Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Kiran V. Mahasenan"'
Autor:
Siseth Martínez-Caballero, Céline Freton, Rafael Molina, Sergio G. Bartual, Virginie Gueguen-Chaignon, Chryslène Mercy, Federico Gago, Kiran V. Mahasenan, Inés G. Muñoz, Mijoon Lee, Dusan Hesek, Shahriar Mobashery, Juan A. Hermoso, Christophe Grangeasse
Publikováno v:
Cell Reports, Vol 42, Iss 7, Pp 112756- (2023)
Summary: Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue be
Externí odkaz:
https://doaj.org/article/d81c8fc5e2aa4f5d9ff7f86ec5f0dc25
Publikováno v:
ACS Omega, Vol 6, Iss 30, Pp 19983-19994 (2021)
Externí odkaz:
https://doaj.org/article/7da29ff0ab894a20996c30c25f9d7507
Autor:
Siseth Martínez-Caballero, Kiran V. Mahasenan, Choon Kim, Rafael Molina, Rhona Feltzer, Mijoon Lee, Renee Bouley, Dusan Hesek, Jed F. Fisher, Inés G. Muñoz, Mayland Chang, Shahriar Mobashery, Juan A. Hermoso
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 5392-5405 (2021)
The penicillin-binding proteins are the enzyme catalysts of the critical transpeptidation crosslinking polymerization reaction of bacterial peptidoglycan synthesis and the molecular targets of the penicillin antibiotics. Here, we report a combined cr
Externí odkaz:
https://doaj.org/article/0af59740be1241078a1417fa0b394874
Autor:
Martín Alcorlo, David A. Dik, Stefania De Benedetti, Kiran V. Mahasenan, Mijoon Lee, Teresa Domínguez-Gil, Dusan Hesek, Elena Lastochkin, Daniel López, Bill Boggess, Shahriar Mobashery, Juan A. Hermoso
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
SPOR domains are present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. Here, Alcorlo et al. show that, indeed, the presence of peptide stems abrogates binding to a SPOR domain, and provide insight
Externí odkaz:
https://doaj.org/article/120e67d6e4b84738995cb033a43e838a
Publikováno v:
ACS Omega, Vol 6, Iss 30, Pp 19983-19994 (2021)
ACS Omega
ACS Omega
The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is the causative agent of the coronavirus disease of 2019 (COVID-19). Its genome encodes two open reading frames for two large proteins, PP1a and PP1ab. Within the two polypeptide stret
Autor:
Kiran V. Mahasenan, Jeshina Janardhanan, Sara Tejera, Elena Lastochkin, Shahriar Mobashery, Yuanyuan Qian, William R. Wolter, Giuseppe Allegretta, Zhihong Peng, Melissa Malia N. Gozun, Mayland Chang, Rhona Feltzer, Valerie A. Schroeder
Publikováno v:
Journal of Medicinal Chemistry. 63:5287-5296
We report herein the syntheses of 79 derivatives of the 4(3H)-quinazolinones and their structure-activity relationship (SAR) against methicillin-resistant Staphylococcus aureus (MRSA). Twenty one analogs were further evaluated in in vitro assays. Sub
Autor:
Julia Sanz-Aparicio, Mijoon Lee, Kiran V. Mahasenan, María T. Batuecas, Shahriar Mobashery, Choon Kim, Juan A. Hermoso, Jed F. Fisher, Neha Rana, Stefania De Benedetti, Dusan Hesek
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
8 pags., 5 figs.
BglX is a heretofore uncharacterized periplasmic glycoside hydrolase (GH) of the human pathogen Pseudomonas aeruginosa. X-ray analysis identifies it as a protein homodimer. The two active sites of the homodimer comprise catalyti
BglX is a heretofore uncharacterized periplasmic glycoside hydrolase (GH) of the human pathogen Pseudomonas aeruginosa. X-ray analysis identifies it as a protein homodimer. The two active sites of the homodimer comprise catalyti
Autor:
Daniel Lopez, Martín Alcorlo, Elena Lastochkin, Teresa Domínguez-Gil, Kiran V. Mahasenan, David A. Dik, Bill Boggess, Mijoon Lee, Shahriar Mobashery, Dusan Hesek, Stefania De Benedetti, Juan A. Hermoso
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
instname
13 pags., 9 figs. -- Open Access funded by Creative Commons Atribution Licence 4.0
SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is
SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is
Autor:
Kiran V. Mahasenan, Rhona Feltzer, Dusan Hesek, Mijoon Lee, Renee Bouley, Siseth Martínez-Caballero, Choon Kim, Jed F. Fisher, Shahriar Mobashery, Rafael Molina, Juan A. Hermoso, Inés G. Muñoz, Mayland Chang
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 5392-5405 (2021)
instname
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 5392-5405 (2021)
Graphical abstract
Highlights • X-ray crystallography, SAXS and MD simulations elucidates the 3D structure for saPBP1. • 3D structure of saPBP1 reveals dynamical mobility for the pedestal and PASTA domains. • Structures with β-lactams and
Highlights • X-ray crystallography, SAXS and MD simulations elucidates the 3D structure for saPBP1. • 3D structure of saPBP1 reveals dynamical mobility for the pedestal and PASTA domains. • Structures with β-lactams and
Publikováno v:
Acc Chem Res
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
13 pags., 7 figs., 5 schs.-- Published as part of the Accounts of Chemical Research special issue “Bacterial Multi-Drug Resistance”.
ConspectusThe need for new classes of antibacterials is genuine in light of the dearth of clinical options f
ConspectusThe need for new classes of antibacterials is genuine in light of the dearth of clinical options f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63cc18732765b8952ad22dacaa684e3a
https://europepmc.org/articles/PMC8176569/
https://europepmc.org/articles/PMC8176569/