Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Alejandro E Leroux"'
Autor:
Rachel B Currier, Kathrin Ulrich, Alejandro E Leroux, Natalie Dirdjaja, Matías Deambrosi, Mariana Bonilla, Yasar Luqman Ahmed, Lorenz Adrian, Haike Antelmann, Ursula Jakob, Marcelo A Comini, R Luise Krauth-Siegel
Publikováno v:
PLoS Pathogens, Vol 15, Iss 9, p e1008065 (2019)
Most known thioredoxin-type proteins (Trx) participate in redox pathways, using two highly conserved cysteine residues to catalyze thiol-disulfide exchange reactions. Here we demonstrate that the so far unexplored Trx2 from African trypanosomes (Tryp
Externí odkaz:
https://doaj.org/article/760db50775bb44a9a0ccbc05aa1486bd
Autor:
Mariana Sacerdoti, Lissy Zoe Florens Gross, Stefan Zeuzem, Ricardo M. Biondi, Albrecht Piiper, Alejandro E. Leroux
Publikováno v:
ChemMedChem
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemmedchem
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemmedchem
Angiotensin Converting Enzyme 2 (ACE2) is the human receptor that interacts with the Spike protein of coronaviruses, including the one that produced the 2020 coronavirus pandemic (COVID-19). Thus, ACE2 is a potential target for drugs that disrupt the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8241b14a9662624e4ed2cc0e358befbe
Publikováno v:
Seminars in Cancer Biology. 48:1-17
The group of AGC kinases consists of 63 evolutionarily related serine/threonine protein kinases comprising PDK1, PKB/Akt, SGK, PKC, PRK/PKN, MSK, RSK, S6K, PKA, PKG, DMPK, MRCK, ROCK, NDR, LATS, CRIK, MAST, GRK, Sgk494, and YANK, while two other fami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::280836555d19adccd8a335ea0a7d721d
https://doi.org/10.1016/j.semcancer.2017.05.011
https://doi.org/10.1016/j.semcancer.2017.05.011
Autor:
Lissy Z. F. Gross, Mariana Sacerdoti, Alejandro E. Leroux, Abhijeet Ghode, Ganesh S. Anand, Jörg O. Schulze, Melissa A. Graewert, Dmitri I. Svergun, Sebastian Klinke, Ricardo M. Biondi
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:C1114-C1114
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b447e7a2be77d4248a2d3728e1528c8
https://doi.org/10.1107/s0108767321085913
https://doi.org/10.1107/s0108767321085913
Publikováno v:
Advances in experimental medicine and biology. 1163
Allostery is a basic principle that enables proteins to process and transmit cellular information. Protein kinases evolved allosteric mechanisms to transduce cellular signals to downstream signalling components or effector molecules. Protein kinases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dbb583775d13e0d71ed9fe8341709712
https://pubmed.ncbi.nlm.nih.gov/31707708
https://pubmed.ncbi.nlm.nih.gov/31707708
Autor:
Ricardo M. Biondi, Alejandro E. Leroux
Publikováno v:
Trends in biochemical sciences. 45(1)
Protein–protein interactions often regulate the activity of protein kinases by allosterically modulating the conformation of the ATP-binding site. Bidirectional allostery implies that reverse modulation (i.e., from the ATP-binding site to the inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01eb6ce0bd0ae419f4eb8fe50561dd2c
https://pubmed.ncbi.nlm.nih.gov/31690482
https://pubmed.ncbi.nlm.nih.gov/31690482
Autor:
Lucila Giordana, Máximo Hernán Sosa, Cristina Nowicki, Alejandro E. Leroux, Elkin Fernando Rodas Mendoza, Patricia B. Petray
Publikováno v:
Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Leishmania parasites cause a broad spectrum of clinical manifestations in humans and the available clinical treatments are far from satisfactory. Since these pathogens require large amounts of NADPH to maintain intracellular redox homeostasis, oxidor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feeae1004694ee9c8e2506225c7d2154
Autor:
Mariana Bonilla, Marcelo A. Comini, Matías Deambrosi, Haike Antelmann, Natalie Dirdjaja, Yasar Luqman Ahmed, Lorenz Adrian, Ursula Jakob, Rachel B. Currier, Alejandro E. Leroux, Kathrin Ulrich, R. Luise Krauth-Siegel
Publikováno v:
PLoS Pathogens
COLIBRI
Universidad de la República
instacron:Universidad de la República
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS Pathogens, Vol 15, Iss 9, p e1008065 (2019)
COLIBRI
Universidad de la República
instacron:Universidad de la República
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS Pathogens, Vol 15, Iss 9, p e1008065 (2019)
Most known thioredoxin-type proteins (Trx) participate in redox pathways, using two highly conserved cysteine residues to catalyze thiol-disulfide exchange reactions. Here we demonstrate that the so far unexplored Trx2 from African trypanosomes (Tryp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1479757250d326147bf104a57ad754d5
https://doi.org/10.1371/journal.ppat.1008065
https://doi.org/10.1371/journal.ppat.1008065
Publikováno v:
The Journal of Biological Chemistry, 288(33), 23751-23764. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Leroux, A E, Haanstra, J R, Bakker, B M & Krauth-Siegel, R L 2013, ' Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modelling. ', Journal of Biological Chemistry, vol. 288, pp. 23751-23764 . https://doi.org/10.1074/jbc.M113.483289
Journal of Biological Chemistry, 288, 23751-23764. American Society for Biochemistry and Molecular Biology Inc.
The Journal of Biological Chemistry
Leroux, A E, Haanstra, J R, Bakker, B M & Krauth-Siegel, R L 2013, ' Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modelling. ', Journal of Biological Chemistry, vol. 288, pp. 23751-23764 . https://doi.org/10.1074/jbc.M113.483289
Journal of Biological Chemistry, 288, 23751-23764. American Society for Biochemistry and Molecular Biology Inc.
The Journal of Biological Chemistry
Background: Trypanothione synthetase catalyzes the conjugation of spermidine with two GSH molecules to form trypanothione. Results: The kinetic parameters were measured under in vivo-like conditions. A mathematical model was developed describing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0633fd58abba23146c12574a249ed956
https://doi.org/10.1074/jbc.m113.483289
https://doi.org/10.1074/jbc.m113.483289