Zobrazeno 1 - 10
of 72
pro vyhledávání: '"W.T. Lowther"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
Biochemistry. 47:2439-2449
The human liver enzyme glycolate oxidase (GO1), also known as the HAOX1 gene product, is a member of the well-characterized FMN-dependent α-hydroxy acid oxidase enzyme family (1, 2). This family includes Pseudomonas putida mandelate dehydrogenase (M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaf7d3661c7178fd438c20f93f72c970
https://doi.org/10.1021/bi701710r
https://doi.org/10.1021/bi701710r
Publikováno v:
Biochemistry. 44:8634-8642
Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. The reduction of the cysteine sulfinic acid moiety within the active site of the Prx by Srx involves nove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77d2842b75dc8590258946d0b47e9c40
https://doi.org/10.1021/bi050131i
https://doi.org/10.1021/bi050131i
Publikováno v:
Biochemistry. 39:13307-13312
Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to both free methionine and methionine within proteins. As such, it helps protect the host organism against stochastic damage that can contribute to cell death. The structure of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eeced11800c0fe6c10d78177287ae2d
https://doi.org/10.1021/bi0020269
https://doi.org/10.1021/bi0020269
Publikováno v:
Biochemistry. 38:14810-14819
In an effort to differentiate between alternative mechanistic schemes that have been postulated for Escherichia coli methionine aminopeptidase (eMetAP), the modes of binding of a series of products and phosphorus-based transition-state analogues were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b43c8c3460ac09e2006304a56c915835
https://doi.org/10.1021/bi991711g
https://doi.org/10.1021/bi991711g
Publikováno v:
Biochemistry. 38:7678-7688
By improving the expression and purification of Escherichia coli methionine aminopeptidase (eMetAP) and using slightly different crystallization conditions, the resolution of the parent structure was extended from 2.4 to 1.9 A resolution. This has pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d39c65f6b58d2c6a26bb6e7346d070d
https://doi.org/10.1021/bi990684r
https://doi.org/10.1021/bi990684r
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12153-12157
Methionine aminopeptidase (MetAP) exists in two forms (type I and type II), both of which remove the N-terminal methionine from proteins. It previously has been shown that the type II enzyme is the molecular target of fumagillin and ovalicin, two epo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0e7c9402eb50ca7b83d458d7fb5567c
https://doi.org/10.1073/pnas.95.21.12153
https://doi.org/10.1073/pnas.95.21.12153
Autor:
W.T. Lowther, Ben M. Dunn, Jonathan B. Cooper, Elizabeth A. Lunney, SI Foundling, Christine Humblet, Tom L. Blundell, Carlos Frazão, W Quail
Publikováno v:
Biochemistry. 31:8142-8150
The crystal structures of endothiapepsin, a fungal aspartic proteinase (EC 3.4.23.6), cocrystallized with two oligopeptide renin inhibitors, PD125967 and PD125754, have been determined at 2.0-A resolution and refined to R-factors of 0.143 and 0.153,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c299d33b399543c4d14d0edda5c44f3
https://doi.org/10.1021/bi00150a005
https://doi.org/10.1021/bi00150a005
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.