C
Chiara Bruckmann
Researcher at University of Edinburgh
Publications - 10
Citations - 431
Chiara Bruckmann is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Active site & Medicine. The author has an hindex of 5, co-authored 7 publications receiving 406 citations.
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Journal ArticleDOI
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
Farhad Forouhar,J. L. Ross Anderson,Christopher G. Mowat,Sergey M. Vorobiev,A. Hussain,Mariam Abashidze,Chiara Bruckmann,Sarah J. Thackray,Jayaraman Seetharaman,Todd Tucker,Rong Xiao,Li Chung Ma,Li Zhao,Thomas Acton,Gaetano T. Montelione,Stephen K Chapman,Liang Tong +16 more
TL;DR: In this paper, structural and biochemical studies of the Xanthomonas campestris TDO and a related protein SO4414 from Shewanella oneidensis were performed.
Journal ArticleDOI
Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
Vinit M. Supekar,Chiara Bruckmann,Paolo Ingallinella,Elisabetta Bianchi,Antonello Pessi,Andrea Carfi +5 more
TL;DR: The structures presented here can open the path to the design of small-molecule inhibitors of viral entry and candidate vaccine antigens against this virus.
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Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus
Paolo Ingallinella,Elisabetta Bianchi,Marco Finotto,Giovanna Cantoni,Debra M. Eckert,Vinit M. Supekar,Chiara Bruckmann,Andrea Carfi,Antonello Pessi +8 more
TL;DR: HR1 and HR2 of SARS-CoV associate into an antiparallel six-helix bundle, with structural features typical of the other known class I fusion proteins, and inhibitors binding to HR regions of fusion proteins have been shown to be efficacious against many viruses, notably HIV.
Journal ArticleDOI
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.
Sarah J. Thackray,Chiara Bruckmann,J.L.R. Anderson,L.P. Campbell,Rong Xiao,Li Zhao,Christopher G. Mowat,Farhad Forouhar,Liang Tong,Stephen K Chapman +9 more
TL;DR: Structural data reveal that histidine 55 is not essential for turnover but greatly disfavors the mechanistically unproductive binding of l-Trp to the oxidized enzyme allowing control of catalysis.
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Oxygen activation in neuronal NO synthase: resolving the consecutive mono-oxygenation steps.
TL;DR: The G586S mutant of nNOS (neuronal NOS), which introduces an additional hydrogen bond in the active site and provides an additional proton source, suggests that the two reaction steps of NO production follow different chemical mechanisms.