Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ana R. Calixto"'
Publikováno v:
QRB Discovery, Vol 5 (2024)
Protein tyrosine phosphatases (PTPs) are crucial regulators of cellular signaling. Their activity is regulated by the motion of a conserved loop, the WPD-loop, from a catalytically inactive open to a catalytically active closed conformation. WPD-loop
Externí odkaz:
https://doaj.org/article/32a8f2bafca546caae7c24425fd85836
Autor:
Ruidan Shen, Rory M. Crean, Keith J. Olsen, Marina Corbella, Ana R. Calixto, Teisha Richan, Tiago A. S. Brandão, Ryan D. Berry, Alex Tolman, J. Patrick Loria, Sean J. Johnson, Shina C. L. Kamerlin, Alvan C. Hengge
Publikováno v:
Chemical Science. 13:13524-13540
Protein tyrosine phosphatases (PTPs) possess a conserved mobile catalytic loop, the WPD-loop, which brings an aspartic acid into the active site where it acts as an acid/base catalyst. Prior experimental and computational studies, focused on the huma
Autor:
Rory M. Crean, Michal Biler, Marina Corbella, Ana R. Calixto, Marc W. van der Kamp, Alvan C. Hengge, Shina C. L. Kamerlin
Publikováno v:
Journal of the American Chemical Society. 144:10091-10093
Autor:
Pedro Ferreira, Pedro A. Fernandes, Ana R. Calixto, Maria J. Ramos, Carmay Lim, Sérgio F. Sousa
Publikováno v:
ACS Catalysis. 10:8444-8453
Enzymes are responsible for controlling many biological processes, catalyzing different reactions using substrates with diverse complexity, size, and chemistry. How enzymes work and achieve their catalytic efficiency are some of the fundamental quest
Publikováno v:
ACS Omega, Vol 5, Iss 9, Pp 4380-4385 (2020)
ACS Omega
ACS Omega
GTP hydrolysis is central to biology, being involved in regulating a wide range of cellular processes. However, the mechanisms by which GTPases hydrolyze this critical reaction remain controversial, with multiple mechanistic possibilities having been
Publikováno v:
Biochemical Society Transactions
Structural and biochemical studies on diverse enzymes have highlighted the importance of ligand-gated conformational changes in enzyme catalysis, where the intrinsic binding energy of the common phosphoryl group of their substrates is used to drive e
Publikováno v:
Chemical Science
One enzyme, one substrate, but two different reaction mechanisms: HIV-1 protease follows different reaction mechanisms depending on its instantaneous conformation.
The role of conformational diversity in enzyme catalysis has been a matter of ana
The role of conformational diversity in enzyme catalysis has been a matter of ana
Publikováno v:
ACS Catalysis. 8:4055-4063
The subset of catalytically competent conformations can be significantly small in comparison with the full conformational landscape of enzyme–substrate complexes. In some enzymes, the probability of finding a reactive conformation can account for u
Autor:
Carsten Kötting, Cátia Moreira, Klaus Gerwert, Ana R. Calixto, Shina Caroline Lynn Kamerlin, Till Rudack, Anna Pabis
Publikováno v:
Journal of the American Chemical Society. 141(27)
GTP hydrolysis is a biologically crucial reaction, being involved in regulating almost all cellular processes. As a result, the enzymes that catalyze this reaction are among the most important drug targets. Despite their vital importance and decades
Autor:
Wael E. Houssen, Marcel Jaspars, Pedro A. Fernandes, James H. Naismith, Maria J. Ramos, Pedro Ferreira, Ana R. Calixto, Natércia F. Brás
Publikováno v:
Chemistry – A European Journal. 27:3569-3569