[ASAP] Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00019/20180410/images/medium/bi-2018-00019w_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00019
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04-12-2018 01:01 AM
Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00861/20171103/images/medium/bi-2017-00861b_0001.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00861
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11-04-2017 12:23 PM
[NMR paper] NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.
NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.
NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.
ACS Chem Biol. 2017 Feb 13;:
Authors: Gimeno A, Reichardt NC, Caņada FJ, Perkams L, Unverzagt C, Jimenez-Barbero J, Arda A
Abstract
Glycans play a key role as recognition elements in the communication of cells and other organisms. Thus, the analysis of carbohydrate-protein interactions has gained...
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02-14-2017 02:05 PM
[NMR paper] Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Related Articles Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Angew Chem Int Ed Engl. 2015 Apr 29;
Authors: Schubert M, Walczak MJ, Aebi M, Wider G
Abstract
Posttranslational modifications (PTMs) are an integral part of the majority of proteins. The characterization of structure and function of PTMs can be very challenging especially for glycans. Existing...
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Cell signaling, post-translational protein modifications and NMR spectroscopy
Cell signaling, post-translational protein modifications and NMR spectroscopy
Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical ...
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09-29-2012 11:56 AM
Postdoctoral Fellow - Post-translational modification, NMR : Duarte ...
Postdoctoral Fellow - Post-translational modification, NMR : Duarte ...
Postdoctoral Fellow - Post-translational modification, NMR, Duarte, United States. View all science jobs and scientific careers from Nature Jobs, the premier ...
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01-10-2012 03:38 PM
[NMR paper] Heteronuclear NMR studies of the specificity of the post-translational modification o
Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
Related Articles Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
FEBS Lett. 2000 Aug 18;479(3):93-8
Authors: Reche PA, Howard MJ, Broadhurst RW, Perham RN
The lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes and the biotinyl domains of biotin-dependent enzymes have homologous structures, but the target lysine...
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11-19-2010 08:29 PM
[NMR paper] Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic m
Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic microcin B17. Structure elucidation and NMR study of a 13C,15N-labelled gyrase inhibitor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic microcin B17. Structure elucidation and NMR study of a 13C,15N-labelled gyrase inhibitor.
Eur J Biochem. 1995 Dec 1;234(2):414-26
Authors: ...