Biochemical and pharmacological properties of a new thrombin-like serine protease (Russelobin) from the venom of Russell's Viper (Daboia russelii russelii) and …
AK Mukherjee, SP Mackessy - … et Biophysica Acta (BBA)-General Subjects, 2013 - Elsevier
BACKGROUND: Snake venoms are rich sources of bioactive molecules, and several venom-
derived proteins have entered clinical trials for use in ischemic disorders; however, late …
derived proteins have entered clinical trials for use in ischemic disorders; however, late …
Size Matters: An Evaluation of the Molecular Basis of Ontogenetic Modifications in the Composition of Bothrops jararacussu Snake Venom
LA Freitas-de-Sousa, PG Nachtigall, JA Portes-Junior… - Toxins, 2020 - mdpi.com
Ontogenetic changes in venom composition have been described in Bothrops snakes, but
only a few studies have attempted to identify the targeted paralogues or the molecular …
only a few studies have attempted to identify the targeted paralogues or the molecular …
[HTML][HTML] The Contrasting Effects of Bothrops lanceolatus and Bothrops atrox Venom on Procoagulant Activity and Thrombus Stability under Blood Flow Conditions
F Radouani, P Jalta, C Rapon, C Lezin, C Branford… - Toxins, 2024 - mdpi.com
Background: Consumption coagulopathy and hemorrhagic syndrome are the typical
features of Bothrops sp. snake envenoming. In contrast, B. lanceolatus envenoming can …
features of Bothrops sp. snake envenoming. In contrast, B. lanceolatus envenoming can …
Towards toxin PEGylation: The example of rCollinein-1, a snake venom thrombin-like enzyme, as a PEGylated biopharmaceutical prototype
EL Pinheiro-Junior, J Boldrini-França… - International Journal of …, 2021 - Elsevier
PEGylation was firstly described around 50 years ago and has been used for more than 30
years as a strategy to improve the drugability of biopharmaceuticals. However, it remains …
years as a strategy to improve the drugability of biopharmaceuticals. However, it remains …
[HTML][HTML] Biochemical characterization and comparative analysis of two distinct serine proteases from Bothrops pirajai snake venom
DL Menaldo, CP Bernardes, NA Santos-Filho… - Biochimie, 2012 - Elsevier
This study reports the isolation and biochemical characterization of two different serine
proteases from Bothrops pirajai snake venom, thus providing a comparative analysis of the …
proteases from Bothrops pirajai snake venom, thus providing a comparative analysis of the …
Biochemical and functional properties of a thrombin-like enzyme isolated from Bothrops pauloensis snake venom
FLS Costa, RS Rodrigues, LFM Izidoro, DL Menaldo… - Toxicon, 2009 - Elsevier
In the present study, a thrombin-like enzyme named BpSP-I was isolated from Bothrops
pauloensis snake venom and its biochemical, enzymatic and pharmacological …
pauloensis snake venom and its biochemical, enzymatic and pharmacological …
[HTML][HTML] Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: molecular sequence analysis of its cDNA and biochemical properties
The thrombin-like enzyme from Bothrops barnetti named barnettobin was purified. We report
some biochemical features of barnettobin including the complete amino acid sequence that …
some biochemical features of barnettobin including the complete amino acid sequence that …
Isolation and Biochemical Characterization of a New Thrombin‐Like Serine Protease from Bothrops pirajai Snake Venom
This paper presents a novel serine protease (SP) isolated from Bothrops pirajai, a
venomous snake found solely in Brazil that belongs to the Viperidae family. The identified …
venomous snake found solely in Brazil that belongs to the Viperidae family. The identified …
Venom-sweet-venom: N-linked glycosylation in snake venom toxins
SG Soares, LL Oliveira - Protein and peptide letters, 2009 - ingentaconnect.com
Protein glycosylation represents one of the most important post-translational events, and is a
mean of diversifying a protein without recourse to the genome. The venoms produced by …
mean of diversifying a protein without recourse to the genome. The venoms produced by …
[HTML][HTML] Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities
ÂAA Megale, FC Magnoli, AK Kuniyoshi… - Journal of Venomous …, 2019 - SciELO Brasil
Background: Bitis arietans is a venomous snake found in sub-Saharan Africa and in parts of
Morocco and Saudi Arabia. The envenomation is characterized by local and systemic …
Morocco and Saudi Arabia. The envenomation is characterized by local and systemic …