Výsledky vyhledávání - "Leandra Watanabe"

Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities

Autor: Jay W. Fox, Leandra Watanabe, R. David G. Theakston, Raghuvir K. Arni, José María Gutiérrez, Aura S. Kamiguti, John D. Shannon, Richard H. Valente, Alexandra Rucavado, Alberto Alape-Girón

Publikováno v: Protein Science; Volumen 12, Número 10. 2003
Kérwá
Universidad de Costa Rica
instacron:UCR
Web of Science
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP

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Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdb5b7d86ffab67bb8a1ad3860d7115b
https://doi.org/10.1110/ps.03102403

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Purification and Characterization of Jararassin-I, A Thrombin-like Enzyme from Bothrops jararaca Snake Venom

Autor: Silvana Marcussi, Suely Vilela Sampaio, Carolina D. Sant’Ana, Andreimar M. Soares, Leandra Watanabe, Raghuvir K. Arni, Débora F. Vieira

Publikováno v: Acta Biochimica et Biophysica Sinica. 36:798-802

A thrombin-like serine protease, jararassin-I, was isolated from the venom of Bothrops jararaca. The protein was obtained in high yield and purity by a single chromatographic step using the affinity resin Benzamidine-Sepharose CL-6B. SDS-PAGE and dyn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::425c7b5abb72fba7fb96f9824c25fe16
https://doi.org/10.1093/abbs/36.12.798

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Structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase fromPseudomonas putida

Autor: B. J. Bell, Leandra Watanabe, Lukasz Lebioda, J. L. Rios-Steiner, Raghuvir K. Arni, Alexander Tulinsky

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 59:1454-1458

2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is a key enzyme in the Entner-Doudoroff pathway which catalyses the cleavage of KDPG via a class I Schiff-base mechanism. The crystal structure of this enzyme has been refined

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b048b04f7a3144d92223f21d655378be
https://doi.org/10.1107/s0907444903013192

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Purification, characterization and crystallization of Jararacussin-I, a fibrinogen-clotting enzyme isolated from the venom of Bothrops jararacussu

Autor: Andreimar M. Soares, Leandra Watanabe, R.K. Bortoleto, Raghuvir K. Arni, Mário T. Murakami

Publikováno v: Toxicon. 40:1307-1312

A fibrinogen-clotting enzyme, Jararacussin-I, was purified from the venom of Bothrops jararacussu by a combination of ion exchange chromatography using Resource 15S resin and affinity chromatography using Benzamidine Sepharose 6B resin. Jararacussin-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a9f763b4fc4b5db4fde0aaf1ee37440
https://doi.org/10.1016/s0041-0101(02)00140-x

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Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to its soluble decoy receptor IL-22BP

Autor: Didier Colau, Jean-Christophe Renauld, Laure Dumoutier, Patricia Ribeiro de Moura, Alessandro S. Nascimento, Igor Polikarpov, Leandra Watanabe

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Interleukin-22 (IL-22) is a pleiotropic cytokine that is involved in inflammatory responses. Human IL-22 was incubated with its soluble decoy receptor IL-22BP (IL-22 binding protein) and the IL-22-IL-22BP complex was crystallized in hanging drops usi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::604ce83ccd0c12cb18ad594e396240ae
https://doi.org/10.1107/s1744309108042309

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Crystallization of the Lys49 PLA2 homologue, myotoxin II, from the venom of Atropoides nummifer

Autor: Leandra Watanabe, Bruno Lomonte, Lisandra M. Gava, Raghuvir K. Arni, Yamileth Angulo

Publikováno v: Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, vol.1703, (1), pp.87-89
Kérwá
Universidad de Costa Rica
instacron:UCR

Myotoxin II, a Lys49 catalytically inactive phospholipase A2 homologue from Atropoides nummifer venom, was purified, characterized and crystallized. The crystals belongs to the tetragonal system, space group P43212, with unit cell parameters (a=b=68.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd2dc4d596a533ea066722467b30c9f2
https://doi.org/10.1016/j.bbapap.2004.09.006

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Initial structural analysis of an α4β4C-type lectin from the venom ofCrotalus durissus terrificus

Autor: S. P. Zela, A. C. O. Cintra, Raghuvir K. Arni, Leandra Watanabe, Lisandra M. Gava, Mário T. Murakami

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 59:1813-1815

Convulxin, an alphabeta C-type lectin, is a potent platelet activator isolated from the venom of the South American rattlesnake Crotalus durissus terrificus. It is a 26.5 kDa alphabeta heterodimer consisting of two homologous disulfide-linked chains.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b2344f631fdb8fb52ce75b60fe56a41
https://doi.org/10.1107/s0907444903016202

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Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia)

Autor: Valery L. Shnyrov, Manuel G. Roig, Libia Sanz, Alicia Pérez, Igor Polikarpov, Juan J. Calvete, Patricia Ribeiro de Moura, Laura S. Zamorano, Lucas Bleicher, Leandra Watanabe, Sergey A. Bursakov, Alessandro S. Nascimento

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Royal palm tree peroxidase (RPTP) is a very stable enzyme in regards to acidity, temperature, H(2)O(2), and organic solvents. Thus, RPTP is a promising candidate for developing H(2)O(2)-sensitive biosensors for diverse applications in industry and an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d533e1fd474863328a5043e2968d708
https://pubmed.ncbi.nlm.nih.gov/19854274

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Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22

Autor: Patricia Ribeiro de Moura, Igor Polikarpov, Laure Dumoutier, Didier Colau, Muriel M. Lemaire, Lucas Bleicher, Jean-Christophe Renauld, Leandra Watanabe

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Interleukin-22 (IL-22) plays an important role in the regulation of immune and inflammatory responses in mammals. The IL-22 binding protein (IL-22BP), a soluble receptor that specifically binds IL-22, prevents the IL-22/interleukin-22 receptor 1 (IL-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b2a13e646bcc2e65545a15f5ebf1fe1

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