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Bothrojaracin, a Bothrops jararaca snake venom-derived (pro)thrombin inhibitor, as an anti-thrombotic molecule.
Zingali RB, Ferreira MS, Assafim M, Frattani FS, Monteiro RQ. Zingali RB, et al. Pathophysiol Haemost Thromb. 2005;34(4-5):160-3. doi: 10.1159/000092416. Pathophysiol Haemost Thromb. 2005. PMID: 16707920 Free article. Review.
Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). ...
Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = …
Targeting exosites on blood coagulation proteases.
Monteiro RQ. Monteiro RQ. An Acad Bras Cienc. 2005 Jun;77(2):275-80. doi: 10.1590/s0001-37652005000200007. Epub 2005 May 9. An Acad Bras Cienc. 2005. PMID: 15895163 Free article. Review.
Some of these inhibitors interact with exosites on coagulation enzymes. Two examples are discussed in this short revision. Bothrojaracin is a snake venom-derived protein that binds to thrombin exosites 1 and 2. Complex formation impairs several exosite-dependent activities …
Some of these inhibitors interact with exosites on coagulation enzymes. Two examples are discussed in this short revision. Bothrojaracin …
Interaction of bothrojaracin with prothrombin.
Zingali RB, Bianconi ML, Monteiro RQ. Zingali RB, et al. Haemostasis. 2001 May-Dec;31(3-6):273-8. doi: 10.1159/000048073. Haemostasis. 2001. PMID: 11910195 Free article. Review.
Bothrojaracin (BJC) is a 27-kD protein from Bothrops jararaca venom that interacts with alpha-thrombin (K(D) = 0.7 nM) through both anion-binding exosites I and II. ...
Bothrojaracin (BJC) is a 27-kD protein from Bothrops jararaca venom that interacts with alpha-thrombin (K(D) = 0.7 nM) through both a …
Exploiting the antithrombotic effect of the (pro)thrombin inhibitor bothrojaracin.
Assafim M, Frattani FS, Ferreira MS, Silva DM, Monteiro RQ, Zingali RB. Assafim M, et al. Toxicon. 2016 Sep 1;119:46-51. doi: 10.1016/j.toxicon.2016.05.007. Epub 2016 May 11. Toxicon. 2016. PMID: 27179421 Free article.
Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. ...It was observed that bothrojaracin interacts with rat prothrombin in plasma. Ex-vivo assays showed stable complex formation even after 24 h of a single bothrojaracin d …
Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. ...It was observed that bothrojaracin …
Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: characterization and mechanism of thrombin inhibition.
Zingali RB, Jandrot-Perrus M, Guillin MC, Bon C. Zingali RB, et al. Biochemistry. 1993 Oct 12;32(40):10794-802. doi: 10.1021/bi00091a034. Biochemistry. 1993. PMID: 8399228
Purified bothrojaracin is devoid of phospholipase A2, amidolytic, or fibrino (geno)lytic activity. ...Bothrojaracin antagonizes the inhibition of thrombin amidolytic activity by hirudin. ...
Purified bothrojaracin is devoid of phospholipase A2, amidolytic, or fibrino (geno)lytic activity. ...Bothrojaracin antagonize …
Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus.
Castro HC, Dutra DL, Oliveira-Carvalho AL, Zingali RB. Castro HC, et al. Toxicon. 1998 Dec;36(12):1903-12. doi: 10.1016/s0041-0101(98)00111-1. Toxicon. 1998. PMID: 9839674
This protein was highly homologous to bothrojaracin (95% in its N-terminal sequence-for residues 1 to 25) but displaying lower inhibitory effect on thrombin induced platelet aggregation (Ic50 = 0.19 microg/ml) compared to bothrojaracin (IC50 = 0.06). Altogether, bot …
This protein was highly homologous to bothrojaracin (95% in its N-terminal sequence-for residues 1 to 25) but displaying lower inhibi …
Bothrojaracin: a potent two-site-directed thrombin inhibitor.
Arocas V, Zingali RB, Guillin MC, Bon C, Jandrot-Perrus M. Arocas V, et al. Biochemistry. 1996 Jul 16;35(28):9083-9. doi: 10.1021/bi960043l. Biochemistry. 1996. PMID: 8703912
In the present report, we show that the high affinity binding of alpha-thrombin to immobilized bothrojaracin (Kd = 0.6 nM) is inhibited by the C-terminal peptide of hirudin and that the gamma-cleavage within exosite 1 reduces the affinity of bothrojaracin for thromb …
In the present report, we show that the high affinity binding of alpha-thrombin to immobilized bothrojaracin (Kd = 0.6 nM) is inhibit …
Inhibition of thrombin-catalyzed factor V activation by bothrojaracin.
Arocas V, Lemaire C, Bouton MC, Bezeaud A, Bon C, Guillin MC, Jandrot-Perrus M. Arocas V, et al. Thromb Haemost. 1998 Jun;79(6):1157-61. Thromb Haemost. 1998. PMID: 9657441
We have previously identified and characterized a potent and specific thrombin inhibitor, isolated from Bothrops jararaca, named bothrojaracin. Bothrojaracin interacts with the two positively charged recognition sites of thrombin referred to as exosite 1 and exosite …
We have previously identified and characterized a potent and specific thrombin inhibitor, isolated from Bothrops jararaca, named bothroja …
Distinct bothrojaracin isoforms produced by individual jararaca (Bothrops jararaca) snakes.
Monteiro RQ, Carlini CR, Guimarães JA, Bon C, Zingali RB. Monteiro RQ, et al. Toxicon. 1997 May;35(5):649-57. doi: 10.1016/s0041-0101(96)00176-6. Toxicon. 1997. PMID: 9203289
In order to determine whether an individual snake produces a single type of bothrojaracin or multiple isoforms, we analyzed the bothrojaracin content of venoms collected individually from six adult B. jararaca snakes. Bothrojaracin was found in all venoms, bu …
In order to determine whether an individual snake produces a single type of bothrojaracin or multiple isoforms, we analyzed the bo …
Identification of bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta.
Castro HC, Fernandes M, Zingali RB. Castro HC, et al. Toxicon. 1999 Oct;37(10):1403-16. doi: 10.1016/s0041-0101(99)00087-2. Toxicon. 1999. PMID: 10414865
Bothrojaracin, a 27 kDa protein isolated from Bothrops jararaca venom, forms a non-covalent complex with thrombin, thus blocking its activity. ...Our results thus suggest that bothrojaracin-like proteins are widely distributed among Bothrops genera....
Bothrojaracin, a 27 kDa protein isolated from Bothrops jararaca venom, forms a non-covalent complex with thrombin, thus blocking its …
22 results