[NMR paper] Small molecule induced toxic human-IAPP species characterized by NMR.
Small molecule induced toxic human-IAPP species characterized by NMR.
Small molecule induced toxic human-IAPP species characterized by NMR.
Chem Commun (Camb). 2020 Oct 02;:
Authors: Cox SJ, Rodriguez Camargo DC, Lee YH, Dubini RCA, Rovó P, Ivanova MI, Padmini V, Reif B, Ramamoorthy A
Abstract
In this study, the effect of CurDAc, a water-soluble curcumin derivative, on the formation and stability of amyloid fibers is revealed. CurDAc interaction with amyloid is structurally selective, which is reflected in a strong...
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10-04-2020 05:33 AM
[NMR paper] Reversible DNA-protein cross-linking at epigenetic DNA marks
Reversible DNA-protein cross-linking at epigenetic DNA marks
5-Formylcytosine (5fC) is an endogenous DNA modification frequently found within regulatory elements of mammalian genes. Although 5fC is an oxidation product of 5-methylcytosine (5mC), the two epigenetic marks show distinct genome-wide distributions and protein affinities, suggesting that they perform different functions in epigenetic signaling. A unique feature of 5fC is the presence of a potentially reactive aldehyde group in its structure. Here, we show that 5fC bases in DNA readily form Schiff base conjugates with Lys side...
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09-12-2017 01:45 PM
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcSCXR38-W1skwr6nJyTpI7ekwp0MTCyjWVm3-nHyO5fN0ai5Hxu348VoeOV77NUFQBjMN6RfXbk
Nature.com
<img alt="" height="1" width="1">
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
Nature.com
We describe an integrated workflow that robustly identifies cross-links from endogenous protein complexes in human cellular lysates. Our approach is based on the application of mass spectrometry (MS)-cleavable cross-linkers,...
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09-29-2015 07:59 AM
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Juan C. Mun?oz-Garci?a, Eric Chabrol, Romain R. Vive?s, Aline Thomas, Jose? L. de Paz, Javier Rojo, Anne Imberty, Franck Fieschi, Pedro M. Nieto and Jesu?s Angulo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja511529x/20150319/images/medium/ja-2014-11529x_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja511529x...
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03-23-2015 08:22 PM
[NMR paper] Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Related Articles Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
J Am Chem Soc. 2015 Mar 6;
Authors: Muñoz-García JC, Chabrol E, Vives RR, Thomas A, de Paz JL, Rojo J, Imberty A, Fieschi F, Nieto PM, Angulo J
Abstract
Langerin is a C-type lectin present...
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03-10-2015 07:22 PM
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...