[NMR paper] Peptide-Directed Binding for the Discovery of Modulators of ?-Helix-Mediated Protein–Protein Interactions: Proof-of-Concept Studies with the Apoptosis Regulator Mcl-1
Peptide-Directed Binding for the Discovery of Modulators of ?-Helix-Mediated Protein–Protein Interactions: Proof-of-Concept Studies with the Apoptosis Regulator Mcl-1
Targeting PPIs with small molecules can be challenging owing to large, hydrophobic binding surfaces. Herein, we describe a strategy that exploits selective ?-helical PPIs, transferring these characteristics to small molecules. The proof of concept is demonstrated with the apoptosis regulator Mcl-1, commonly exploited by cancers to avoid cell death. Peptide-directed binding uses few synthetic transformations, requires the...
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[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] Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Related Articles Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Chemistry. 2017 Jun 25;:
Authors: Diniz A, S Dias J, Jiménez-Barbero J, Marcelo F, Cabrita EJ
Abstract
Protein-glycan interactions as modulators for quinary structure in crowding environments were explored. The interaction between human galectin 3 (Gal-3) and distinct macromolecular crowders, such as bovine and human serum albumin (BSA...
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06-27-2017 05:28 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, Cañada 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
Drugs Modulate Interactions between the First Nucleotide-BindingDomain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein
Drugs Modulate Interactions between the First Nucleotide-BindingDomain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00233/20160511/images/medium/bi-2016-00233f_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00233
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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05-11-2016 08:04 PM
[NMR paper] Probing Protein Quinary Interactions by in-cell NMR.
Probing Protein Quinary Interactions by in-cell NMR.
Related Articles Probing Protein Quinary Interactions by in-cell NMR.
Biochemistry. 2015 Apr 20;
Authors: Majumder S, Xue J, DeMott CM, Reverdatto S, Burz DS, Shekhtman A
Abstract
Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, protein weak (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro....
[NMR paper] K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse rel
K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse relaxation rates in the cytoplasm of Escherichia coli K-12.
Related Articles K(+)-ribosome interactions determine the large enhancements of 39K NMR transverse relaxation rates in the cytoplasm of Escherichia coli K-12.
Biochemistry. 1995 Jan 31;34(4):1393-404
Authors: Guttman HJ, Cayley S, Li M, Anderson CF, Record MT
As a probe of physical chemical properties of the intracellular environment, we measured 39K NMR transverse relaxation rates in concentrated cell...
Ribosome Mediated Quinary Interactions Modulate In-CellProtein Activities
Linear Mode
