[NMR paper] In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation.
In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation.
In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation.
Acc Chem Res. 2018 Jun 05;:
Authors: Luchinat E, Banci L
Abstract
Cellular structural biology methods are needed to characterize biological processes at atomic resolution in the physiological environment of the cell. Toward this goal, solution in-cell NMR is a powerful approach because it provides...
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06-06-2018 01:42 PM
'Rheostat' identified that helps regulate cell death versus survival decisions - Phys.Org
http://www.bionmr.com//t3.gstatic.com/images?q=tbn:ANd9GcRRgmdouMLffzhui4bI-9zmifhZCNSw-SZDoZb92H0UvEvAnArK8VB26wYu7CPNl79gpMJ2-Lno
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'Rheostat' identified that helps regulate cell death versus survival decisions
Phys.Org
Researchers used nuclear magnetic resonance (NMR) spectroscopy and other tests to determine how modification of the protein's IDR influenced cell survival. For example, investigators reported that "adjusting" an amino acid in the intrinsically ...
'Rheostat' identified that helps regulate cell death versus survival...
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03-06-2018 03:20 PM
[NMR paper] 15N isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study.
15N isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study.
15N isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study.
Analyst. 2018 Feb 06;:
Authors: Mitri E, Barbieri L, Vaccari L, Luchinat E
Abstract
The ultimate goal of modern structural biology is to probe protein structures and dynamics in their physiological microenvironment. In-cell NMR...
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02-07-2018 03:41 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] Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Biochim Biophys Acta. 2015 Nov 14;
Authors: Mercatelli E, Barbieri L, Luchinat E, Banci L
Abstract
The redox properties of cellular environments are critical to many functional processes, and are strictly controlled in all living organisms. The glutathione-glutathione disulfide (GSH-GSSG) couple is the most abundant intracellular redox couple. A GSH redox potential can be...
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11-22-2015 03:54 PM
Direct structural evidence of protein redox regulation obtained by in-cell NMR
Direct structural evidence of protein redox regulation obtained by in-cell NMR
Publication date: Available online 14 November 2015
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Eleonora Mercatelli, Letizia Barbieri, Enrico Luchinat, Lucia Banci</br>
The redox properties of cellular environments are critical to many functional processes, and are strictly controlled in all living organisms. The glutathione-glutathione disulfide (GSH-GSSG) couple is the most abundant intracellular redox couple. A GSH redox potential can be...
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11-17-2015 02:57 PM
[NMR paper] Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Biochim Biophys Acta. 1997 Mar 15;1334(2-3):117-22
Authors: Yoshida T, Tanaka M, Mori Y, Ueda I
An obvious difficulty of the study of binding of volatile anesthetics to proteins is to prevent loss of the ligand during the procedure. A novel NMR tube was designed that...