[NMR paper] Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Biochemistry. 2017 Dec 21;:
Authors: Breindel LM, DeMott CM, Burz DS, Shekhtman A
Abstract
It is not well understood how ribosome antibiotics affect a wide range of biochemical pathways; changes in RNA-mediated protein quinary interactions and consequent activity inside the crowded cytosol may provide one possible mechanism. We developed real-time...
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12-22-2017 07:55 PM
[NMR paper] Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.
Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.
Related Articles Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.
ACS Synth Biol. 2017 Sep 15;:
Authors: Panthu B, Ohlmann T, Perrier J, Schlattner U, Jalinot P, Elena-Herrmann B, Rautureau GJP
Abstract
A counter-intuitive cell-free protein synthesis (CFPS) strategy, based on reducing the ribosomal fraction in rabbit...
[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] Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.
Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.
Related Articles Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.
Pharmaceuticals (Basel). 2017 Apr 15;10(2):
Authors: Takechi-Haraya Y, Aki K, Tohyama Y, Harano Y, Kawakami T, Saito H, Okamura E
Abstract
Glycosaminoglycans (GAGs), which are covalently-linked membrane proteins at the cell...
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04-20-2017 06:14 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....
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04-22-2015 03:33 PM
[NMR paper] Real-Time Monitoring of Cancer Cell Metabolism and Effects of an Anticancer Agent using 2D In-Cell NMR Spectroscopy.
Real-Time Monitoring of Cancer Cell Metabolism and Effects of an Anticancer Agent using 2D In-Cell NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Real-Time Monitoring of Cancer Cell Metabolism and Effects of an Anticancer Agent using 2D In-Cell NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Mar 5;
Authors: Wen H, An YJ, Xu WJ, Kang KW, Park S
Abstract
Altered metabolism is a critical part of...
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03-11-2015 09:59 PM
[NMR paper] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Related Articles Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Chembiochem. 2013 Jun 6;
Authors: Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M
Abstract
Intrinsically disordered regions (IDRs) are preferred sites for post-translational modifications essential for regulating protein function. The enhanced local...
Real-Time In-Cell Nuclear Magnetic Resonance: Ribosome-TargetedAntibiotics Modulate Quinary Protein Interactions
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