Zobrazeno 1 - 10
of 45
pro vyhledávání: '"José R., Pires"'
Autor:
Bruna Maria de Carvalho Martins, Danielle M.P. Oliveira, Cristiane D. Anobom, Leonardo Bartkevihi, Fabio C. L. Almeida, José R. Pires
Publikováno v:
Biomolecular NMR Assignments. 14:119-122
Tuberculosis is one of the deadliest diseases worldwide affecting approximately 10 million people in 2018. This classifies tuberculosis as epidemic in several countries and leads to an increasing number of multidrug-resistant strains. Thus, the devel
Publikováno v:
Economics & Sociology, Vol 8, Iss 4 (2015)
Externí odkaz:
https://doaj.org/article/91929fd344d447ce99272d4c2e250798
Autor:
Pedro A. Valiente, Aymara Cabrera-Muñoz, Laritza Rojas, Maday Alonso-del-Rivero Antigua, José R. Pires
Publikováno v:
Journal of Structural Biology. 206:280-294
Subtilisin-like proteases play crucial roles in host-pathogen interactions. Thus, protease inhibitors constitute important tools in the regulation of this interaction. CmPI-II is a Kazal proteinase inhibitor isolated from Cenchritis muricatus that in
Autor:
Guilherme Caldas Andrade, Cristiane D. Anobom, Fabio C. L. Almeida, Danielle M.P. Oliveira, José R. Pires, Luis Felipe Correa Silva
Publikováno v:
Biomolecular NMR Assignments. 13:239-243
FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis-trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction
Autor:
Petr Kuzmic, Mey Ling Reytor González, Lizbeth Hedstrom, Maday Alonso-del-Rivero Antigua, José R. Pires
Publikováno v:
Biochimie. 150:37-47
Multi-domain inhibitors capable to block the activity of different classes of proteases are not very common in nature. However, these kinds of molecules are attractive systems for biomedical or biotechnological applications, where two or more differe
Autor:
José R. Pires, Anne Diehl, J. Retel, Peter Schmieder, Hartmut Oschkinat, Éverton Dias D'Andréa
Publikováno v:
Journal of Structural Biology. 213:107715
The 106-residue protein Q4DY78 (UniProt accession number) from Trypanosoma cruzi is highly conserved in the related kinetoplastid pathogens Trypanosoma brucei and Leishmania major. Given the essentiality of its orthologue in T. brucei, the high seque
Autor:
Yvette Roske, Anne Diehl, Peter Schmieder, Udo Heinemann, José R. Pires, Éverton Dias D'Andréa, Hartmut Oschkinat, Nils Cremer, Guilherme A. P. de Oliveira
Publikováno v:
Journal of Structural Biology. 211:107536
Complete genome sequencing of the kinetoplastid protozoans Trypanosoma cruzi, Trypanosoma brucei and Leishmania major (Tritryp), published in 2005, opened up new perspectives for drug development targeting Chagas disease, African sleeping sickness an
Autor:
Manso, José R. Pires1
Publikováno v:
Kondratieff Waves, Warfare & World Security. 2006, Vol. 5 Issue 1, p48-56. 9p. 1 Chart, 3 Graphs.
Publikováno v:
Biomolecular NMR Assignments. 10:153-156
A protease inhibitor (CmPI-II) (UNIPROT: IPK2_CENMR) from the marine mollusc Cenchritis muricatus, has been isolated and characterized. It is the first member of a new group (group 3) of non-classical Kazal-type inhibitors. CmPI-II is a tight-binding
Publikováno v:
Journal of Structural Biology. 190:11-20
Q4D059 (UniProt accession number), is an 86-residue protein from Trypanosoma cruzi, conserved in the related kinetoplastid parasites Trypanosoma brucei and Leishmania major. These pathogens are the causal agents of the neglected diseases: Chagas, sle