[NMR paper] Cryptophane nanoscale assemblies expand 129Xe NMR biosensing.
Cryptophane nanoscale assemblies expand 129Xe NMR biosensing.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Cryptophane nanoscale assemblies expand 129Xe NMR biosensing.
Anal Chem. 2018 May 21;:
Authors: Zemerov SD, Roose BW, Greenberg ML, Wang Y, Dmochowski IJ
Abstract
Cryptophane-based biosensors are promising agents for the ultrasensitive detection of biomedically relevant targets via 129Xe NMR. Dynamic light scattering revealed that cryptophanes...
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05-22-2018 08:59 PM
[NMR paper] Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.
Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.
Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.
FEBS Open Bio. 2018 Feb;8(2):264-270
Authors: Takada K, Amano R, Nomura Y, Tanaka Y, Sugiyama S, Nagata T, Katahira M, Nakamura Y, Kozu T, Sakamoto T
Abstract
Since the invention of systematic evolution of ligands by exponential enrichment, many short oligonucleotides (or aptamers) have been reported that can bind to a wide...
[NMR paper] NMR dispersion investigations of enzymatically degraded bovine articular cartilage.
NMR dispersion investigations of enzymatically degraded bovine articular cartilage.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR dispersion investigations of enzymatically degraded bovine articular cartilage.
Magn Reson Med. 2014 May 13;
Authors: Rössler E, Mattea C, Stapf S
Abstract
PURPOSE: Cross-relaxation of protons with (14) N nuclei in proteins enhances relaxivity in the quadrupolar dip range of...
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05-16-2014 08:06 PM
[NMR paper] NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
PLoS One. 2013;8(2):e56360
Authors: Ramm Sander P, Peer M, Grandl M, Bogdahn U, Schmitz G, Kalbitzer...
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08-29-2013 01:53 PM
[NMR paper] Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Bioorg Med Chem Lett. 2013 Jul 22;
Authors: Chu S, Gochin M
Abstract
The HIV-1 envelope glycoprotein gp41 fusion intermediate is a promising drug target for inhibiting viral entry. However, drug development has been impeded by challenges inherent in mediating the underlying protein-protein interaction. Here...
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08-13-2013 04:26 PM
[NMR paper] Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
J Am Chem Soc. 2013 Jan 29;
Authors: Arda A, Blasco P, Varon Silva D, Schubert V, André S, Bruix M, Cańada FJ, Gabius HJ, Unverzagt C, Jimenez-Barbero J
Abstract
The current surge in defining...
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02-03-2013 10:19 AM
The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method
The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method
Abstract Protein internal motions influence observables of NMR experiments. The effect of internal motions occurring at the sub-nanosecond timescale can be described by NMR order parameters. Here, we report that the use of order parameters derived from Molecular Dynamics (MD) simulations of two holo-structures of Protein Kinase A increase the discrimination power of INPHARMA, an NMR based methodology that selects docked ligand orientations by maximizing the correlation of...