[NMR paper] A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
Related ArticlesA Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
ChemMedChem. 2017 Sep 07;12(17):1458-1463
Authors: Dalvit C, Santi S, Neier R
Abstract
Over the years a significant amount of effort has been put into the development of rapid and reliable methods to monitor the aggregation dynamics of the ?1-42 amyloid peptide in real time. We present an alternative approach based on a suitable reporter or spy molecule and three different NMR experiments: WaterLOGSY, (1) H selective T1 filter, and (19) F T2 filter, for monitoring the initial self-aggregation process kinetics of the ?1-42 amyloid peptide and identifying molecules that retard or accelerate the self-aggregation process. Although the proposed method is not a high-throughput assay, it avoids problems associated with interference events that are sometimes observed in fluorescence-based assays.
Identification of Two Secondary Ligand Binding Sites in 14-3-3 Proteins Using Fragment Screening
Identification of Two Secondary Ligand Binding Sites in 14-3-3 Proteins Using Fragment Screening
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00153/20170721/images/medium/bi-2017-00153s_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00153
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07-22-2017 05:57 AM
[NMR paper] Identification of Small-Molecule Inhibitors of the HuR/RNA Interaction Using a Fluorescence Polarization Screening Assay Followed by NMR Validation.
Identification of Small-Molecule Inhibitors of the HuR/RNA Interaction Using a Fluorescence Polarization Screening Assay Followed by NMR Validation.
Related Articles Identification of Small-Molecule Inhibitors of the HuR/RNA Interaction Using a Fluorescence Polarization Screening Assay Followed by NMR Validation.
PLoS One. 2015;10(9):e0138780
Authors: Wang Z, Bhattacharya A, Ivanov DN
Abstract
The human antigen R (HuR) stabilizes many mRNAs of proto-oncogene, transcription factors, cytokines and growth factors by recognizing...
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09-22-2015 06:40 PM
[NMR paper] High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
J Agric Food Chem. 2014 Jun 18;62(24):5595-602
Authors: Kongstad KT, Wubshet SG, Johannesen A, Kjellerup L, Winther AM, Jäger AK, Staerk D
...
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04-14-2015 01:24 PM
[NMR paper] Structure-based drug design: NMR-based approach for ligand-protein interactions.
Structure-based drug design: NMR-based approach for ligand-protein interactions.
Related Articles Structure-based drug design: NMR-based approach for ligand-protein interactions.
Drug Discov Today Technol. 2006;3(3):241-5
Authors: Zhang X, Tang H, Ye C, Liu M
Abstract
The realization of the powerfulness in analyzing ligand-protein interactions at the atomic resolution has made NMR techniques increasingly attractive in drug discovery and development. With some significant new method developments during the past few years,...
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07-06-2014 08:28 PM
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
J Biol Chem. 2014 Apr 4;289(14):9998-10010
Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
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05-31-2014 01:57 PM
[NMR paper] Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
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 Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
Biomed Chromatogr. 2013 Feb;27(2):148-55
Authors: Tao Y, Zhang Y, Cheng Y, Wang Y
...
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06-05-2013 06:53 PM
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Curr Protein Pept Sci. 2011 Feb 24;
Authors: Orcellet ML, Fernández CO
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a...
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02-26-2011 11:56 AM
[NMR paper] Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Related Articles Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors.
Chembiochem. 2005 Sep;6(9):1607-10
Authors: Jahnke W, Blommers MJ, Fernández C, Zwingelstein C, Amstutz R