Related ArticlesReal-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Jan 23;
Authors: Ma J, McLeod S, Maccormack K, Sriram S, Gao N, Breeze AL, Hu J
Abstract
Disconnections between in vitro responses and those observed in whole cells confound many attempts to design drugs in areas of serious medical need. A method based on 1D (1) H NMR spectroscopy is reported that affords the ability to monitor the hydrolytic decomposition of the carbapenem antibiotic meropenem inside Escherichia coli cells expressing New Delhi metallo-?-lactamase subclass 1 (NDM-1), an emerging antibiotic-resistance threat. Cell-based NMR studies demonstrated that two known NDM-1 inhibitors, L-captopril and ethylenediaminetetraacetic acid (EDTA), inhibit the hydrolysis of meropenem in vivo. NDM-1 activity in cells was also shown to be inhibited by spermine, a porin inhibitor, although in an in vitro assay, the influence of spermine on the activity of isolated NDM-1 protein is minimal. This new approach may have generic utility for monitoring reactions involving diffusible metabolites in other complex biological matrices and whole-cell settings, including mammalian cells.
PMID: 24458501 [PubMed - as supplied by publisher]
[NMR paper] In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
Related Articles In-cell NMR: an emerging approach for monitoring metal-related events in living cells.
Metallomics. 2013 Nov 8;
Authors: Li H, Sun H
Abstract
In-cell NMR, an isotope-assisted multi-dimensional NMR technique, has been proven to be successful in the investigation of protein dynamics, folding, conformational changes induced by binding events, posttranslational modification in the complex native environments, as well as in vivo drug...
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[NMR paper] Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Anal Chem. 2013 Sep 12;
Authors: Yamasaki K, Obara Y, Hasegawa M, Tanaka H, Yamasaki T, Wakuda T, Okada M, Kohzuma T
Abstract
An NMR method was developed that allows for real-time monitoring of reactions (on the order of seconds) induced by temperature jump. In a recycle flow system, heating and cooling baths were integrated, with the latter...
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09-14-2013 03:02 PM
[NMR paper] Protein dynamics in living cells studied by in-cell NMR spectroscopy.
Protein dynamics in living cells studied by in-cell NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein dynamics in living cells studied by in-cell NMR spectroscopy.
FEBS Lett. 2013 Jan 11;
Authors: Li C, Liu M
Abstract
Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques...
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Watching protein structure at work in living cells using NMR spectroscopy
Watching protein structure at work in living cells using NMR spectroscopy
December 2012
Publication year: 2012
Source:Current Opinion in Chemical Biology, Volume 16, Issues 5–6</br>
</br>
Isotope-assisted multi-dimensional NMR spectroscopy can now be applied to proteins inside living cells. The technique, called in-cell NMR, aims to investigate the structures, interactions and dynamics of proteins under their native conditions, ideally at an atomic resolution. The application has begun with bacterial cells but has now expanded to mammalian cultured cells, such as HeLa...
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02-03-2013 10:13 AM
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Zulay D. Pardo, Gregory L. Olsen, Mari?a Encarnacio?n Ferna?ndez-Valle, Lucio Frydman, Roberto Marti?nez-A?lvarez and Antonio Herrera
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210154g/aop/images/medium/ja-2011-10154g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210154g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/tEFGGh16-DU
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01-28-2012 05:27 AM
13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
Angew Chem Int Ed Engl. 2011 Mar 1;50(10):2339-41
Authors: Bertini I, Felli IC, Gonnelli L, Kumar M V V, Pierattelli R
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06-18-2011 01:10 PM
[NMR paper] Real time NMR monitoring of local unfolding of HIV-1 protease tethered dimer driven b
Real time NMR monitoring of local unfolding of HIV-1 protease tethered dimer driven by autolysis.
Related Articles Real time NMR monitoring of local unfolding of HIV-1 protease tethered dimer driven by autolysis.
FEBS Lett. 2001 May 18;497(1):59-64
Authors: Panchal SC, Bhavesh NS, Hosur RV
Structural studies in proteases have been hampered because of their inherent autolytic function. However, since autolysis is known to be mediated via protein unfolding, careful monitoring of the autolytic reaction has the potential to throw light on the...
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11-19-2010 08:32 PM
[NMR paper] NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its
NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Related Articles NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Biochemistry. 1999 Nov 2;38(44):14507-14
Authors: Scrofani SD, Chung J, Huntley JJ, Benkovic SJ, Wright PE, Dyson HJ
Understanding the structure and dynamics of the enzymes that mediate antibiotic resistance of...
Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
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