The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity.

Autor: Petit GA; Griffith Institute for Drug Discovery, Griffith University, Don Young Road, Nathan, QLD 4111, Australia., Hong Y; Centre for Immunology and Infection Control and School of Biomedical Sciences, Queensland University of Technology, Herston, QLD 4006, Australia., Djoko KY; Department of Biosciences, Durham University, Durham DH1 3LE, United Kingdom., Whitten AE; Australian Nuclear Science and Technology Organization (ANSTO), New Illawarra Road, Lucas Heights, NSW 2234, Australia., Furlong EJ; Griffith Institute for Drug Discovery, Griffith University, Don Young Road, Nathan, QLD 4111, Australia., McCoy AJ; Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom., Gulbis JM; Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia., Totsika M; Centre for Immunology and Infection Control and School of Biomedical Sciences, Queensland University of Technology, Herston, QLD 4006, Australia., Martin JL; Griffith Institute for Drug Discovery, Griffith University, Don Young Road, Nathan, QLD 4111, Australia., Halili MA; Griffith Institute for Drug Discovery, Griffith University, Don Young Road, Nathan, QLD 4111, Australia.

Publikováno v: Acta crystallographica. Section D, Structural biology [Acta Crystallogr D Struct Biol] 2022 Mar 01; Vol. 78 (Pt 3), pp. 337-352. Date of Electronic Publication: 2022 Feb 21.

The Glitazone Class of Drugs as Carbonic Anhydrase Inhibitors-A Spin-Off Discovery from Fragment Screening.

Autor: Mueller SL; Griffith Institute for Drug Discovery, Griffith University, Nathan, Brisbane, QLD 4111, Australia.; ARC Centre for Fragment-Based Design, Griffith University, Nathan, Brisbane, QLD 4111, Australia.; CSIRO, Biomedical Manufacturing Program, Parkville, Melbourne, VIC 3052, Australia., Chrysanthopoulos PK; Griffith Institute for Drug Discovery, Griffith University, Nathan, Brisbane, QLD 4111, Australia., Halili MA; Griffith Institute for Drug Discovery, Griffith University, Nathan, Brisbane, QLD 4111, Australia.; ARC Centre for Fragment-Based Design, Griffith University, Nathan, Brisbane, QLD 4111, Australia., Hepburn C; Waters Australia Pty Ltd., Rydalmere, NSW 2116, Australia., Nebl T; CSIRO, Biomedical Manufacturing Program, Parkville, Melbourne, VIC 3052, Australia., Supuran CT; Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche Nutraceutiche, Università Degli Studi di Firenze, Sesto Fiorentino, 50019 Florence, Italy., Nocentini A; Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche Nutraceutiche, Università Degli Studi di Firenze, Sesto Fiorentino, 50019 Florence, Italy., Peat TS; CSIRO, Biomedical Manufacturing Program, Parkville, Melbourne, VIC 3052, Australia., Poulsen SA; Griffith Institute for Drug Discovery, Griffith University, Nathan, Brisbane, QLD 4111, Australia.; ARC Centre for Fragment-Based Design, Griffith University, Nathan, Brisbane, QLD 4111, Australia.

Publikováno v: Molecules (Basel, Switzerland) [Molecules] 2021 May 18; Vol. 26 (10). Date of Electronic Publication: 2021 May 18.

NMR fragment screening reveals a novel small molecule binding site near the catalytic surface of the disulfide-dithiol oxidoreductase enzyme DsbA from Burkholderia pseudomallei.

Autor: Nebl S; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Alwan WS; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Williams ML; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Sharma G; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Taylor A; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Doak BC; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Wilde KL; National Deuteration Facility, Australian Nuclear Science and Technology Organization (ANSTO), Locked Bag 2001, Kirrawee DC, NSW, 2232, Australia., McMahon RM; Griffith Institute for Drug Discovery, Griffith University, Brisbane, Australia., Halili MA; Griffith Institute for Drug Discovery, Griffith University, Brisbane, Australia., Martin JL; Griffith Institute for Drug Discovery, Griffith University, Brisbane, Australia.; Vice-Chancellor's Unit, University of Wollongong, Northfields Avenue, Wollongong, NSW, 2522, Australia., Capuano B; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia., Fenwick RB; Department of Integrative Structural and Computational Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA., Mohanty B; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia. biswaranjan.mohanty@monash.edu.; ARC Centre for Fragment-Based Design, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia. biswaranjan.mohanty@monash.edu., Scanlon MJ; Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia. martin.scanlon@monash.edu.; ARC Centre for Fragment-Based Design, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia. martin.scanlon@monash.edu.

Publikováno v: Journal of biomolecular NMR [J Biomol NMR] 2020 Nov; Vol. 74 (10-11), pp. 595-611. Date of Electronic Publication: 2020 Aug 06.

Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development.

Autor: Christensen S; Institute for Molecular Bioscience, University of Queensland, St Lucia, Queensland, Australia.; Griffith Institute for Drug Discovery, Griffith University, Nathan, Queensland, Australia., Halili MA; Griffith Institute for Drug Discovery, Griffith University, Nathan, Queensland, Australia., Strange N; School of Life Sciences, University of Technology Sydney, Broadway, New South Wales, Australia., Petit GA; Griffith Institute for Drug Discovery, Griffith University, Nathan, Queensland, Australia., Huston WM; School of Life Sciences, University of Technology Sydney, Broadway, New South Wales, Australia., Martin JL; Griffith Institute for Drug Discovery, Griffith University, Nathan, Queensland, Australia., McMahon RM; Griffith Institute for Drug Discovery, Griffith University, Nathan, Queensland, Australia.

Publikováno v: PloS one [PLoS One] 2019 Sep 19; Vol. 14 (9), pp. e0222595. Date of Electronic Publication: 2019 Sep 19 (Print Publication: 2019).

Author Correction: A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.

Autor: Furlong EJ; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia., Lo AW; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia.; Australian Infectious Diseases Research Centre, University of Queensland, St. Lucia, QLD, 4072, Australia., Kurth F; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia.; Bristol-Myers Squibb, Arnulfstraße 29, 80636, Munich, Germany., Premkumar L; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia.; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia.; Department of Microbiology and Immunology, School of Medicine, University of North Carolina, Chapel Hill, NC, 27514, USA., Totsika M; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia.; Australian Infectious Diseases Research Centre, University of Queensland, St. Lucia, QLD, 4072, Australia.; Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Queensland University of Technology, Kelvin Grove, QLD, 4059, Australia., Achard MES; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia.; Australian Infectious Diseases Research Centre, University of Queensland, St. Lucia, QLD, 4072, Australia.; School of Human Movement and Nutrition Sciences, University of Queensland, St. Lucia, QLD, 4072, Australia., Halili MA; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia., Heras B; La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC, 3068, Australia., Whitten AE; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia. awh@ansto.gov.au.; Australian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organization, Lucas Heights, New South Wales, 2234, Australia. awh@ansto.gov.au., Choudhury HG; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia.; Cello Health Consulting, Farnham Surrey, GU9 7DN, UK., Schembri MA; School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD, 4072, Australia. m.schembri@uq.edu.au.; Australian Infectious Diseases Research Centre, University of Queensland, St. Lucia, QLD, 4072, Australia. m.schembri@uq.edu.au., Martin JL; Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD, 4072, Australia. jlm@griffith.edu.au.; Griffith Institute for Drug Discovery, Griffith University, Nathan, QLD, 4111, Australia. jlm@griffith.edu.au.

Publikováno v: Nature communications [Nat Commun] 2019 Mar 01; Vol. 10 (1), pp. 976. Date of Electronic Publication: 2019 Mar 01.