Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lucas R. de Souza"'
Autor:
Lucas Villas Bôas Hoelz, Marcelo B. Zani, Lucas R. de Souza, Luiza R.S. Dias, Sergio Pinheiro, Silvia G. Passos, Bruna C. Zorzanelli, Pedro H.R. de A. Azevedo, Luciano Puzer, Estela M.F. Muri
Publikováno v:
European Journal of Medicinal Chemistry. 112:39-47
Human kallikrein 5 (KLK5) is a potential target for the treatment of skin inflammation and cancer. A new series of statine based peptidomimetic compounds were designed and synthesized through simple and efficient reactions. Some KLK5 inhibitors (2a-c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f6abb669a29bd6ae72c32310f6f5760
https://doi.org/10.1016/j.ejmech.2016.01.060
https://doi.org/10.1016/j.ejmech.2016.01.060
Autor:
Lucas R, de Souza, Benjamin M, Scott, Varsha, Bhakta, David A, Donkor, Darian L, Perruzza, William P, Sheffield
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1826
Phage display is a protein engineering approach that involves construction of libraries of variant proteins displayed on the surface of bacteriophage as capsid fusion proteins and their screening for binding and inhibitory function through the use of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bc54c51fe4db6f896173f01616ad1a11
https://pubmed.ncbi.nlm.nih.gov/30194592
https://pubmed.ncbi.nlm.nih.gov/30194592
Autor:
William P. Sheffield, Benjamin M. Scott, Darian L. Perruzza, Lucas R. de Souza, David A. Donkor, Varsha Bhakta
Publikováno v:
Methods in Molecular Biology ISBN: 9781493986446
Phage display is a protein engineering approach that involves construction of libraries of variant proteins displayed on the surface of bacteriophage as capsid fusion proteins and their screening for binding and inhibitory function through the use of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2903cb189cc4a35bbaddb475f5482e8
https://doi.org/10.1007/978-1-4939-8645-3_3
https://doi.org/10.1007/978-1-4939-8645-3_3
Autor:
Ivarne L.S. Tersariol, Lucas R. de Souza, Daniela L. Jabes, Valquíria Campos Alencar, Luciano Puzer, Maria Cecília Zorél Meneghetti, Regina Costa de Oliveira, Marcelo A. Lima, Luiz R. Nunes, Guilherme L. Sassaki, Fabiano Bezerra Menegidio
Publikováno v:
Biochemistry. 56(5)
Xylella fastidiosa is a plant-infecting bacillus, responsible for many important crop diseases, such as Pierce's disease of vineyards, citrus variegated chlorosis, and coffee leaf scorch (CLS), among others. Recent genomic comparisons involving two C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bb81a7180d6cf3dc35f27d2aaaa0088
https://pubmed.ncbi.nlm.nih.gov/28125217
https://pubmed.ncbi.nlm.nih.gov/28125217
Autor:
Luciano Puzer, Marcelo B. Zani, Natália Salazar, Arlei Marcili, Silvia G. Passos, Regiane A. de Andrade, Jocelia P. C. Oliveira, Lucas R. de Souza, Aquiles M. Sant'Ana, Márcia Aparecida Sperança
Publikováno v:
Biochimie. 127
Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f79b6d2bab6062e8c97a50695b96018c
https://pubmed.ncbi.nlm.nih.gov/27157268
https://pubmed.ncbi.nlm.nih.gov/27157268
Autor:
Michael Blaber, Lucas R. de Souza, Karina F. Devienne, Renato F. Freitas, Luiz Juliano, Odonírio Abrahão, Sachico I. Blaber, Marcia Y. Kondo, Thiago S.P. Teixeira, Luciano Puzer, Maria A. Juliano
Publikováno v:
Bioorganicmedicinal chemistry letters. 21(20)
Human kallikrein 5 and 7 (KLK5 and KLK7) are trypsin-like and chymotrypsin-like serine proteases, respectively, and promising targets for the treatment of skin desquamation, inflammation and cancer. In an effort to develop new inhibitors for these en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63d431e87c009b2fa1e43438b1ca24ea
https://pubmed.ncbi.nlm.nih.gov/21903387
https://pubmed.ncbi.nlm.nih.gov/21903387