Zobrazeno 1 - 10
of 76
pro vyhledávání: '"David A R Sanders"'
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e85735 (2014)
Deletion or repression of Aspergillus nidulans ugmA (AnugmA), involved in galactofuranose biosynthesis, impairs growth and increases sensitivity to Caspofungin, a β-1,3-glucan synthesis antagonist. The A. fumigatus UgmA (AfUgmA) crystal structure ha
Externí odkaz:
https://doaj.org/article/092ab9391e294d87a7d07a3db932d2e2
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e76803 (2013)
The frequency of invasive fungal infections has rapidly increased in recent years. Current clinical treatments are experiencing decreased potency due to severe host toxicity and the emergence of fungal drug resistance. As such, new targets and their
Externí odkaz:
https://doaj.org/article/4660968a854049678ad7556ac5b18a36
Publikováno v:
Pharmaceuticals, Vol 15, Iss 2, p 197 (2022)
UDP-galactopyranose mutase (UGM) is an essential enzyme involved in the bacterial cell wall synthesis, and is not present in mammalian cells. Thus, UGM from Mycobacterium tuberculosis (Mtb) represents a novel and attractive drug target for developing
Externí odkaz:
https://doaj.org/article/ed15a3e25e424bc09d3063742b997473
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867:426-433
The thioredoxin system is a ubiquitous oxidoreductase system that consists of the enzyme thioredoxin reductase (TrxR), its cofactor nicotinamide adenine dinucleotide phosphate (NAD(P)H) and the protein thioredoxin (Trx). The system has been comprehen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34dd1811753dafccdd7c2f58c144693
https://doi.org/10.1016/j.bbapap.2019.01.011
https://doi.org/10.1016/j.bbapap.2019.01.011
Publikováno v:
Journal of Structural Biology. 213:107744
Kanosamine is an antibiotic and antifungal monosaccharide. The kanosamine biosynthetic pathway from glucose 6-phosphate in Bacillus cereus UW85 was recently reported, and the functions of each of the three enzymes in the pathway, KabA, KabB and KabC,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bde816f0c3bb83202da0e111394fe5a1
https://doi.org/10.1016/j.jsb.2021.107744
https://doi.org/10.1016/j.jsb.2021.107744
Autor:
B. Mario Pinto, Karin E. van Straaten, Cinzia Colombo, Sankar Mohan, Yun Shi, Jijin R. A. Kuttiyatveetil, David A. R. Sanders, Nataliya Zalatar
Publikováno v:
ChemBioChem. 17:2264-2273
UDP-galactopyranose mutase (UGM), a key enzyme in the biosynthesis of mycobacterial cell walls, is a potential target for the treatment of tuberculosis. In this work, we investigate binding models of a non-substrate-like inhibitor, MS-208, with M. tu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a99895bfc25e883e032f180d7e074c8c
https://doi.org/10.1002/cbic.201600469
https://doi.org/10.1002/cbic.201600469
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 72:443-447
Thioredoxin is a small ubiquitous protein that plays a role in many biological processes. A putative thioredoxin, Trx1, fromThermosipho africanusstrain TCF52B, which has low sequence identity to its closest homologues, was successfully cloned, overex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef244cccb050939e036ab2c870d03353
https://doi.org/10.1107/s2053230x16007214
https://doi.org/10.1107/s2053230x16007214
Autor:
Sagar Saran, David A. R. Sanders
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 76:a186-a186
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53a3640a206a1c0f77b78a099c3cfe76
https://doi.org/10.1107/s0108767320098153
https://doi.org/10.1107/s0108767320098153
Autor:
Brian A.A. Novakovski, Julien J. H. Cotelesage, Hughes Goldie, Aaron White, AkosiereremS. Sokaribo, David A. R. Sanders
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1864:129517
Background Phosphoenolpyruvate carboxykinase (PEPCK) is a metabolic enzyme in the gluconeogenesis pathway, where it catalyzes the reversible conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) and CO2. The substrates for Escherichia coli PE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::372df218bcf40ba41e7dbefbef13f01a
https://doi.org/10.1016/j.bbagen.2020.129517
https://doi.org/10.1016/j.bbagen.2020.129517
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1866(11)
Many bacteria can use myo-inositol as the sole carbon source using enzymes encoded in the iol operon. The first step is catalyzed by the well-characterized myo-inositol dehydrogenase (mIDH), which oxidizes the axial hydroxyl group of the substrate to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f24ef95d7e14522c2f2223452bc79031
https://pubmed.ncbi.nlm.nih.gov/30282609
https://pubmed.ncbi.nlm.nih.gov/30282609