Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Plínio Delatorre"'
Autor:
Bruno A.M. Rocha, Lívia de Paulo Pereira, Benildo Sousa Cavada, Ana Maria Sampaio Assreuy, Mayara Queiroz Santiago, Kyria S. Nascimento, J.C. Silva-Filho, Vinicius Jose Da Silva Osterne, Plínio Delatorre, Cornevile Correia Neto, Alfa Umaro Bari, Claudener S. Teixeira, Vanir Reis Pinto-Junior, Henri Debray
Publikováno v:
International Journal of Biological Macromolecules. 92:194-201
The relation structure-activity of the Mimosoideae lectins of Parkia platycephala (PPL) and Parkia biglobosa (PBL) was analyzed in this study. PBL was solved by X-ray crystallography at a resolution of 2.1 y, and the crystal structure belonged to the
Autor:
Raphael Batista da Nóbrega, Carmem Gottfried, José Couras Silva-Filho, Plínio Delatorre, Daniel Barroso de Alencar, Alexandre Holanda Sampaio, Kyria S. Nascimento, Claudener S. Teixeira, Silvana Saker-Sampaio, Benildo Sousa Cavada, Celso S. Nagano, Bruno A.M. Rocha, Valder N. Freire
Publikováno v:
International Journal of Biological Macromolecules. 72:1136-1142
a b s t r a c t Resveratrol can also inhibit the activation of proinflammatory mediators and cytokines at the early gene expression stage. It is well known that lectins are sugar-binding proteins that act as both pro- and anti- inflammatory molecules
Autor:
Vinicius Jose Da Silva Osterne, Benildo Sousa Cavada, Bruno A.M. Rocha, Kyria S. Nascimento, Ito L. Barroso-Neto, Francisco N. Pereira-Junior, Ana Maria Sampaio Assreuy, Rafael da Conceição Simões, Maria Gonçalves Pereira, Alexandre Holanda Sampaio, Alana de Freitas Pires, Celso Shiniti Nagano, Maria Júlia Barbosa Bezerra, Plínio Delatorre
Publikováno v:
Archives of Biochemistry and Biophysics. 543:31-39
Lectins are comprised of a large family of proteins capable of the specific and reversible recognition of carbohydrates. Legume lectins, the most studied plant lectins, show high structural similarity, but with modifications that imply a variation in
Autor:
Maria Júlia Barbosa Bezerra, Bruno A.M. Rocha, Pedro Marcos Gomes Soares, Kássia Lys de Lima Alencar, Plínio Delatorre, Natália Velloso Fontenelle Camelo Rodrigues, Ana Maria Sampaio Assreuy, Jorge Luiz Martins, Benildo Sousa Cavada, Camila Bezerra Nobre, Alana de Freitas Pires, Celso Shiniti Nagano, Kyria S. Nascimento, Gustavo Arruda Bezerra, Alexandre Holanda Sampaio, Karl Gruber
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 45:807-815
Lectins from Diocleinae subtribe belong to the family of legume lectins and are characterized by high identity between their amino acids sequences. It has been shown that punctual differences in amino acid sequences, such as one single amino acid or
Autor:
Vinicius Jose Da Silva Osterne, Mayara Queiroz Santiago, Alysson Chaves Almeida, Claudener S. Teixeira, J.C. Silva-Filho, Bruno A.M. Rocha, Ana Maria Sampaio Assreuy, Kyria S. Nascimento, Rodrigo B. Leal, Claudia Figueiredo Lossio, Francisco Lucas Faustino do Nascimento, Vanir Reis Pinto-Junior, Ricardo Patricio Honorato Almeida, Benildo Sousa Cavada, Plínio Delatorre
Publikováno v:
Archives of biochemistry and biophysics. 596
A glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from Dalbergieae tribe. It was isolated by mannose-sepharose affinity chromatography. The primar
Autor:
Bruno A.M. Rocha, Benildo Sousa Cavada, Plínio Delatorre, T.R. Moura, Francisco N. Pereira-Junior, Kyria S. Nascimento, Helton C. Silva, Claudener S. Teixeira, Alexandre Holanda Sampaio, Celso Shiniti Nagano
Publikováno v:
Journal of Biochemistry. 152:87-98
Lectins have been used as models for studies of the molecular basis of protein-carbohydrate interaction and specificity by deciphering codes present in the glycan structures. The purpose of the present study was to purify and solve the complete prima
Autor:
Plínio Delatorre, Raquel G. Benevides, Bruno A.M. Rocha, Henri Debray, Walter Filgueira de Azevedo, Ana Maria Sampaio Assreuy, Alana de Freitas Pires, Albertina Antonielly Sydney de Sousa, Taiana Maia de Oliveira, Alexandre Holanda Sampaio, Luis A. G. Souza, Benildo Sousa Cavada
Publikováno v:
Repositório Institucional do INPA
Instituto Nacional de Pesquisas da Amazônia (INPA)
instacron:INPA
Instituto Nacional de Pesquisas da Amazônia (INPA)
instacron:INPA
Legume lectins, despite high sequence homology, express diverse biological activities that vary in potency and efficacy. In studies reported here, the mannose-specific lectin from Cymbosema roseum (CRLI), which binds N-glycoproteins, shows both pro-i
Autor:
Marcos H. Toyama, Carlos Alberto de Almeida Gadelha, Benildo Sousa Cavada, Bruno A.M. Rocha, Plínio Delatorre, Tatiane Santi-Gadelha
Publikováno v:
Biochimie. 93(3):513-518
The LYS49-PLA2s myotoxins have attracted attention as models for the induction of myonecrosis by a catalytically independent mechanism of action. Structural studies and biological activities have demonstrated that the myotoxic activity of LYS49-PLA2
Autor:
Bruno A.M. Rocha, Mário Rogério Lima Mota, Carlos Alberto de Almeida Gadelha, Benildo Sousa Cavada, Emmanuel P. Souza, Tatiane Santi-Gadelha, Walter Filgueira de Azevedo, Ana Maria Sampaio Assreuy, Plínio Delatorre, A.V.P. Meireles, Beatriz Tupinamba Freitas, João Batista Cajazeiras, Fernanda Canduri, Frederico Bruno Mendes Batista Moreno, Júlio César Borges, David N. Criddle, Nilson Vieira Pinto
Publikováno v:
Journal of Structural Biology. 152:185-194
Here, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of prote
Autor:
Raquel G. Benevides, T.R. Moura, T.M. de Oliveira, Benildo Sousa Cavada, Valder N. Freire, Frederico Bruno Mendes Batista Moreno, W.F. de Azevedo, Gustavo Arruda Bezerra, B.A.M. da Rocha, E.P. de Souza, Eduardo Henrique Salviano Bezerra, Kyria S. Nascimento, Plínio Delatorre
Publikováno v:
Journal of structural biology. 164(2)
The legume lectins from the subtribe Diocleinae, often referred to as concanavalin A-like lectins, are a typical example of highly similar proteins that show distinct biological activities. The pH-dependent oligomerization that some of these lectins