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Factor IX

January 01, 1970

Factor IX (or Christmas factor) (EC 3.4.21.22) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes haemophilia B. It was discovered in 1952 after a young boy named Stephen Christmas was found to be lacking this exact factor, leading to haemophilia.[5]

F9
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesF9, F9 p22, FIX, HEMB, P19, PTC, THPH8, coagulation factor IX, Blood coagulation factor IX, Christmas Factor
External IDsOMIM: 300746 MGI: 88384 HomoloGene: 106 GeneCards: F9
Orthologs
SpeciesHumanMouse
Entrez

2158

14071

Ensembl

ENSG00000101981

ENSMUSG00000031138

UniProt

P00740

P16294

RefSeq (mRNA)

NM_000133
NM_001313913

NM_007979
NM_001305797

RefSeq (protein)

NP_000124
NP_001300842

NP_001292726
NP_032005

Location (UCSC)Chr X: 139.53 – 139.56 MbChr X: 59.04 – 59.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Coagulation factor IX is on the World Health Organization's List of Essential Medicines.[6]

Physiology edit

 
The blood coagulation and Protein C pathway.

Factor IX is produced as a zymogen, an inactive precursor. It is processed to remove the signal peptide, glycosylated and then cleaved by factor XIa (of the contact pathway) or factor VIIa (of the tissue factor pathway) to produce a two-chain form, where the chains are linked by a disulfide bridge.[7][8] When activated into factor IXa, in the presence of Ca2+, membrane phospholipids, and a Factor VIII cofactor, it hydrolyses one arginine-isoleucine bond in factor X to form factor Xa.

Factor IX is inhibited by antithrombin.[7]

Factor IX expression increases with age in humans and mice. In mouse models, mutations within the promoter region of factor IX have an age-dependent phenotype.[9]

Domain architecture edit

Factors VII, IX, and X all play key roles in blood coagulation and also share a common domain architecture.[10] The factor IX protein is composed of four protein domains: the Gla domain, two tandem copies of the EGF domain and a C-terminal trypsin-like peptidase domain which carries out the catalytic cleavage.

 
Human factor IX protein domain architecture, where each protein domain is represented by a coloured box

The N-terminal EGF domain has been shown to at least in part be responsible for binding tissue factor.[10] Wilkinson et al. conclude that residues 88 to 109 of the second EGF domain mediate binding to platelets and assembly of the factor X activating complex.[11]

The structures of all four domains have been solved. A structure of the two EGF domains and the trypsin-like domain was determined for the pig protein.[12] The structure of the Gla domain, which is responsible for Ca(II)-dependent phospholipid binding, was also determined by NMR.[13]

Several structures of 'super active' mutants have been solved,[14] which reveal the nature of factor IX activation by other proteins in the clotting cascade.

Genetics edit

 
In human, the F9 gene is located on the X chromosome at position q27.1.

Because the gene for factor IX is located on the X chromosome (Xq27.1-q27.2), loss-of-function mutations thereof are X-linked recessive: males experience the disease phenotype much more frequently than females. At least 534 disease-causing mutations in this gene have been discovered.[15] The F9 gene was first cloned in 1982 by Kotoku Kurachi and Earl Davie.[16]

Polly, a transgenic cloned Poll Dorset sheep carrying the gene for factor IX, was produced by Dr Ian Wilmut at the Roslin Institute in 1997.[17]

Role in disease edit

See also: Prothrombin complex concentrate

Factor IX
INN: nonacog alfa
Clinical data
Trade namesBenefix
License data
ATC code
  • None
Legal status
Legal status
  • AU: S4 (Prescription only)
Factor IX
INN: albutrepenonacog alfa
Clinical data
Trade namesIdelvion
License data
ATC code
  • None
Legal status
Legal status
Factor IX
INN: eftrenonacog alfa
Clinical data
Trade namesAlprolix
License data
ATC code
  • None
Legal status
Legal status
  • AU: S4 (Prescription only)
Factor IX
INN: nonacog beta pegol
Clinical data
Trade namesRefixia
ATC code
  • None
Legal status
Legal status
  • AU: S4 (Prescription only)

Deficiency of factor IX causes Christmas disease (hemophilia B).[5] Over 3000 variants of factor IX have been described, affecting 73% of the 461 residues;[19] some cause no symptoms, but many lead to a significant bleeding disorder. The original Christmas disease mutation was identified by sequencing of Christmas' DNA, revealing a mutation which changed a cysteine to a serine.[20] Recombinant factor IX is used to treat Christmas disease. Formulations include:

  • nonacog alfa (brand name Benefix)[21]
  • albutrepenonacog alfa (brand name Idelvion)[22]
  • eftrenonacog alfa (brand name Alprolix)[23]
  • nonacog beta pegol (brand name Refixia)[24]
  • coagulation factor IX [recombinant] (Benefix)[25]
  • coagulation factor IX [recombinant] (Idelvion)[26]
  • coagulation factor IX (recombinant), Fc fusion protein (Alprolix)[27]
  • coagulation factor IX [recombinant] (Ixinity)[28][29]
  • coagulation factor IX [recombinant] (Rebinyn)[30]
  • coagulation factor IX [recombinant] (Rixubis)[31]
  • coagulation factor IX (human) (Alphanine SD)[32]

Some rare mutations of factor IX result in elevated clotting activity, and can result in clotting diseases, such as deep vein thrombosis. This gain of function mutation renders the protein hyperfunctional and is associated with familial early-onset thrombophilia.[33]

Factor IX deficiency is treated by injection of purified factor IX produced through cloning in various animal or animal cell vectors. Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding.[34]

A list of all the mutations in Factor IX is compiled and maintained by EAHAD.[35]

Coagulation factor IX is on the World Health Organization's List of Essential Medicines.[6]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101981 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031138 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Biggs R, Douglas AS, Macfarlane RG, Dacie JV, Pitney WR (Dec 1952). "Christmas disease: a condition previously mistaken for haemophilia". British Medical Journal. 2 (4799): 1378–82. doi:10.1136/bmj.2.4799.1378. PMC 2022306. PMID 12997790.
  6. ^ a b World Health Organization (2019). World Health Organization model list of essential medicines: 21st list 2019. Geneva: World Health Organization. hdl:10665/325771. WHO/MVP/EMP/IAU/2019.06. License: CC BY-NC-SA 3.0 IGO.
  7. ^ a b Di Scipio RG, Kurachi K, Davie EW (Jun 1978). "Activation of human factor IX (Christmas factor)". The Journal of Clinical Investigation. 61 (6): 1528–38. doi:10.1172/JCI109073. PMC 372679. PMID 659613.
  8. ^ Taran LD (Jul 1997). "Factor IX of the blood coagulation system: a review". Biochemistry. Biokhimiia. 62 (7): 685–93. PMID 9331959.
  9. ^ Boland EJ, Liu YC, Walter CA, Herbert DC, Weaker FJ, Odom MW, Jagadeeswaran P (Sep 1995). "Age-specific regulation of clotting factor IX gene expression in normal and transgenic mice". Blood. 86 (6): 2198–205. doi:10.1182/blood.V86.6.2198.bloodjournal8662198. PMID 7662969.
  10. ^ a b Zhong D, Bajaj MS, Schmidt AE, Bajaj SP (Feb 2002). "The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor". The Journal of Biological Chemistry. 277 (5): 3622–31. doi:10.1074/jbc.M111202200. PMID 11723140.
  11. ^ Wilkinson FH, Ahmad SS, Walsh PN (Feb 2002). "The factor IXa second epidermal growth factor (EGF2) domain mediates platelet binding and assembly of the factor X activating complex". The Journal of Biological Chemistry. 277 (8): 5734–41. doi:10.1074/jbc.M107753200. PMID 11714704.
  12. ^ Brandstetter H, Bauer M, Huber R, Lollar P, Bode W (Oct 1995). "X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B". Proceedings of the National Academy of Sciences of the United States of America. 92 (21): 9796–800. Bibcode:1995PNAS...92.9796B. doi:10.1073/pnas.92.21.9796. PMC 40889. PMID 7568220.
  13. ^ Freedman SJ, Furie BC, Furie B, Baleja JD (Sep 1995). "Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX". Biochemistry. 34 (38): 12126–37. doi:10.1021/bi00038a005. PMID 7547952.
  14. ^ Zögg T, Brandstetter H (Dec 2009). "Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa". Structure. 17 (12): 1669–78. doi:10.1016/j.str.2009.10.011. PMID 20004170.
  15. ^ Šimčíková D, Heneberg P (December 2019). "Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases". Scientific Reports. 9 (1): 18577. Bibcode:2019NatSR...918577S. doi:10.1038/s41598-019-54976-4. PMC 6901466. PMID 31819097.
  16. ^ Kurachi K, Davie EW (Nov 1982). "Isolation and characterization of a cDNA coding for human factor IX". Proceedings of the National Academy of Sciences of the United States of America. 79 (21): 6461–4. Bibcode:1982PNAS...79.6461K. doi:10.1073/pnas.79.21.6461. PMC 347146. PMID 6959130.
  17. ^ Nicholl D. (2002). An Introduction to Genetic Engineering Second Edition. Cambridge University Press. p. 257.
  18. ^ "Health Canada New Drug Authorizations: 2016 Highlights". Health Canada. 14 March 2017. Retrieved 7 April 2024.
  19. ^ Goodeve AC (2015). "Hemophilia B: Molecular pathogenesis and mutation analysis". Journal of Thrombosis and Haemostasis. 13 (7): 1184–1195. doi:10.1111/jth.12958. PMC 4496316. PMID 25851415.
  20. ^ Taylor SA, Duffin J, Cameron C, Teitel J, Garvey B, Lillicrap DP (Jan 1992). "Characterization of the original Christmas disease mutation (cysteine 206----serine): from clinical recognition to molecular pathogenesis". Thrombosis and Haemostasis. 67 (1): 63–5. doi:10.1055/s-0038-1648381. PMID 1615485. S2CID 25251813.
  21. ^ "BeneFIX EPAR". European Medicines Agency (EMA). 17 September 2018. from the original on 17 June 2020. Retrieved 17 June 2020.
  22. ^ "Idelvion EPAR". European Medicines Agency (EMA). 17 September 2018. from the original on 17 June 2020. Retrieved 17 June 2020.
  23. ^ "Alprolix EPAR". European Medicines Agency (EMA). 17 September 2018. from the original on 11 August 2020. Retrieved 17 June 2020.
  24. ^ "Refixia EPAR". European Medicines Agency (EMA). 17 September 2018. from the original on 18 June 2020. Retrieved 17 June 2020.
  25. ^ "Benefix (coagulation factor ix- recombinant kit". DailyMed. 1 March 2023. from the original on 29 January 2023. Retrieved 23 March 2024.
  26. ^ "Idelvion- coagulation factor ix recombinant human kit". DailyMed. 30 June 2023. from the original on 27 January 2023. Retrieved 23 March 2024.
  27. ^ "Alprolix (coagulation factor ix- recombinant, fc fusion protein kit". DailyMed. 25 May 2023. from the original on 7 February 2023. Retrieved 23 March 2024.
  28. ^ "Ixinity (coagulation factor ix- recombinant kit". DailyMed. 23 February 2021. from the original on 28 September 2023. Retrieved 23 March 2024.
  29. ^ "Ixinity (coagulation factor ix- recombinant kit". DailyMed. 9 January 2024. from the original on 3 December 2022. Retrieved 23 March 2024.
  30. ^ "Rebinyn ((coagulation factor ix- recombinant, glycopegylated kit". DailyMed. 11 August 2022. from the original on 29 November 2022. Retrieved 23 March 2024.
  31. ^ "Rixubis (coagulation factor ix- recombinant kit". DailyMed. 22 March 2023. from the original on 2 July 2022. Retrieved 23 March 2024.
  32. ^ "Alphanine SD (coagulation factor ix- human kit". DailyMed. 18 January 2024. from the original on 18 February 2024. Retrieved 23 March 2024.
  33. ^ Simioni P, Tormene D, Tognin G, Gavasso S, Bulato C, Iacobelli NP, Finn JD, Spiezia L, Radu C, Arruda VR (Oct 2009). "X-linked thrombophilia with a mutant factor IX (factor IX Padua)". The New England Journal of Medicine. 361 (17): 1671–5. doi:10.1056/NEJMoa0904377. PMID 19846852.
  34. ^ Rossi M, Jayaram R, Sayeed R (Sep 2011). "Do patients with haemophilia undergoing cardiac surgery have good surgical outcomes?". Interactive Cardiovascular and Thoracic Surgery. 13 (3): 320–31. doi:10.1510/icvts.2011.272401. PMID 21712351.
  35. ^ "Home: EAHAD Factor 9 Gene Variant Database". from the original on 2020-10-28. Retrieved 2020-10-23.

Further reading edit

  • Davie EW, Fujikawa K (1975). "Basic mechanisms in blood coagulation". Annual Review of Biochemistry. 44: 799–829. doi:10.1146/annurev.bi.44.070175.004055. PMID 237463.
  • Sommer SS (Jul 1992). "Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene". FASEB Journal. 6 (10): 2767–74. doi:10.1096/fasebj.6.10.1634040. PMID 1634040. S2CID 15211597.
  • Lenting PJ, van Mourik JA, Mertens K (Dec 1998). "The life cycle of coagulation factor VIII in view of its structure and function". Blood. 92 (11): 3983–96. doi:10.1182/blood.V92.11.3983. PMID 9834200.
  • Lowe GD (Dec 2001). "Factor IX and thrombosis" (PDF). British Journal of Haematology. 115 (3): 507–13. doi:10.1046/j.1365-2141.2001.03186.x. PMID 11736930. S2CID 44650866. (PDF) from the original on 2021-06-19. Retrieved 2019-12-11.
  • O'Connell NM (Jun 2003). "Factor XI deficiency--from molecular genetics to clinical management". Blood Coagulation & Fibrinolysis. 14 (Suppl 1): S59-64. doi:10.1097/00001721-200306001-00014. PMID 14567539.
  • Du X (May 2007). "Signaling and regulation of the platelet glycoprotein Ib-IX-V complex". Current Opinion in Hematology. 14 (3): 262–9. doi:10.1097/MOH.0b013e3280dce51a. PMID 17414217. S2CID 39904506.

External links edit

  • Overview of all the structural information available in the PDB for UniProt: P00740 (Coagulation factor IX) at the PDBe-KB.
  • GeneReviews/NCBI/NIH/UW entry on Hemophilia B
  • The MEROPS online database for peptidases and their inhibitors: S01.214 2005-05-05 at the Wayback Machine

January 01, 1970
factor, christmas, factor, serine, proteases, coagulation, system, belongs, peptidase, family, deficiency, this, protein, causes, haemophilia, discovered, 1952, after, young, named, stephen, christmas, found, lacking, this, exact, factor, leading, haemophilia,. Factor IX or Christmas factor EC 3 4 21 22 is one of the serine proteases of the coagulation system it belongs to peptidase family S1 Deficiency of this protein causes haemophilia B It was discovered in 1952 after a young boy named Stephen Christmas was found to be lacking this exact factor leading to haemophilia 5 F9Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1CFH 1CFI 1EDM 1IXA 1MGX 1NL0 1RFN 2WPH 2WPI 2WPJ 2WPK 2WPL 2WPM 3KCG 3LC3 3LC5 4YZU 4Z0K 4ZAE 4WM0 4WMA 4WMI 4WMK 4WN2 4WNH 5EGM 5JBC 5JB9 5JBB 5JB8 5JBAIdentifiersAliasesF9 F9 p22 FIX HEMB P19 PTC THPH8 coagulation factor IX Blood coagulation factor IX Christmas FactorExternal IDsOMIM 300746 MGI 88384 HomoloGene 106 GeneCards F9Gene location Human Chr X chromosome human 1 BandXq27 1Start139 530 739 bp 1 End139 563 459 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX A6 X 33 5 cMStart59 044 824 bp 2 End59 076 119 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright lobe of liversecondary oocytepancreatic ductal cellkidneybloodhuman musculoskeletal systemmuscular systemmusclemusclekidneyTop expressed inleft lobe of livergallbladdersexually immature organismthoracic diaphragmdentate gyruspiriform cortexjejunumentorhinal cortexhippocampus properbrown adipose tissueMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionendopeptidase activity metal ion binding peptidase activity serine type peptidase activity hydrolase activity calcium ion binding serine type endopeptidase activity protein bindingCellular componentendoplasmic reticulum lumen plasma membrane Golgi lumen extracellular exosome extracellular region extracellular space collagen containing extracellular matrixBiological processhemostasis blood coagulation intrinsic pathway zymogen activation endoplasmic reticulum to Golgi vesicle mediated transport signal peptide processing blood coagulation extrinsic pathway peptidyl glutamic acid carboxylation proteolysis blood coagulationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez215814071EnsemblENSG00000101981ENSMUSG00000031138UniProtP00740P16294RefSeq mRNA NM 000133NM 001313913NM 007979NM 001305797RefSeq protein NP 000124NP 001300842NP 001292726NP 032005Location UCSC Chr X 139 53 139 56 MbChr X 59 04 59 08 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Coagulation factor IX is on the World Health Organization s List of Essential Medicines 6 Contents 1 Physiology 2 Domain architecture 3 Genetics 4 Role in disease 5 References 6 Further reading 7 External linksPhysiology edit nbsp The blood coagulation and Protein C pathway Factor IX is produced as a zymogen an inactive precursor It is processed to remove the signal peptide glycosylated and then cleaved by factor XIa of the contact pathway or factor VIIa of the tissue factor pathway to produce a two chain form where the chains are linked by a disulfide bridge 7 8 When activated into factor IXa in the presence of Ca2 membrane phospholipids and a Factor VIII cofactor it hydrolyses one arginine isoleucine bond in factor X to form factor Xa Factor IX is inhibited by antithrombin 7 Factor IX expression increases with age in humans and mice In mouse models mutations within the promoter region of factor IX have an age dependent phenotype 9 Domain architecture editFactors VII IX and X all play key roles in blood coagulation and also share a common domain architecture 10 The factor IX protein is composed of four protein domains the Gla domain two tandem copies of the EGF domain and a C terminal trypsin like peptidase domain which carries out the catalytic cleavage nbsp Human factor IX protein domain architecture where each protein domain is represented by a coloured box The N terminal EGF domain has been shown to at least in part be responsible for binding tissue factor 10 Wilkinson et al conclude that residues 88 to 109 of the second EGF domain mediate binding to platelets and assembly of the factor X activating complex 11 The structures of all four domains have been solved A structure of the two EGF domains and the trypsin like domain was determined for the pig protein 12 The structure of the Gla domain which is responsible for Ca II dependent phospholipid binding was also determined by NMR 13 Several structures of super active mutants have been solved 14 which reveal the nature of factor IX activation by other proteins in the clotting cascade Genetics edit nbsp In human the F9 gene is located on the X chromosome at position q27 1 Because the gene for factor IX is located on the X chromosome Xq27 1 q27 2 loss of function mutations thereof are X linked recessive males experience the disease phenotype much more frequently than females At least 534 disease causing mutations in this gene have been discovered 15 The F9 gene was first cloned in 1982 by Kotoku Kurachi and Earl Davie 16 Polly a transgenic cloned Poll Dorset sheep carrying the gene for factor IX was produced by Dr Ian Wilmut at the Roslin Institute in 1997 17 Role in disease editSee also Prothrombin complex concentrate Factor IXINN nonacog alfaClinical dataTrade namesBenefixLicense dataUS DailyMed Coagulation Factor IXATC codeNoneLegal statusLegal statusAU S4 Prescription only Factor IXINN albutrepenonacog alfaClinical dataTrade namesIdelvionLicense dataUS DailyMed Coagulation Factor IXATC codeNoneLegal statusLegal statusAU S4 Prescription only CA only 18 Factor IXINN eftrenonacog alfaClinical dataTrade namesAlprolixLicense dataUS DailyMed Coagulation Factor IXATC codeNoneLegal statusLegal statusAU S4 Prescription only Factor IXINN nonacog beta pegolClinical dataTrade namesRefixiaATC codeNoneLegal statusLegal statusAU S4 Prescription only Deficiency of factor IX causes Christmas disease hemophilia B 5 Over 3000 variants of factor IX have been described affecting 73 of the 461 residues 19 some cause no symptoms but many lead to a significant bleeding disorder The original Christmas disease mutation was identified by sequencing of Christmas DNA revealing a mutation which changed a cysteine to a serine 20 Recombinant factor IX is used to treat Christmas disease Formulations include nonacog alfa brand name Benefix 21 albutrepenonacog alfa brand name Idelvion 22 eftrenonacog alfa brand name Alprolix 23 nonacog beta pegol brand name Refixia 24 coagulation factor IX recombinant Benefix 25 coagulation factor IX recombinant Idelvion 26 coagulation factor IX recombinant Fc fusion protein Alprolix 27 coagulation factor IX recombinant Ixinity 28 29 coagulation factor IX recombinant Rebinyn 30 coagulation factor IX recombinant Rixubis 31 coagulation factor IX human Alphanine SD 32 Some rare mutations of factor IX result in elevated clotting activity and can result in clotting diseases such as deep vein thrombosis This gain of function mutation renders the protein hyperfunctional and is associated with familial early onset thrombophilia 33 Factor IX deficiency is treated by injection of purified factor IX produced through cloning in various animal or animal cell vectors Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding 34 A list of all the mutations in Factor IX is compiled and maintained by EAHAD 35 Coagulation factor IX is on the World Health Organization s List of Essential Medicines 6 References edit a b c GRCh38 Ensembl release 89 ENSG00000101981 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000031138 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Biggs R Douglas AS Macfarlane RG Dacie JV Pitney WR Dec 1952 Christmas disease a condition previously mistaken for haemophilia British Medical Journal 2 4799 1378 82 doi 10 1136 bmj 2 4799 1378 PMC 2022306 PMID 12997790 a b World Health Organization 2019 World Health Organization model list of essential medicines 21st list 2019 Geneva World Health Organization hdl 10665 325771 WHO MVP EMP IAU 2019 06 License CC BY NC SA 3 0 IGO a b Di Scipio RG Kurachi K Davie EW Jun 1978 Activation of human factor IX Christmas factor The Journal of Clinical Investigation 61 6 1528 38 doi 10 1172 JCI109073 PMC 372679 PMID 659613 Taran LD Jul 1997 Factor IX of the blood coagulation system a review Biochemistry Biokhimiia 62 7 685 93 PMID 9331959 Boland EJ Liu YC Walter CA Herbert DC Weaker FJ Odom MW Jagadeeswaran P Sep 1995 Age specific regulation of clotting factor IX gene expression in normal and transgenic mice Blood 86 6 2198 205 doi 10 1182 blood V86 6 2198 bloodjournal8662198 PMID 7662969 a b Zhong D Bajaj MS Schmidt AE Bajaj SP Feb 2002 The N terminal epidermal growth factor like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor The Journal of Biological Chemistry 277 5 3622 31 doi 10 1074 jbc M111202200 PMID 11723140 Wilkinson FH Ahmad SS Walsh PN Feb 2002 The factor IXa second epidermal growth factor EGF2 domain mediates platelet binding and assembly of the factor X activating complex The Journal of Biological Chemistry 277 8 5734 41 doi 10 1074 jbc M107753200 PMID 11714704 Brandstetter H Bauer M Huber R Lollar P Bode W Oct 1995 X ray structure of clotting factor IXa active site and module structure related to Xase activity and hemophilia B Proceedings of the National Academy of Sciences of the United States of America 92 21 9796 800 Bibcode 1995PNAS 92 9796B doi 10 1073 pnas 92 21 9796 PMC 40889 PMID 7568220 Freedman SJ Furie BC Furie B Baleja JD Sep 1995 Structure of the calcium ion bound gamma carboxyglutamic acid rich domain of factor IX Biochemistry 34 38 12126 37 doi 10 1021 bi00038a005 PMID 7547952 Zogg T Brandstetter H Dec 2009 Structural basis of the cofactor and substrate assisted activation of human coagulation factor IXa Structure 17 12 1669 78 doi 10 1016 j str 2009 10 011 PMID 20004170 Simcikova D Heneberg P December 2019 Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases Scientific Reports 9 1 18577 Bibcode 2019NatSR 918577S doi 10 1038 s41598 019 54976 4 PMC 6901466 PMID 31819097 Kurachi K Davie EW Nov 1982 Isolation and characterization of a cDNA coding for human factor IX Proceedings of the National Academy of Sciences of the United States of America 79 21 6461 4 Bibcode 1982PNAS 79 6461K doi 10 1073 pnas 79 21 6461 PMC 347146 PMID 6959130 Nicholl D 2002 An Introduction to Genetic Engineering Second Edition Cambridge University Press p 257 Health Canada New Drug Authorizations 2016 Highlights Health Canada 14 March 2017 Retrieved 7 April 2024 Goodeve AC 2015 Hemophilia B Molecular pathogenesis and mutation analysis Journal of Thrombosis and Haemostasis 13 7 1184 1195 doi 10 1111 jth 12958 PMC 4496316 PMID 25851415 Taylor SA Duffin J Cameron C Teitel J Garvey B Lillicrap DP Jan 1992 Characterization of the original Christmas disease mutation cysteine 206 serine from clinical recognition to molecular pathogenesis Thrombosis and Haemostasis 67 1 63 5 doi 10 1055 s 0038 1648381 PMID 1615485 S2CID 25251813 BeneFIX EPAR European Medicines Agency EMA 17 September 2018 Archived from the original on 17 June 2020 Retrieved 17 June 2020 Idelvion EPAR European Medicines Agency EMA 17 September 2018 Archived from the original on 17 June 2020 Retrieved 17 June 2020 Alprolix EPAR European Medicines Agency EMA 17 September 2018 Archived from the original on 11 August 2020 Retrieved 17 June 2020 Refixia EPAR European Medicines Agency EMA 17 September 2018 Archived from the original on 18 June 2020 Retrieved 17 June 2020 Benefix coagulation factor ix recombinant kit DailyMed 1 March 2023 Archived from the original on 29 January 2023 Retrieved 23 March 2024 Idelvion coagulation factor ix recombinant human kit DailyMed 30 June 2023 Archived from the original on 27 January 2023 Retrieved 23 March 2024 Alprolix coagulation factor ix recombinant fc fusion protein kit DailyMed 25 May 2023 Archived from the original on 7 February 2023 Retrieved 23 March 2024 Ixinity coagulation factor ix recombinant kit DailyMed 23 February 2021 Archived from the original on 28 September 2023 Retrieved 23 March 2024 Ixinity coagulation factor ix recombinant kit DailyMed 9 January 2024 Archived from the original on 3 December 2022 Retrieved 23 March 2024 Rebinyn coagulation factor ix recombinant glycopegylated kit DailyMed 11 August 2022 Archived from the original on 29 November 2022 Retrieved 23 March 2024 Rixubis coagulation factor ix recombinant kit DailyMed 22 March 2023 Archived from the original on 2 July 2022 Retrieved 23 March 2024 Alphanine SD coagulation factor ix human kit DailyMed 18 January 2024 Archived from the original on 18 February 2024 Retrieved 23 March 2024 Simioni P Tormene D Tognin G Gavasso S Bulato C Iacobelli NP Finn JD Spiezia L Radu C Arruda VR Oct 2009 X linked thrombophilia with a mutant factor IX factor IX Padua The New England Journal of Medicine 361 17 1671 5 doi 10 1056 NEJMoa0904377 PMID 19846852 Rossi M Jayaram R Sayeed R Sep 2011 Do patients with haemophilia undergoing cardiac surgery have good surgical outcomes Interactive Cardiovascular and Thoracic Surgery 13 3 320 31 doi 10 1510 icvts 2011 272401 PMID 21712351 Home EAHAD Factor 9 Gene Variant Database Archived from the original on 2020 10 28 Retrieved 2020 10 23 Further reading editDavie EW Fujikawa K 1975 Basic mechanisms in blood coagulation Annual Review of Biochemistry 44 799 829 doi 10 1146 annurev bi 44 070175 004055 PMID 237463 Sommer SS Jul 1992 Assessing the underlying pattern of human germline mutations lessons from the factor IX gene FASEB Journal 6 10 2767 74 doi 10 1096 fasebj 6 10 1634040 PMID 1634040 S2CID 15211597 Lenting PJ van Mourik JA Mertens K Dec 1998 The life cycle of coagulation factor VIII in view of its structure and function Blood 92 11 3983 96 doi 10 1182 blood V92 11 3983 PMID 9834200 Lowe GD Dec 2001 Factor IX and thrombosis PDF British Journal of Haematology 115 3 507 13 doi 10 1046 j 1365 2141 2001 03186 x PMID 11736930 S2CID 44650866 Archived PDF from the original on 2021 06 19 Retrieved 2019 12 11 O Connell NM Jun 2003 Factor XI deficiency from molecular genetics to clinical management Blood Coagulation amp Fibrinolysis 14 Suppl 1 S59 64 doi 10 1097 00001721 200306001 00014 PMID 14567539 Du X May 2007 Signaling and regulation of the platelet glycoprotein Ib IX V complex Current Opinion in Hematology 14 3 262 9 doi 10 1097 MOH 0b013e3280dce51a PMID 17414217 S2CID 39904506 External links editOverview of all the structural information available in the PDB for UniProt P00740 Coagulation factor IX at the PDBe KB GeneReviews NCBI NIH UW entry on Hemophilia B The MEROPS online database for peptidases and their inhibitors S01 214 Archived 2005 05 05 at the Wayback Machine Portals nbsp Biology nbsp Medicine Retrieved from https en wikipedia org w index php title Factor IX amp oldid 1217672528, wikipedia, wiki, book, books, library,

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