168
G. Yang and Y. Huang
62. Parunov LA, Fadeeva OA, Balandina AN, Soshitova NP, Kopylov KG, Kumskova MA, Gilbert
JC, Schaub RG, McGinness KE, Ataullakhanov FI, Panteleev MA (2011) Improvement of
spatial fibrin formation by the anti-TFPI aptamer BAX499: changing clot size by targeting
extrinsic pathway initiation. J Thromb Haemost 9(9):1825–1834
63. Gorczyca ME, Nair SC, Jilma B, Priya S, Male C, Reitter S, Knoebl P, Gilbert JC, Schaub
RG, Dockal M, McGinness KE, Pabinger I, Srivastava A (2012) Inhibition of tissue factor
pathway inhibitor by the aptamer BAX499 improves clotting of hemophilic blood and plasma.
J Thromb Haemost 10(8):1581–1590
64. Vandghanooni S, Eskandani M, Barar J, Omidi Y (2018) AS1411 aptamer-decorated cisplatinloaded poly(lactic-co-glycolic acid) nanoparticles for targeted therapy of miR-21-inhibited
ovarian cancer cells. Nanomedicine (Lond) 13(21):2729–2758
65. Swami A, Kaur V (2017) von Willebrand disease: a concise review and update for the
practicing physician. Clin Appl Thromb Hemost 23(8):900–910
66. Jilma B, Paulinska P, Jilma-Stohlawetz P, Gilbert JC, Hutabarat R, Knobl P (2010) A
randomised pilot trial of the anti-von Willebrand factor aptamer ARC1779 in patients with
type 2b von Willebrand disease. Thromb Haemost 104(3):563–570
67. Firbas C, Siller-Matula JM, Jilma B (2010) Targeting von willebrand factor and platelet
glycoprotein Ib receptor. Expert Rev Cardiovasc Ther 8(12):1689–1701
68. Sakai K, Someya T, Harada K, Yagi H, Matsui T, Matsumoto M (2019) Novel aptamer to
von willebrand factor A1 domain (TAGX-0004) shows total inhibition of thrombus formation
superior to ARC1779 and comparable to caplacizumab. Haematologica
69. Nimjee SM, Dornbos D 3rd, Pitoc GA, Wheeler DG, Layzer JM, Venetos N, Huttinger A,
Talentino SE, Musgrave NJ, Moody H, Rempel RE, Jones C, Carlisle K, Wilson J, Bratton
C, Joseph ME, Khan S, Hoffman MR, Sommerville L, Becker RC, Zweier JL, Sullenger BA
(2019) Preclinical development of a vWF aptamer to limit thrombosis and engender arterial
recanalization of occluded vessels. Mol Ther 27(7):1228–1241
70. Boncler MA, Koziolkiewicz M, Watala C (2001) Aptamer inhibits degradation of platelet
proteolytically activatable receptor, PAR-1, by thrombin. Thromb Res 104(3):215–222
71. Borissoff JI, Spronk HM, Heeneman S, ten Cate H (2009) Is thrombin a key player in the
‘coagulation-atherogenesis’ maze? Cardiovasc Res 82(3):392–403
72. Marson G, Palumbo M, Sissi C (2012) Folding versus charge: understanding selective target
recognition by the thrombin aptamers. Curr Pharm Des 18(14):2027–2035
73. Negrier C, Shima M, Hoffman M (2019) The central role of thrombin in bleeding disorders.
Blood Rev 38 (1532–1681 Electronic):100582
74. Verhamme IM, Olson ST, Tollefsen DM, Bock PE (2002) Binding of exosite ligands to human
thrombin−Re-evaluation of allosteric linkage between thrombin exosites I and II. J Biol Chem
277(9):6788–6798
75. Bock PE, Panizzi P, Verhamme IM (2007) Exosites in the substrate specificity of blood
coagulation reactions. J Thromb Haemost 5 Suppl 1 (1538–7933 Print):81–94
76. Muller J, Freitag D, Mayer G, Potzsch B (2008) Anticoagulant characteristics of HD1-22, a
bivalent aptamer that specifically inhibits thrombin and prothrombinase. J Thromb Haemost
6(12):2105–2112
77. Zhang J, Loo RRO, Loo JA (2017) Structural characterization of a thrombin-aptamer complex
by high resolution native top-down mass spectrometry. J Am Soc Mass Spectrom 28(9):1815–
1822
78. Griffin LC, Tidmarsh GF, Bock LC, Toole JJ, Leung LL (1993) In vivo anticoagulant properties
of a novel nucleotide-based thrombin inhibitor and demonstration of regional anticoagulation
in extracorporeal circuits. Blood 81(12):3271–3276
79. Mendelboum Raviv S, Horvath A, Aradi J, Bagoly Z, Fazakas F, Batta Z, Muszbek L, Harsfalvi
J (2008) 4-thio-deoxyuridylate-modified thrombin aptamer and its inhibitory effect on fibrin
clot formation, platelet aggregation and thrombus growth on subendothelial matrix. J Thromb
Haemost 6(10):1764–1771
80. Bompiani KM, Monroe DM, Church FC, Sullenger BA (2012) A high affinity, antidotecontrollable prothrombin and thrombin-binding RNA aptamer inhibits thrombin generation
and thrombin activity. J Thromb Haemost 10(5):870–880
G. Yang and Y. Huang
62. Parunov LA, Fadeeva OA, Balandina AN, Soshitova NP, Kopylov KG, Kumskova MA, Gilbert
JC, Schaub RG, McGinness KE, Ataullakhanov FI, Panteleev MA (2011) Improvement of
spatial fibrin formation by the anti-TFPI aptamer BAX499: changing clot size by targeting
extrinsic pathway initiation. J Thromb Haemost 9(9):1825–1834
63. Gorczyca ME, Nair SC, Jilma B, Priya S, Male C, Reitter S, Knoebl P, Gilbert JC, Schaub
RG, Dockal M, McGinness KE, Pabinger I, Srivastava A (2012) Inhibition of tissue factor
pathway inhibitor by the aptamer BAX499 improves clotting of hemophilic blood and plasma.
J Thromb Haemost 10(8):1581–1590
64. Vandghanooni S, Eskandani M, Barar J, Omidi Y (2018) AS1411 aptamer-decorated cisplatinloaded poly(lactic-co-glycolic acid) nanoparticles for targeted therapy of miR-21-inhibited
ovarian cancer cells. Nanomedicine (Lond) 13(21):2729–2758
65. Swami A, Kaur V (2017) von Willebrand disease: a concise review and update for the
practicing physician. Clin Appl Thromb Hemost 23(8):900–910
66. Jilma B, Paulinska P, Jilma-Stohlawetz P, Gilbert JC, Hutabarat R, Knobl P (2010) A
randomised pilot trial of the anti-von Willebrand factor aptamer ARC1779 in patients with
type 2b von Willebrand disease. Thromb Haemost 104(3):563–570
67. Firbas C, Siller-Matula JM, Jilma B (2010) Targeting von willebrand factor and platelet
glycoprotein Ib receptor. Expert Rev Cardiovasc Ther 8(12):1689–1701
68. Sakai K, Someya T, Harada K, Yagi H, Matsui T, Matsumoto M (2019) Novel aptamer to
von willebrand factor A1 domain (TAGX-0004) shows total inhibition of thrombus formation
superior to ARC1779 and comparable to caplacizumab. Haematologica
69. Nimjee SM, Dornbos D 3rd, Pitoc GA, Wheeler DG, Layzer JM, Venetos N, Huttinger A,
Talentino SE, Musgrave NJ, Moody H, Rempel RE, Jones C, Carlisle K, Wilson J, Bratton
C, Joseph ME, Khan S, Hoffman MR, Sommerville L, Becker RC, Zweier JL, Sullenger BA
(2019) Preclinical development of a vWF aptamer to limit thrombosis and engender arterial
recanalization of occluded vessels. Mol Ther 27(7):1228–1241
70. Boncler MA, Koziolkiewicz M, Watala C (2001) Aptamer inhibits degradation of platelet
proteolytically activatable receptor, PAR-1, by thrombin. Thromb Res 104(3):215–222
71. Borissoff JI, Spronk HM, Heeneman S, ten Cate H (2009) Is thrombin a key player in the
‘coagulation-atherogenesis’ maze? Cardiovasc Res 82(3):392–403
72. Marson G, Palumbo M, Sissi C (2012) Folding versus charge: understanding selective target
recognition by the thrombin aptamers. Curr Pharm Des 18(14):2027–2035
73. Negrier C, Shima M, Hoffman M (2019) The central role of thrombin in bleeding disorders.
Blood Rev 38 (1532–1681 Electronic):100582
74. Verhamme IM, Olson ST, Tollefsen DM, Bock PE (2002) Binding of exosite ligands to human
thrombin−Re-evaluation of allosteric linkage between thrombin exosites I and II. J Biol Chem
277(9):6788–6798
75. Bock PE, Panizzi P, Verhamme IM (2007) Exosites in the substrate specificity of blood
coagulation reactions. J Thromb Haemost 5 Suppl 1 (1538–7933 Print):81–94
76. Muller J, Freitag D, Mayer G, Potzsch B (2008) Anticoagulant characteristics of HD1-22, a
bivalent aptamer that specifically inhibits thrombin and prothrombinase. J Thromb Haemost
6(12):2105–2112
77. Zhang J, Loo RRO, Loo JA (2017) Structural characterization of a thrombin-aptamer complex
by high resolution native top-down mass spectrometry. J Am Soc Mass Spectrom 28(9):1815–
1822
78. Griffin LC, Tidmarsh GF, Bock LC, Toole JJ, Leung LL (1993) In vivo anticoagulant properties
of a novel nucleotide-based thrombin inhibitor and demonstration of regional anticoagulation
in extracorporeal circuits. Blood 81(12):3271–3276
79. Mendelboum Raviv S, Horvath A, Aradi J, Bagoly Z, Fazakas F, Batta Z, Muszbek L, Harsfalvi
J (2008) 4-thio-deoxyuridylate-modified thrombin aptamer and its inhibitory effect on fibrin
clot formation, platelet aggregation and thrombus growth on subendothelial matrix. J Thromb
Haemost 6(10):1764–1771
80. Bompiani KM, Monroe DM, Church FC, Sullenger BA (2012) A high affinity, antidotecontrollable prothrombin and thrombin-binding RNA aptamer inhibits thrombin generation
and thrombin activity. J Thromb Haemost 10(5):870–880