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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:48
Primary Accession Number DB00569
Secondary Accession Number
  • APRD00500
Name Fondaparinux sodium
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Fondaparinux (Arixtra) is an anticoagulant medication. It contains a synthetic pentasaccharide. Apart from the O-methyl group at the reducing end of the molecule, the identity and sequence of the five monomeric sugar units contained in Fondaparinux is identical to a sequence of five monomeric sugar units that can be isolated after either chemical or enzymatic cleavage of the polymeric glycosaminoglycans heparin and heparan sulfate (HS). Within heparin and heparan sulfate this monomeric sequence is thought to form the high affinity binding site for the anti-coagulant factor antithrombin III (ATIII). Binding of heparin/HS to ATIII has been shown to increase the anti-coagulant activity of antithrombin III 1000 fold. Clinically, fondaparinux is used for the prevention of deep vein thrombosis in patients who have had orthopedic surgery as well as for the treatment of deep vein thrombosis and pulmonary embolism.
Synonyms
  1. Arixtra
Brand Names
  1. Arixtra
  2. Fondaparinux
  3. fondaparinux sodium
Brand Mixtures Not Available
Chemical IUPAC Name decasodium (2R,3S,4S,5R,6R)-3-[(2R,3R,4R,5R,6R)-5-[(2R,3R,4R,5S,6S)-6-carboxylato-5-[(2R,3R,4R,5S,6R)-4,5-dihydroxy-3-(sulfonatoamino)-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,4-dihydroxyoxan-2-yl]oxy-3-(sulfonatoamino)-4-sulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-4-hydroxy-6-[(2R,3S,4R,5R,6S)-4-hydroxy-6-methoxy-5-(sulfonatoamino)-2-(sulfonatooxymethyl)oxan-3-yl]oxy-5-sulfonatooxyoxane-2-carboxylate
Chemical Formula C31H43N3Na10O49S8
Chemical Structure Structure
CAS Registry Number 114870-03-0
InChI Identifier InChI=1/C31H53N3O49S8.10Na/c1-69-27-9(33-85(48,49)50)13(37)17(6(74-27)3-71-88(57,58)59)76-31-22(83-91(66,67)68)16(40)21(24(81-31)26(43)44)79-29-10(34-86(51,52)53)19(82-90(63,64)65)18(7(75-29)4-72-89(60,61)62)77-30-15(39)14(38)20(23(80-30)25(41)42)78-28-8(32-84(45,46)47)12(36)11(35)5(73-28)2-70-87(54,55)56;;;;;;;;;;/h5-24,27-40H,2-4H2,1H3,(H,41,42)(H,43,44)(H,45,46,47)(H,48,49,50)(H,51,52,53)(H,54,55,56)(H,57,58,59)(H,60,61,62)(H,63,64,65)(H,66,67,68);;;;;;;;;;/q;10*+1/p-10/t5-,6-,7-,8-,9-,10-,11-,12-,13-,14-,15-,16+,17-,18-,19-,20+,21+,22-,23+,24-,27+,28-,29-,30-,31-;;;;;;;;;;/m1........../s1/fC31H43N3O49S8.10Na/q-10;10m
InChI Key XEKSTYNIJLDDAZ-IEJHTQPCDI
KEGG Drug D01844 Link Image
KEGG Compound Not Available
PubChem Compound 636380 Link Image
PubChem Substance 7848906 Link Image
ChEBI ID Not Available
PharmGKB ID PA10083 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02245531 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/arixtra.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Fondaparinux_sodium Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 1728.0820
Monoisotopic Molecular Weight 1726.7708
State Liquid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.74e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 0.72 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.00 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1JVQ Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].CO[C@H]1O[C@H](COS([O-])(=O)=O)[C@@H](O[C@@H]2O[C@H]([C@@H](O[C@H]3O[C@H](COS([O-])(=O)=O)[C@@H](O[C@@H]4O[C@@H]([C@@H](O[C@H]5O[C@H](COS([O-])(=O)=O)[C@@H](O)[C@H](O)[C@H]5NS([O-])(=O)=O)[C@H](O)[C@H]4O)C([O-])=O)[C@H](OS([O-])(=O)=O)[C@H]3NS([O-])(=O)=O)[C@H](O)[C@H]2OS([O-])(=O)=O)C([O-])=O)[C@H](O)[C@H]1NS([O-])(=O)=O
Canonical SMILES [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].COC1OC(COS([O-])(=O)=O)C(OC2OC(C(OC3OC(COS([O-])(=O)=O)C(OC4OC(C(OC5OC(COS([O-])(=O)=O)C(O)C(O)C5NS([O-])(=O)=O)C(O)C4O)C([O-])=O)C(OS([O-])(=O)=O)C3NS([O-])(=O)=O)C(O)C2OS([O-])(=O)=O)C([O-])=O)C(O)C1NS([O-])(=O)=O
Drug Category
  • Anticoagulants
  • Antithrombotics
ATC Codes
AHFS Codes
  • 20:12.04.92
Indication For the treatment of prophylaxis of deep vein thrombosis.
Pharmacology Fondaparinux is a synthetic and specific inhibitor of activated Factor X (Xa) indicated for the prophylaxis of deep vein thrombosis, which may lead to pulmonary embolism. Fondaparinux is also indicated for the treatment of acute deep vein thrombosis when administered in conjunction with warfarin, and the treatment of acute pulmonary embolism when administered in conjunction with warfarin. Fondaparinux does not inactivate thrombin (activated Factor II) and has no known effect on platelet function. At the recommended dose, Fondaparinux does not affect fibrinolytic activity or bleeding time.
Mechanism of Action The antithrombotic activity of Fondaparinux is the result of antithrombin III (ATIII)-mediated selective inhibition of Factor Xa. By selectively binding to ATIII, Fondaparinux potentiates (about 300 times) the innate neutralization of Factor Xa by ATIII. Neutralization of Factor Xa interrupts the blood coagulation cascade and thus inhibits thrombin formation and thrombus development.
Absorption 100%
Toxicity Not Available
Protein Binding 94%
Biotransformation Not Available
Half Life 17-21 hours
Dosage Forms
Form Route
Solution Subcutaneous
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways
Name SMPDB Link KEGG Link
Fondaparinux Pathway SMP00273 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Antithrombin-III
Drug Target 1 [top]
Target 1 ID 309
Target 1 Name Antithrombin-III
Target 1 Synonyms
  1. ATIII
  2. Antithrombin-III precursor
Target 1 Gene Name SERPINC1
Target 1 Protein Sequence >Antithrombin-III precursor 
MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEK
KATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFA
MTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFG
DKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAIN
ELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQ
VLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDG
FSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAV
VIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK
Target 1 Number of Residues 471
Target 1 Molecular Weight 52603
Target 1 Theoretical pI 6.68
Target 1 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
serine-type endopeptidase inhibitor activity
Process
Not Available
Component
Not Available
Target 1 General Function Involved in serine-type endopeptidase inhibitor activity
Target 1 Specific Function Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-32
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 179161 Link Image
Target 1 UniProtKB/Swiss-Prot ID P01008 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ANT3_HUMAN Link Image
Target 1 PDB ID 1JVQ Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Secreted protein
  • extracellular space
Target 1 Gene Sequence >1395 bp 
ATGTATTCCAATGTGATAGGAACTGTAACCTCTGGAAAAAGGAAGGTTTATCTTTTGTCC
TTGCTGCTCATTGGCTTCTGGGACTGCGTGACCTGTCACGGGAGCCCTGTGGACATCTGC
ACAGCCAAGCCGCGGGACATTCCCATGAATCCCATGTGCATTTACCGCTCCCCGGAGAAG
AAGGCAACTGAGGATGAGGGCTCAGAACAGAAGATCCCGGAGGCCACCAACCGGCGTGTC
TGGGAACTGTCCAAGGCCAATTCCCGCTTTGCTACCACTTTCTATCAGCACCTGGCAGAT
TCCAAGAATGACAATGATAACATTTTCCTGTCACCCCTGAGTATCTCCACGGCTTTTGCT
ATGACCAAGCTGGGTGCCTGTAATGACACCCTCCAGCAACTGATGGAGGTATTTAAGTTT
GACACCATATCTGAGAAAACATCTGATCAGATCCACTTCTTCTTTGCCAAACTGAACTGC
CGACTCTATCGAAAAGCCAACAAATCCTCCAAGTTAGTATCAGCCAATCGCCTTTTTGGA
GACAAATCCCTTACCTTCAATGAGACCTACCAGGACATCAGTGAGTTGGTATATGGAGCC
AAGCTCCAGCCCCTGGACTTCAAGGAAAATGCAGAGCAATCCAGAGCGGCCATCAACAAA
TGGGTGTCCAATAAGACCGAAGGCCGAATCACCGATGTCATTCCCTCGGAAGCCATCAAT
GAGCTCACTGTTCTGGTGCTGGTTAACACCATTTACTTCAAGGGCCTGTGGAAGTCAAAG
TTCAGCCCTGAGAACACAAGGAAGGAACTGTTCTACAAGGCTGATGGAGAGTCGTGTTCA
GCATCTATGATGTACCAGGAAGGCAAGTTCCGTTATCGGCGCGTGGCTGAAGGCACCCAG
GTGCTTGAGTTGCCCTTCAAAGGTGATGACATCACCATGGTCCTCATCTTGCCCAAGCCT
GAGAAGAGCCTGGCCAAGGTGGAGAAGGAACTCACCCCAGAGGTGCTGCAGGAGTGGCTG
GATGAATTGGAGGAGATGATGCTGGTGGTCCACATGCCCCGCTTCCGCATTGAGGACGGC
TTCAGTTTGAAGGAGCAGCTGCAAGACATGGGCCTTGTCGATCTGTTCAGCCCTGAAAAG
TCCAAACTCCCAGGTATTGTTGCAGAAGGCCGAGATGACCTCTATGTCTCAGATGCATTC
CATAAGGCATTTCTTGAGGTAAATGAAGAAGGCAGTGAAGCAGCTGCAAGTACCGCTGTT
GTGATTGCTGGCCGTTCGCTAAACCCCAACAGGGTGACTTTCAAGGCCAACAGGCTTTTC
CTGGTTTTTATAAGAGAAGTTCCTCTGAACACTATTATCTTCATGGGCAGAGTAGCCAAC
CCTTGTGTTAAGTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SERPINC1 Link Image
Target 1 GenAtlas ID SERPINC1 Link Image
Target 1 HGNC ID HGNC:775 Link Image
Target 1 Chromosome Location 1
Target 1 Locus 1q23-q25.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Bayston TA, Tripodi A, Mannucci PM, Thompson E, Ireland H, Fitches AC, Hananeia L, Olds RJ, Lane DA: Familial overexpression of beta antithrombin caused by an Asn135Thr substitution. Blood. 1999 Jun 15;93(12):4242-7. [PubMed Link Image]
  2. Niiya K, Kiguchi T, Dansako H, Fujimura K, Fujimoto T, Iijima K, Tanimoto M, Harada M: Two novel gene mutations in type I antithrombin deficiency. Int J Hematol. 2001 Dec;74(4):469-72. [PubMed Link Image]
  3. Blajchman MA, Fernandez-Rachubinski F, Sheffield WP, Austin RC, Schulman S: Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. Blood. 1992 Mar 15;79(6):1428-34. [PubMed Link Image]
  4. Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL: Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. FEBS Lett. 1992 Apr 6;300(3):241-6. [PubMed Link Image]
  5. Perry DJ, Daly M, Harper PL, Tait RC, Price J, Walker ID, Carrell RW: Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins. FEBS Lett. 1991 Jul 22;285(2):248-50. [PubMed Link Image]
  6. Daly M, Bruce D, Perry DJ, Price J, Harper PL, O'Meara A, Carrell RW: Antithrombin Dublin (-3 Val----Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site. FEBS Lett. 1990 Oct 29;273(1-2):87-90. [PubMed Link Image]
  7. Austin RC, Rachubinski RA, Blajchman MA: Site-directed mutagenesis of alanine-382 of human antithrombin III. FEBS Lett. 1991 Mar 25;280(2):254-8. [PubMed Link Image]
  8. Mourey L, Samama JP, Delarue M, Choay J, Lormeau JC, Petitou M, Moras D: Antithrombin III: structural and functional aspects. Biochimie. 1990 Aug;72(8):599-608. [PubMed Link Image]
  9. Gandrille S, Aiach M, Lane DA, Vidaud D, Molho-Sabatier P, Caso R, de Moerloose P, Fiessinger JN, Clauser E: Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine. J Biol Chem. 1990 Nov 5;265(31):18997-9001. [PubMed Link Image]
  10. Borg JY, Brennan SO, Carrell RW, George P, Perry DJ, Shaw J: Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding. FEBS Lett. 1990 Jun 18;266(1-2):163-6. [PubMed Link Image]
  11. 2781509 Erdjument H, Lane DA, Panico M, Di Marzo V, Morris HR, Bauer K, Rosenberg RD: Antithrombin Chicago, amino acid substitution of arginine 393 to histidine. Thromb Res. 1989 Jun 15;54(6):613-9.
  12. 3080419 Chang JY, Tran TH: Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. J Biol Chem. 1986 Jan 25;261(3):1174-6.
  13. 3162733 Erdjument H, Lane DA, Panico M, Di Marzo V, Morris HR: Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. J Biol Chem. 1988 Apr 25;263(12):5589-93.
  14. 3179438 Devraj-Kizuk R, Chui DH, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA: Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood. 1988 Nov;72(5):1518-23.
  15. 3191114 Bock SC, Marrinan JA, Radziejewska E: Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry. 1988 Aug 9;27(16):6171-8.
  16. 3805013 Stephens AW, Thalley BS, Hirs CH: Antithrombin-III Denver, a reactive site variant. J Biol Chem. 1987 Jan 25;262(3):1044-8.
  17. 6298709 Bock SC, Wion KL, Vehar GA, Lawn RM: Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res. 1982 Dec 20;10(24):8113-25.
  18. 6305982 Prochownik EV, Markham AF, Orkin SH: Isolation of a cDNA clone for human antithrombin III. J Biol Chem. 1983 Jul 10;258(13):8389-94.
  19. 6572945 Chandra T, Stackhouse R, Kidd VJ, Woo SL: Isolation and sequence characterization of a cDNA clone of human antithrombin III. Proc Natl Acad Sci U S A. 1983 Apr;80(7):1845-8.
  20. 6582486 Koide T, Odani S, Takahashi K, Ono T, Sakuragawa N: Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proc Natl Acad Sci U S A. 1984 Jan;81(2):289-93.
  21. 6693405 Blackburn MN, Smith RL, Carson J, Sibley CC: The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence. J Biol Chem. 1984 Jan 25;259(2):939-41.
  22. 7238875 Bjork I, Danielsson A, Fenton JW, Jornvall: The site in human antithrombin for functional proteolytic cleavage by human thrombin. FEBS Lett. 1981 Apr 20;126(2):257-60.
  23. 7656006 Schreuder HA, de Boer B, Dijkema R, Mulders J, Theunissen HJ, Grootenhuis PD, Hol WG: The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat Struct Biol. 1994 Jan;1(1):48-54.
  24. 7749926 Stein PE, Carrell RW: What do dysfunctional serpins tell us about molecular mobility and disease? Nat Struct Biol. 1995 Feb;2(2):96-113.
  25. 7832187 Okajima K, Abe H, Wagatsuma M, Okabe H, Takatsuki K: Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin. Am J Hematol. 1995 Jan;48(1):12-8.
  26. 7878627 Emmerich J, Chadeuf G, Alhenc-Gelas M, Gouault-Heilman M, Toulon P, Fiessinger JN, Aiach M: Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6. Thromb Haemost. 1994 Oct;72(4):534-9.
  27. 7959685 Millar DS, Wacey AI, Ribando J, Melissari E, Laursen B, Woods P, Kakkar VV, Cooper DN: Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Hum Genet. 1994 Nov;94(5):509-12.
  28. 7989582 Bruce D, Perry DJ, Borg JY, Carrell RW, Wardell MR: Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp) J Clin Invest. 1994 Dec;94(6):2265-74.
  29. 7994035 van Boven HH, Olds RJ, Thein SL, Reitsma PH, Lane DA, Briet E, Vandenbroucke JP, Rosendaal FR: Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families. Blood. 1994 Dec 15;84(12):4209-13.
  30. 8087553 Carrell RW, Stein PE, Fermi G, Wardell MR: Biological implications of a 3 A structure of dimeric antithrombin. Structure. 1994 Apr 15;2(4):257-70.
  31. 8236149 Lane DA, Olds RJ, Boisclair M, Chowdhury V, Thein SL, Cooper DN, Blajchman M, Perry D, Emmerich J, Aiach M: Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb Haemost. 1993 Aug 2;70(2):361-9.
  32. 8274732 Jochmans K, Lissens W, Vervoort R, Peeters S, De Waele M, Liebaers I: Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 antithrombin deficiency and neonatal thrombosis. Blood. 1994 Jan 1;83(1):146-51.
  33. 8443391 Okajima K, Abe H, Maeda S, Motomura M, Tsujihata M, Nagataki S, Okabe H, Takatsuki K: Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis. Blood. 1993 Mar 1;81(5):1300-5.
  34. 8476848 Olds RJ, Lane DA, Chowdhury V, De Stefano V, Leone G, Thein SL: Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia. Biochemistry. 1993 Apr 27;32(16):4216-24.
  35. 8486379 Olds RJ, Lane DA, Beresford CH, Abildgaard U, Hughes PM, Thein SL: A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), identified by DNA heteroduplex detection. Genomics. 1993 Apr;16(1):298-9.
  36. 8664906 Perry DJ, Carrell RW: Molecular genetics of human antithrombin deficiency. Hum Mutat. 1996;7(1):7-22.
  37. 9067613 Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR: The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site. J Mol Biol. 1997 Feb 28;266(3):601-9.
  38. 9761669 Skinner R, Chang WS, Jin L, Pei X, Huntington JA, Abrahams JP, Carrell RW, Lomas DA: Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin. J Mol Biol. 1998;283(1):9-14.
  39. 9845533 Fitches AC, Appleby R, Lane DA, De Stefano V, Leone G, Olds RJ: Impaired cotranslational processing as a mechanism for type I antithrombin deficiency. Blood. 1998 Dec 15;92(12):4671-6.
Target 1 Drug References
  1. Donat F, Duret JP, Santoni A, Cariou R, Necciari J, Magnani H, de Greef R: The pharmacokinetics of fondaparinux sodium in healthy volunteers. Clin Pharmacokinet. 2002;41 Suppl 2:1-9. [PubMed Link Image]
  2. Paolucci F, Clavies MC, Donat F, Necciari J: Fondaparinux sodium mechanism of action: identification of specific binding to purified and human plasma-derived proteins. Clin Pharmacokinet. 2002;41 Suppl 2:11-8. [PubMed Link Image]
  3. Cheng JW: Fondaparinux: a new antithrombotic agent. Clin Ther. 2002 Nov;24(11):1757-69; discussion 1719. [PubMed Link Image]
  4. Dager WE, Andersen J, Nutescu E: Special considerations with fondaparinux therapy: heparin-induced thrombocytopenia and wound healing. Pharmacotherapy. 2004 Jul;24(7 Pt 2):88S-94S. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.