Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Vincenzo Venditti"'
Publikováno v:
PLoS Computational Biology, Vol 19, Iss 10, p e1011545 (2023)
TRPV Ion channels are sophisticated molecular sensors designed to respond to distinct temperature thresholds. The recent surge in cryo-EM structures has provided numerous insights into the structural rearrangements accompanying their opening and clos
Externí odkaz:
https://doaj.org/article/4e53378dcd544e9c95c81b44a0d0bd5c
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/e7d18d5bbc8f4bd3b992078607d9ab24
Autor:
Aayushi Singh, Daniel Burns, Sergey L. Sedinkin, Brett Van Veller, Davit A. Potoyan, Vincenzo Venditti
Publikováno v:
Biomolecules, Vol 13, Iss 1, p 160 (2023)
Substrate selectivity is an important preventive measure to decrease the possibility of cross interactions between enzymes and metabolites that share structural similarities. In addition, understanding the mechanisms that determine selectivity toward
Externí odkaz:
https://doaj.org/article/49396d0ab19347ffa19719b0e308d030
Autor:
Jeffrey A. Purslow, Jolene N. Thimmesch, Valeria Sivo, Trang T. Nguyen, Balabhadra Khatiwada, Rochelle R. Dotas, Vincenzo Venditti
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Enzyme I (EI) of the bacterial phosphotransferase system (PTS) is a master regulator of bacterial metabolism and a promising target for development of a new class of broad-spectrum antibiotics. The catalytic activity of EI is mediated by several intr
Externí odkaz:
https://doaj.org/article/afd92738c1f648a1b8c9afc8cf617b6f
An allosteric pocket for inhibition of bacterial Enzyme I identified by NMR-based fragment screening
Autor:
Trang T. Nguyen, Vincenzo Venditti
Publikováno v:
Journal of Structural Biology: X, Vol 4, Iss , Pp 100034- (2020)
Enzyme I (EI), which is the key enzyme to activate the bacterial phosphotransferase system, plays an important role in the regulation of several metabolic pathways and controls the biology of bacterial cells at multiple levels. The conservation and u
Externí odkaz:
https://doaj.org/article/eea6b0f5ca6e4ad4b37ba133962800b1
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Protein-protein interactions and the complexes thus formed are critical elements in a wide variety of cellular events that require an atomic-level description to understand them in detail. Such complexes typically constitute challenging systems to ch
Externí odkaz:
https://doaj.org/article/ea39d389ca774652800f04e4387f60a1
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
Developing sustainable and scalable nanocrystal syntheses is challenging but necessary for future technologies and the environment. Here, the authors show that using an ionic liquid to stabilize a highly reactive precursor can fulfill the major aims
Externí odkaz:
https://doaj.org/article/e1d783f265f1440aabc9c7c9c6004947
Autor:
Thomas Evangelidis, Santrupti Nerli, Jiří Nováček, Andrew E. Brereton, P. Andrew Karplus, Rochelle R. Dotas, Vincenzo Venditti, Nikolaos G. Sgourakis, Konstantinos Tripsianes
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Further automation of NMR structure determination is needed to increase the throughput and accessibility of this method. Here the authors present 4D-CHAINS/autoNOE-Rosetta, a complete pipeline that allows rapid and fully automated structure determina
Externí odkaz:
https://doaj.org/article/da44ac29a8c6451eba4c6afcde1322d3
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Homologous enzymes with identical folds often exhibit different thermal and kinetic behaviors. Understanding how enzyme sequence encodes catalytic activity at functionally optimal temperatures is a fundamental problem in biophysics. Recently it was s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c0358bc55bd0c090ebaa55f38598c49
https://doi.org/10.1073/pnas.2210537119
https://doi.org/10.1073/pnas.2210537119
Autor:
Igor I. Slowing, Pranjali Naik, Vincenzo Venditti, Daniel J. Freppon, Yeongseo An, Sergey L. Sedinkin, Hayley Masching, Emily A. Smith
Publikováno v:
ACS Catalysis. 11:10553-10564
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::103505fd1eba67da3fb65fe7ef6b7607
https://doi.org/10.1021/acscatal.1c02716
https://doi.org/10.1021/acscatal.1c02716