Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Joacir Stolarz Oliveira"'
Publikováno v:
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 20, Iss 0 (2015)
Scorpions, mainly those belonging to the genus Tityus cause many deaths and injuries in Brazil, with tens of thousands of envenomations notified every year. However, injuries involving other scorpion species are scarcely registered. Among the sixteen
Externí odkaz:
https://doaj.org/article/dde1dfe706d8455ba8f565047b6a1ee7
Autor:
Claudiran de Oliveira Braz, Joacir Stolarz-Oliveira, Rômulo Sarmento Barbosa, Geraldo Walter de Almeida Neto, Deyanira Fuentes-Silva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1f9343dc045e240341ecc72f0c31fd5
https://doi.org/10.22533/at.ed.3492231035
https://doi.org/10.22533/at.ed.3492231035
Autor:
José Carlos de Freitas, André J. Zaharenko, Katsuhiro Konno, Michael K. Richardson, Wilson Alves Ferreira, Fernanda C. V. Portaro, Daniel C. Pimenta, Joacir Stolarz Oliveira
Publikováno v:
Comparative Biochemistry and Physiology Part D: Genomics and Proteomics. 3:219-225
In contrast to the many studies on the venoms of scorpions, spiders, snakes and cone snails, up to now there has been no report of the proteomic analysis of sea anemones venoms. In this work we report for the first time the peptide mass fingerprint a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1aa0dd6017328338b40fff48a50bc6d
https://doi.org/10.1016/j.cbd.2008.04.002
https://doi.org/10.1016/j.cbd.2008.04.002
Autor:
Kanami Mori, Marcia Perez dos Santos Cabrera, Izumi Hide, Joacir Stolarz Oliveira, Izaura Y. Hirata, Setsuko Sekita, Renato Fontana, Hiroyuki Fuchino, João Ruggiero Neto, Marii Kawano, Marisa Rangel, Katsuhiro Konno, Yoshihiro Nakata
Publikováno v:
Peptides. 28:2320-2327
A novel peptide, decoralin, was isolated from the venom of the solitary eumenine wasp Oreumenes decoratus. Its sequence, Ser-Leu-Leu-Ser-Leu-Ile-Arg-Lys-Leu-Ile-Thr, was determined by Edman degradation and corroborated by solid-phase synthesis. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff6c2451c84d716a98927a9422f9b6c6
https://doi.org/10.1016/j.peptides.2007.09.017
https://doi.org/10.1016/j.peptides.2007.09.017
Autor:
Hideo Naoki, Marisa Rangel, João Ruggiero Neto, Yasuhiro Itagaki, Renato Fontana, Terumi Nakajima, Izumi Hide, Katsuhiro Konno, Marcia Perez dos Santos Cabrera, Joacir Stolarz Oliveira, Miki Hisada, Yoshihiro Nakata, Tadashi Yasuhara
Publikováno v:
Peptides. 27:2624-2631
A novel antimicrobial peptide, eumenitin, was isolated from the venom of the solitary eumenine wasp Eumenes rubronotatus. The sequence of eumenitin, Leu-Asn-Leu-Lys-Gly-Ile-Phe-Lys-Lys-Val-Ala-Ser-Leu-Leu-Thr, was mostly analyzed by mass spectrometry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fbeae96773e622aaa9e2c71237bce0b
https://doi.org/10.1016/j.peptides.2006.04.013
https://doi.org/10.1016/j.peptides.2006.04.013
Toxicity and toxin identification in Colomesus asellus, an Amazonian (Brazil) freshwater puffer fish
Autor:
Carlos Alberto Schwartz, José Carlos de Freitas, Carlos Bloch, Osmindo Rodrigues Pires, Solange Cristina Rego Fernandes, J. A. T. Melo, Joacir Stolarz Oliveira
Publikováno v:
Toxicon. 48:55-63
Toxicity and toxin identification in Colomesus asellus , an Amazonian (Brazil) freshwater puffer fish. By using four different techniques—mouse bioassay, ELISA, HPLC and mass spectrometry—we evaluated the toxicity in the extracts of C. asellus ,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c0c03ef8e60ac3ce2c95c2cc39e8ed9
https://doi.org/10.1016/j.toxicon.2006.04.009
https://doi.org/10.1016/j.toxicon.2006.04.009
Autor:
Enzo Wanke, Katsuhiro Konno, José Carlos de Freitas, André J. Zaharenko, Elisa Redaelli, Rita Restano Cassulini, Jeffrey J. Clare, Daniel C. Pimenta, Joacir Stolarz Oliveira
Publikováno v:
Journal of Biological Chemistry. 279:33323-33335
Sea anemones are an important source of various biologically active peptides, and it is known that ATX-II from Anemonia sulcata slows sodium current inactivation. Using six different sodium channel genes (from Nav1.1 to Nav1.6), we investigated the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4faccefed7b7cedff79e03239019129d
https://doi.org/10.1074/jbc.m404344200
https://doi.org/10.1074/jbc.m404344200
Autor:
Thiago Verano-Braga, Maria Elena de Lima, Gabriela Montandon, Joacir Stolarz Oliveira, Adriano Monteiro de Castro Pimenta, Camila Takeno Cologna, Frank Kjeldsen, Peter Roepstorff, Juliana S. Cassoli, Jan Tytgat, Steve Peigneur
Publikováno v:
Cassoli, J S, Verano-Braga, T, Oliveira, J S, Montandon, G G, Cologna, C T, Peigneur, S, Pimenta, A M D C, Kjeldsen, F, Roepstorff, P, Tytgat, J & de Lima, M E 2013, ' The proteomic profile of Stichodactyla duerdeni secretion reveals the presence of a novel O-linked glycopeptide ', Journal of Proteomics, vol. 87, pp. 89-102 . https://doi.org/10.1016/j.jprot.2013.05.022
Journal of Proteomics
Journal of Proteomics
UNLABELLED: Sea anemones represent one of the emerging groups of interest concerning venomous animals in toxinology and the goal of the present work was the prospection, and the structural and functional characterization of the compounds present in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::948e1bc7cb6b419322b7dc6e327b416c
https://pubmed.ncbi.nlm.nih.gov/23727489
https://pubmed.ncbi.nlm.nih.gov/23727489
Publikováno v:
Toxicon : official journal of the International Society on Toxinology. 60(4)
Sea anemone toxins are predominantly peptide and proteins that act mainly on sodium and potassium channels, as well as in a variety of target cells causing lysis. Over recent years, the number of sea anemone peptide toxins as well as cytolytic pore-f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e399766dad585745fe41d889b1197c0
https://pubmed.ncbi.nlm.nih.gov/22683676
https://pubmed.ncbi.nlm.nih.gov/22683676
Autor:
José Carlos de Freitas, Wilson Alves Ferreira, André J. Zaharenko, Michael K. Richardson, Enzo Wanke, Joacir Stolarz Oliveira, Emanuele Schiavon, Katsuhiro Konno
Sodium channel toxins from sea anemones are employed as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::691da43a44e99d798631b7314dfeaa6c
http://hdl.handle.net/10281/8057
http://hdl.handle.net/10281/8057