Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Helen K. Opel Reading"'
Autor:
Alice-Roza Eruera, Alice M. McSweeney, Geena M. McKenzie-Goldsmith, Helen K. Opel-Reading, Simone X. Thomas, Ashley C. Campbell, Louise Stubbing, Andrew Siow, Jonathan G. Hubert, Margaret A. Brimble, Vernon K. Ward, Kurt L. Krause
Publikováno v:
Viruses, Vol 15, Iss 11, p 2202 (2023)
Norovirus is the leading cause of viral gastroenteritis worldwide, and there are no approved vaccines or therapeutic treatments for chronic or severe norovirus infections. The structural characterisation of the norovirus protease and drug development
Externí odkaz:
https://doaj.org/article/86ca3c78c4f045989589594a543e6b57
Autor:
Kiel Hards, Chen-Yi Cheung, Natalie Waller, Cara Adolph, Laura Keighley, Zhi Shean Tee, Liam K. Harold, Ayana Menorca, Richard S. Bujaroski, Benjamin J. Buckley, Joel D. A. Tyndall, Matthew B. McNeil, Kyu Y. Rhee, Helen K. Opel-Reading, Kurt Krause, Laura Preiss, Julian D. Langer, Thomas Meier, Erik J. Hasenoehrl, Michael Berney, Michael J. Kelso, Gregory M. Cook
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-11 (2022)
Derivatives of the FDA-approved drug, amiloride, can eliminate drug-resistant Mycobacterium tuberculosis in vitro by interfering with bacterial energy conservation.
Externí odkaz:
https://doaj.org/article/dae3bf53428948ca8c7fbb2eb80c8d45
Autor:
Schara Safarian, Helen K. Opel-Reading, Di Wu, Ahmad R. Mehdipour, Kiel Hards, Liam K. Harold, Melanie Radloff, Ian Stewart, Sonja Welsch, Gerhard Hummer, Gregory M. Cook, Kurt L. Krause, Hartmut Michel
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
M. tuberculosis cytochrome bd oxidase is of interest as a TB drug target. Here, the authors present the 2.5 Å cryo-EM structure of M. tuberculosis cytochrome bd oxidase and identify a disulfide bond within the canonical quinol binding and oxidation
Externí odkaz:
https://doaj.org/article/d59d3dd24560451195a1764a95c9ea6d
Autor:
Andrew P. Cording, Guillaume Lessene, Rebekah L. Bower, Ian D. Billinghurst, Emma M. Barnes, Bill C. Hawkins, Michael P. Badart, Veera V. Shivaji R. Edupuganti, Kurt L. Krause, Rhonda J. Rosengren, Zohaib Rana, Abigail R. Bland, Helen K. Opel Reading, Gregory M. Cook, Selena C. L. Gilmer, John C. Ashton, Allan B. Gamble, Scott A. Ferguson
Publikováno v:
ChemMedChem. 16:1308-1315
A second-generation enantiospecific synthesis of spiroleucettadine is described. The original reported antibacterial activity was not observed when the experiment was repeated on the synthetic samples; however, significant anti-proliferative activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93e503d1e32e0d748f03355cf4ff99b9
https://doi.org/10.1002/cmdc.202000954
https://doi.org/10.1002/cmdc.202000954
Autor:
Kiel, Hards, Chen-Yi, Cheung, Natalie, Waller, Cara, Adolph, Laura, Keighley, Zhi Shean, Tee, Liam K, Harold, Ayana, Menorca, Richard S, Bujaroski, Benjamin J, Buckley, Joel D A, Tyndall, Matthew B, McNeil, Kyu Y, Rhee, Helen K, Opel-Reading, Kurt, Krause, Laura, Preiss, Julian D, Langer, Thomas, Meier, Erik J, Hasenoehrl, Michael, Berney, Michael J, Kelso, Gregory M, Cook
Publikováno v:
Communications biology. 5(1)
Increasing antimicrobial resistance compels the search for next-generation inhibitors with differing or multiple molecular targets. In this regard, energy conservation in Mycobacterium tuberculosis has been clinically validated as a promising new dru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::27d4818343c40ab81f2a54807685303c
https://pubmed.ncbi.nlm.nih.gov/35210534
https://pubmed.ncbi.nlm.nih.gov/35210534
Autor:
Helen K. Opel-Reading, Htin Lin Aung, Torsten Kleffmann, Roman Mortuza, Kurt L. Krause, George Taiaroa, Gregory M. Cook
Publikováno v:
Molecular Microbiology. 107:198-213
Glutamate racemase (MurI) has been proposed as a target for anti-tuberculosis drug development based on the inability of ΔmurI mutants of Mycobacterium smegmatis to grow in the absence of d-glutamate. In this communication, we identify ΔmurI suppre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f653755b507bf9151dffff5c58ce7d31
https://doi.org/10.1111/mmi.13877
https://doi.org/10.1111/mmi.13877
Autor:
Robert D, Fagerlund, Timothy J, Ferguson, Howard W R, Maxwell, Helen K, Opel-Reading, Kurt L, Krause, Peter C, Fineran
Publikováno v:
Methods in enzymology. 616
CRISPR adaptation is the initial step in CRISPR-Cas immunity and involves the acquisition of foreign invading DNA. Acquisition is facilitated by the almost universally conserved proteins Cas1 and Cas2, which form an adaptation complex. The Cas1-Cas2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1cd8e46600ea2b653d00838c810b36b5
https://pubmed.ncbi.nlm.nih.gov/30691653
https://pubmed.ncbi.nlm.nih.gov/30691653
Publikováno v:
Bio Protoc
D-amino acid transaminase (D-AAT) is able to synthesize both D-glutamate and D-alanine, according to the following reaction: D-alanine + α-ketoglutarate ⇌ D-glutamate + pyruvate. These two D-amino acids are essential components of the peptidoglyca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8e94027505fe77281b4c43275dec8ee
https://europepmc.org/articles/PMC7854199/
https://europepmc.org/articles/PMC7854199/
Autor:
Timothy J Ferguson, Peter C. Fineran, Kurt L. Krause, Helen K. Opel-Reading, Howard W. R. Maxwell, Robert D. Fagerlund
CRISPR adaptation is the initial step in CRISPR-Cas immunity and involves the acquisition of foreign invading DNA. Acquisition is facilitated by the almost universally conserved proteins Cas1 and Cas2, which form an adaptation complex. The Cas1-Cas2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc91c6f6a030422a94d206f79d4fa4a6
https://doi.org/10.1016/bs.mie.2018.10.024
https://doi.org/10.1016/bs.mie.2018.10.024
Autor:
Yoshio Nakatani, Sinothai Poen, Moritz Lassé, Helen K. Opel-Reading, Kurt L. Krause, Renwick C. J. Dobson
Publikováno v:
Biochemical Journal. 473:1267-1280
Glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria and has been a favoured target in pharmaceutical drug design efforts. It has recently been proven to be essential in Mycobacterium tuberculo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7be6d55b2b0408191abe839fa7bcdb3d
https://doi.org/10.1042/bcj20160186
https://doi.org/10.1042/bcj20160186