Brian L. Mark, Ph.D.
Institution:
University of Alberta (Canada)Area:
protein crystallographyGoogle:
"Brian Mark"Mean distance: 9.3 | S | N | B | C | P |
Parents
Sign in to add mentorMichael N.G. James | grad student | 2003 | University of Alberta (Canada) | |
(X-ray crystallographic studies of human and bacterial beta-hexosaminidase: Understanding the molecular basis of Tay -Sachs and Sandhoff disease.) |
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Publications
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Slater CL, Winogrodzki J, Fraile-Ribot PA, et al. (2020) Adding insult to injury: mechanistic basis for how AmpC mutations allow to accelerate cephalosporin hydrolysis and evade avibactam. Antimicrobial Agents and Chemotherapy |
Tchesnokov EP, Bailey-Elkin BA, Mark BL, et al. (2020) Independent inhibition of the polymerase and deubiquitinase activities of the Crimean-Congo Hemorrhagic Fever Virus full-length L-protein. Plos Neglected Tropical Diseases. 14: e0008283 |
Mangat CS, Vadlamani G, Holicek V, et al. (2019) Molecular basis for the potent inhibition of the emerging carbapenemase VCC-1 by avibactam. Antimicrobial Agents and Chemotherapy |
Ho LA, Winogrodzki JL, Debowski AW, et al. (2018) A mechanism-based GlcNAc-inspired cyclophellitol inactivator of the peptidoglycan recycling enzyme NagZ reverses resistance to β-lactams in Pseudomonas aeruginosa. Chemical Communications (Cambridge, England) |
Macdonald SS, Patel A, Larmour VLC, et al. (2018) Structural and mechanistic analysis of a β-glycoside phosphorylase identified by screening a metagenomic library. The Journal of Biological Chemistry |
Abbott W, Alber O, Bayer E, et al. (2018) Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes Glycobiology. 28: 3-8 |
Bailey-Elkin BA, Knaap RCM, Kikkert M, et al. (2017) Structure and function of viral deubiquitinating enzymes. Journal of Molecular Biology |
Zhang W, Bailey-Elkin BA, Knaap RCM, et al. (2017) Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants. Plos Pathogens. 13: e1006372 |
Bouquet J, King DT, Vadlamani G, et al. (2017) Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibiotics. Organic & Biomolecular Chemistry |
Vadlamani G, Stubbs KA, Désiré J, et al. (2017) Conformational flexibility of the glycosidase NagZ allows it to bind structurally diverse inhibitors to suppress β-lactam antibiotic resistance. Protein Science : a Publication of the Protein Society |