Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Tommaso Cupido"'
Publikováno v:
ARKIVOC, Vol 2005, Iss 6, Pp 191-199 (2005)
Externí odkaz:
https://doaj.org/article/92008e3d96ee43a6bea7a4ee112b8108
Publikováno v:
Nature chemical biology
Spastin is a microtubule-severing AAA (ATPases associated with diverse cellular activities) protein needed for cell division and intracellular vesicle transport. Currently, we lack chemical inhibitors to probe spastin function in such dynamic cellula
Publikováno v:
Nat Struct Mol Biol
The structural conservation across the AAA (ATPases associated with diverse cellular activities) protein family makes designing selective chemical inhibitors challenging. Here, we identify a triazolopyridine-based fragment that binds the AAA domain o
Publikováno v:
Cell Chem Biol
Summary Drug-like inhibitors are often designed by mimicking cofactor or substrate interactions with enzymes. However, as active sites are comprised of conserved residues, it is difficult to identify the critical interactions needed to design selecti
The bump-hole approach is a powerful chemical biology strategy to specifically probe the functions of closely related proteins. However, for many protein families, such as the ATPases associated with diverse cellular activities (AAA), we lack structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78cec0fb780905f70bbacdfff913d43b
https://europepmc.org/articles/PMC6637947/
https://europepmc.org/articles/PMC6637947/
Publikováno v:
SSRN Electronic Journal.
Drug-like inhibitors are often designed by mimicking cofactor or substrate interactions with enzymes. However, as active sites are comprised of conserved residues, it is difficult to identify the critical interactions needed to design selective inhib
Autor:
Ruta Zalyte, Maxence V. Nachury, Andrew P. Carter, Rand M. Miller, Fan Ye, Tommaso Cupido, Jonathan B. Steinman, Andrew H. Chung, Tarun M. Kapoor, Sascha Hoogendoorn, Stephanie K. See, Tomoyo Sakata-Kato, James K. Chen
Publikováno v:
See, SK; Hoogendoorn, S; Chung, AH; Ye, F; Steinman, JB; Sakata-Kato, T; et al.(2016). Cytoplasmic Dynein Antagonists with Improved Potency and Isoform Selectivity. ACS CHEMICAL BIOLOGY, 11(1), 53-60. doi: 10.1021/acschembio.5b00895. UCSF: Retrieved from: http://www.escholarship.org/uc/item/3tn1x71x
ACS Chemical Biology
ACS Chemical Biology
Cytoplasmic dyneins 1 and 2 are related members of the AAA+ superfamily (ATPases associated with diverse cellular activities) that function as the predominant minus-end-directed microtubule motors in eukaryotic cells. Dynein 1 controls mitotic spindl
Autor:
Javier Ruiz-Rodríguez, Jaume Adan, Jaume Piulats, Fernando Albericio, Jan Spengler, Tommaso Cupido, Francesc Mitjans
Publikováno v:
Angewandte Chemie. 122:2792-2797
Natural or designed peptide ligands rarely bind to cognate receptors in their most stable conformation when in solution. The receptor, through reciprocal induced fitting, applies pressure on the conformational ensemble of the peptide to select its co
Autor:
Tommaso Cupido, Paul G. Rack, Ari J. Firestone, Joel M. Hyman, Kyuho Han, Surajit Sinha, Cory A. Ocasio, James K. Chen
Publikováno v:
Angewandte Chemie. 121:2357-2360
Autor:
Surajit Sinha, Joel M. Hyman, Ari J. Firestone, James K. Chen, Kyuho Han, Cory A. Ocasio, Paul G. Rack, Tommaso Cupido
Publikováno v:
Angewandte Chemie International Edition. 48:2321-2324
Eradicating hedgehogs: The title molecule has been previously identified as a potent inhibitor of the Hedgehog signaling pathway, which gives embryonic cells information needed to develop properly. This molecule is shown to modulate Hedgehog target g