Výsledky vyhledávání - "Cristhian Boetsch"

Structural Insights into the Inhibition Site in the Phosphorylcholine Phosphatase Enzyme of

Autor: Daniel, Bustos, Erix W, Hernández-Rodríguez, Horacio, Poblete, Jans, Alzate-Morales, Cecilia, Challier, Cristhian, Boetsch, Ariela, Vergara-Jaque, Paola, Beassoni

Publikováno v: Journal of chemical information and modeling. 62(12)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::022ef7e53aa9e38b197539a5c04c8da4
https://pubmed.ncbi.nlm.nih.gov/35670773

Zobrazit plný text záznamu

Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach

Autor: Fernando D. González-Nilo, Paola Rita Beassoni, Daniel R. Aguayo-Villegas, Á. Teresita Lisa, Cristhian Boetsch

Publikováno v: Archives of biochemistry and biophysics. 606

The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx(-) or ppk(-) mutants and on the double mutant, demonstrate a relation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e110a2856bdb59cd9b44f9494809dda
https://pubmed.ncbi.nlm.nih.gov/27424154

Zobrazit plný text záznamu

Pseudomonas aeruginosa Exopolyphosphatase Is Also a Polyphosphate: ADP Phosphotransferase

Autor: Paola Rita Beassoni, Mónica N. Garrido, Cristhian Boetsch, Angela T. Lisa, Lucas Antonio Gallarato

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Enzyme Research
Enzyme Research, Vol 2015 (2015)

Pseudomonas aeruginosaexopolyphosphatase (paPpx; EC 3.6.1.11) catalyzes the hydrolysis of polyphosphates (polyP), producing polyPn−1plus inorganic phosphate(Pi). In a recent work we have shown thatpaPpx is involved in the pathogenesis ofP. aerugino

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fabed140d36d90ced2c42f992aee354
https://www.hindawi.com/journals/er/2015/404607/

Zobrazit plný text záznamu

Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein

Autor: Cecilia Challier, Paola Rita Beassoni, M. A. Biasutti, Cristhian Boetsch, Norman A. García, Susana Criado

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c52db5fd6dcb382d821eb2e92b23c80
https://www.sciencedirect.com/science/article/pii/S1011134414003273

Zobrazit plný text záznamu

The structural domains of Pseudomonas aeruginosa phosphorylcholine phosphatase cooperate in substrate hydrolysis: 3D structure and enzymatic mechanism

Autor: Lisandro H. Otero, Angela T. Lisa, Armando Albert, Carlos E. Domenech, Lourdes Infantes, Paola Rita Beassoni, Cristhian Boetsch

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname

Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen. It colonizes different tissues by the utilization of diverse mechanisms. One of these may involve the breakdown of the host cell membrane through the sequential action of hemolytic ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1858d67d29af49621805cbf2a12f1c58
https://pubmed.ncbi.nlm.nih.gov/22922065

Zobrazit plný text záznamu

Different Effects of Mg and Zn on the Two Sites for Alkylammonium Compounds in Pseudomonas aeruginosa Phosphorylcholine Phosphatase

Autor: Lisandro Horacio, Otero, Paola Rita, Beassoni, Cristhian, Boetsch, Angela Teresita, Lisa, Carlos Eduardo, Domenech

Publikováno v: Enzyme Research

Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine (Pcho), is activated by Mg(2+) or Zn(2+), and is inhibited by high concentrations of substrate. This study has shown that PchP contains two site

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0874523ad9aec9d110dc2291ddbdf9b1
https://pubmed.ncbi.nlm.nih.gov/21660097

Zobrazit plný text záznamu

Different Effects of Mg2+ and Zn2+ on the Two Sites for Alkylammonium Compounds in Pseudomonas aeruginosa Phosphorylcholine Phosphatase

Autor: Carlos E. Domenech, Paola Rita Beassoni, Cristhian Boetsch, Lisandro H. Otero, Angela T. Lisa

Publikováno v: Enzyme Research, Vol 2011 (2011)

Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine (Pcho), is activated by Mg2+ or Zn2+, and is inhibited by high concentrations of substrate. This study has shown that PchP contains two sites fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4876b0b76e0481895417617cf1f75a8b

Zobrazit plný text záznamu

Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase

Autor: Angela T. Lisa, Lisandro H. Otero, Cristhian Boetsch, Paola Rita Beassoni, Fernado D. González-Nilo, Carlos E. Domenech

Publikováno v: Biochimica et biophysica acta. 1814(7)

Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine (Pcho) to produce choline and inorganic phosphate. PchP belongs to the haloacid dehalogenase superfamily (HAD) and possesses the three character

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::386f29996b0cbe5d11ada1218053dd08
https://pubmed.ncbi.nlm.nih.gov/21515416

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání