Zobrazeno 1 - 10
of 543
pro vyhledávání: '"enzyme–substrate complex"'
Publikováno v:
IUCrJ, Vol 8, Iss 6, Pp 973-979 (2021)
SARS-CoV-2 emerged at the end of 2019 to cause an unprecedented pandemic of the deadly respiratory disease COVID-19 that continues to date. The viral main protease (Mpro) is essential for SARS-CoV-2 replication and is therefore an important drug targ
Externí odkaz:
https://doaj.org/article/53704c447e1746098f45e3c77c49f7ca
Autor:
Vega Miguel-Ruano, Ivanna Rivera, Jelena Rajkovic, Kamila Knapik, Ana Torrado, José Manuel Otero, Elisa Beneventi, Manuel Becerra, Mercedes Sánchez-Costa, Aurelio Hidalgo, José Berenguer, María-Isabel González-Siso, Jacobo Cruces, María L. Rúa, Juan A. Hermoso
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 1214-1232 (2021)
A novel esterase, EstD11, has been discovered in a hot spring metagenomic library. It is a thermophilic and thermostable esterase with an optimum temperature of 60°C. A detailed substrate preference analysis of EstD11 was done using a library of chr
Externí odkaz:
https://doaj.org/article/e0e968e378104a6e9475a7f546816be6
Autor:
Jone Paesmans, Ella Martin, Babette Deckers, Marjolijn Berghmans, Ritika Sethi, Yannick Loeys, Els Pardon, Jan Steyaert, Patrik Verstreken, Christian Galicia, Wim Versées
Publikováno v:
eLife, Vol 9 (2020)
Synaptojanin1 (Synj1) is a phosphoinositide phosphatase, important in clathrin uncoating during endocytosis of presynaptic vesicles. It was identified as a potential drug target for Alzheimer’s disease, Down syndrome, and TBC1D24-associated epileps
Externí odkaz:
https://doaj.org/article/7af11ac4f55145eba6933fc35aa0a442
Akademický článek
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Publikováno v:
IUCrJ, Vol 8, Iss 6, Pp 973-979 (2021)
IUCrJ
IUCrJ
Understanding the catalytic mechanism of SARS-CoV-2 main protease (Mpro) can help in guiding drug design of specific small-molecule antivirals. A 2.0 Å resolution room-temperature X-ray crystal structure of inactive C145A mutant Mpro in complex with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bcbe27bc197b3c173fd9644f287a292
http://scripts.iucr.org/cgi-bin/paper?S2052252521010113
http://scripts.iucr.org/cgi-bin/paper?S2052252521010113
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 3, p e1004811 (2016)
PLoS Computational Biology
PLoS Computational Biology
Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step in the diaminopimelate pathway of bacteria, yielding amino acids required for cell wall and protein biosyntheses. The essentiality of the enzyme to bacteria, coupled with its abs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d8a23a2a0a6000afb8184439de56acd
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
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Publikováno v:
Microbiology Insights
CenA is an endoglucanase secreted by the Gram-positive cellulolytic bacterium, Cellulomonas fimi, to the environment as a glycosylated protein. The role of glycosylation in CenA is unclear. However, it seems not crucial for functional activity and se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f83a1415dc8de384845ac1bf77effd81
http://europepmc.org/articles/PMC8209791
http://europepmc.org/articles/PMC8209791
Autor:
Jelena Rajkovic, Juan A. Hermoso, José Berenguer, Elisa Beneventi, Mercedes Sánchez-Costa, Aurelio Hidalgo, Jacobo Cruces, María-Isabel González-Siso, Ana Torrado, Ivanna Rivera, Vega Miguel-Ruano, María L. Rúa, Kamila Knapik, Manuel Becerra, José M. Otero
Publikováno v:
Investigo. Repositorio Institucional de la Universidade de Vigo
Universidade de Vigo (UVigo)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
RUC. Repositorio da Universidade da Coruña
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1214-1232 (2021)
Computational and Structural Biotechnology Journal
RUC: Repositorio da Universidade da Coruña
Universidade da Coruña (UDC)
Universidade de Vigo (UVigo)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
RUC. Repositorio da Universidade da Coruña
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1214-1232 (2021)
Computational and Structural Biotechnology Journal
RUC: Repositorio da Universidade da Coruña
Universidade da Coruña (UDC)
Graphical abstract
Highlights • A novel thermophilic esterase discovered from hot-spring metagenomic library. • EstD11 shows broad substrate specificity including substrates of industrial interest. • Atomic resolution crystallographic comp
Highlights • A novel thermophilic esterase discovered from hot-spring metagenomic library. • EstD11 shows broad substrate specificity including substrates of industrial interest. • Atomic resolution crystallographic comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5cb848bc105fe00f6966a667d7b1477
https://linkinghub.elsevier.com/retrieve/pii/S2001037021000519
https://linkinghub.elsevier.com/retrieve/pii/S2001037021000519
Autor:
Carol Robinson, Tika R. Malla, Ioannis Vakonakis, Victor A. Mikhailov, Nicole Zitzmann, Tarick J. El-Baba, Anastassia L. Kantsadi, Christopher J. Schofield, Jani Reddy Bolla, Corinne A. Lutomski, Tobias John
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie
Angewandte Chemie (International Ed. in English)
Angewandte Chemie
The SARS‐CoV‐2 main protease (Mpro) cleaves along the two viral polypeptides to release non‐structural proteins required for viral replication MPro is an attractive target for antiviral therapies to combat the coronavirus‐2019 disease Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b5fae261782a82f4fea78221895ff64