Benedito C Prezoto
Overview
Explore the profile of Benedito C Prezoto including associated specialties, affiliations and a list of published articles.
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10
Citations
107
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Recent Articles
1.
Mina N, Guido V, Prezoto B, Oliva M, Sousa A
ACS Omega
. 2025 Jan;
9(52):51306-51319.
PMID: 39758662
Polyamidoamine (PAMAM) dendrimers, with their unique structural versatility and tunable surface functionalities, have emerged as promising nanomaterials for a wide range of biomedical applications. However, their in vivo use raises...
2.
Guido V, Olivieri Jr P, Brito M, Prezoto B, Martinez D, Oliva M, et al.
Langmuir
. 2024 May;
40(23):12167-12178.
PMID: 38808371
Gold nanoparticles (AuNPs) hold promise in biomedicine, but challenges like aggregation, protein corona formation, and insufficient biocompatibility must be thoroughly addressed before advancing their clinical applications. Designing AuNPs with specific...
3.
Sousa L, Freitas A, Cardoso B, Del-Rei T, Mendes V, Orefice D, et al.
Toxins (Basel)
. 2022 Aug;
14(8).
PMID: 36006204
The evolution of snake venoms resulted in multigene toxin families that code for structurally similar isoforms eventually harboring distinct functions. PLAs are dominant toxins in viper venoms, and little is...
4.
Prezoto B, Oguiura N
Toxins (Basel)
. 2020 Jan;
12(2).
PMID: 31979411
The sensitivity of vertebrate citrated plasma to pro- and anticoagulant venom or toxins occurs on a microscale level (micrograms). Although it improves responses to agonists, recalcification triggers a relatively fast...
5.
Bernardoni J, Sousa L, Wermelinger L, Lopes A, Prezoto B, Serrano S, et al.
PLoS One
. 2014 Oct;
9(10):e109651.
PMID: 25313513
Snake venom metalloproteinases (SVMPs) are major components in most viperid venoms that induce disturbances in the hemostatic system and tissues of animals envenomated by snakes. These disturbances are involved in...
6.
Rioli V, Prezoto B, Konno K, Melo R, Klitzke C, Ferro E, et al.
FEBS J
. 2008 Apr;
275(10):2442-54.
PMID: 18400032
Characterization of the peptide content of venoms has a number of potential benefits for basic research, clinical diagnosis, development of new therapeutic agents, and production of antiserum. Here, we use...
7.
Gomes C, Konno K, Conceicao I, Ianzer D, Yamanouye N, Prezoto B, et al.
Biochem Pharmacol
. 2007 Aug;
74(9):1350-60.
PMID: 17714693
Aiming to extend the knowledge about the diversity of bradykinin-potentiating peptides (BPPs) and their precursor proteins, a venom gland cDNA library from the South American rattlesnake (Crotalus dursissus terrificus, Cdt)...
8.
Pimenta D, Prezoto B, Konno K, Melo R, Furtado M, Camargo A, et al.
Rapid Commun Mass Spectrom
. 2007 Feb;
21(6):1034-42.
PMID: 17315274
Variation in the snake venom proteome is well documented and it is a ubiquitous phenomenon at all taxonomical levels. However, variation in the snake venom peptidome is so far not...
9.
Conceicao K, Konno K, de Melo R, Antoniazzi M, Jared C, Sciani J, et al.
Peptides
. 2006 Nov;
28(3):515-23.
PMID: 17098329
Bradykinin potentiating peptides (BPPs) from Bothrops jararaca venom were first described in the middle of 1960s and were the first natural inhibitors of the angiotensin-converting enzyme (ACE). BPPs present a...
10.
Hayashi M, Murbach A, Ianzer D, Portaro F, Prezoto B, Fernandes B, et al.
J Neurochem
. 2003 Apr;
85(4):969-77.
PMID: 12716428
The bradykinin-potentiating peptides from Bothrops jararaca venom are the most potent natural inhibitors of the angiotensin-converting enzyme. The biochemical and biological features of these peptides were crucial to demonstrate the...