Zobrazeno 1 - 10
of 903
pro vyhledávání: '"Morkos A"'
Autor:
Ju-Sim Kim, Alexandra Born, James Karl A. Till, Lin Liu, Sashi Kant, Morkos A. Henen, Beat Vögeli, Andrés Vázquez-Torres
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The response regulator SsrB, a master activator of the Salmonella pathogenicity island-2 gene cluster, is under allosteric control of thioredoxin. Authors utilise in vitro and in vivo models to investigate if other members of the response regulator f
Externí odkaz:
https://doaj.org/article/0efe26c693194b90b5cbf85edd28c641
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-17 (2022)
Abstract Design and synthesis of a new series of benzofuran derivatives has been performed. 1H-NMR, 13C-NMR, elemental analysis, and IR were used to confirm the structures of the produced compounds. Hepatocellular carcinoma (HePG2), mammary gland bre
Externí odkaz:
https://doaj.org/article/0ccd84446f5c44658b65cf0892f12866
Autor:
Alexandra Born, Janne Soetbeer, Morkos A. Henen, Frauke Breitgoff, Yevhen Polyhach, Gunnar Jeschke, Beat Vögeli
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-9 (2022)
Born et al. describe interdomain allostery in the two domain peptidyl-prolyl isomerase Pin1 upon binding of two ligands. These ligands couple population shifts of extended and compact states to changes in the catalytic site of Pin1.
Externí odkaz:
https://doaj.org/article/9444f470131e41d4b1a5ac4920e3a5e4
On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins
Publikováno v:
Magnetic Resonance Letters, Vol 2, Iss 2, Pp 61-68 (2022)
Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic fie
Externí odkaz:
https://doaj.org/article/a53558b5d6784be7aae1350403da9d49
Publikováno v:
Magnetochemistry, Vol 9, Iss 7, p 166 (2023)
Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adap
Externí odkaz:
https://doaj.org/article/ea0e34622404486887191c50a7925d88
Publikováno v:
Molecules, Vol 28, Iss 2, p 843 (2023)
Despite structural differences between the right-handed conformations of A-RNA and B-DNA, both nucleic acids adopt very similar, left-handed Z-conformations. In contrast to their structural similarities and sequence preferences, RNA and DNA exhibit d
Externí odkaz:
https://doaj.org/article/43bf6fe3323f483abeee199be5a8d287
Publikováno v:
Molecules, Vol 27, Iss 16, p 5245 (2022)
Benzimidazole derivatives are known to be key players in the development of novel anticancer agents. Herein, we aimed to synthesize novel derivatives to target breast cancer. A new series of benzimidazole derivatives conjugated with either six- and f
Externí odkaz:
https://doaj.org/article/b39a7f4c0b404df59bccf25bed53809b
Publikováno v:
Gut Microbes, Vol 13, Iss 1 (2021)
The gut microbiota is essential for human health. Microbial supply of short-chain fatty acids (SCFAs), particularly butyrate, is a well-established contributor to gut homeostasis and disease resistance. Reaching millimolar luminal concentrations, but
Externí odkaz:
https://doaj.org/article/22fe9f5cc6314661806c1bdaa0f12f49
Autor:
Ricardo Celestino, Morkos A Henen, José B Gama, Cátia Carvalho, Maxwell McCabe, Daniel J Barbosa, Alexandra Born, Parker J Nichols, Ana X Carvalho, Reto Gassmann, Beat Vögeli
Publikováno v:
PLoS Biology, Vol 17, Iss 1, p e3000100 (2019)
All animal cells use the motor cytoplasmic dynein 1 (dynein) to transport diverse cargo toward microtubule minus ends and to organize and position microtubule arrays such as the mitotic spindle. Cargo-specific adaptors engage with dynein to recruit a
Externí odkaz:
https://doaj.org/article/1692fc10ac154afba4ba231eaae5b7bb
Publikováno v:
Magnetochemistry, Vol 4, Iss 2, p 25 (2018)
We present a strategy for stereospecific NMR assignment of Hβ2 and Hβ3 protons in mid-size proteins (~150 residues). For such proteins, resonance overlap in standard experiments is severe, thereby preventing unambiguous assignment of a large fracti
Externí odkaz:
https://doaj.org/article/39f58d7826f94c4c96fada9f6f6dccec