Post-translational modification (PTM) of proteins is of critical importance to the regulation of many cellular processes in eukaryotic organisms. One of the most well-studied protein PTMs is methylation, wherein an enzyme catalyzes the transfer of a methyl group from a cofactor to a lysine or arginine side chain. Lysine methylation is especially abundant in the histone tails and is an important marker for denoting active or repressed genes. Given their relevance to transcriptional regulation,...
[ASAP] Multiplexed Real-Time NMR GTPase Assay for Simultaneous Monitoring of Multiple Guanine Nucleotide Exchange Factor Activities from Human Cancer Cells and Organoids
Multiplexed Real-Time NMR GTPase Assay for Simultaneous Monitoring of Multiple Guanine Nucleotide Exchange Factor Activities from Human Cancer Cells and Organoids
Teklab Gebregiworgis, Christopher B. Marshall, Tadateru Nishikawa, Nikolina Radulovich, María-José Sandí, Zhenhao Fang, Robert Rottapel, Ming-Sound Tsao, Mitsuhiko Ikura
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b13703/20180322/images/medium/ja-2017-13703a_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b13703...
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03-22-2018 06:35 PM
[NMR paper] Multiplexed real-time NMR GTPase assay for simultaneous monitoring of multiple GEF activities from human cancer cells and organoids.
Multiplexed real-time NMR GTPase assay for simultaneous monitoring of multiple GEF activities from human cancer cells and organoids.
Multiplexed real-time NMR GTPase assay for simultaneous monitoring of multiple GEF activities from human cancer cells and organoids.
J Am Chem Soc. 2018 Mar 15;:
Authors: Gebregiworgis T, Marshall CB, Nishikawa T, Radulovich N, Sandi MJ, Fang Z, Rottapel R, Tsao MS, Ikura M
Abstract
Small GTPases (sGTPases) are critical switch-like regulators that mediate several important cellular functions and...
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03-16-2018 12:12 PM
[NMR paper] Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
J Am Chem Soc. 2017 Jan 11;:
Authors: Franco R, Gil-Caballero S, Ayala I, Favier A, Brutscher B
Abstract
NMR spectroscopy is a powerful tool for studying...
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01-12-2017 03:48 AM
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Abstract
Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here....
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03-04-2015 08:56 AM
[NMR paper] Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
J Phys Chem B. 2014 Mar 14;
Authors: Calligari PA, Abergel D
Abstract
Fluctuations of NMR resonance frequency shifts and their relation with protein exchanging conformations are usually...
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03-19-2014 10:43 PM
[NMR paper] Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Related Articles Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Molecules. 2013;18(8):9451-76
Authors: Giachin G, Biljan I, Ilc G, Plavec J, Legname G
Abstract
The post-translational conversion of the ubiquitously expressed cellular form of the prion protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a key role in prion diseases. These maladies are denoted transmissible spongiform...
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08-24-2013 04:53 PM
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Franc?ois-Xavier Theillet, Stamatios Liokatis, Jan Oliver Jost, Beata Bekei, Honor May Rose, Andres Binolfi, Dirk Schwarzer and Philipp Selenko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja301895f/aop/images/medium/ja-2012-01895f_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja301895f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/tV2dPnMa4Qc
Probing multiple enzymatic methylation events in real time with NMR spectroscopy
Linear Mode
