[NMR paper] Deciphering the Binding Interactions between Acinetobacter baumannii ACP and beta-ketoacyl ACP Synthase III to Improve Antibiotic Targeting Using NMR Spectroscopy
Deciphering the Binding Interactions between Acinetobacter baumannii ACP and beta-ketoacyl ACP Synthase III to Improve Antibiotic Targeting Using NMR Spectroscopy
Fatty acid synthesis is essential for bacterial viability. Thus, fatty acid synthases (FASs) represent effective targets for antibiotics. Nevertheless, multidrug-resistant bacteria, including the human opportunistic bacteria, Acinetobacter baumannii, are emerging threats. Meanwhile, the FAS pathway of A. baumannii is relatively unexplored. Considering that acyl carrier protein (ACP) has an important role in the delivery of fatty acyl intermediates to other FAS enzymes, we elucidated the solution...
[NMR paper] Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
Glycobiology. 2021 Feb 06;:
Authors: Préchoux A, Simorre JP, Lortat-Jacob H, Laguri C
Abstract
Heparan sulfates (HS) is a polysaccharide...
[NMR paper] Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-advances.gif Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
Sci Adv. 2020 Sep;6(40):
Authors: Mizukoshi Y, Takeuchi K, Tokunaga Y, Matsuo H, Imai M, Fujisaki M, Kamoshida H, Takizawa T, Hanzawa H, Shimada I
...
[NMR paper] Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Chemistry. 2014 Nov 6;
Authors: Diana D, Russomanno A, Rosa LD, Di Stasi R, Capasso D, Di Gaetano S, Romanelli A, Russo L, D'Andrea LD, Fattorusso R
Abstract
In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined...
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[NMR paper] Thiolactomycin-based ?-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy.
Thiolactomycin-based ?-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Thiolactomycin-based ?-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy.
J Biol Chem. 2013 Mar 1;288(9):6045-52
...
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Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Lui?s Mafra, Se?rgio M. Santos, Rene?e Siegel, Ine?s Alves, Filipe A. Almeida Paz, Dmytro Dudenko and Hans W. Spiess
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja208647n/aop/images/medium/ja-2011-08647n_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja208647n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
Deciphering the Binding Interactions between Acinetobacter baumannii ACP and beta-ketoacyl ACP Synthase III to Improve Antibiotic Targeting Using NMR Spectroscopy
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