Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Steven M Kwasny"'
Autor:
Jamal Chauhan, Steven Cardinale, Lei Fang, Jing Huang, Steven M Kwasny, M Ross Pennington, Kelly Basi, Robert diTargiani, Benedict R Capacio, Alexander D MacKerell, Timothy J Opperman, Steven Fletcher, Erik P H de Leeuw
Publikováno v:
PLoS ONE, Vol 11, Iss 10, p e0164515 (2016)
Recently we described a novel di-benzene-pyrylium-indolene (BAS00127538) inhibitor of Lipid II. BAS00127538 (1-Methyl-2,4-diphenyl-6-((1E,3E)-3-(1,3,3-trimethylindolin-2-ylidene)prop-1-en-1-yl)pyryl-1-ium) tetrafluoroborate is the first small molecul
Externí odkaz:
https://doaj.org/article/3b20d0e6c31f4ac6bf0d0a03d1cf8c71
Autor:
Cecilia Gutierrez-Perez, Charles Puerner, Jane T. Jones, Sandeep Vellanki, Elisa M. Vesely, Mark A. Xatse, Andre F. C. Viera, Carissa P. Olsen, Keren O. Attiku, Steven Cardinale, Steven M. Kwasny, Narendran G-Dayanandan, Timothy J. Opperman, Robert A. Cramer
Publikováno v:
mBio, Vol 15, Iss 7 (2024)
ABSTRACT Contemporary antifungal therapies utilized to treat filamentous fungal infections are inhibited by intrinsic and emerging drug resistance. Consequently, there is an urgent need to develop novel antifungal compounds that are effective against
Externí odkaz:
https://doaj.org/article/6c6f0dfdb29846f4968aadcda7933aa2
Autor:
Zachary D. Aron, Atousa Mehrani, Eric D. Hoffer, Kristie L. Connolly, Pooja Srinivas, Matthew C. Torhan, John N. Alumasa, Mynthia Cabrera, Divya Hosangadi, Jay S. Barbor, Steven C. Cardinale, Steven M. Kwasny, Lucas R. Morin, Michelle M. Butler, Timothy J. Opperman, Terry L. Bowlin, Ann Jerse, Scott M. Stagg, Christine M. Dunham, Kenneth C. Keiler
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Antibiotic-resistant bacterial pathogens pose a substantial threat to human health. Here, aided by structural analyses, the authors describe the molecular mechanism behind the activity of a series of compounds that inhibit trans-translation and are e
Externí odkaz:
https://doaj.org/article/65f0e506e42e4cd09c551a4db2d7e630
Autor:
Michelle M Butler, Samanthi L. Waidyarachchi, Jinfeng Shao, Son T. Nguyen, Xiaoyuan Ding, Steven C. Cardinale, Lucas R. Morin, Steven M. Kwasny, Mai Ito, Jeanine Gezelle, Maria B. Jiminez-Diaz, Inigo Angulo-Barturen, Robert T. Jacobs, Jeremy N. Burrows, Zachary D. Aron, Terry L. Bowlin, Sanjay A. Desai
Publikováno v:
Mol Pharmacol
Human and animal malaria parasites increase their host erythrocyte permeability to a broad range of solutes as mediated by parasite-associated ion channels. Molecular and pharmacological studies have implicated an essential role in parasite nutrient
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cd2cfbfaccb951c5eceaee13a146c87
https://europepmc.org/articles/PMC9450958/
https://europepmc.org/articles/PMC9450958/
Autor:
Andrea J. Parsons, Sabrina I. Ophir, Thomas J. Gardner, Jailene Casado Paredes, Kathryn R. Stein, Steven M. Kwasny, Steven C. Cardinale, Matthew Torhan, Mark N. Prichard, Scott H. James, Kristina E. Atanasoff, Narendran G-Dayanandan, Terry L. Bowlin, Timothy J. Opperman, Domenico Tortorella
Publikováno v:
Antiviral Research. 209:105474
Human cytomegalovirus (CMV) is a ubiquitous β-herpesvirus that establishes latent asymptomatic infections in healthy individuals but can cause serious infections in immunocompromised people, resulting in increased risk of morbidity and mortality. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33efc4316f8c6a98fd65200109a1564e
https://doi.org/10.1016/j.antiviral.2022.105474
https://doi.org/10.1016/j.antiviral.2022.105474
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 29:1849-1853
Lipid II is an essential precursor of bacterial cell wall biosynthesis and an attractive target for antibiotics. Lipid II is comprised of specialized lipid (bactoprenol) linked to a hydrophilic head group consisting of a peptidoglycan subunit (N-acet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::324fc88dc03e261734d64417243c72fd
https://doi.org/10.1016/j.bmcl.2019.04.046
https://doi.org/10.1016/j.bmcl.2019.04.046
Autor:
Atousa Mehrani, Mynthia Cabrera, Kenneth C. Keiler, Michelle M. Butler, Steven M. Kwasny, Pooja Srinivas, Lucas R. Morin, Divya Hosangadi, John N. Alumasa, Jay S. Barbor, Steven C. Cardinale, Scott M. Stagg, Zachary D. Aron, Christine M. Dunham, Ann E. Jerse, Matthew C. Torhan, Timothy J. Opperman, Eric D. Hoffer, Terry L. Bowlin, Kristie L. Connolly
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Bacterial ribosome rescue pathways that remove ribosomes stalled on mRNAs during translation have been proposed as novel antibiotic targets because they are essential in bacteria and are not conserved in humans. We previously reported the discovery o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::411f83145a0e100fbdf1e585bbf3dfa6
https://doi.org/10.1038/s41467-021-22012-7
https://doi.org/10.1038/s41467-021-22012-7
Autor:
Divya Hosangadi, Lucas R. Morin, Kristie L. Connolly, Terry L. Bowlin, Michelle M. Butler, Christine M. Dunham, Atousa Mehrani, Zachary D. Aron, Jay S. Barbor, John N. Alumasa, Pooja Srinivas, Kenneth C. Keiler, Eric D. Hoffer, Mynthia Cabrera, Matthew C. Torhan, Scott M. Stagg, Steven M. Kwasny, Timothy J. Opperman, Ann E. Jerse, Steven C. Cardinale
The trans-translation pathway for rescuing stalled ribosomes is conserved and essential in bacterial pathogens but has no mammalian homolog, making it an ideal target for new antibiotics. We previously reported the discovery of a family of acylaminoo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c60f516b4139e9bac172634fa60d14b
https://doi.org/10.1101/2020.06.04.132530
https://doi.org/10.1101/2020.06.04.132530
Autor:
Panatda Saenkham, Steven M. Kwasny, Timothy J. Opperman, Donald T. Moir, Terry L. Bowlin, Charles O. Rock, John D. Williams, Debra M. Mills, Joselynn R. Wallace, Nicholas O. Bowlin
Publikováno v:
Antimicrobial Agents and Chemotherapy. 59:5775-5787
Novel, cellular, gain-of-signal, bioluminescent reporter assays for fatty acid synthesis type II (FASII) inhibitors were constructed in an efflux-deficient strain of Pseudomonas aeruginosa and based on the discovery that FASII genes in P. aeruginosa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8acca0fd70bf12f47059a0e9bea8ed83
https://doi.org/10.1128/aac.00686-15
https://doi.org/10.1128/aac.00686-15
Autor:
Steven M. Kwasny, Timothy J. Opperman, Xiaoyuan Ding, Hanno Sjuts, Terry L. Bowlin, Alina R. Ornik, Attilio Vittorio Vargiu, Son T. Nguyen, Paolo Ruggerone, Hiroshi Nikaido, Hong-Suk Kim, Klaas M. Pos
Publikováno v:
Sjuts, H; Vargiu, AV; Kwasny, SM; Nguyen, ST; Kim, HS; Ding, X; et al.(2016). Molecular basis for inhibition of AcrB multidrug efflux pump by novel and powerful pyranopyridine derivatives. Proceedings of the National Academy of Sciences of the United States of America, 113(13), 3509-3514. doi: 10.1073/pnas.1602472113. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/36v4w9g5
Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 13
Proceedings of the National Academy of Sciences of the United States of America 113(13), 3509-3514 (2016). doi:10.1073/pnas.1602472113
Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 13
Proceedings of the National Academy of Sciences of the United States of America 113(13), 3509-3514 (2016). doi:10.1073/pnas.1602472113
Proceedings of the National Academy of Sciences of the United States of America 113(13), 3509 - 3514(2016). doi:10.1073/pnas.1602472113
The Escherichia coli AcrAB-TolC efflux pump is the archetype of the resistance nodulation cell division (RND)
The Escherichia coli AcrAB-TolC efflux pump is the archetype of the resistance nodulation cell division (RND)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e985e03830e4a69fcfc3e2102d8c7b56
https://pubmed.ncbi.nlm.nih.gov/26976576
https://pubmed.ncbi.nlm.nih.gov/26976576