Relevant bibliographies by topics / Bungarus fasciatus

Academic literature on the topic 'Bungarus fasciatus'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Bungarus fasciatus"

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Shin, I., I. Silman, C. Bon, and L. Weiner. "Unfolding of acetylcholinesterase from Bungarus fasciatus." Neuroscience Letters 237 (November 1997): S46. http://dx.doi.org/10.1016/s0304-3940(97)90190-7.

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Utkin, Yu N., E. A. Gantsova, T. V. Andreeva, V. G. Starkov, R. H. Ziganshin, Hoang Ngoc Anh, Nguyen Thi Thanh Thao, Nguyen Cuu Khoa, and V. I. Tsetlin. "Venoms of kraits Bungarus multicinctus and Bungarus fasciatus contain anticoagulant proteins." Doklady Biochemistry and Biophysics 460, no. 1 (January 2015): 53–58. http://dx.doi.org/10.1134/s1607672915010159.

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Cousin, X., N. Duval, J. Massoulié, and C. Bon. "Cloning of acetylcholinesterase from Bungarus fasciatus venom." Toxicon 35, no. 4 (April 1997): 484–85. http://dx.doi.org/10.1016/s0041-0101(97)84731-9.

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Cousin, X., and C. Bon. "Cloning of acetylcholinesterase from Bungarus fasciatus venom." Toxicon 34, no. 10 (October 1996): 1085–86. http://dx.doi.org/10.1016/0041-0101(96)83807-4.

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Rusmili, Muhamad Rusdi Ahmad, Tee Ting Yee, Mohd Rais Mustafa, Wayne C. Hodgson, and Iekhsan Othman. "Proteomic characterization and comparison of Malaysian Bungarus candidus and Bungarus fasciatus venoms." Journal of Proteomics 110 (October 2014): 129–44. http://dx.doi.org/10.1016/j.jprot.2014.08.001.

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LU, Xiang-Yun, Ai-Li WANG, Hai-Long YANG, and Ren LAI. "A Novel Trypsin Inhibitor from Bungarus fasciatus Venom." Chinese Journal of Natural Medicines 6, no. 2 (March 2008): 153–58. http://dx.doi.org/10.1016/s1875-5364(09)60014-5.

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7

Ahsan, M. F., and M. M. Rahman. "Status, distribution and threats of kraits (Squamata: Elapidae: Bungarus) in Bangladesh." Journal of Threatened Taxa 9, no. 3 (March 26, 2017): 9903. http://dx.doi.org/10.11609/jott.2929.9.3.9903-9910.

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Kraits (Bungarus spp.) of Bangladesh were studied between January 2014 and March 2015. Five species of kraits are known to occur in Bangladesh. These are the Common Krait Bungarus caeruleus, Banded Krait B. fasciatus, Lesser Black Krait B. lividus, Greater Black Krait B. niger and Wall’s Krait B. walli. Banded Krait is the commonest and Lesser Black Krait is the rarest krait species in the country. The status of these five kraits in Bangladesh has been assessed. The distributions have been compiled and discussed, and some reasons for their population decline have also been pointed out.
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Ahmad Rusmili, Muhamad Rusdi, Iekhsan Othman, Mohd Rais Mustafa, and Wayne Hodgson. "145. In vitro Vascular Activity of Crude Bungarus candidus and Bungarus fasciatus Crude Venoms." Toxicon 60, no. 2 (August 2012): 169. http://dx.doi.org/10.1016/j.toxicon.2012.04.146.

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Kang, Tse Siang, Wan Chen, Leng Chuan Goh, and Manjunatha Kini. "Identification and characterisation of novel inhibitors on extrinsic tenase complex from Bungarus fasciatus (banded krait) venom." Thrombosis and Haemostasis 112, no. 10 (2014): 700–715. http://dx.doi.org/10.1160/th13-12-1063.

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SummarySnake venoms are excellent sources of pharmacologically active proteins and peptides, and hence are potential sources of leads for drug developments. It has been previously established that krait (Bungarus genus) venoms contain mainly neurotoxins. A screening for anticoagulants showed that Bungarus fasciatus venom exhibits potent anticoagulant effect in standard clotting assays. Through sequential fractionation of the venom by size exclusion and high performance liquid chromatographies, coupled with functional screening for anticoagulant activities, we have isolated and purified two anticoagulant proteins, termed BF-AC1 ( Bungarus fasciatus anticoagulant 1) and BFAC2. They have potent inhibitory activities (IC50 of 10 nM) on the extrinsic tenase complex. Structurally, these proteins each has two subunits covalently held together by disulfide bond(s). The N-terminal sequences of the individual subunits of BF-AC1 and BF-AC2 showed that the larger subunit is homologous to phospholipase A2, while the smaller subunit is homologous to Kunitz type serine proteinase inhibitor. Functionally, in addition to their anticoagulant activity, these proteins showed presynaptic neurotoxic effects in both in vivo and ex vivo experiments. Thus, BF-AC1 and BF-AC2 are structurally and functionally similar to β-bungarotoxins, a class of neurotoxins. The enzymatic activity of phospholipase A2 subunit plays a significant role in the anticoagulant activities. This is the first report on the anticoagulant activity of β-bungarotoxins and these results expand on the existing catalogue of haemostatically active snake venom proteins.
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Yesmin Roly, Zahida, SM Naimul Hasan, KMKB Ferdaus, and Md Abu Reza. "Predicted structure model of bungarotoxin from Bungarus fasciatus snake." Bioinformation 10, no. 10 (October 30, 2014): 617–22. http://dx.doi.org/10.6026/97320630010617.

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Dissertations / Theses on the topic "Bungarus fasciatus"

1

COUSIN, XAVIER. "Genetique et structure des acetylcholinesterases de vertebres : - clonage d'une sous-unite hydrophobe d'ancrage - etude de l'ache de bungarus fasciatus - creation et developpement d'une banque de donnees dediee aux cholinesterases: esther." Paris 6, 1995. http://www.theses.fr/1995PA066573.

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Dans cette these, nous nous sommes interesses a divers aspects concernant la structure moleculaire de l'acetylcholinesterase. Dans une premiere partie nous avons cherche a caracteriser l'ancrage membranaire de la forme majeure d'acetylcholinesterase du cerveau de mammiferes, qui comporte une sous-unite structurale hydrophobe de 20 kda, liee a un tetramere de sous-unites catalytiques de type t. Nous avons clone un adnc qui pourrait coder pour cette proteine, mais les experiences de co-transfection que nous avons realisees n'ont pas permis de reconstituer l'assemblage de cette proteine avec les tetrameres t. Dans une deuxieme partie, nous nous sommes interesses a l'acetylcholinesterase de certains serpents, dont le venin possede une forte activite de cette enzyme. Il s'agit d'une forme moleculaire inhabituelle, correspondant a des monomeres solubles. Nous avons clone cette enzyme chez le bungare (bungarus fasciatus) et montre que sa region c-terminale est codee par un nouvel exon alternatif, qui code pour un petit peptide hydrophile ce qui explique que l'acetylcholinesterase de venin forme des monomeres solubles. Nous avons egalement caracterise et clone l'acetylcholinesterase du muscle de bungare, et montre qu'il s'agit d'une sous-unite t, comme chez les autres vertebres. La comparaison de la sequence d'acetylcholinesterase de bungare avec celles d'acetylcholinesterases d'autres vertebres, a permis de mettre en evidence deux differences majeures, une methionine en position 70 au lieu d'une tyrosine, et une lysine en position 285 au lieu d'une residu acide. Le remplacement par mutagenese dirigee de ces acides amines dans l'acetylcholinesterase de bungare par leurs homologues chez la torpille et l'expression dans les cellules cos permet d'obtenir une enzyme possedant les proprietes de l'acetylcholinesterase de torpille vis-a-vis des ligands du site peripherique. Parallelement a ces travaux experimentaux, nous avons mis en place une banque de donnees accessible par internet et dediee aux cholinesterases
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Book chapters on the topic "Bungarus fasciatus"

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Shin, Irina, Israel Silman, Cassian Bon, and Lev Weiner. "Membrane-Promoted Unfolding of Torpedo Californica and Bungarus Fasciatus Acetylcholinesterase." In Structure and Function of Cholinesterases and Related Proteins, 438–39. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_120.

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You might also be interested in the extended bibliographies on the topic 'Bungarus fasciatus' for particular source types:
Journal articles
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