Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Autor: Dong, YY, Wang, H, Pike, ACW, Cochrane, SA, Hamedzadeh, S, Wyszyński, FJ, Bushell, SR, Royer, SF, Widdick, DA, Sajid, A, Boshoff, HI, Park, Y, Lucas, R, Liu, W-M, Lee, SS, Machida, T, Minall, L, Mehmood, S, Belaya, K, Liu, W-W, Chu, A, Shrestha, L, Mukhopadhyay, SMM, Strain-Damerell, C, Chalk, R, Burgess-Brown, NA, Bibb, MJ, Barry, CE, Robinson, CV, Beeson, D, Davis, BG, Carpenter, EP

Publikováno v: Cell
Dong, Y Y, Wang, H, Pike, A C W, Cochrane, S A, Hamedzadeh, S, Wyszynski, F, Bushell, S, Royer, S F, Widdick, D A, Sajid, A, Boshoff, H I, Park, Y, Lucas, R, Liu, W-M, Lee, S S, Machida, T, Minall, L, Mehmood, S, Belaya, K, Liu, W-W, Chu, A, Shrestha, L, Mukhopadhyay, S M M, Strain-Damerell, C, Chalk, R, Burgess-Brown, N A, Bibb, M, Barry 3rd, C, Robinson, C, Beeson, D, Davis, B & Carpenter, E P 2018, ' Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design ', Cell, vol. 175, pp. 1045-1058 . https://doi.org/10.1016/j.cell.2018.10.037

Summary Protein N-glycosylation is a widespread post-translational modification. The first committed step in this process is catalysed by dolichyl-phosphate N-acetylglucosamine-phosphotransferase DPAGT1 (GPT/E.C. 2.7.8.15). Missense DPAGT1 variants c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::6d9917953453a97d263ef06d74a47569
https://ora.ox.ac.uk/objects/uuid:515d9416-1e72-4e91-87e4-39eb4f426368

Fragment-Sized EthR Inhibitors Exhibit Exceptionally Strong Ethionamide Boosting Effect in Whole-Cell $\textit{Mycobacterium tuberculosis}$ Assays

Autor: Nikiforov, PO, Blaszczyk, M, Surade, S, Boshoff, HI, Sajid, A, Delorme, V, Deboosere, N, Brodin, P, Baulard, AR, Barry, CE, Blundell, TL, Abell, C

Small-molecule inhibitors of the mycobacterial transcriptional repressor EthR have previously been shown to act as boosters of the second-line antituberculosis drug ethionamide. Fragment-based drug discovery approaches have been used in the past to m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ee35687cd78a2fe6a063946be294534

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Inhibition of DXR in the MEP pathway with lipophilic N -alkoxyaryl FR900098 analogs.

Autor: Bague D; Department of Chemistry, George Washington University Washington D.C. 20052 USA cdowd@gwu.edu., Wang R; Department of Chemistry, George Washington University Washington D.C. 20052 USA cdowd@gwu.edu., Hodge D; Division of Infectious Diseases, Children's Hospital of Philadelphia Philadelphia PA 19104 USA., Mikati MO; Department of Molecular Microbiology, Washington University School of Medicine St. Louis MO 63110 USA., Roma JS; Tuberculosis Research Section, LCIM, NIAID/NIH Bethesda MD 20892 USA., Boshoff HI; Tuberculosis Research Section, LCIM, NIAID/NIH Bethesda MD 20892 USA., Dailey AL; Department of Chemistry and Biochemistry, George Mason University Fairfax VA 22030 USA., Girma M; Department of Chemistry and Biochemistry, George Mason University Fairfax VA 22030 USA., Couch RD; Department of Chemistry and Biochemistry, George Mason University Fairfax VA 22030 USA., Odom John AR; Division of Infectious Diseases, Children's Hospital of Philadelphia Philadelphia PA 19104 USA.; Department of Molecular Microbiology, Washington University School of Medicine St. Louis MO 63110 USA., Dowd CS; Department of Chemistry, George Washington University Washington D.C. 20052 USA cdowd@gwu.edu.

Publikováno v: RSC medicinal chemistry [RSC Med Chem] 2024 May 22; Vol. 15 (7), pp. 2422-2439. Date of Electronic Publication: 2024 May 22 (Print Publication: 2024).