Reprint
Celebrating 120 Years of Butantan Institute Contributions for Toxinology
Edited by
February 2022
408 pages
- ISBN978-3-0365-3188-5 (Hardback)
- ISBN978-3-0365-3189-2 (PDF)
This book is a reprint of the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology that was published in
Biology & Life Sciences
Medicine & Pharmacology
Public Health & Healthcare
Summary
This is collection of original and review articles selected in recognition of the contribution of Instituto Butantan to the field of toxinology and its continued and relevant role in this field in the 120 years since its foundation. Congratulations to the Butantan Institute, its house scientists, and collaborators on its 120th anniversary!
Format
- Hardback
License
© 2022 by the authors; CC BY-NC-ND license
Keywords
mass spectrometry; proteome; snake venom; Bothrops jararaca; breast cancer; Bothrops jararaca; HF3; human plasma; proteolysis; snake venom metalloproteinase; Bothrops atrox; blister; local damage; DAMPs; snake venom; antivenom; snakebite; Bothrops; metalloproteases; inflammation; microcirculation; adhesion molecules; leukocyte-endothelium interactions; Bothrops atrox; individual variability; venom heterogeneity; STEC; Stx2; antibody fragment; monoclonal antibody; neurodegenerative disease; neurodegeneration; inflammation; IL-17; glial cells; crotoxin; epithelial–mesenchymal transition; spheroid model; tumor stroma; Lonomia; envenoming; innovation; Tityus serrulatus; venom components; hypotensins; NEP inhibition; cytokines; toxins; venoms; skin secretion; drug discovery; scorpion accidents; lactation; maternal care; seizure threshold; leech; Haementeria vizottoi; cysteine proteases inhibitor; recombinant cystatin; cathepsin L; Cryptops iheringi; centipede; venom; toxin; transcriptome; proteome; recombinant protein; venomics; chilopoda; oral tolerance; Bothrops jararaca; snake venom; ELISA; Bothrops phospholipases A2; inflammation; lipid mediators; signaling pathways; fish venoms; cytolysins; multifunctionality; pore formation; Bitis arietans venom (BaV); Kn-Ba; inflammation; cytokines and chemokines; PGE2; THP-1 macrophages; analgesic peptide; protein kinase C; hyperalgesia; cell-signaling; Hyalomma dromedarii; salivary glands; serpin; anticoagulants; thrombin inhibitor; β-defensins; snakes; antimicrobial activity; bioisosterism; peptides; Thalassophryne; nattectin; reverse-phase HPLC; MALDI-ToF; hemagglutinating activity; antibacterial activity; inflammation; toxinology; animal toxins; n/a