Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Michelle F Homsher"'
Autor:
Elisabeth MacColl, Paul Zuck, Victor N. Uebele, Michelle F Homsher, Jeffrey D. Hermes, Jason Cassaday, Jennifer Nothstein
Publikováno v:
SLAS Technology. 22:485-492
Automated mechanism of action studies are introducing the need for tailored compound delivery, which can be challenging for standard compound management procedures. Jump dilution assays investigating inhibitor reversibility require compound delivery
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::956e7b3fb6d3ae7591d1a0972d3e9c2e
https://doi.org/10.1177/2472630316684807
https://doi.org/10.1177/2472630316684807
Autor:
Douglas C. Beshore, Stephen Day, Jason Cassaday, Michelle F. Homsher, Brian Squadroni, David Pechter, Michelle Smith, Lei Ma, Jeffrey D. Hermes, Elizabeth Mohammed, Michelle Hartnett, Paul Zuck, Michael F.A. Finley, Victor N. Uebele, Fredrick Monsma
Publikováno v:
SLAS Discovery. 22:1060-1066
Agonist shift assays feature cross-titrations of allosteric modulators and orthosteric ligands. Information generated in agonist shift assays can include a modulator's effect on the orthosteric agonist's potency (alpha) and efficacy (beta), as well a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4aa4a57a20f8bcde2680cb5a7bfd7c52
https://doi.org/10.1177/2472555217705373
https://doi.org/10.1177/2472555217705373
Autor:
Michelle F. Homsher, Louis Locco, Shannon L. Stahler, Michael Weber, Jennifer E. Nothstein, Eleftheria N. Finger, Evelyn Boots, Mee Ra Heo, Amita Patel, Gregory O'Donnell, Alex Wolicki, Michael F.A. Finley, J. Christopher Culberson, Paul Zuck, Juncai Meng, Kenneth Roberts, David J. Bell, Peter S. Kutchukian, Gregory C. Adam, Carissa Quinn, Patrick Cocchiarella, Meir Glick, S. Alex May, Victor N. Uebele, Edward Hudak, Brian Squadroni, Daniel Riley, Andrew Rusinko, Kelli Solly, Michelle Hartnett, Dante A. Pertusi, Adam Amoss, Anthony Kreamer, Tara White, Anne Mai Wassermann
Publikováno v:
SLAS Discovery. 22:995-1006
High-throughput screening (HTS) is a widespread method in early drug discovery for identifying promising chemical matter that modulates a target or phenotype of interest. Because HTS campaigns involve screening millions of compounds, it is often desi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::561e5ff95861fbde45cdff3f2132d673
https://doi.org/10.1177/2472555217706058
https://doi.org/10.1177/2472555217706058
Autor:
Anna Konovalova, Hao Wang, Holly A. Sutterlin, Xiaoqing Han, Smaranda Bodea, Frances P. Rodriguez-Rivera, Adam G. Schwaid, Thomas J. Silhavy, Jessica Ruolin Sheng, Todd A. Black, Terry Roemer, Elizabeth M. Hart, Marcin Grabowicz, Carl J. Balibar, Qian Si, Scott S. Walker, Deborah M. Rothman, Ronald E. Painter, Juliana C. Malinverni, Michelle F. Homsher, Angela M. Mitchell, Anthony Ogawa
The development of new antimicrobial drugs is a priority to combat the increasing spread of multidrug-resistant bacteria. This development is especially problematic in gram-negative bacteria due to the outer membrane (OM) permeability barrier and mul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d37bc56f3a1463af9d150c6c6855d4a
https://europepmc.org/articles/PMC6815139/
https://europepmc.org/articles/PMC6815139/
Autor:
Michelle F, Homsher, Douglas C, Beshore, Jason, Cassaday, Brian, Squadroni, Elizabeth, Mohammed, Michelle, Hartnett, Stephen, Day, Lei, Ma, David, Pechter, Michelle D, Smith, Fredrick, Monsma, Paul, Zuck, Michael F, Finley, Victor N, Uebele, Jeffrey D, Hermes
Publikováno v:
SLAS discovery : advancing life sciences RD. 22(8)
Agonist shift assays feature cross-titrations of allosteric modulators and orthosteric ligands. Information generated in agonist shift assays can include a modulator's effect on the orthosteric agonist's potency (alpha) and efficacy (beta), as well a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d7c79a7b5f4df8eb76db0b4627102a9f
https://pubmed.ncbi.nlm.nih.gov/28426939
https://pubmed.ncbi.nlm.nih.gov/28426939