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In this paper we describe a new methodology, which was applied to the creation of a glycopeptide library used to probe binding to MHC II proteins and subsequent T-cell activation in in vitro model systems of human and murine autoimmune arthritis.
He and Ma conjugated 4-amino-phenylarsine 4-amino-phenylarsine 4-amino-phenylarsineds, which were used toxidebe binding of arsenic to Kelch-like ECH-Affigeltod protein 1 (Keap1), nuclear factor erythroid 2-related factor 2 (Nrf2), and the carboxyl half of makel-activated transcriPAOon faffinity(MTF1).
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Docking of serotonin, palonosetron and granisetron into these binding interfaces was used to probe the binding characteristics of palonosetron (Fig. 1), with the aim of providing a viable explanation for the higher efficacy of palonosetron, as well as investigating the allosteric binding and positive cooperativity.
Protein structure prediction codes based on the associative memory Hamiltonian were used to probe the binding modes between the nuclear localization signal (NLS) polypeptide of NF-κB and the inhibitors IκBα and IκBβ.
High-resolution footprinting by RNases A and CV1 has been used to probe the binding to 5 S RNA of three TFIIIA peptides Tf 1-6), Tf 4-6) and Tf 4-7), consisting of fingers 1 to 6, 4 to 6, and 4 to 7, respectively, and of full-length TFIIIA.
Both AII and [Y]-AII were used to probe the binding pocket of AT2R and its variants.
Using standard methods, resonances from 75% of the SwH-NOX residues (∼140 residues) could be assigned, and these assignments were used to probe the binding of SwHaCE.
Herein we show that NH4+ can be used to probe K+ binding sites in medium-sized enzymes (>40 kDa) by NMR spectroscopy.
Microarrays with isoenergetic pentamer and hexamer 2′- O-methyl oligonucleotide probes with LNA (locked nucleic acid) and 2,6-diaminopurine substitutions were used to probe the binding sites on the RNase P RNA specificity domain of Bacillus subtilis.
To glean further molecular insight into the UP1 SL3ESS3 binding mechanism, saturation transfer difference NMR (STD-NMR) was used to probe the SL3ESS3 binding epitopes.
The promoter region of vraFG (P vraFG ), spanning between +28 to -168 with respect to the transcription start site, was amplified and used to probe the DNA-binding activity of GraR.
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