2127:
thrombokinase was a proteolytic enzyme that, by itself, could activate prothrombin. Its activity was greatly enhanced by addition of calcium, other serum factors, and tissue extracts, which represented the thromboplastins that promoted the conversion of prothrombin to thrombin by their interaction with thrombokinase. In 1964 Milstone summarized his work and that of others: “There are many chemical reactions which are so slow that they would not be of physiological use if they were not accelerated by enzymes. We are now confronted with a reaction, catalyzed by an enzyme, which is still too slow unless aided by accessory factors.”
4449:
843:
4464:
820:
3759:
4299:
4284:
742:
717:
4164:
4074:
4254:
4149:
4434:
4269:
4344:
3834:
4479:
4614:
4599:
4239:
4224:
4209:
4194:
4179:
3804:
3789:
3774:
4059:
3879:
1770:
the major component of selectivity and binding. The S2 sub-pocket is small, shallow and not well defined. It merges with the S4 subpocket. The S3 sub-pocket is located on the rim of the S1 pocket and is quite exposed to solvent. The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site. Factor Xa inhibitors generally bind in an L-shaped conformation, where one group of the ligand occupies the anionic S1 pocket lined by residues
4404:
4584:
4569:
4554:
4539:
4524:
4509:
4494:
4419:
4314:
1094:
4044:
4029:
4014:
3999:
3984:
3969:
3954:
3939:
3924:
3909:
3894:
4389:
4374:
4329:
849:
748:
4104:
4134:
4119:
4089:
3819:
2123:
prothrombin. Morawitz believed that his enzyme came from cells such as platelets yet, in keeping with the state of knowledge about enzymes at that time, he had no clear idea about the chemical nature of his thrombokinase or its mechanism of action. Those uncertainties led to decades during which the terms thrombokinase and thromboplastin were both used to describe the activator of prothrombin and led to controversy about its chemical nature and origin.
38:
1902:
4629:
3864:
3849:
4359:
5899:
2086:
Xa compared to unfractionated heparin, and fondaparinux, an agent based on the critical pentasacharide sequence of heparin, shows more selectivity than LMWH. This inactivation of Factor Xa by heparins is termed "indirect" since it relies on the presence of AT and not a direct interaction with Factor Xa.
2085:
to inactivate several coagulation factors IIa, Xa, XIa and XIIa. The affinity of unfractionated heparin and the various LMWHs for Factor Xa varies considerably. The efficacy of heparin-based anticoagulants increases as selectivity for Factor Xa increases. LMWH shows increased inactivation of Factor
1769:
The first crystal structure of human factor Xa was deposited in May 1993. To date, 191 crystal structures of factor Xa with various inhibitors have been deposited in the protein data bank. The active site of factor Xa is divided into four subpockets as S1, S2, S3 and S4. The S1 subpocket determines
1983:
A new model, the cell-based model of anticoagulation appears to explain more fully the steps in coagulation. This model has three stages: 1) initiation of coagulation on TF-bearing cells, 2) amplification of the procoagulant signal by thrombin generated on the TF-bearing cell and 3) propagation of
2118:
American and
British scientists described deficiency of factor X independently in 1953 and 1956, respectively. As with some other coagulation factors, the factor was initially named after these patients, a Mr Rufus Stuart (1921) and a Miss Audrey Prower (1934). At that time, those investigators
2126:
In 1947, J Haskell
Milstone isolated a proenzyme from bovine plasma which, when activated, converted prothrombin to thrombin. Following Morawitz’s designation, he called it prothrombokinase and by 1951 had purified the active enzyme, thrombokinase. Over the next several years he showed that
2122:
Thrombokinase was the name coined by Paul
Morawitz in 1904 to describe the substance that converted prothrombin to thrombin and caused blood to clot. That name embodied an important new concept in understanding blood coagulation – that an enzyme was critically important in the activation of
1892:
that improve expression or purification of a protein of interest. Its preferred cleavage site (after the arginine in the sequence Ile-Glu/Asp-Gly-Arg, IEGR or IDGR) can easily be engineered between a tag sequence and the protein of interest. After expression and purification, the tag is then
4448:
2109:
and 813893. These agents have several theoretical advantages over current therapy. They may be given orally. They have rapid onset of action. And they may be more effective against Factor Xa in that they inhibit both free Factor Xa and Factor Xa in the prothrombinase complex.
64:
3479:
Morgenstern KA, Sprecher C, Holth L, Foster D, Grant FJ, Ching A, et al. (March 1994). "Complementary DNA cloning and kinetic characterization of a novel intracellular serine proteinase inhibitor: mechanism of action with trypsin and factor Xa as model proteinases".
3441:
Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio MG, Ruggieri M, et al. (August 1995). "Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain".
3411:
McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, et al. (June 1983). "Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid".
4463:
2467:
2353:
The flurry of interest reflects increasing understanding of what doctors call the coagulation cascade... Four new blood thinners target an enzyme called factor Xa, one of several enzymes that play an important role in the
1824:(bleeding into joints) and gastrointestinal blood loss. Apart from congenital deficiency, low factor X levels may occur occasionally in a number of disease states. For example, factor X deficiency may be seen in
2033:. This "tenase" complex activates more Factor X, which in turn forms new prothrombinase complexes with Factor Va. Factor Xa is the prime component of the prothrombinase complex which converts large amounts of
856:
755:
3758:
4298:
4283:
3329:
Leytus SP, Foster DC, Kurachi K, Davie EW (September 1986). "Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C".
4163:
4457:: Factor Xa in complex with the inhibitor 1-(3-amino-1,2-benzisoxazol-5-yl)-6-(2'-(((3r)-3-hydroxy-1-pyrrolidinyl)methyl)-4-biphenylyl)-3-(trifluoromethyl)-1,4,5,6-tetrahydro-7h-pyrazolopyridin-7-one
2070:(VKA), inhibit the vitamin K-dependent carboxylation of Factors II (prothrombin), VII, IX, X in the hepatocyte. This carboxylation after the translation is essential for the physiological activity.
2051:
Factor Xa also plays a role in other biological processes that are not directly related to coagulation, like wound healing, tissue remodelling, inflammation, angiogenesis and atherosclerosis.
1853:
Polymorphisms in Factor X have been associated with an increased prevalence in bacterial infections, suggesting a possible role directly regulating the immune response to bacterial pathogens.
4073:
4253:
4148:
3564:"Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X"
3275:"The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action"
2918:"The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action"
2578:
3180:
Jagadeeswaran P, Reddy SV, Rao KJ, Hamsabhushanam K, Lyman G (December 1989). "Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X".
3034:
Messier TL, Pittman DD, Long GL, Kaufman RJ, Church WR (March 1991). "Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X".
4472:: Factor Xa in complex with the inhibitor 3-(6-(2'-((dimethylamino)methyl)-4-biphenylyl)-7-oxo-3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-pyrazolopyridin-1-yl)benzamide
4433:
3308:
Gilgenkrantz S, Briquel ME, André E, Alexandre P, Jalbert P, Le Marec B, et al. (1986). "Structural genes of coagulation factors VII and X located on 13q34".
4268:
4343:
3597:
Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, et al. (August 1993). "Structure of human des(1-45) factor Xa at 2.2 A resolution".
5553:
3833:
4478:
2515:
4613:
4598:
4238:
2054:
Inhibition of the synthesis or activity of Factor X is the mechanism of action for many anticoagulants in use today. Warfarin, a synthetic derivative of
2571:"Kcentra- prothrombin, coagulation factor vii human, coagulation factor ix human, coagulation factor x human, protein c, protein s human, and water kit"
1337:
678:
5413:
4223:
4208:
4193:
4178:
3803:
3788:
3773:
1318:
2455:
Until today's orphan drug approval, no specific coagulation factor replacement therapy was available for patients with hereditary Factor X deficiency.
2438:
4058:
2305:
1999:
TF on the surface of cells and is converted to Factor VIIa. The result is a Factor VIIa/TF complex, which catalyzes the activation of Factor X and
5153:
3878:
4669:
2962:
Cooper DN, Millar DS, Wacey A, Pemberton S, Tuddenham EG (July 1997). "Inherited factor X deficiency: molecular genetics and pathophysiology".
1880:
Kcentra, manufactured by CSL Behring, is a concentrate containing coagulation
Factors II, VII, IX and X, and antithrombotic Proteins C and S.
1877:
and approved for use in the United States by the FDA in
October 2015, and in the EU in March 2016, after earlier acceptance by CHMP and COMP.
2220:
2119:
could not know that the human genetic defect they had identified would be found in the previously characterized enzyme called thrombokinase.
2202:
1964:
pathway and the intrinsic pathway. These pathways converge to a common point, the formation of the Factor Xa/Va complex which together with
2037:—the "thrombin burst". Each molecule of Factor Xa can generate 1000 molecules of thrombin. This large burst of thrombin is responsible for
5061:
4403:
2548:
1561:
2660:
Turpie AG (June 2007). "Oral, direct factor Xa inhibitors in development for the prevention and treatment of thromboembolic diseases".
1755:. Defects in protein Z lead to increased factor Xa activity and a propensity for thrombosis. The half life of factor X is 40–45 hours.
4583:
4568:
4553:
4538:
4523:
4508:
4493:
4418:
3244:
Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P (1986). "Isolation and characterization of human blood-coagulation factor X cDNA".
3767:: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
1568:
4313:
5173:
4172:: Crystal Structure of 3-chloro-N-carbonyl]-6-methoxyphenyl]-4-[methyl]-2-thiophenecarboxamide Complexed with Human Factor Xa
2014:
In stage 2, the amplification stage, if enough thrombin has been generated, then activation of platelets and platelet-associated
1865:
and the prothrombinase complex. There are two commercially available Factor X concentrates: "Factor X P Behring" manufactured by
4043:
4028:
4013:
3998:
3983:
3968:
3953:
3938:
3923:
3908:
3893:
2570:
4388:
4373:
4328:
1740:
3065:"Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation"
2341:
5919:
3738:
2644:
2185:
4930:
4103:
3001:"Blood coagulation factors in human embryonic-fetal development: preferential expression of the FVII/tissue factor pathway"
1835:(or similar medication) leads to the production of an inactive factor X. In warfarin therapy, this is desirable to prevent
61:
4133:
4118:
4088:
5146:
4307:: FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S)-(3'-AMIDINO-3-BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID
4292:: FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S)-(3'-AMIDINO-3-BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID
2164:
4662:
5618:
5131:
5056:
4978:
4973:
3818:
3098:
España F, Berrettini M, Griffin JH (August 1989). "Purification and characterization of plasma protein C inhibitor".
2089:
Recently a new series of specific, direct acting inhibitors of Factor Xa has been developed. These include the drugs
5107:
842:
4935:
4771:
2189:
2168:
2140:
819:
4761:
2058:, is the most widely used oral anticoagulant in the US. In some European countries, other coumarin derivatives (
5139:
4711:
4082:: Factor Xa in complex with (R)-2-(3-adamantan-1-yl-ureido)-3-(3-carbamimidoyl-phenyl)-N-phenethyl-propionamide
2507:
2424:
1382:
5774:
5011:
4655:
2493:
741:
716:
4262:: Factor Xa in complex with the inhibitor 1- carbonyl-2-carbamoyl-4-(6-chloronaphth-2-ylsulphonyl)piperazine
1363:
5373:
4963:
4816:
4157:: Crystal Structure of 3-chloro-N-carbonyl]phenyl]-4--2-thiophenecarboxamide Complexed with Human Factor Xa
2442:
2074:
658:
5929:
4628:
3863:
3848:
2309:
2136:
3670:
Schwartz RA, Steen CJ, Gascon P, Schick P (18 March 2024). Talavera F, Sacher RA, Thiagarajan P (eds.).
2366:
Choby JE, Monteith AJ, Himmel LE, Margaritis P, Shirey-Rice JK, Pruijssers A, et al. (March 2019).
1960:
Traditional models of coagulation developed in the 1960s envisaged two separate cascades, the extrinsic
5889:
855:
754:
5875:
5862:
5849:
5836:
5823:
5810:
5797:
5759:
5288:
5273:
5051:
3731:
2542:
1744:
22:
848:
747:
645:
5769:
5723:
5666:
5170:
2999:
Hassan HJ, Leonardi A, Chelucci C, Mattia G, Macioce G, Guerriero R, et al. (September 1990).
2674:
1624:
1540:
1519:
1515:
1481:
1460:
1456:
666:
2439:"FDA approves first Factor X concentrate to treat patients with rare hereditary bleeding disorder"
5671:
5563:
5528:
5523:
2336:
2015:
1874:
4442:: Factor Xa in complex with the inhibitor 2-[piperazin-1-yl] carbonyl]thienopyridine n-oxide
4358:
2824:
Milstone LM (August 2021). "Factor Xa: Thrombokinase from Paul
Morawitz to J Haskell Milstone".
1544:
1511:
1485:
1452:
4877:
4873:
2669:
2258:"Blood coagulation factor X: molecular biology, inherited disease, and engineered therapeutics"
1747:(serpin). The affinity of this protein for factor Xa is increased 1000-fold by the presence of
4841:
2368:"A Phenome-Wide Association Study Uncovers a Pathological Role of Coagulation Factor X during
2025:
activates free Factor IX on the surface of activated platelets. The activated Factor IXa with
1782:
228, and another group of the ligand occupies the aromatic S4 pocket lined by residues Tyr99,
5692:
5611:
5518:
5368:
4992:
4736:
4705:
4695:
2869:"Thrombokinase as prime activator of prothrombin: historical perspectives and present status"
2537:
2067:
1996:
1786:
174, and Trp215. Typically, a fairly rigid linker group bridges these two interaction sites.
730:
3129:"Characterization of an almost full-length cDNA coding for human blood coagulation factor X"
5764:
5508:
3724:
3522:
3371:
3140:
2782:
2773:
Milstone JH (December 1947). "Prothrombokinase and the Three Stages of Blood
Coagulation".
1926:
1647:
5033:
4277:: Factor Xa in complex with the inhibitor 4--2-(2-methylpropyl)-1-[carbonyl]piperazine
3671:
8:
5728:
5408:
5398:
5215:
5210:
5043:
5020:
5001:
4983:
4678:
3691:
1862:
1847:
1811:
1764:
1639:
686:
3526:
3375:
3144:
2786:
5924:
5661:
4686:
3580:
3563:
3467:
3455:
2987:
2893:
2868:
2849:
2806:
2695:
2600:
Hoffman M, Monroe DM (February 2007). "Coagulation 2006: a modern view of hemostasis".
2396:
2367:
2282:
2257:
1930:
1914:
690:
5161:
3644:
3627:
3394:
3359:
3163:
3128:
3081:
3064:
1252:
1247:
1242:
1237:
1232:
1227:
1222:
1206:
1201:
1196:
1191:
1186:
1181:
1165:
1160:
1155:
1150:
1145:
1140:
1135:
5390:
5071:
5028:
3649:
3614:
3585:
3550:
3545:
3510:
3497:
3459:
3429:
3399:
3346:
3317:
3296:
3273:
Broze GJ, Warren LA, Novotny WF, Higuchi DA, Girard JJ, Miletich JP (February 1988).
3261:
3257:
3232:
3197:
3193:
3168:
3115:
3111:
3086:
3051:
3047:
3022:
2979:
2939:
2916:
Broze GJ, Warren LA, Novotny WF, Higuchi DA, Girard JJ, Miletich JP (February 1988).
2898:
2853:
2841:
2798:
2755:
2750:
2733:
2687:
2640:
2617:
2487:
2401:
2287:
638:
54:
3471:
3209:
Reddy SV, Zhou ZQ, Rao KJ, Scott JP, Watzke H, High KA, et al. (October 1989).
2991:
2810:
2331:
5707:
5702:
5676:
5604:
5182:
5084:
5079:
3639:
3606:
3575:
3540:
3530:
3489:
3451:
3421:
3389:
3379:
3338:
3286:
3253:
3222:
3189:
3158:
3148:
3107:
3076:
3043:
3012:
2971:
2929:
2888:
2880:
2833:
2794:
2790:
2745:
2699:
2679:
2609:
2391:
2383:
2277:
2269:
935:
866:
810:
765:
670:
3227:
3210:
3017:
3000:
5754:
5738:
5651:
5423:
5418:
5190:
5166:
4751:
4730:
4716:
3842:: CRYSTAL STRUCTURE OF THE INHIBITOR ZK-807834 (CI-1031) COMPLEXED WITH FACTOR XA
3705:
910:
694:
3291:
3274:
2934:
2917:
2225:
National Center for
Biotechnology Information, U.S. National Library of Medicine
2207:
National Center for
Biotechnology Information, U.S. National Library of Medicine
5903:
5792:
5733:
5089:
4487:: Crystal Structure of the Antithrombin-S195A Factor Xa-Pentasaccharide Complex
3515:
Proceedings of the
National Academy of Sciences of the United States of America
3364:
Proceedings of the National Academy of Sciences of the United States of America
3133:
Proceedings of the National Academy of Sciences of the United States of America
2837:
2683:
2273:
2041:
2008:
1942:
1816:
Inborn deficiency of factor X is very rare (1:1,000,000), and may present with
1733:
1011:
4622:: SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND FACTOR XA
4607:: SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND FACTOR XA
4247:: Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R
2613:
2011:
which generates small amounts of thrombin on the surface of TF-bearing cells.
5913:
5697:
5656:
5568:
5441:
5430:
5162:
4902:
4826:
4781:
3509:
Heeb MJ, Rosing J, Bakker HM, Fernandez JA, Tans G, Griffin JH (March 1994).
2238:
2063:
2059:
1969:
1961:
1840:
1799:
1783:
1771:
1686:
1122:
3384:
3153:
1071:
949:
5646:
5464:
5358:
5200:
5099:
4945:
4910:
4232:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR200095
4217:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR208944
4202:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR209685
4187:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR132747
3812:: Crystal Structure of Human Coagulation Factor XA Complexed with RPR208707
3797:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR208815
3782:: CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR128515
3610:
3535:
2975:
2902:
2845:
2802:
2759:
2691:
2621:
2405:
2291:
2082:
2078:
1954:
1934:
1821:
928:
707:
3653:
3618:
3589:
3554:
3501:
3463:
3433:
3403:
3350:
3321:
3300:
3265:
3236:
3201:
3172:
3119:
3090:
3055:
3026:
2983:
2943:
1846:
Inhibiting Factor Xa would offer an alternate method for anticoagulation.
1608:
1603:
1093:
5870:
5805:
5641:
5583:
5578:
5227:
4953:
4888:
4859:
4806:
2884:
2387:
2090:
2034:
2026:
1977:
1889:
1866:
1825:
1705:
1674:
1427:
1408:
4067:: Crystal Structure of Human Coagulation Factor XA Complexed with FXV673
3493:
3425:
3342:
2003:. Factor Xa formed on the surface of the TF-bearing cell interacts with
1828:, where factor X is adsorbed to the amyloid fibrils in the vasculature.
1627:
5545:
5487:
5268:
5263:
5243:
4869:
4831:
4791:
4786:
4776:
3628:"Carbohydrate residues modulate the activation of coagulation factor X"
2098:
1992:
1836:
1728:. This process is optimized when factor Xa is complexed with activated
1721:
1682:
827:
724:
674:
37:
4647:
1901:
615:
611:
607:
603:
599:
595:
591:
587:
583:
579:
575:
571:
567:
563:
559:
555:
551:
547:
543:
539:
535:
531:
527:
523:
519:
515:
511:
507:
503:
499:
495:
491:
487:
483:
479:
475:
471:
467:
463:
459:
455:
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447:
443:
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431:
427:
423:
419:
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411:
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403:
399:
395:
391:
387:
383:
379:
375:
371:
367:
363:
359:
355:
351:
347:
343:
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335:
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327:
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319:
315:
311:
307:
303:
299:
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283:
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199:
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155:
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147:
143:
139:
135:
131:
127:
123:
119:
115:
111:
107:
103:
99:
95:
91:
87:
83:
5844:
5818:
5573:
5559:
5378:
5258:
5248:
4968:
4925:
4920:
4915:
4801:
4796:
2637:
Principles of Pharmacology The Pathophysiologic Basis of Drug Therapy
2102:
2022:
2000:
1817:
1752:
1748:
1713:
1670:
1659:
1282:
894:
881:
793:
780:
682:
3887:: STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 ANGSTROMS RESOLUTION
5898:
5459:
5454:
5403:
5238:
5205:
4864:
4854:
3179:
2106:
2094:
2055:
2045:
2004:
1985:
1973:
1946:
1832:
1779:
1729:
1725:
1717:
1709:
1592:
3596:
3243:
1988:
surface. Factor Xa plays a key role in all three of these stages.
5513:
5503:
5449:
5363:
5195:
5116:
4958:
3307:
1965:
1950:
1888:
The factor Xa protease can be used in biochemistry to cleave off
1651:
1394:
1349:
1267:
1263:
3358:
Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW (June 1984).
2639:. Philadelphia: Lippincott Williams & Wilkins. p. 387.
662:
5857:
5627:
5540:
5482:
4883:
4740:
4352:: CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH COMPOUND ""1""
3696:
2038:
2030:
1922:
1775:
1690:
1678:
1635:
1576:
1304:
1102:
3716:
3478:
3440:
3410:
5831:
5549:
5535:
5474:
5348:
5343:
5338:
5333:
5328:
5323:
4931:
Protein Z-related protease inhibitor (ZPI) (inhibits FX, FXI)
4725:
4720:
2365:
1957:, act to inhibit the action of Factor Xa in various degrees.
1938:
1655:
4412:: CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH COMPOUND 45
2998:
5318:
5313:
5308:
5303:
5298:
5293:
5283:
5278:
4745:
1795:
5596:
4592:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4577:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4562:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4547:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4532:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4517:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
4502:: Crystal Structure of FXa/selectide/NAPC2 ternary complex
4427:: CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
2961:
2474:. 28 June 2017. Archived from the original on 22 July 2017
1751:, while it does not require protein Z for inactivation of
3669:
3508:
3272:
3211:"Molecular characterization of human factor XSan Antonio"
3033:
2915:
2866:
2441:(Press release). US FDA. October 20, 2015. Archived from
1248:
endoplasmic reticulum to Golgi vesicle-mediated transport
3357:
3328:
2329:
918:
4322:: Crystal Structure of Factor Xa complexed to Razaxaban
3097:
2867:
Milstone JH, Oulianoff N, Milstone VK (November 1963).
2713:
Morawitz P. "Beitrage zur Kenntnis der Blutgerinnung".
1187:
intrinsic component of external side of plasma membrane
4936:
Tissue factor pathway inhibitor (TFPI) (inhibits FIII)
3692:"Summary for peptidase S01.216: coagulation factor Xa"
3360:"Characterization of a cDNA coding for human factor X"
5887:
2073:
Heparin (unfractionated heparin) and its derivatives
1083:
4052:: Human coagulation factor Xa in complex with M55192
4037:: Human coagulation factor Xa in complex with M54471
4022:: Human coagulation factor Xa in complex with M54476
4007:: Human coagulation factor Xa in complex with M55113
3992:: Human coagulation factor Xa in complex with M55124
3977:: Human coagulation factor Xa in complex with M55125
3962:: Human coagulation factor Xa in complex with M55143
3947:: Human coagulation factor Xa in complex with M55159
3932:: Human coagulation factor Xa in complex with M55165
3917:: Human coagulation factor Xa in complex with M55590
3902:: Human coagulation factor Xa in complex with M55532
4397:: CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 43
4382:: CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 21
4337:: CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 50
3126:
5002:Thrombin-activatable fibrinolysis inhibitor (TAFI)
2662:Arteriosclerosis, Thrombosis, and Vascular Biology
2181:
2179:
2177:
2160:
2158:
2156:
1929:, which plays a key role at several stages of the
5062:Activated protein C–protein C inhibitor (APC–PCI)
3208:
1228:positive regulation of protein kinase B signaling
865:
764:
5911:
4911:Antithrombin (inhibits FII, FIX, FX, FXI, FXII)
4112:: CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 125.
3700:. European Molecular Biology Laboratory (EMBL).
2174:
2153:
4142:: CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.
4127:: CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 41.
4097:: CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 79.
3127:Fung MR, Hay CW, MacGillivray RT (June 1985).
2186:GRCm38: Ensembl release 89: ENSMUSG00000031444
1839:. As of late 2007, four out of five emerging
5612:
5147:
4663:
3732:
2599:
2306:"Presentation on Direct Factor Xa Inhibitors"
3062:
2602:Hematology/Oncology Clinics of North America
3561:
3511:"Protein S binds to and inhibits factor Xa"
2909:
2734:"On the evolution of blood clotting theory"
2165:GRCh38: Ensembl release 89: ENSG00000126218
1909:showing the central role played by thrombin
1665:Factor X is activated, by hydrolysis, into
5619:
5605:
5154:
5140:
4670:
4656:
3739:
3725:
2231:
1693:. It is therefore the first member of the
4979:Plasminogen activator inhibitor-2 (PAI-2)
4974:Plasminogen activator inhibitor-1 (PAI-1)
3827:: COAGULATION FACTOR XA INHIBITOR COMPLEX
3643:
3625:
3579:
3544:
3534:
3393:
3383:
3290:
3226:
3162:
3152:
3080:
3016:
2933:
2892:
2749:
2673:
2395:
2330:Ron Winslow, Avery Johnson (2007-12-10).
2323:
2281:
1831:Deficiency of vitamin K or antagonism by
1038:fetal liver hematopoietic progenitor cell
2823:
2772:
2731:
2421:Registry of Clotting Factor Concentrates
1900:
4677:
2418:
2332:"Race Is on for the Next Blood Thinner"
1913:Factor Xa is the activated form of the
18:Mammalian protein found in Homo sapiens
5912:
5167:serine proteases/serine endopeptidases
4772:High-molecular-weight kininogen (HMWK)
2826:Journal of Thrombosis and Thrombolysis
2715:Deutsches Archiv für Klinische Medizin
2659:
2262:Journal of Thrombosis and Thrombolysis
2255:
1893:proteolytically removed by factor Xa.
1883:
1741:protein Z-dependent protease inhibitor
5600:
5135:
4651:
3720:
2634:
2593:
2551:from the original on 30 December 2019
2518:from the original on 17 December 2019
2249:
1233:positive regulation of cell migration
870:
831:
826:
769:
728:
723:
3662:
2712:
2653:
1765:Factor IX § Domain architecture
1253:blood coagulation, extrinsic pathway
5057:Thrombin–antithrombin complex (TAT)
3632:The Journal of Biological Chemistry
3562:Inoue K, Morita T (November 1993).
3069:The Journal of Biological Chemistry
2075:low molecular weight heparin (LMWH)
1843:therapeutics targeted this enzyme.
13:
4964:Tissue plasminogen activator (tPA)
4921:Protein S (cofactor for protein C)
3626:Sinha U, Wolf DL (February 1993).
3581:10.1111/j.1432-1033.1993.tb18361.x
3456:10.1111/j.1365-2141.1995.tb05214.x
2954:
2581:from the original on 25 March 2021
2066:) are used. These agents known as
1856:
1805:
1654:). Factor X is synthesized in the
1156:serine-type endopeptidase activity
14:
5941:
3684:
2873:The Journal of General Physiology
2512:U.S. Food and Drug Administration
2472:U.S. Food and Drug Administration
2021:In stage 3, thrombin generation,
5897:
4627:
4612:
4597:
4582:
4567:
4552:
4537:
4522:
4507:
4492:
4477:
4462:
4447:
4432:
4417:
4402:
4387:
4372:
4357:
4342:
4327:
4312:
4297:
4282:
4267:
4252:
4237:
4222:
4207:
4192:
4177:
4162:
4147:
4132:
4117:
4102:
4087:
4072:
4057:
4042:
4027:
4012:
3997:
3982:
3967:
3952:
3937:
3922:
3907:
3892:
3877:
3862:
3847:
3832:
3817:
3802:
3787:
3772:
3757:
3568:European Journal of Biochemistry
2751:10.1097/00005792-195212000-00004
2239:"F10 gene: MedlinePlus Genetics"
1092:
854:
847:
841:
818:
753:
746:
740:
715:
36:
5052:Prothrombin fragment 1+2 (F1+2)
4712:Platelet membrane glycoproteins
3746:
2860:
2817:
2766:
2725:
2706:
2628:
2563:
2530:
2500:
2460:
2431:
2412:
2344:from the original on 2016-03-10
2141:Tissue factor pathway inhibitor
2130:
1724:bond), which yields the active
649:, FX, FXA, coagulation factor X
4916:Protein C (inhibits FV, FVIII)
3444:British Journal of Haematology
2795:10.1126/science.106.2762.546-a
2425:World Federation of Hemophilia
2359:
2298:
2213:
2195:
1151:serine-type peptidase activity
1103:More reference expression data
1072:More reference expression data
1:
5379:Urinary plasminogen activator
4637:: FACTOR XA INHIBITOR COMPLEX
3872:: FACTOR XA INHIBITOR COMPLEX
3857:: FACTOR XA INHIBITOR COMPLEX
3645:10.1016/S0021-9258(18)53657-7
3228:10.1182/blood.V74.5.1486.1486
3082:10.1016/S0021-9258(19)39652-8
3063:Krishnaswamy S (March 1990).
3018:10.1182/blood.V76.6.1158.1158
2732:Milstone JH (December 1952).
2146:
1953:series of anticoagulants and
1042:epithelium of small intestine
839:
738:
5920:Genes on human chromosome 13
5374:Tissue plasminogen activator
3599:Journal of Molecular Biology
3258:10.1016/0378-1119(86)90112-5
3194:10.1016/0378-1119(89)90529-5
3112:10.1016/0049-3848(89)90069-8
3048:10.1016/0378-1119(91)90141-W
1896:
1850:are popular anticoagulants.
1758:
1739:Factor Xa is inactivated by
7:
5626:
4792:Factor XII (Hageman factor)
4706:von Willebrand factor (vWF)
3710:Canadian Hemophilia Society
3292:10.1182/blood.V71.2.335.335
2935:10.1182/blood.V71.2.335.335
2135:Factor X has been shown to
1984:thrombin generation on the
1905:Blood coagulation pathways
1869:, and high purity Factor X
1789:
1182:endoplasmic reticulum lumen
964:stromal cell of endometrium
10:
5946:
5112:-antiplasmin complex (PAP)
4827:Factor III (tissue factor)
2964:Thrombosis and Haemostasis
2838:10.1007/s11239-021-02387-6
2684:10.1161/ATVBAHA.107.139402
2274:10.1007/s11239-021-02456-w
2113:
1809:
1762:
1562:Chr 13: 113.12 – 113.15 Mb
1050:sexually immature organism
20:
5783:
5775:Michaelis–Menten kinetics
5747:
5716:
5685:
5634:
5496:
5473:
5465:Proteinase 3/Myeloblastin
5439:
5389:
5226:
5181:
5098:
5070:
5042:
5019:
5010:
4944:
4901:
4840:
4815:
4760:
4694:
4685:
3752:
2614:10.1016/j.hoc.2006.11.004
2543:European Medicines Agency
2492:: CS1 maint: unfit URL (
2256:Camire RM (August 2021).
2221:"Mouse PubMed Reference:"
2203:"Human PubMed Reference:"
1941:. The most commonly used
1745:serine protease inhibitor
1607:
1602:
1598:
1591:
1575:
1556:
1537:
1533:
1508:
1504:
1497:
1478:
1474:
1449:
1445:
1438:
1425:
1421:
1406:
1402:
1393:
1380:
1376:
1361:
1357:
1348:
1335:
1331:
1316:
1312:
1303:
1288:
1281:
1277:
1261:
1121:
1117:
1100:
1091:
1082:
1069:
1018:
1009:
956:
947:
917:
909:
905:
888:
875:
838:
817:
808:
804:
787:
774:
737:
714:
705:
701:
656:
653:
643:
636:
631:
80:
75:
58:
53:
48:
44:
35:
30:
23:Factor X (disambiguation)
5667:Diffusion-limited enzyme
5034:β-Thromboglobulin (β-TG)
2419:Brooker M (April 2008).
5029:Platelet factor 4 (PF4)
4926:Protein Z (inhibits FX)
4860:Prothrombin (factor II)
3385:10.1073/pnas.81.12.3699
3154:10.1073/pnas.82.11.3591
2370:Acinetobacter baumannii
2337:The Wall Street Journal
1978:prothrombin (Factor II)
1875:Bio Products Laboratory
1642:, encoded in humans by
1569:Chr 8: 13.09 – 13.11 Mb
5519:Proprotein convertases
5085:Fibrinopeptide B (FpB)
5080:Fibrinopeptide A (FpA)
4752:Glycoprotein VI (GPVI)
4717:Glycoprotein Ib (GPIb)
3611:10.1006/jmbi.1993.1441
3536:10.1073/pnas.91.7.2728
2976:10.1055/s-0038-1657520
2376:Infection and Immunity
2009:prothrombinase complex
1945:in clinical practice,
1910:
1689:in a complex known as
1677:in a complex known as
5760:Eadie–Hofstee diagram
5693:Allosteric regulation
5369:Plasminogen activator
4903:Anticoagulant factors
4870:Fibrinogen (factor I)
4865:Thrombin (factor IIa)
4737:Glycoprotein IIb/IIIa
4731:Glycoprotein IX (GP9)
4698:(platelet activation)
3706:"Factor X deficiency"
3672:"Factor X Deficiency"
2547:. 17 September 2018.
2514:. 21 September 2018.
2068:vitamin K antagonists
1997:transmembrane protein
1974:thrombin (Factor IIa)
1904:
992:right coronary artery
872:8 A1.1|8 5.73 cM
731:Chromosome 13 (human)
5770:Lineweaver–Burk plot
5509:Prolyl endopeptidase
5090:Fibrin monomers (FM)
4946:Fibrinolytic factors
4764:(contact activation)
4367:: FACTOR XA - CATION
3310:Annales de Genetique
2885:10.1085/jgp.47.2.315
2388:10.1128/IAI.00031-19
1962:(tissue factor (TF))
1927:serine endopeptidase
1861:Factor X is part of
1848:Direct Xa inhibitors
1704:It acts by cleaving
1695:final common pathway
1650:(protease group S1,
1648:serine endopeptidase
1621:Coagulation factor X
1197:extracellular region
1161:phospholipid binding
833:Chromosome 8 (mouse)
76:List of PDB id codes
49:Available structures
21:For other uses, see
5044:Thrombin generation
5021:Platelet activation
5012:Coagulation markers
4687:Coagulation factors
4679:Coagulation cascade
3527:1994PNAS...91.2728H
3494:10.1021/bi00177a037
3426:10.1021/bi00281a016
3376:1984PNAS...81.3699L
3343:10.1021/bi00366a018
3145:1985PNAS...82.3591F
3100:Thrombosis Research
2787:1947Sci...106..546M
2577:. 22 October 2018.
2445:on October 21, 2015
2423:(Eighth ed.).
2382:(5): IAI.00031–19.
1884:Use in biochemistry
1863:fresh frozen plasma
1812:Factor X deficiency
1794:The human factor X
1685:with its cofactor,
1673:with its cofactor,
1662:for its synthesis.
1640:coagulation cascade
1207:extracellular space
1136:calcium ion binding
972:canal of the cervix
960:right lobe of liver
5930:Coagulation system
5729:Enzyme superfamily
5662:Enzyme promiscuity
4884:Fibrin (factor Ia)
4696:Primary hemostasis
1972:surface, generate
1931:coagulation system
1915:coagulation factor
1911:
1708:in two places (an
1383:ENSMUSG00000031444
1216:Biological process
1175:Cellular component
1166:hydrolase activity
1141:peptidase activity
1129:Molecular function
1022:left lobe of liver
5885:
5884:
5594:
5593:
5391:Complement system
5183:Digestive enzymes
5129:
5128:
5125:
5124:
5072:Fibrin generation
4897:
4896:
4817:Extrinsic pathway
4762:Intrinsic pathway
4645:
4644:
3488:(11): 3432–3441.
3420:(12): 2875–2884.
3370:(12): 3699–3702.
3337:(18): 5098–5102.
3139:(11): 3591–3595.
2781:(2762): 546–547.
2646:978-1-4511-1805-6
2635:Golan DE (2012).
2083:antithrombin (AT)
1921:. Factor X is an
1917:X, also known as
1691:extrinsic pathway
1679:intrinsic pathway
1618:
1617:
1614:
1613:
1587:
1586:
1552:
1551:
1527:
1526:
1493:
1492:
1468:
1467:
1434:
1433:
1415:
1414:
1389:
1388:
1370:
1369:
1344:
1343:
1325:
1324:
1273:
1272:
1238:blood coagulation
1113:
1112:
1109:
1108:
1078:
1077:
1065:
1064:
1003:
1002:
996:left uterine tube
901:
900:
800:
799:
627:
626:
623:
622:
59:Ortholog search:
5937:
5902:
5901:
5893:
5765:Hanes–Woolf plot
5708:Enzyme activator
5703:Enzyme inhibitor
5677:Enzyme catalysis
5621:
5614:
5607:
5598:
5597:
5156:
5149:
5142:
5133:
5132:
5017:
5016:
4692:
4691:
4672:
4665:
4658:
4649:
4648:
4631:
4616:
4601:
4586:
4571:
4556:
4541:
4526:
4511:
4496:
4481:
4466:
4451:
4436:
4421:
4406:
4391:
4376:
4361:
4346:
4331:
4316:
4301:
4286:
4271:
4256:
4241:
4226:
4211:
4196:
4181:
4166:
4151:
4136:
4121:
4106:
4091:
4076:
4061:
4046:
4031:
4016:
4001:
3986:
3971:
3956:
3941:
3926:
3911:
3896:
3881:
3866:
3851:
3836:
3821:
3806:
3791:
3776:
3761:
3741:
3734:
3727:
3718:
3717:
3713:
3701:
3679:
3657:
3647:
3638:(5): 3048–3051.
3622:
3593:
3583:
3558:
3548:
3538:
3521:(7): 2728–2732.
3505:
3475:
3437:
3407:
3397:
3387:
3354:
3325:
3304:
3294:
3269:
3252:(2–3): 311–314.
3240:
3230:
3221:(5): 1486–1490.
3205:
3176:
3166:
3156:
3123:
3094:
3084:
3075:(7): 3708–3718.
3059:
3030:
3020:
3011:(6): 1158–1164.
2995:
2948:
2947:
2937:
2913:
2907:
2906:
2896:
2864:
2858:
2857:
2821:
2815:
2814:
2770:
2764:
2763:
2753:
2729:
2723:
2722:
2710:
2704:
2703:
2677:
2668:(6): 1238–1247.
2657:
2651:
2650:
2632:
2626:
2625:
2597:
2591:
2590:
2588:
2586:
2567:
2561:
2560:
2558:
2556:
2534:
2528:
2527:
2525:
2523:
2504:
2498:
2497:
2491:
2483:
2481:
2479:
2464:
2458:
2457:
2452:
2450:
2435:
2429:
2428:
2416:
2410:
2409:
2399:
2363:
2357:
2356:
2350:
2349:
2327:
2321:
2320:
2318:
2317:
2308:. Archived from
2302:
2296:
2295:
2285:
2253:
2247:
2246:
2235:
2229:
2228:
2217:
2211:
2210:
2199:
2193:
2183:
2172:
2162:
2031:"tenase" complex
1841:anti-coagulation
1699:thrombin pathway
1600:
1599:
1571:
1564:
1547:
1531:
1530:
1522:
1502:
1501:
1498:RefSeq (protein)
1488:
1472:
1471:
1463:
1443:
1442:
1419:
1418:
1400:
1399:
1374:
1373:
1355:
1354:
1329:
1328:
1310:
1309:
1279:
1278:
1119:
1118:
1105:
1096:
1089:
1088:
1074:
1014:
1012:Top expressed in
1007:
1006:
952:
950:Top expressed in
945:
944:
924:
923:
907:
906:
897:
884:
873:
858:
851:
845:
834:
822:
806:
805:
796:
783:
772:
757:
750:
744:
733:
719:
703:
702:
697:
648:
641:
618:
73:
72:
67:
46:
45:
40:
28:
27:
5945:
5944:
5940:
5939:
5938:
5936:
5935:
5934:
5910:
5909:
5908:
5896:
5888:
5886:
5881:
5793:Oxidoreductases
5779:
5755:Enzyme kinetics
5743:
5739:List of enzymes
5712:
5681:
5652:Catalytic triad
5630:
5625:
5595:
5590:
5492:
5469:
5435:
5385:
5222:
5191:Enteropeptidase
5177:
5160:
5130:
5121:
5111:
5094:
5066:
5038:
5006:
4996:
4987:
4940:
4893:
4836:
4819:(tissue factor)
4818:
4811:
4763:
4756:
4697:
4681:
4676:
4646:
4641:
4638:
4632:
4623:
4617:
4608:
4602:
4593:
4587:
4578:
4572:
4563:
4557:
4548:
4542:
4533:
4527:
4518:
4512:
4503:
4497:
4488:
4482:
4473:
4467:
4458:
4452:
4443:
4437:
4428:
4422:
4413:
4407:
4398:
4392:
4383:
4377:
4368:
4362:
4353:
4347:
4338:
4332:
4323:
4317:
4308:
4302:
4293:
4287:
4278:
4272:
4263:
4257:
4248:
4242:
4233:
4227:
4218:
4212:
4203:
4197:
4188:
4182:
4173:
4167:
4158:
4152:
4143:
4137:
4128:
4122:
4113:
4107:
4098:
4092:
4083:
4077:
4068:
4062:
4053:
4047:
4038:
4032:
4023:
4017:
4008:
4002:
3993:
3987:
3978:
3972:
3963:
3957:
3948:
3942:
3933:
3927:
3918:
3912:
3903:
3897:
3888:
3882:
3873:
3867:
3858:
3852:
3843:
3837:
3828:
3822:
3813:
3807:
3798:
3792:
3783:
3777:
3768:
3762:
3748:
3745:
3704:
3690:
3687:
3682:
3665:
3663:Further reading
3660:
2957:
2955:Further reading
2952:
2951:
2914:
2910:
2865:
2861:
2822:
2818:
2771:
2767:
2730:
2726:
2711:
2707:
2658:
2654:
2647:
2633:
2629:
2598:
2594:
2584:
2582:
2569:
2568:
2564:
2554:
2552:
2538:"Coagadex EPAR"
2536:
2535:
2531:
2521:
2519:
2506:
2505:
2501:
2485:
2484:
2477:
2475:
2466:
2465:
2461:
2448:
2446:
2437:
2436:
2432:
2417:
2413:
2364:
2360:
2347:
2345:
2340:. p. A12.
2328:
2324:
2315:
2313:
2304:
2303:
2299:
2254:
2250:
2243:medlineplus.gov
2237:
2236:
2232:
2219:
2218:
2214:
2201:
2200:
2196:
2184:
2175:
2163:
2154:
2149:
2133:
2116:
1968:and bound on a
1899:
1886:
1859:
1857:Therapeutic use
1814:
1808:
1806:Role in disease
1792:
1767:
1761:
1609:View/Edit Mouse
1604:View/Edit Human
1567:
1560:
1557:Location (UCSC)
1543:
1539:
1518:
1514:
1510:
1484:
1480:
1459:
1455:
1451:
1364:ENSG00000126218
1257:
1211:
1192:plasma membrane
1170:
1146:protein binding
1101:
1070:
1061:
1056:
1052:
1048:
1044:
1040:
1036:
1032:
1028:
1024:
1010:
999:
994:
990:
986:
982:
978:
974:
970:
966:
962:
948:
892:
879:
871:
861:
860:
859:
852:
832:
809:Gene location (
791:
778:
770:
760:
759:
758:
751:
729:
706:Gene location (
695:F10 - orthologs
657:
644:
637:
82:
60:
26:
19:
12:
11:
5:
5943:
5933:
5932:
5927:
5922:
5907:
5906:
5883:
5882:
5880:
5879:
5866:
5853:
5840:
5827:
5814:
5801:
5787:
5785:
5781:
5780:
5778:
5777:
5772:
5767:
5762:
5757:
5751:
5749:
5745:
5744:
5742:
5741:
5736:
5731:
5726:
5720:
5718:
5717:Classification
5714:
5713:
5711:
5710:
5705:
5700:
5695:
5689:
5687:
5683:
5682:
5680:
5679:
5674:
5669:
5664:
5659:
5654:
5649:
5644:
5638:
5636:
5632:
5631:
5624:
5623:
5616:
5609:
5601:
5592:
5591:
5589:
5588:
5587:
5586:
5581:
5571:
5566:
5557:
5543:
5538:
5533:
5532:
5531:
5526:
5516:
5511:
5506:
5500:
5498:
5494:
5493:
5491:
5490:
5485:
5479:
5477:
5471:
5470:
5468:
5467:
5462:
5457:
5452:
5446:
5444:
5437:
5436:
5434:
5433:
5428:
5427:
5426:
5421:
5411:
5406:
5401:
5395:
5393:
5387:
5386:
5384:
5383:
5382:
5381:
5376:
5366:
5354:
5353:
5352:
5351:
5346:
5341:
5336:
5331:
5326:
5321:
5316:
5311:
5306:
5301:
5296:
5291:
5286:
5281:
5276:
5266:
5261:
5256:
5251:
5246:
5241:
5232:
5230:
5224:
5223:
5221:
5220:
5219:
5218:
5213:
5203:
5198:
5193:
5187:
5185:
5179:
5178:
5163:Endopeptidases
5159:
5158:
5151:
5144:
5136:
5127:
5126:
5123:
5122:
5120:
5119:
5114:
5109:
5104:
5102:
5096:
5095:
5093:
5092:
5087:
5082:
5076:
5074:
5068:
5067:
5065:
5064:
5059:
5054:
5048:
5046:
5040:
5039:
5037:
5036:
5031:
5025:
5023:
5014:
5008:
5007:
5005:
5004:
4999:
4997:-Macroglobulin
4994:
4990:
4985:
4981:
4976:
4971:
4966:
4961:
4956:
4950:
4948:
4942:
4941:
4939:
4938:
4933:
4928:
4923:
4918:
4913:
4907:
4905:
4899:
4898:
4895:
4894:
4892:
4891:
4886:
4881:
4867:
4862:
4857:
4852:
4846:
4844:
4842:Common pathway
4838:
4837:
4835:
4834:
4829:
4823:
4821:
4813:
4812:
4810:
4809:
4804:
4799:
4794:
4789:
4784:
4779:
4774:
4768:
4766:
4758:
4757:
4755:
4754:
4749:
4743:
4734:
4728:
4723:
4708:
4702:
4700:
4689:
4683:
4682:
4675:
4674:
4667:
4660:
4652:
4643:
4642:
4640:
4639:
4633:
4626:
4624:
4618:
4611:
4609:
4603:
4596:
4594:
4588:
4581:
4579:
4573:
4566:
4564:
4558:
4551:
4549:
4543:
4536:
4534:
4528:
4521:
4519:
4513:
4506:
4504:
4498:
4491:
4489:
4483:
4476:
4474:
4468:
4461:
4459:
4453:
4446:
4444:
4438:
4431:
4429:
4423:
4416:
4414:
4408:
4401:
4399:
4393:
4386:
4384:
4378:
4371:
4369:
4363:
4356:
4354:
4348:
4341:
4339:
4333:
4326:
4324:
4318:
4311:
4309:
4303:
4296:
4294:
4288:
4281:
4279:
4273:
4266:
4264:
4258:
4251:
4249:
4243:
4236:
4234:
4228:
4221:
4219:
4213:
4206:
4204:
4198:
4191:
4189:
4183:
4176:
4174:
4168:
4161:
4159:
4153:
4146:
4144:
4138:
4131:
4129:
4123:
4116:
4114:
4108:
4101:
4099:
4093:
4086:
4084:
4078:
4071:
4069:
4063:
4056:
4054:
4048:
4041:
4039:
4033:
4026:
4024:
4018:
4011:
4009:
4003:
3996:
3994:
3988:
3981:
3979:
3973:
3966:
3964:
3958:
3951:
3949:
3943:
3936:
3934:
3928:
3921:
3919:
3913:
3906:
3904:
3898:
3891:
3889:
3883:
3876:
3874:
3868:
3861:
3859:
3853:
3846:
3844:
3838:
3831:
3829:
3823:
3816:
3814:
3808:
3801:
3799:
3793:
3786:
3784:
3778:
3771:
3769:
3763:
3756:
3753:
3750:
3749:
3744:
3743:
3736:
3729:
3721:
3715:
3714:
3702:
3686:
3685:External links
3683:
3681:
3680:
3666:
3664:
3661:
3659:
3658:
3623:
3605:(3): 947–966.
3594:
3574:(1): 153–163.
3559:
3506:
3476:
3450:(4): 910–915.
3438:
3408:
3355:
3326:
3305:
3285:(2): 335–343.
3270:
3241:
3206:
3188:(2): 517–519.
3177:
3124:
3106:(3): 369–384.
3095:
3060:
3042:(2): 291–294.
3031:
2996:
2970:(1): 161–172.
2958:
2956:
2953:
2950:
2949:
2928:(2): 335–343.
2908:
2879:(2): 315–327.
2859:
2832:(2): 364–370.
2816:
2765:
2744:(4): 411–447.
2724:
2705:
2675:10.1.1.536.872
2652:
2645:
2627:
2592:
2562:
2529:
2499:
2459:
2430:
2411:
2358:
2322:
2297:
2268:(2): 383–390.
2248:
2230:
2212:
2194:
2173:
2151:
2150:
2148:
2145:
2132:
2129:
2115:
2112:
2042:polymerization
1943:anticoagulants
1933:. Factor X is
1898:
1895:
1885:
1882:
1858:
1855:
1820:(nosebleeds),
1810:Main article:
1807:
1804:
1798:is located on
1791:
1788:
1760:
1757:
1734:prothrombinase
1646:gene. It is a
1616:
1615:
1612:
1611:
1606:
1596:
1595:
1589:
1588:
1585:
1584:
1582:
1580:
1573:
1572:
1565:
1558:
1554:
1553:
1550:
1549:
1535:
1534:
1528:
1525:
1524:
1506:
1505:
1499:
1495:
1494:
1491:
1490:
1476:
1475:
1469:
1466:
1465:
1447:
1446:
1440:
1436:
1435:
1432:
1431:
1423:
1422:
1416:
1413:
1412:
1404:
1403:
1397:
1391:
1390:
1387:
1386:
1378:
1377:
1371:
1368:
1367:
1359:
1358:
1352:
1346:
1345:
1342:
1341:
1333:
1332:
1326:
1323:
1322:
1314:
1313:
1307:
1301:
1300:
1295:
1290:
1286:
1285:
1275:
1274:
1271:
1270:
1259:
1258:
1256:
1255:
1250:
1245:
1240:
1235:
1230:
1225:
1219:
1217:
1213:
1212:
1210:
1209:
1204:
1199:
1194:
1189:
1184:
1178:
1176:
1172:
1171:
1169:
1168:
1163:
1158:
1153:
1148:
1143:
1138:
1132:
1130:
1126:
1125:
1115:
1114:
1111:
1110:
1107:
1106:
1098:
1097:
1086:
1080:
1079:
1076:
1075:
1067:
1066:
1063:
1062:
1060:
1059:
1055:
1051:
1047:
1043:
1039:
1035:
1031:
1027:
1023:
1019:
1016:
1015:
1004:
1001:
1000:
998:
997:
993:
989:
985:
981:
980:gastric mucosa
977:
973:
969:
965:
961:
957:
954:
953:
941:
940:
932:
921:
915:
914:
911:RNA expression
903:
902:
899:
898:
890:
886:
885:
877:
874:
869:
863:
862:
853:
846:
840:
836:
835:
830:
824:
823:
815:
814:
802:
801:
798:
797:
789:
785:
784:
776:
773:
768:
762:
761:
752:
745:
739:
735:
734:
727:
721:
720:
712:
711:
699:
698:
655:
651:
650:
642:
634:
633:
629:
628:
625:
624:
621:
620:
78:
77:
69:
68:
57:
51:
50:
42:
41:
33:
32:
17:
9:
6:
4:
3:
2:
5942:
5931:
5928:
5926:
5923:
5921:
5918:
5917:
5915:
5905:
5900:
5895:
5894:
5891:
5877:
5873:
5872:
5867:
5864:
5860:
5859:
5854:
5851:
5847:
5846:
5841:
5838:
5834:
5833:
5828:
5825:
5821:
5820:
5815:
5812:
5808:
5807:
5802:
5799:
5795:
5794:
5789:
5788:
5786:
5782:
5776:
5773:
5771:
5768:
5766:
5763:
5761:
5758:
5756:
5753:
5752:
5750:
5746:
5740:
5737:
5735:
5734:Enzyme family
5732:
5730:
5727:
5725:
5722:
5721:
5719:
5715:
5709:
5706:
5704:
5701:
5699:
5698:Cooperativity
5696:
5694:
5691:
5690:
5688:
5684:
5678:
5675:
5673:
5670:
5668:
5665:
5663:
5660:
5658:
5657:Oxyanion hole
5655:
5653:
5650:
5648:
5645:
5643:
5640:
5639:
5637:
5633:
5629:
5622:
5617:
5615:
5610:
5608:
5603:
5602:
5599:
5585:
5582:
5580:
5577:
5576:
5575:
5572:
5570:
5569:Streptokinase
5567:
5565:
5561:
5558:
5555:
5551:
5547:
5544:
5542:
5539:
5537:
5534:
5530:
5527:
5525:
5522:
5521:
5520:
5517:
5515:
5512:
5510:
5507:
5505:
5502:
5501:
5499:
5495:
5489:
5486:
5484:
5481:
5480:
5478:
5476:
5472:
5466:
5463:
5461:
5458:
5456:
5453:
5451:
5448:
5447:
5445:
5443:
5442:immune system
5438:
5432:
5431:C3-convertase
5429:
5425:
5422:
5420:
5417:
5416:
5415:
5412:
5410:
5407:
5405:
5402:
5400:
5397:
5396:
5394:
5392:
5388:
5380:
5377:
5375:
5372:
5371:
5370:
5367:
5365:
5362:
5360:
5356:
5355:
5350:
5347:
5345:
5342:
5340:
5337:
5335:
5332:
5330:
5327:
5325:
5322:
5320:
5317:
5315:
5312:
5310:
5307:
5305:
5302:
5300:
5297:
5295:
5292:
5290:
5287:
5285:
5282:
5280:
5277:
5275:
5272:
5271:
5270:
5267:
5265:
5262:
5260:
5257:
5255:
5252:
5250:
5247:
5245:
5242:
5240:
5237:
5234:
5233:
5231:
5229:
5225:
5217:
5214:
5212:
5209:
5208:
5207:
5204:
5202:
5199:
5197:
5194:
5192:
5189:
5188:
5186:
5184:
5180:
5175:
5172:
5168:
5164:
5157:
5152:
5150:
5145:
5143:
5138:
5137:
5134:
5118:
5115:
5113:
5106:
5105:
5103:
5101:
5097:
5091:
5088:
5086:
5083:
5081:
5078:
5077:
5075:
5073:
5069:
5063:
5060:
5058:
5055:
5053:
5050:
5049:
5047:
5045:
5041:
5035:
5032:
5030:
5027:
5026:
5024:
5022:
5018:
5015:
5013:
5009:
5003:
5000:
4998:
4991:
4989:
4982:
4980:
4977:
4975:
4972:
4970:
4967:
4965:
4962:
4960:
4957:
4955:
4952:
4951:
4949:
4947:
4943:
4937:
4934:
4932:
4929:
4927:
4924:
4922:
4919:
4917:
4914:
4912:
4909:
4908:
4906:
4904:
4900:
4890:
4887:
4885:
4882:
4879:
4875:
4871:
4868:
4866:
4863:
4861:
4858:
4856:
4853:
4851:
4848:
4847:
4845:
4843:
4839:
4833:
4830:
4828:
4825:
4824:
4822:
4820:
4814:
4808:
4805:
4803:
4800:
4798:
4795:
4793:
4790:
4788:
4785:
4783:
4782:Prekallikrein
4780:
4778:
4775:
4773:
4770:
4769:
4767:
4765:
4759:
4753:
4750:
4747:
4744:
4742:
4738:
4735:
4732:
4729:
4727:
4724:
4722:
4718:
4715:
4713:
4709:
4707:
4704:
4703:
4701:
4699:
4693:
4690:
4688:
4684:
4680:
4673:
4668:
4666:
4661:
4659:
4654:
4653:
4650:
4636:
4630:
4625:
4621:
4615:
4610:
4606:
4600:
4595:
4591:
4585:
4580:
4576:
4570:
4565:
4561:
4555:
4550:
4546:
4540:
4535:
4531:
4525:
4520:
4516:
4510:
4505:
4501:
4495:
4490:
4486:
4480:
4475:
4471:
4465:
4460:
4456:
4450:
4445:
4441:
4435:
4430:
4426:
4420:
4415:
4411:
4405:
4400:
4396:
4390:
4385:
4381:
4375:
4370:
4366:
4360:
4355:
4351:
4345:
4340:
4336:
4330:
4325:
4321:
4315:
4310:
4306:
4300:
4295:
4291:
4285:
4280:
4276:
4270:
4265:
4261:
4255:
4250:
4246:
4240:
4235:
4231:
4225:
4220:
4216:
4210:
4205:
4201:
4195:
4190:
4186:
4180:
4175:
4171:
4165:
4160:
4156:
4150:
4145:
4141:
4135:
4130:
4126:
4120:
4115:
4111:
4105:
4100:
4096:
4090:
4085:
4081:
4075:
4070:
4066:
4060:
4055:
4051:
4045:
4040:
4036:
4030:
4025:
4021:
4015:
4010:
4006:
4000:
3995:
3991:
3985:
3980:
3976:
3970:
3965:
3961:
3955:
3950:
3946:
3940:
3935:
3931:
3925:
3920:
3916:
3910:
3905:
3901:
3895:
3890:
3886:
3880:
3875:
3871:
3865:
3860:
3856:
3850:
3845:
3841:
3835:
3830:
3826:
3820:
3815:
3811:
3805:
3800:
3796:
3790:
3785:
3781:
3775:
3770:
3766:
3760:
3755:
3754:
3751:
3742:
3737:
3735:
3730:
3728:
3723:
3722:
3719:
3711:
3707:
3703:
3699:
3698:
3693:
3689:
3688:
3677:
3673:
3668:
3667:
3655:
3651:
3646:
3641:
3637:
3633:
3629:
3624:
3620:
3616:
3612:
3608:
3604:
3600:
3595:
3591:
3587:
3582:
3577:
3573:
3569:
3565:
3560:
3556:
3552:
3547:
3542:
3537:
3532:
3528:
3524:
3520:
3516:
3512:
3507:
3503:
3499:
3495:
3491:
3487:
3483:
3477:
3473:
3469:
3465:
3461:
3457:
3453:
3449:
3445:
3439:
3435:
3431:
3427:
3423:
3419:
3415:
3409:
3405:
3401:
3396:
3391:
3386:
3381:
3377:
3373:
3369:
3365:
3361:
3356:
3352:
3348:
3344:
3340:
3336:
3332:
3327:
3323:
3319:
3315:
3311:
3306:
3302:
3298:
3293:
3288:
3284:
3280:
3276:
3271:
3267:
3263:
3259:
3255:
3251:
3247:
3242:
3238:
3234:
3229:
3224:
3220:
3216:
3212:
3207:
3203:
3199:
3195:
3191:
3187:
3183:
3178:
3174:
3170:
3165:
3160:
3155:
3150:
3146:
3142:
3138:
3134:
3130:
3125:
3121:
3117:
3113:
3109:
3105:
3101:
3096:
3092:
3088:
3083:
3078:
3074:
3070:
3066:
3061:
3057:
3053:
3049:
3045:
3041:
3037:
3032:
3028:
3024:
3019:
3014:
3010:
3006:
3002:
2997:
2993:
2989:
2985:
2981:
2977:
2973:
2969:
2965:
2960:
2959:
2945:
2941:
2936:
2931:
2927:
2923:
2919:
2912:
2904:
2900:
2895:
2890:
2886:
2882:
2878:
2874:
2870:
2863:
2855:
2851:
2847:
2843:
2839:
2835:
2831:
2827:
2820:
2812:
2808:
2804:
2800:
2796:
2792:
2788:
2784:
2780:
2776:
2769:
2761:
2757:
2752:
2747:
2743:
2739:
2735:
2728:
2720:
2716:
2709:
2701:
2697:
2693:
2689:
2685:
2681:
2676:
2671:
2667:
2663:
2656:
2648:
2642:
2638:
2631:
2623:
2619:
2615:
2611:
2607:
2603:
2596:
2580:
2576:
2572:
2566:
2550:
2546:
2544:
2539:
2533:
2517:
2513:
2509:
2503:
2495:
2489:
2473:
2469:
2463:
2456:
2444:
2440:
2434:
2426:
2422:
2415:
2407:
2403:
2398:
2393:
2389:
2385:
2381:
2377:
2373:
2371:
2362:
2355:
2343:
2339:
2338:
2333:
2326:
2312:on 2016-03-03
2311:
2307:
2301:
2293:
2289:
2284:
2279:
2275:
2271:
2267:
2263:
2259:
2252:
2244:
2240:
2234:
2226:
2222:
2216:
2208:
2204:
2198:
2191:
2187:
2182:
2180:
2178:
2170:
2166:
2161:
2159:
2157:
2152:
2144:
2142:
2138:
2128:
2124:
2120:
2111:
2108:
2104:
2100:
2096:
2092:
2087:
2084:
2080:
2076:
2071:
2069:
2065:
2064:acenocoumarol
2061:
2060:phenprocoumon
2057:
2052:
2049:
2047:
2043:
2040:
2036:
2032:
2028:
2024:
2019:
2017:
2012:
2010:
2006:
2002:
1998:
1995:binds to the
1994:
1989:
1987:
1981:
1979:
1975:
1971:
1970:phospholipids
1967:
1963:
1958:
1956:
1952:
1948:
1944:
1940:
1936:
1932:
1928:
1924:
1920:
1919:thrombokinase
1916:
1908:
1903:
1894:
1891:
1881:
1878:
1876:
1872:
1868:
1864:
1854:
1851:
1849:
1844:
1842:
1838:
1834:
1829:
1827:
1823:
1819:
1813:
1803:
1801:
1800:chromosome 13
1797:
1787:
1785:
1781:
1777:
1773:
1766:
1756:
1754:
1750:
1746:
1742:
1737:
1735:
1731:
1727:
1723:
1719:
1715:
1711:
1707:
1702:
1700:
1696:
1692:
1688:
1687:tissue factor
1684:
1680:
1676:
1672:
1668:
1663:
1661:
1658:and requires
1657:
1653:
1649:
1645:
1641:
1637:
1633:
1632:Stuart factor
1629:
1626:
1622:
1610:
1605:
1601:
1597:
1594:
1590:
1583:
1581:
1578:
1574:
1570:
1566:
1563:
1559:
1555:
1548:
1546:
1542:
1536:
1532:
1529:
1523:
1521:
1517:
1513:
1507:
1503:
1500:
1496:
1489:
1487:
1483:
1477:
1473:
1470:
1464:
1462:
1458:
1454:
1448:
1444:
1441:
1439:RefSeq (mRNA)
1437:
1430:
1429:
1424:
1420:
1417:
1411:
1410:
1405:
1401:
1398:
1396:
1392:
1385:
1384:
1379:
1375:
1372:
1366:
1365:
1360:
1356:
1353:
1351:
1347:
1340:
1339:
1334:
1330:
1327:
1321:
1320:
1315:
1311:
1308:
1306:
1302:
1299:
1296:
1294:
1291:
1287:
1284:
1280:
1276:
1269:
1265:
1260:
1254:
1251:
1249:
1246:
1244:
1241:
1239:
1236:
1234:
1231:
1229:
1226:
1224:
1221:
1220:
1218:
1215:
1214:
1208:
1205:
1203:
1200:
1198:
1195:
1193:
1190:
1188:
1185:
1183:
1180:
1179:
1177:
1174:
1173:
1167:
1164:
1162:
1159:
1157:
1154:
1152:
1149:
1147:
1144:
1142:
1139:
1137:
1134:
1133:
1131:
1128:
1127:
1124:
1123:Gene ontology
1120:
1116:
1104:
1099:
1095:
1090:
1087:
1085:
1081:
1073:
1068:
1057:
1053:
1049:
1045:
1041:
1037:
1033:
1029:
1025:
1021:
1020:
1017:
1013:
1008:
1005:
995:
991:
987:
983:
979:
975:
971:
968:right auricle
967:
963:
959:
958:
955:
951:
946:
943:
942:
939:
937:
933:
931:
930:
926:
925:
922:
920:
916:
912:
908:
904:
896:
891:
887:
883:
878:
868:
864:
857:
850:
844:
837:
829:
825:
821:
816:
812:
807:
803:
795:
790:
786:
782:
777:
767:
763:
756:
749:
743:
736:
732:
726:
722:
718:
713:
709:
704:
700:
696:
692:
688:
684:
680:
676:
672:
668:
664:
660:
652:
647:
640:
635:
630:
619:
617:
613:
609:
605:
601:
597:
593:
589:
585:
581:
577:
573:
569:
565:
561:
557:
553:
549:
545:
541:
537:
533:
529:
525:
521:
517:
513:
509:
505:
501:
497:
493:
489:
485:
481:
477:
473:
469:
465:
461:
457:
453:
449:
445:
441:
437:
433:
429:
425:
421:
417:
413:
409:
405:
401:
397:
393:
389:
385:
381:
377:
373:
369:
365:
361:
357:
353:
349:
345:
341:
337:
333:
329:
325:
321:
317:
313:
309:
305:
301:
297:
293:
289:
285:
281:
277:
273:
269:
265:
261:
257:
253:
249:
245:
241:
237:
233:
229:
225:
221:
217:
213:
209:
205:
201:
197:
193:
189:
185:
181:
177:
173:
169:
165:
161:
157:
153:
149:
145:
141:
137:
133:
129:
125:
121:
117:
113:
109:
105:
101:
97:
93:
89:
85:
79:
74:
71:
70:
66:
63:
56:
52:
47:
43:
39:
34:
29:
24:
16:
5871:Translocases
5868:
5855:
5842:
5829:
5816:
5806:Transferases
5803:
5790:
5647:Binding site
5359:fibrinolysis
5357:
5253:
5235:
5201:Chymotrypsin
5117:D-Dimer (DD)
5100:Fibrinolysis
4988:-Antiplasmin
4849:
4710:
4634:
4619:
4604:
4589:
4574:
4559:
4544:
4529:
4514:
4499:
4484:
4469:
4454:
4439:
4424:
4409:
4394:
4379:
4364:
4349:
4334:
4319:
4304:
4289:
4274:
4259:
4244:
4229:
4214:
4199:
4184:
4169:
4154:
4139:
4124:
4109:
4094:
4079:
4064:
4049:
4034:
4019:
4004:
3989:
3974:
3959:
3944:
3929:
3914:
3899:
3884:
3869:
3854:
3839:
3824:
3809:
3794:
3779:
3764:
3709:
3695:
3678:. WebMD LLC.
3675:
3635:
3631:
3602:
3598:
3571:
3567:
3518:
3514:
3485:
3482:Biochemistry
3481:
3447:
3443:
3417:
3414:Biochemistry
3413:
3367:
3363:
3334:
3331:Biochemistry
3330:
3316:(1): 32–35.
3313:
3309:
3282:
3278:
3249:
3245:
3218:
3214:
3185:
3181:
3136:
3132:
3103:
3099:
3072:
3068:
3039:
3035:
3008:
3004:
2967:
2963:
2925:
2921:
2911:
2876:
2872:
2862:
2829:
2825:
2819:
2778:
2774:
2768:
2741:
2737:
2727:
2718:
2714:
2708:
2665:
2661:
2655:
2636:
2630:
2605:
2601:
2595:
2583:. Retrieved
2574:
2565:
2553:. Retrieved
2541:
2532:
2520:. Retrieved
2511:
2502:
2476:. Retrieved
2471:
2462:
2454:
2447:. Retrieved
2443:the original
2433:
2420:
2414:
2379:
2375:
2369:
2361:
2352:
2346:. Retrieved
2335:
2325:
2314:. Retrieved
2310:the original
2300:
2265:
2261:
2251:
2242:
2233:
2224:
2215:
2206:
2197:
2134:
2131:Interactions
2125:
2121:
2117:
2101:, LY517717,
2088:
2072:
2053:
2050:
2027:Factor VIIIa
2020:
2013:
2007:to form the
1991:In stage 1,
1990:
1982:
1959:
1955:fondaparinux
1918:
1912:
1906:
1890:protein tags
1887:
1879:
1873:produced by
1870:
1860:
1852:
1845:
1830:
1822:hemarthrosis
1815:
1793:
1768:
1738:
1716:and then an
1703:
1698:
1694:
1666:
1664:
1643:
1631:
1620:
1619:
1541:NP_001229297
1538:
1520:NP_001299604
1516:NP_001299603
1509:
1482:NM_001242368
1479:
1461:NM_001312675
1457:NM_001312674
1450:
1426:
1407:
1381:
1362:
1336:
1317:
1297:
1292:
934:
927:
792:113,149,529
779:113,122,799
654:External IDs
81:
15:
5642:Active site
5264:Factor XIIa
5244:Factor VIIa
5228:Coagulation
4954:Plasminogen
4889:Factor XIII
4807:Factor VIII
3747:PDB gallery
2608:(1): 1–11.
2449:October 21,
2091:rivaroxaban
2035:prothrombin
1935:synthesized
1867:CSL Behring
1826:amyloidosis
1730:co-factor V
1706:prothrombin
1675:factor VIII
1243:proteolysis
1202:Golgi lumen
1058:bone marrow
1054:granulocyte
1030:gallbladder
984:right ovary
893:13,106,676
880:13,087,308
632:Identifiers
5914:Categories
5845:Isomerases
5819:Hydrolases
5686:Regulation
5546:Subtilisin
5488:Batroxobin
5269:Kallikrein
5259:Factor XIa
5249:Factor IXa
5216:Pancreatic
5211:Neutrophil
4832:Factor VII
4787:Kallikrein
4777:Bradykinin
2721:: 432–442.
2508:"Coagadex"
2468:"Coagadex"
2372:Infection"
2348:2008-01-06
2316:2010-04-08
2192:, May 2017
2171:, May 2017
2147:References
2099:betrixaban
2081:cofactor,
2077:bind to a
2044:to form a
2029:forms the
2023:Factor XIa
1993:Factor VII
1837:thrombosis
1763:See also:
1683:factor VII
1223:hemostasis
988:left ovary
976:ectocervix
938:(ortholog)
675:HomoloGene
5925:EC 3.4.21
5724:EC number
5574:Cathepsin
5560:Sedolisin
5536:Prostasin
5254:Factor Xa
5108:Plasmin-α
4969:Urokinase
4802:Factor IX
4797:Factor XI
2854:231682954
2670:CiteSeerX
2105:(YM150),
2103:darexaban
2016:cofactors
2005:Factor Va
2001:Factor IX
1897:Factor Xa
1818:epistaxis
1802:(13q34).
1778:195, and
1759:Structure
1753:factor XI
1749:protein Z
1743:(ZPI), a
1736:complex.
1671:factor IX
1667:factor Xa
1660:vitamin K
1545:NP_031998
1512:NP_000495
1486:NM_007972
1453:NM_000504
1283:Orthologs
683:GeneCards
5748:Kinetics
5672:Cofactor
5635:Activity
5475:Venombin
5460:Tryptase
5455:Granzyme
5409:Factor I
5404:Factor D
5399:Factor B
5239:Thrombin
5236:factors:
5206:Elastase
4855:Factor V
4850:Factor X
3676:MedScape
3472:29324903
2992:27129058
2903:14080818
2846:33484373
2811:35643683
2803:17741228
2760:13012730
2738:Medicine
2692:17379841
2622:17258114
2585:21 April
2579:Archived
2575:DailyMed
2555:21 April
2549:Archived
2516:Archived
2488:cite web
2406:30782860
2354:cascade.
2342:Archived
2292:33886037
2188:–
2167:–
2137:interact
2107:edoxaban
2095:apixaban
2056:coumarin
2046:thrombus
2018:occurs.
1986:platelet
1949:and the
1947:warfarin
1871:Coagadex
1833:warfarin
1790:Genetics
1726:thrombin
1669:by both
1634:, is an
1628:3.4.21.6
1593:Wikidata
1262:Sources:
1026:yolk sac
5904:Biology
5858:Ligases
5628:Enzymes
5514:Pronase
5504:Acrosin
5450:Chymase
5364:Plasmin
5196:Trypsin
4959:Plasmin
3654:8428982
3619:8355279
3590:8243461
3555:8146182
3523:Bibcode
3502:8136380
3464:7669671
3434:6871167
3404:6587384
3372:Bibcode
3351:3768336
3322:3487272
3301:3422166
3266:3011603
3237:2790181
3202:2612918
3173:2582420
3141:Bibcode
3120:2551064
3091:2303476
3056:1902434
3027:1698100
2984:9198147
2944:3422166
2894:2195336
2783:Bibcode
2775:Science
2700:2998452
2522:2 April
2478:2 April
2397:6479028
2283:8531165
2190:Ensembl
2169:Ensembl
2114:History
1966:calcium
1951:heparin
1937:in the
1907:in vivo
1732:in the
1652:PA clan
1638:of the
1630:), or
1395:UniProt
1350:Ensembl
1289:Species
1268:QuickGO
913:pattern
639:Aliases
5890:Portal
5832:Lyases
5541:Reelin
5483:Ancrod
5440:Other
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4746:GPIIIa
3697:MEROPS
3652:
3617:
3588:
3553:
3543:
3500:
3470:
3462:
3432:
3402:
3395:345286
3392:
3349:
3320:
3299:
3264:
3235:
3200:
3171:
3164:397831
3161:
3118:
3089:
3054:
3025:
2990:
2982:
2942:
2901:
2891:
2852:
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2643:
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280:2G00
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268:2EI7
264:2EI6
260:2D1J
256:2CJI
252:2BQW
248:2BQ7
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232:2BMG
228:1Z6E
224:1XKB
220:1XKA
216:1WU1
212:1V3X
208:1P0S
204:1NFY
200:1NFX
196:1NFW
192:1NFU
188:1MQ6
184:1MQ5
180:1LQD
176:1LPZ
172:1LPK
168:1LPG
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160:1IQN
156:1IQM
152:1IQL
148:1IQK
144:1IQJ
140:1IQI
136:1IQH
132:1IQG
128:1IQF
124:1IQE
120:1IOE
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112:1G2M
108:1G2L
104:1FJS
100:1FAX
96:1F0S
92:1F0R
88:1EZQ
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65:RCSB
62:PDBe
5554:S1P
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4878:FGG
4874:FGA
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3607:doi
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889:End
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687:F10
667:MGI
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