[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] Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Related Articles Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Nucleic Acids Res. 2015 Jan 13;
Authors: Collins KM, Oregioni A, Robertson LE, Kelly G, Ramos A
Abstract
Defining the RNA target selectivity of the proteins regulating mRNA metabolism is a key issue in RNA biology. Here we present a novel use of principal component analysis (PCA) to extract the RNA sequence preference of RNA binding...
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01-15-2015 06:10 PM
[NMR paper] APSY-NMR for protein backbone assignment in high-throughput structural biology.
APSY-NMR for protein backbone assignment in high-throughput structural biology.
APSY-NMR for protein backbone assignment in high-throughput structural biology.
J Biomol NMR. 2014 Nov 27;
Authors: Dutta SK, Serrano P, Proudfoot A, Geralt M, Pedrini B, Herrmann T, Wüthrich K
Abstract
A standard set of three APSY-NMR experiments has been used in daily practice to obtain polypeptide backbone NMR assignments in globular proteins with sizes up to about 150 residues, which had been identified as targets for structure determination by...
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11-28-2014 11:37 AM
APSY-NMR for protein backbone assignment in high-throughput structural biology
APSY-NMR for protein backbone assignment in high-throughput structural biology
Abstract
A standard set of three APSY-NMR experiments has been used in daily practice to obtain polypeptide backbone NMR assignments in globular proteins with sizes up to about 150 residues, which had been identified as targets for structure determination by the Joint Center for Structural Genomics (JCSG) under the auspices of the Protein Structure Initiative (PSI). In a representative sample of 30 proteins, initial fully automated data analysis with the software...
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11-26-2014 10:50 PM
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...
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11-25-2010 08:21 PM
[NMR paper] Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignm
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Related Articles Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8009-14
Authors: Szyperski T, Yeh DC, Sukumaran DK, Moseley HN, Montelione GT
A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR experiments is presented for rapid and complete protein resonance assignment. Even when using short measurement times, these experiments allow one to retain...
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11-24-2010 08:49 PM
[NMR paper] Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein r
Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Related Articles Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Biochemistry. 2001 Mar 20;40(11):3282-8
Authors: Verhoeven MA, Creemers AF, Bovee-Geurts PH, De Grip WJ, Lugtenburg J, de Groot HJ
...
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11-19-2010 08:32 PM
NMR in a crystallography-based high-throughput protein structure-determination enviro
NMR in a crystallography-based high-throughput protein structure-determination environment.
Related Articles NMR in a crystallography-based high-throughput protein structure-determination environment.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1365-6
Authors: Wüthrich K
An introduction is provided to three papers which compare corresponding protein crystal and NMR solution structures determined by the Joint Center for Structural Genomics (JCSG). Special mention is made of the JCSG strategy for combined use of the two...
Quantification of Membrane Protein Self-Associationwith a High-Throughput Compatible Fluorescence Assay
Linear Mode
