: Human Thrombin complexed with a d-Phe-Pro-Arg-type Inhibitor and a C-terminal Hirudin derived exo-site inhibitor  1o2g: Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors  1o5g: Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)  1ook: Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin  1oyt: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED FLUORINATED INHIBITOR  1p8v: CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A  1ppb: THE REFINED 1.9 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN: INTERACTION WITH D-PHE-PRO-ARG CHLOROMETHYLKETONE AND SIGNIFICANCE OF THE TYR-PRO-PRO-TRP INSERTION SEGMENT  1qbv: CRYSTAL STRUCTURE OF THROMBIN COMPLEXED WITH AN GUANIDINE-MIMETIC INHIBITOR  1qhr: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS  1qj1: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS  1qj6: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS  1qj7: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS  1qur: HUMAN ALPHA-THROMBIN IN COMPLEX WITH BIVALENT, BENZAMIDINE-BASED SYNTHETIC INHIBITOR  1rd3: 2.5A Structure of Anticoagulant Thrombin Variant E217K  1riw: Thrombin in complex with natural product inhibitor Oscillarin  1sb1: Novel Non-Covalent Thrombin Inhibitors Incorporating P1 4,5,6,7-Tetrahydrobenzothiazole Arginine Side Chain Mimetics  1sfq: Fast form of thrombin mutant R(77a)A bound to PPACK  1sgi: Crystal structure of the anticoagulant slow form of thrombin  1shh: Slow form of Thrombin Bound with PPACK  1sl3: crystal structure of Thrombin in complex with a potent P1 heterocycle-Aryl based inhibitor  1sr5: ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE  1t4u: Crystal Structure Analysis of a novel Oxyguanidine bound to Thrombin  1t4v: Crystal Structure Analysis of a novel Oxyguanidine bound to Thrombin  1ta2: Crystal structure of thrombin in complex with compound 1  1ta6: Crystal structure of thrombin in complex with compound 14b  1tb6: 2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex  1tbz: HUMAN THROMBIN WITH ACTIVE SITE N-METHYL-D PHENYLALANYL-N-[5-(AMINOIMINOMETHYL)AMINO]-1-[(BENZOTHIAZOLYL)CARBONYL] BUTYL]-L-PROLINAMIDE TRIFLUROACETATE AND EXOSITE-HIRUGEN  1thp: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225P MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE  1thr: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR  1ths: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR  1tmb: MOLECULAR BASIS FOR THE INHIBITION OF HUMAN ALPHA-THROMBIN BY THE MACROCYCLIC PEPTIDE CYCLOTHEONAMIDE A  1tmt: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS  1tmu: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS  1tom: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN  1tq0: Crystal structure of the potent anticoagulant thrombin mutant W215A/E217A in free form  1tq7: Crystal structure of the anticoagulant thrombin mutant W215A/E217A bound to PPACK  1twx: Crystal structure of the thrombin mutant D221A/D222K  1ucy: THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A ALPHA (RESIDUES 7-19). THREE COMPLEXES, ONE WITH EPSILON-THROMBIN AND TWO WITH ALPHA-THROMBIN  1uma: ALPHA-THROMBIN (HIRUGEN) COMPLEXED WITH NA-(N,N-DIMETHYLCARBAMOYL)-ALPHA-AZALYSINE  1uvs: BOVINE THROMBIN--BM51.1011 COMPLEX  1vit: THROMBIN:HIRUDIN 51-65 COMPLEX  1vr1: Specificity for Plasminogen Activator Inhibitor-1  1vzq: COMPLEX OF THROMBIN WITH DESIGNED INHIBITOR 7165  1w7g: ALPHA-THROMBIN COMPLEX WITH SULFATED HIRUDIN (RESIDUES 54-65) AND L-ARGININE TEMPLATE INHIBITOR CS107  1way: ACTIVE SITE THROMBIN INHIBITORS  1wbg: ACTIVE SITE THROMBIN INHIBITORS  1xm1: Nonbasic Thrombin Inhibitor Complex  1xmn: Crystal structure of thrombin bound to heparin  1ycp: THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16  1ype: Thrombin Inhibitor Complex  1ypg: Thrombin Inhibitor Complex  1ypj: Thrombin Inhibitor Complex  1ypk: Thrombin Inhibitor Complex  1ypl: X-ray crystal structure of thrombin inhibited by synthetic cyanopeptide analogue RA-1008  1ypm: X-ray crystal structure of thrombin inhibited by synthetic cyanopeptide analogue RA-1014  1z71: thrombin and P2 pyridine N-oxide inhibitor complex structure  1z8i: Crystal structure of the thrombin mutant G193A bound to PPACK  1z8j: Crystal structure of the thrombin mutant G193P bound to PPACK  1zgi: thrombin in complex with an oxazolopyridine inhibitor 21  1zgv: Thrombin in complex with an oxazolopyridine inhibitor 2  1zrb: Thrombin in complex with an azafluorenyl inhibitor 23b  2a0q: Structure of thrombin in 400 mM potassium chloride  2a2x: Orally Active Thrombin Inhibitors in Complex with Thrombin Inh12  2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin  2afq: 1.9 angstrom crytal structure of wild-type human thrombin in the sodium free state  2ank: orally active thrombin inhibitors in complex with thrombin and an exosite decapeptide  2anm: Ternary complex of an orally active thrombin inhibitor with human thrombin and a c-terminal hirudin derived exo-sit inhibitor  2b5t: 2.1 Angstrom structure of a nonproductive complex between antithrombin, synthetic heparin mimetic SR123781 and two S195A thrombin molecules  2bdy: thrombin in complex with inhibitor  2bvr: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET  2bvs: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET  2bvx: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER  2bxt: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER  2bxu: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER  2c8w: THROMBIN INHIBITORS  2c8x: THROMBIN INHIBITORS  2c8y: THROMBIN INHIBITORS  2c8z: THROMBIN INHIBITORS  2c90: THROMBIN INHIBITORS  2c93: THROMBIN INHIBITORS  2cf8: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR  2cf9: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR  2cn0: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED INHIBITOR  2feq: orally active thrombin inhibitors  2fes: Orally active thrombin inhibitors  2gde: Thrombin in complex with inhibitor  2gp9: Crystal structure of the slow form of thrombin in a self-inhibited conformation  2h9t: Crystal structure of human alpha-thrombin in complex with suramin  2hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN  2hnt: CRYSTALLOGRAPHIC STRUCTURE OF HUMAN GAMMA-THROMBIN  2hpp: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN  2hpq: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN  2hwl: Crystal structure of thrombin in complex with fibrinogen gamma' peptide  2jh0: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.  2jh5: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.  2jh6: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.  2od3: Human thrombin chimera with human residues 184a, 186, 186a, 186b, 186c and 222 replaced by murine thrombin equivalents.  2thf: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE  3hat: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN  4htc: THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX  4thn: THE CRYSTAL STRUCTURE OF ALPHA-THROMBIN-HIRUNORM IV COMPLEX REVEALS A NOVEL SPECIFICITY SITE RECOGNITION MODE.  5gds: HIRUNORMS ARE TRUE HIRUDIN MIMETICS. THE CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN:HIRUNORM V COMPLEX  7kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2711.  8kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2770.  v t e Proteins involved in coagulation Coagulation factors Primary hemostasis vWF platelet membrane glycoproteins: Ib (A B IX) IIb/IIIa (IIb IIIa) VI Intrinsic pathway HMWK/Bradykinin Prekallikrein/Kallikrein XII "Hageman" XI IX VIII Extrinsic pathway III "Tissue factor" VII Common pathway X V II "(Pro)thrombin" I "Fibrin" Fibrinogen (FGA, FGG) XIII Coagulation inhibitors Antithrombin (inhibits II, IX, X, XI, XII) Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) Protein Z (inhibits X) ZPI (inhibits X, XI) TFPI (inhibits III) Thrombolysis/fibrinolysis Plasmin tPA/urokinase PAI-1/2 α2-AP α2-macroglobulin TAFI v t e Antigens: Autoantigens Dehydrogenase Branched-chain alpha-keto acid dehydrogenase complex Oxoglutarate dehydrogenase Pyruvate dehydrogenase Transglutaminase Epidermal transglutaminase Tissue transglutaminase Nucleoporins NUP35 NUP37 NUP43 NUP50 NUP54 NUP62 NUP85 NUP88 NUP93 NUP98 NUP107 NUP133 NUP153 NUP155 NUP160 NUP188 NUP210 NUP205 NUP214 Other Acetylcholine receptor Actin Apolipoprotein H Cardiolipin Centromere Filaggrin (Citrullinate) Gangliosides Sp100 nuclear antigen Thrombin Topoisomerase v t e Antihemorrhagics (B02) Antihemorrhagics (coagulation) Systemic Vitamin K Phytomenadione (K1) Menadione (K3) Coagulation factors intrinsic: IX/Nonacog alfa VIII/Moroctocog alfa/Turoctocog alfa extrinsic: VII/Eptacog alfa common: X II/Thrombin I/Fibrinogen XIII/Catridecacog combinations: Prothrombin complex concentrate (II, VII, IX, X, protein C and S) Other systemic Etamsylate Carbazochrome Batroxobin thrombopoietin receptor agonist (Romiplostim Eltrombopag) Local Absorbable gelatin sponge Oxidized cellulose Tetragalacturonic acid hydroxymethylester Thrombin Collagen Calcium alginate Epinephrine/Adrenalone Antifibrinolytics amino acids (Aminocaproic acid Tranexamic acid Aminomethylbenzoic acid) serpins (Aprotinin Alfa1 antitrypsin C1-inhibitor Camostat) v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21) Digestive enzymes Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic Coagulation factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator Complement system Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase Other immune system Chymase Granzyme Tryptase Proteinase 3/Myeloblastin Venombin Ancrod Batroxobin Other Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) Molecular and Cellular Biology portal Retrieved from "https://en.wikipedia.org/w/index.php?title=Thrombin&oldid=809922124" Categories: Genes on human chromosome 11Coagulation systemAcute phase proteinsEC 3.4.21Peripheral membrane proteinsHidden categories: Pages using citations with accessdate and no URLCS1 Swedish-language sources (sv)


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Thrombin - Photos and All Basic Informations

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Protein Data BankGene NomenclatureMendelian Inheritance In ManMouse Genome InformaticsHomoloGeneGeneCardsChromosome 11 (human)ChromosomeChromosome 11 (human)Chromosome 11 (human)Genomic Location For F2Genomic Location For F2Locus (genetics)Base PairBase PairChromosome 2 (mouse)ChromosomeChromosome 2 (mouse)Genomic Location For F2Genomic Location For F2Locus (genetics)Base PairBase PairGene ExpressionGene OntologyEntrezEnsemblUniProtPubMedWikidataEnlargeEnzyme Commission NumberSerine ProteaseEnzymeGeneProteolysisCoagulationFibrinogenFibrinAlexander Schmidt (physiologist)ProthrombinFactor XFactor VVitamin KGamma-carboxyglutamic AcidWarfarinAntithrombinFactor XIFactor VIIIFactor VFibrinogenFibrinFactor XIIIFactor XIIIaTransglutaminaseProtein-protein InteractionThrombomodulinPlateletProtease-activated ReceptorProtein CThrombomodulinProteinEndothelialProtein SAntithrombinSerpinEnlargeGla DomainAtomic Mass UnitPA ClanGla DomainKringle DomainTrypsinSerine ProteaseFactor XaFactor VSerine ProteaseProthrombinBeta BarrelThrombomodulinChromosomeProthrombin G20210AHeterozygousHomozygousThrombosisInflammatory Bowel DiseaseCrohn's DiseaseUlcerative ColitisFactor VHypoprothrombinemiaAntibodyAutoimmune DiseaseLupus AnticoagulantAntiphospholipid SyndromeHyperprothrombinemiaVasoconstrictorMitogenVasospasmSubarachnoid HemorrhageCerebral AneurysmArteryCerebral IschemiaInfarctionStrokeBlood ClotIron OxideUrineRecombinant Fusion ProteinPurification TagProthrombin Complex ConcentrateFresh Frozen PlasmaWarfarinAnticoagulantWarfarinVitamin KHeparinFactor XDirect Thrombin InhibitorAqueous SolutionTopicalHemostasisPorcineBovineSwedish Consumers' AssociationCerastocytinFibrin GlueFibrinogenPA ClanThe Proteolysis MapEnsembl Genome Database ProjectEnsembl Genome Database ProjectProthrombinCeruloplasminDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierHelp:CS1 ErrorsPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierProtein Data BankDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierInternational Standard Serial NumberDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierMEROPSYouTubeThe Proteolysis MapThe Proteolysis MapTemplate:PDB GalleryTemplate Talk:PDB Gallery1a2c: STRUCTURE OF THROMBIN INHIBITED BY AERUGINOSIN298-A FROM A BLUE-GREEN ALGA1a3b: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG11a3e: COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG21a46: THROMBIN COMPLEXED WITH HIRUGEN AND A BETA-STRAND MIMETIC INHIBITOR1a4w: CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1' BINDING SITE1a5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN1a61: THROMBIN COMPLEXED WITH A BETA-MIMETIC THIAZOLE-CONTAINING INHIBITOR1abi: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS1abj: STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF THE S' SUBSITES OF SUBSTRATES AND INHIBITORS1ad8: COMPLEX OF THROMBIN WITH AND INHIBITOR CONTAINING A NOVEL P1 MOIETY1ae8: HUMAN ALPHA-THROMBIN INHIBITION BY EOC-D-PHE-PRO-AZALYS-ONP1aht: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND P-AMIDINOPHENYLPYRUVATE) AT 1.6 ANGSTROMS RESOLUTION1ai8: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG1aix: HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL1awf: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT1awh: NOVEL COVALENT THROMBIN INHIBITOR FROM PLANT EXTRACT1ay6: THROMBIN INHIBITOR FROM THEONALLA, CYCLOTHEANAMIDE-BASED MACROCYCLIC TRIPEPTIDE MOTIF1b5g: HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN1b7x: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225I MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE1ba8: THROMBIN INHIBITOR WITH A RIGID TRIPEPTIDYL ALDEHYDES1bb0: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES1bbr: THE STRUCTURE OF RESIDUES 7-16 OF THE A ALPHA CHAIN OF HUMAN FIBRINOGEN BOUND TO BOVINE THROMBIN AT 2.3 ANGSTROMS RESOLUTION1bcu: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN1bhx: X-RAY STRUCTURE OF THE COMPLEX OF HUMAN ALPHA THROMBIN WITH THE INHIBITOR SDZ 229-3571bth: STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR1c1u: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES1c1v: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES1c1w: RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES1c4u: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.1c4v: SELECTIVE NON ELECTROPHILIC THROMBIN INHIBITORS WITH CYCLOHEXYL MOIETIES.1c4y: SELECTIVE NON-ELECTROPHILIC THROMBIN INHIBITORS1c5l: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR1c5n: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR1c5o: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR1ca8: THROMBIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES1d3d: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZOTHIOPHENE INHIBITOR 41d3p: CRYSTAL STRUCTURE OF HUMAN APLHA-THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 31d3q: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 21d3t: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH BENZO[B]THIOPHENE INHIBITOR 11d4p: CRYSTAL STRUCTURE OF HUMAN ALPHA THROMBIN IN COMPLEX WITH 5-AMIDINOINDOLE-4-BENZYLPIPERIDINE INHIBITOR1d6w: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTROPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P11d9i: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTOPHILIC INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P11de7: INTERACTION OF FACTOR XIII ACTIVATION PEPTIDE WITH ALPHA-THROMBIN: CRYSTAL STRUCTURE OF THE ENZYME-SUBSTRATE COMPLEX1dit: COMPLEX OF A DIVALENT INHIBITOR WITH THROMBIN1dm4: SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)1doj: Crystal Structure Of Human Alpha-thrombin*RWJ-51438 Complex At 1.7 A1dwb: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS1dwc: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS1dwd: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS1dwe: CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS1dx5: CRYSTAL STRUCTURE OF THE THROMBIN-THROMBOMODULIN COMPLEX1e0f: CRYSTAL STRUCTURE OF THE HUMAN ALPHA-THROMBIN-HAEMADIN COMPLEX: AN EXOSITE II-BINDING INHIBITOR1eb1: COMPLEX STRUCTURE OF HUMAN THROMBIN WITH N-METHYL-ARGININE INHIBITOR1eoj: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES1eol: DESIGN OF P1' AND P3' RESIDUES OF TRIVALENT THROMBIN INHIBITORS AND THEIR CRYSTAL STRUCTURES1fpc: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN1fph: THE INTERACTION OF THROMBIN WITH FIBRINOGEN: A STRUCTURAL BASIS FOR ITS SPECIFICITY1g30: THROMBIN INHIBITOR COMPLEX1g32: THROMBIN INHIBITOR COMPLEX1g37: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH-10556 AND EXOSITE-DIRECTED PEPTIDE1ghv: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE1ghw: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE1ghx: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE1ghy: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE1gj4: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN1gj5: SELECTIVITY AT S1, H2O DISPLACEMENT, UPA, TPA, SER190/ALA190 PROTEASE, STRUCTURE-BASED DRUG DESIGN1h8d: X-RAY STRUCTURE OF THE HUMAN ALPHA-THROMBIN COMPLEX WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.1h8i: X-RAY CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN WITH A TRIPEPTIDE PHOSPHONATE INHIBITOR.1hag: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN1hah: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN1hai: THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN1hao: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON NMR MODEL OF DNA1hap: COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON X-RAY MODEL OF DNA)1hbt: HUMAN ALPHA-THROMBIN COMPLEXED WITH A PEPTIDYL PYRIDINIUM METHYL KETONE CONTAINING BIVALENT INHIBITOR1hdt: STRUCTURE OF A RETRO-BINDING PEPTIDE INHIBITOR COMPLEXED WITH HUMAN ALPHA-THROMBIN1hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN1hlt: THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN1hut: THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER1hxe: SERINE PROTEASE1hxf: HUMAN THROMBIN COMPLEX WITH HIRUDIN VARIANT1ihs: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-61iht: CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN ALPHA-THROMBIN AND NON-HYDROLYZABLE BIFUNCTIONAL INHIBITORS, HIRUTONIN-2 AND HIRUTONIN-61jmo: Crystal Structure Of The Heparin Cofactor II-S195A Thrombin Complex1jou: Crystal Structure Of Native S195A Thrombin With An Unoccupied Active Site1jwt: CRYSTAL STRUCTURE OF THROMBIN IN COMPLEX WITH A NOVEL BICYCLIC LACTAM INHIBITOR1k21: HUMAN THROMBIN-INHIBITOR COMPLEX1k22: HUMAN THROMBIN-INHIBITOR COMPLEX1kts: Thrombin Inhibitor Complex1ktt: Thrombin Inhibitor Complex1lhc: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROARG-OH1lhd: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH1lhe: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-N-BUTYL-AMIDINO-GLYCINE-OH1lhf: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BORO-HOMOLYS-OH1lhg: HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROORNITHINE-OH1mh0: Crystal Structure Of The Anticoagulant Slow Form Of Thrombin1mu6: Crystal Structure Of Thrombin In Complex With L-378,6221mu8: Thrombin-hirugen_l-378,6501mue: Thrombin-Hirugen-L405,4261nm6: Thrombin In Complex With Selective Macrocyclic Inhibitor At 1.8A1no9: Design Of Weakly Basic Thrombin Inhibitors Incorporating Novel P1 Binding Functions: Molecular And X-ray Crystallographic Studies.1nrn: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nro: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nrp: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nrq: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nrr: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nrs: CRYSTALLOGRAPHIC STRUCTURES OF THROMBIN COMPLEXED WITH THROMBIN RECEPTOR PEPTIDES: EXISTENCE OF EXPECTED AND NOVEL BINDING MODES1nt1: Thrombin In Complex With Selective Macrocyclic Inhibitor1nu7: Staphylocoagulase-Thrombin Complex1nu9: Staphylocoagulase-Prethrombin-2 Complex1ny2: Human Alpha Thrombin Inhibited By RPPGF And Hirugen1nzq: D-Phe-Pro-Arg-Type Thrombin Inhibitor1o0d: Human Thrombin Complexed With A D-Phe-Pro-Arg-type Inhibitor And A C-terminal Hirudin Derived Exo-site Inhibitor1o2g: Elaborate Manifold Of Short Hydrogen Bond Arrays Mediating Binding Of Active Site-Directed Serine Protease Inhibitors1o5g: Dissecting And Designing Inhibitor Selectivity Determinants At The S1 Site Using An Artificial Ala190 Protease (Ala190 UPA)1ook: Crystal Structure Of The Complex Of Platelet Receptor GPIb-alpha And Human Alpha-Thrombin1oyt: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED FLUORINATED INHIBITOR1p8v: CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A1ppb: THE REFINED 1.9 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN: INTERACTION WITH D-PHE-PRO-ARG CHLOROMETHYLKETONE AND SIGNIFICANCE OF THE TYR-PRO-PRO-TRP INSERTION SEGMENT1qbv: CRYSTAL STRUCTURE OF THROMBIN COMPLEXED WITH AN GUANIDINE-MIMETIC INHIBITOR1qhr: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS1qj1: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS1qj6: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS1qj7: NOVEL COVALENT ACTIVE SITE THROMBIN INHIBITORS1qur: HUMAN ALPHA-THROMBIN IN COMPLEX WITH BIVALENT, BENZAMIDINE-BASED SYNTHETIC INHIBITOR1rd3: 2.5A Structure Of Anticoagulant Thrombin Variant E217K1riw: Thrombin In Complex With Natural Product Inhibitor Oscillarin1sb1: Novel Non-Covalent Thrombin Inhibitors Incorporating P1 4,5,6,7-Tetrahydrobenzothiazole Arginine Side Chain Mimetics1sfq: Fast Form Of Thrombin Mutant R(77a)A Bound To PPACK1sgi: Crystal Structure Of The Anticoagulant Slow Form Of Thrombin1shh: Slow Form Of Thrombin Bound With PPACK1sl3: Crystal Structure Of Thrombin In Complex With A Potent P1 Heterocycle-Aryl Based Inhibitor1sr5: ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE1t4u: Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin1t4v: Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin1ta2: Crystal Structure Of Thrombin In Complex With Compound 11ta6: Crystal Structure Of Thrombin In Complex With Compound 14b1tb6: 2.5A Crystal Structure Of The Antithrombin-Thrombin-Heparin Ternary Complex1tbz: HUMAN THROMBIN WITH ACTIVE SITE N-METHYL-D PHENYLALANYL-N-[5-(AMINOIMINOMETHYL)AMINO]-1-[(BENZOTHIAZOLYL)CARBONYL] BUTYL]-L-PROLINAMIDE TRIFLUROACETATE AND EXOSITE-HIRUGEN1thp: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225P MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE1thr: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR1ths: STRUCTURES OF THROMBIN COMPLEXES WITH A DESIGNED AND A NATURAL EXOSITE INHIBITOR1tmb: MOLECULAR BASIS FOR THE INHIBITION OF HUMAN ALPHA-THROMBIN BY THE MACROCYCLIC PEPTIDE CYCLOTHEONAMIDE A1tmt: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS1tmu: CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS1tom: ALPHA-THROMBIN COMPLEXED WITH HIRUGEN1tq0: Crystal Structure Of The Potent Anticoagulant Thrombin Mutant W215A/E217A In Free Form1tq7: Crystal Structure Of The Anticoagulant Thrombin Mutant W215A/E217A Bound To PPACK1twx: Crystal Structure Of The Thrombin Mutant D221A/D222K1ucy: THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A ALPHA (RESIDUES 7-19). THREE COMPLEXES, ONE WITH EPSILON-THROMBIN AND TWO WITH ALPHA-THROMBIN1uma: ALPHA-THROMBIN (HIRUGEN) COMPLEXED WITH NA-(N,N-DIMETHYLCARBAMOYL)-ALPHA-AZALYSINE1uvs: BOVINE THROMBIN--BM51.1011 COMPLEX1vit: THROMBIN:HIRUDIN 51-65 COMPLEX1vr1: Specificity For Plasminogen Activator Inhibitor-11vzq: COMPLEX OF THROMBIN WITH DESIGNED INHIBITOR 71651w7g: ALPHA-THROMBIN COMPLEX WITH SULFATED HIRUDIN (RESIDUES 54-65) AND L-ARGININE TEMPLATE INHIBITOR CS1071way: ACTIVE SITE THROMBIN INHIBITORS1wbg: ACTIVE SITE THROMBIN INHIBITORS1xm1: Nonbasic Thrombin Inhibitor Complex1xmn: Crystal Structure Of Thrombin Bound To Heparin1ycp: THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-161ype: Thrombin Inhibitor Complex1ypg: Thrombin Inhibitor Complex1ypj: Thrombin Inhibitor Complex1ypk: Thrombin Inhibitor Complex1ypl: X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue RA-10081ypm: X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue RA-10141z71: Thrombin And P2 Pyridine N-oxide Inhibitor Complex Structure1z8i: Crystal Structure Of The Thrombin Mutant G193A Bound To PPACK1z8j: Crystal Structure Of The Thrombin Mutant G193P Bound To PPACK1zgi: Thrombin In Complex With An Oxazolopyridine Inhibitor 211zgv: Thrombin In Complex With An Oxazolopyridine Inhibitor 21zrb: Thrombin In Complex With An Azafluorenyl Inhibitor 23b2a0q: Structure Of Thrombin In 400 MM Potassium Chloride2a2x: Orally Active Thrombin Inhibitors In Complex With Thrombin Inh122a45: Crystal Structure Of The Complex Between Thrombin And The Central ""E"" Region Of Fibrin2afq: 1.9 Angstrom Crytal Structure Of Wild-type Human Thrombin In The Sodium Free State2ank: Orally Active Thrombin Inhibitors In Complex With Thrombin And An Exosite Decapeptide2anm: Ternary Complex Of An Orally Active Thrombin Inhibitor With Human Thrombin And A C-terminal Hirudin Derived Exo-sit Inhibitor2b5t: 2.1 Angstrom Structure Of A Nonproductive Complex Between Antithrombin, Synthetic Heparin Mimetic SR123781 And Two S195A Thrombin Molecules2bdy: Thrombin In Complex With Inhibitor2bvr: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET2bvs: HUMAN THROMBIN COMPLEXED WITH FRAGMENT-BASED SMALL MOLECULES OCCUPYING THE S1 POCKET2bvx: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER2bxt: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER2bxu: DESIGN AND DISCOVERY OF NOVEL, POTENT THROMBIN INHIBITORS WITH A SOLUBILIZING CATIONIC P1-P2-LINKER2c8w: THROMBIN INHIBITORS2c8x: THROMBIN INHIBITORS2c8y: THROMBIN INHIBITORS2c8z: THROMBIN INHIBITORS2c90: THROMBIN INHIBITORS2c93: THROMBIN INHIBITORS2cf8: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR2cf9: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A INHIBITOR2cn0: COMPLEX OF RECOMBINANT HUMAN THROMBIN WITH A DESIGNED INHIBITOR2feq: Orally Active Thrombin Inhibitors2fes: Orally Active Thrombin Inhibitors2gde: Thrombin In Complex With Inhibitor2gp9: Crystal Structure Of The Slow Form Of Thrombin In A Self-inhibited Conformation2h9t: Crystal Structure Of Human Alpha-thrombin In Complex With Suramin2hgt: STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN2hnt: CRYSTALLOGRAPHIC STRUCTURE OF HUMAN GAMMA-THROMBIN2hpp: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN2hpq: STRUCTURES OF THE NONCOVALENT COMPLEXES OF HUMAN AND BOVINE PROTHROMBIN FRAGMENT 2 WITH HUMAN PPACK-THROMBIN2hwl: Crystal Structure Of Thrombin In Complex With Fibrinogen Gamma' Peptide2jh0: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.2jh5: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.2jh6: HUMAN THROMBIN HIRUGEN INHIBITOR COMPLEX.2od3: Human Thrombin Chimera With Human Residues 184a, 186, 186a, 186b, 186c And 222 Replaced By Murine Thrombin Equivalents.2thf: STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE3hat: ACTIVE SITE MIMETIC INHIBITION OF THROMBIN4htc: THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX4thn: THE CRYSTAL STRUCTURE OF ALPHA-THROMBIN-HIRUNORM IV COMPLEX REVEALS A NOVEL SPECIFICITY SITE RECOGNITION MODE.5gds: HIRUNORMS ARE TRUE HIRUDIN MIMETICS. THE CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN:HIRUNORM V COMPLEX7kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2711.8kme: CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN INHIBITED WITH SEL2770.Template:CoagulationTemplate Talk:CoagulationProteinCoagulationCoagulationCoagulationVon Willebrand FactorPlatelet Membrane GlycoproteinGlycoprotein IbGP1BAGP1BBGlycoprotein IXGlycoprotein IIb/IIIaITGA2BCD61GPVICoagulationHigh-molecular-weight KininogenBradykininPrekallikreinKallikreinFactor XIIFactor XIFactor IXFactor VIIICoagulationTissue FactorFactor VIICoagulationFactor XFactor VFibrinFibrinogenFibrinogen Alpha ChainFibrinogen Gamma ChainFactor XIIIAnticoagulantAntithrombinProtein CProtein SProtein ZProtein Z-related Protease InhibitorTissue Factor Pathway InhibitorThrombolysisFibrinolysisPlasminTissue Plasminogen ActivatorUrokinasePlasminogen Activator Inhibitor-1Plasminogen Activator Inhibitor-2Alpha 2-antiplasminAlpha-2-MacroglobulinCarboxypeptidase B2Template:AutoantigensTemplate Talk:AutoantigensAntigenAutoimmunityDehydrogenaseBranched-chain Alpha-keto Acid Dehydrogenase ComplexOxoglutarate DehydrogenasePyruvate DehydrogenaseTransglutaminaseKeratinocyte TransglutaminaseTissue TransglutaminaseNucleoporinNucleoporin 35Nucleoporin 37Nucleoporin 43Nucleoporin 50Nucleoporin 54Nucleoporin 62Nucleoporin 85Nucleoporin 88Nucleoporin 93NUP98Nucleoporin 107Nucleoporin 133Nucleoporin 153Nucleoporin 155Nucleoporin 160Nucleoporin 188Nucleoporin 210kDaNucleoporin 205Nucleoporin 214Nicotinic Acetylcholine ReceptorActinApolipoprotein HCardiolipinCentromereFilaggrinGangliosidesSp100 Nuclear AntigenTopoisomeraseTemplate:AntihemorrhagicsTemplate Talk:AntihemorrhagicsAntihemorrhagicATC Code B02AntihemorrhagicCoagulationVitamin KPhylloquinoneMenadioneCoagulationFactor IXNonacog AlfaFactor VIIIMoroctocog AlfaTuroctocog AlfaFactor VIIRecombinant Factor VIIaFactor XFibrinogenFactor XIIICatridecacogProthrombin Complex ConcentrateEtamsylateCarbazochromeBatroxobinThrombopoietin Receptor AgonistRomiplostimEltrombopagAbsorbable Gelatin SpongeOxidized CelluloseTetragalacturonic Acid HydroxymethylesterCollagenCalcium AlginateEpinephrineAdrenaloneAntifibrinolyticAmino AcidAminocaproic AcidTranexamic AcidAminomethylbenzoic AcidSerpinAprotininAlpha 1-antitrypsinC1-inhibitorCamostatTemplate:Serine EndopeptidasesTemplate Talk:Serine EndopeptidasesEndopeptidaseSerine ProteaseEnzyme Commission NumberList Of EC Numbers (EC 3)Digestive EnzymeEnteropeptidaseTrypsinChymotrypsinElastaseNeutrophil ElastasePancreatic ElastaseCoagulationFactor VIIFactor IXFactor XFactor XIFactor XIIKallikreinProstate-specific AntigenKLK1KLK2Prostate-specific AntigenKLK4KLK5KLK6KLK7KLK8KLK9KLK10KLK11KLK12KLK13KLK14KLK15FibrinolysisPlasminPlasminogen ActivatorTissue Plasminogen ActivatorUrokinaseComplement SystemComplement Factor BFactor DComplement Factor IMannose-binding Protein-associated Serine ProteaseMASP1 (protein)MASP2 (protein)C3-convertaseImmune SystemChymaseGranzymeTryptaseProteinase 3VenomAncrodBatroxobinAcrosinProlyl EndopeptidasePronaseProprotein ConvertaseProprotein Convertase 1Proprotein Convertase 2PRSS8ReelinSubtilisinFurinStreptokinaseMembrane-bound Transcription Factor Peptidase, Site 1CathepsinCathepsin ACathepsin GTemplate:EnzymesTemplate Talk:EnzymesEnzymeActive SiteBinding SiteCatalytic TriadOxyanion HoleEnzyme PromiscuityCatalytically Perfect EnzymeCoenzymeCofactor (biochemistry)Enzyme CatalysisAllosteric RegulationCooperativityEnzyme InhibitorEnzyme Commission NumberEnzyme SuperfamilyEnzyme FamilyList Of EnzymesEnzyme KineticsEadie–Hofstee DiagramHanes–Woolf PlotLineweaver–Burk PlotMichaelis–Menten KineticsOxidoreductaseList Of EC Numbers (EC 1)TransferaseList Of EC Numbers (EC 2)HydrolaseList Of EC Numbers (EC 3)LyaseList Of EC Numbers (EC 4)IsomeraseList Of EC Numbers (EC 5)LigaseList Of EC Numbers (EC 6)Portal:Molecular And Cellular BiologyHelp:CategoryCategory:Genes On Human Chromosome 11Category:Coagulation SystemCategory:Acute Phase ProteinsCategory:EC 3.4.21Category:Peripheral Membrane ProteinsCategory:Pages Using Citations With Accessdate And No URLCategory:CS1 Swedish-language Sources (sv)Discussion About Edits From This IP Address [n]A List Of Edits Made From This IP Address [y]View The Content Page [c]Discussion About The Content Page [t]Edit This Page [e]Visit The Main Page [z]Guides To Browsing WikipediaFeatured Content – The Best Of WikipediaFind Background Information On Current EventsLoad A Random Article [x]Guidance On How To Use And Edit WikipediaFind Out About WikipediaAbout The Project, What You Can Do, Where To Find ThingsA List Of Recent Changes In The Wiki [r]List Of All English Wikipedia Pages Containing Links To This Page [j]Recent Changes In Pages Linked From This Page [k]Upload Files [u]A List Of All Special Pages [q]Wikipedia:AboutWikipedia:General Disclaimer



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