Ubiquitylation, the modification of proteins by ubiquitin (Ub), is one of the most prevalent and versatile post-translational modifications in eukaryotic cells. As Ub also serves as its own substrate, proteins can be modified by numerous different Ub chains, in which the individual moieties are linked via one or several of the seven lysines of Ub. Homogeneous Ub chains, in which the moieties are sequentially linked via the same residue, have been most extensively studied. Yet, due to their restricted availability, the functions of Ub chains linked via K27, K29 or K33 are poorly understood. We have developed an approach that, for the first time, allows the generation of all seven homogeneous Ub chains in large quantities. We show that the chains enable the identification of Ub chain binding proteins by affinity-based proteomics. The potential of our approach is demonstrated by the identification of previously unknown interaction partners of K27-, K29-, and K33-linked Ub chains.
[NMR paper] NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules.
NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules.
Prog Nucl Magn Reson Spectrosc. 2016 Nov;97:82-125
Authors: Gossert AD, Jahnke W
Abstract
Protein-ligand interactions are at the heart of drug discovery...
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11-29-2016 12:57 AM
NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules
NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules
Publication date: November 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 97</br>
Author(s): Alvar D. Gossert, Wolfgang Jahnke</br>
Protein-ligand interactions are at the heart of drug discovery research. NMR spectroscopy is an excellent technology to identify and validate protein-ligand interactions. A plethora of NMR methods are available which are powerful, robust and information-rich, but also have pitfalls...
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11-19-2016 08:35 PM
[NMR paper] High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
Related Articles High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
Subcell Biochem. 2015;72:199-214
Authors: Kitahara R
Abstract
High-pressure nuclear magnetic resonance (NMR) spectroscopy has revealed that ubiquitin has at least two high-energy states - an alternatively folded state N2 and a locally disordered state I - between the basic folded state N1 and totally unfolded U...
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07-16-2015 11:21 AM
[NMR paper] NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR identification of endogenous metabolites interacting with fatted and non-fatted human serum albumin in blood plasma: Fatty acids influence the HSA-metabolite interaction.
J Magn Reson. 2013 Jan 8;228C:81-94
Authors: Jupin M, Michiels PJ, Girard FC, Spraul M,...
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02-03-2013 10:19 AM
NMR Identification of Endogenous Metabolites interacting with Fatted and Non-Fatted Human Serum Albumin in Blood Plasma: Fatty Acids influence the HSA-Metabolite Interaction
NMR Identification of Endogenous Metabolites interacting with Fatted and Non-Fatted Human Serum Albumin in Blood Plasma: Fatty Acids influence the HSA-Metabolite Interaction
Available online 8 January 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Metabolites and their concentrations are direct reporters on body biochemistry. Thanks to technical developments metabolic profiling of body fluids, such as blood plasma, by for instance NMR has in the past decade become increasingly accurate enabling successful clinical diagnostics. Human Serum...
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01-09-2013 10:01 AM
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
Abstract Ubiquitin is a post-translational modifier that is involved in cellular functions through its covalent attachment to target proteins. Ubiquitin can also be conjugated to itself at seven lysine residues and at its amino terminus to form eight linkage-specific polyubiquitin chains for individual cellular processes. The Lys63-linked polyubiquitin chain is recognized by tandem ubiquitin-interacting motifs (tUIMs) of Rap80 for the regulation of DNA repair. To understand the...
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02-25-2012 12:16 AM
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Solid State Nucl Magn Reson. 2011 Mar 23;
Authors: Mao Y, Jeong M, Wang T, Ba Y
Antifreeze proteins (AFPs) provide survival mechanism for species living in subzero environments by lowering the freezing points of their...
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[NMR paper] Calbindin D28K interacts with Ran-binding protein M: identification of interacting do
Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Related Articles Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92
Authors: Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R
Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts...
Identification of Ubiquitin Chain Interacting Proteins
Linear Mode
