Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Timothy R. Stachowski"'
Publikováno v:
IUCrJ, Vol 7, Iss 2, Pp 238-252 (2020)
Transforming growth factor β-1 (TGFβ-1) is a secreted signalling protein that directs many cellular processes and is an attractive target for the treatment of several diseases. The primary endogenous activity regulatory mechanism for TGFβ-1 is seq
Externí odkaz:
https://doaj.org/article/69422d07dfa046da8581ea5d100be7ce
Autor:
Timothy R. Stachowski, Marcus Fischer
Publikováno v:
Acta Crystallographica Section D Structural Biology. 79:354-367
Protein conformational dynamics that may inform biology often lie dormant in high-resolution electron-density maps. While an estimated ∼18% of side chains in high-resolution models contain alternative conformations, these are underrepresented in cu
Autor:
Timothy R. Stachowski, Stanley Nithianantham, Murugendra Vanarotti, Karlo Lopez, Marcus Fischer
Publikováno v:
Protein Science. 32
Autor:
Mladen Koravovic, Anand Mayasundari, Gordana Tasic, Fatemeh Keramatnia, Timothy R. Stachowski, Huarui Cui, Sergio C. Chai, Barbara Jonchere, Lei Yang, Yong Li, Xiang Fu, Ryan Hiltenbrand, Leena Paul, Vibhor Mishra, Jeffery M. Klco, Martine F. Roussel, William CK. Pomerantz, Marcus Fischer, Zoran Rankovic, Vladimir Savic
Publikováno v:
European Journal of Medicinal Chemistry
An X-ray structure of a CLICK chemistry-based BET PROTAC bound to BRD2(BD2) inspired synthesis of JQ1 derived heterocyclic amides. This effort led to the discovery of potent BET inhibitors displaying overall improved profiles when compared to JQ1 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5648b26b4c7d2361e3341b7c58a3cd9
https://farfar.pharmacy.bg.ac.rs/handle/123456789/4513
https://farfar.pharmacy.bg.ac.rs/handle/123456789/4513
Publikováno v:
Journal of Synchrotron Radiation
A system engineered to produce a large-scale structural change from X-ray-induced disulfide bond cleavage allows residue-specific changes to be interpreted with SAXS. This system is used to investigate how radical scavengers reduce bond breakage du
Autor:
Timothy R. Stachowski, Murugendra Vanarotti, Jayaraman Seetharaman, Karlo Lopez, Marcus Fischer
Publikováno v:
Angewandte Chemie. 134
Autor:
Timothy R. Stachowski, Murugendra Vanarotti, Jayaraman Seetharaman, Karlo Lopez, Marcus Fischer
Publikováno v:
Angewandte Chemie International Edition. 61
High-resolution crystal structures highlight the importance of water networks in protein-ligand interactions. However, as these are typically determined at cryogenic temperature, resulting insights may be structurally precise but not biologically acc
Publikováno v:
J Synchrotron Radiat
Dissociation of transforming growth factor beta-1 (TGFβ-1) from the inhibitory protein latency-associated peptide (LAP) can occur from low doses of X-ray irradiation of the LAP–TGFβ-1 complex, resulting in the activation of TGFβ-1, and can have
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:C204-C204
Publikováno v:
IUCrJ
IUCrJ, Vol 7, Iss 2, Pp 238-252 (2020)
IUCrJ, Vol 7, Iss 2, Pp 238-252 (2020)
Analysis of crystallographic, solution scattering and biochemical experiments suggests a mechanism for the sequestration of transforming growth factor β-1 by latency-associated peptide (LAP) that includes a structural change in LAP from an open to a