[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
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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04-12-2018 01:01 AM
[NMR paper] Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1
Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1
Targeting PPIs with small molecules can be challenging due to large, hydrophobic binding surfaces. Here, we describe a strategy that exploits selective alpha-helical PPIs, transferring these characteristics to small molecules. The proof-of-concept is exemplified with the apoptosis regulator Mcl-1, commonly exploited by cancers to avoid cell death. Peptide directed binding uses few synthetic transformations, requires...
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07-03-2017 02:31 AM
[NMR paper] Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
Angew Chem Int Ed Engl. 2017 Apr 07;:
Authors: Wälti MA, Riek R, Orts J
Abstract
In early drug discovery approaches, screening hits are often weak affinity binders that are difficult to characterize in structural detail, particularly towards obtaining the 3D structure of...
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04-08-2017 10:57 AM
[NMR paper] The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence.
The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence.
Related Articles The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence.
Protein Pept Lett. 2016 Sep 20;
Authors: Chen TC, Hsiao CL, Huang SJ, Huang JR
Abstract
In NMR experiments, the chemical shift is typically the first parameter measured and is a source of structural information for biomolecules. Indeed, secondary chemical shifts, the difference...
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09-23-2016 12:55 PM
[NMR paper] Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
Related Articles Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
FEBS J. 2015 Aug 11;
Authors: Tomaselli S, Pagano K, Boulton S, Zanzoni S, Melacini G, Molinari H, Ragona L
Abstract
Primary bile acids, differing in the hydroxylation pattern, are synthesized from cholesterol in the liver and, once formed, can undergo extensive enzyme-catalyzed glycine/taurine conjugation, giving rise to a...
[NMR paper] Insights into tyrosine phosphorylation control of protein-protein association from th
Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Related Articles Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Biochemistry. 1998 Jan 20;37(3):867-77
Authors: Eisenmesser EZ, Post CB
A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR...
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11-17-2010 11:06 PM
[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Related Articles Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Biochemistry. 1994 Oct 11;33(40):12032-41
Authors: Yi Q, Erman JE, Satterlee JD
Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...