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A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase
The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been
Structural basis for telmisartan-mediated partial activation of PPAR gamma
Crystallographic analysis revealed that telmisartan exhibits an unexpected binding mode in which the central benzimidazole ring is engaged in a non-canonical—and suboptimal—hydrogen-bonding network around helix 12 (H12).
Coumarin and chromen-4-one analogues as tautomerase inhibitors of macrophage migration inhibitory factor: discovery and X-ray crystallography.
To the knowledge, these compounds are the most potent tautomerase inhibitors of MIF.
Structural Basis for the Interaction of CCR5 with a Small Molecule, Functionally Selective CCR5 Agonist
A novel small molecule, functionally selective CCR5 agonist, 2,2-dichloro-1-(triphenylphosphonio)vinyl formamide perchlorate (YM-370749), down-modulates CCR 5 from the cell surface without inducing a chemotactic response and inhibits HIV-1 replication.
Computational Insights into Binding of Bisphosphates to Farnesyl Pyrophosphate Synthase
The FMO result revealed that not only hydrogen bond and electrostatic interaction but also CH-O and π-π interaction with FPPS are important for N-BP’s potency, and the structure-activity relationship (SAR) of the series of minodronate derivatives is discussed.
Distinct Properties of Telmisartan on Agonistic Activities for Peroxisome Proliferator-Activated Receptor γ among Clinically Used Angiotensin II Receptor Blockers: Drug-Target Interaction Analyses
Telmisartan superbly activates PPARγ among the ARBs tested, thereby providing a fresh avenue for treating hypertensive patients with metabolic derangement and demonstrating the highest affinity of binding forPPARγ as well as the highest cell permeability.
High-resolution NMR study of a synthetic oligoribonucleotide with a tetranucleotide GAGA loop that is a substrate for the cytotoxic protein, ricin.
The overall structure of the GAGA loop is similar to the GAAA and GCAA loops that have been described but that are not recognized by ricin, and the neighboring guanosine on the 3' side (7G) may also play a role in the recognition mechanism together with 5G and 8A.
Novel 7H-pyrrolo[2,3-d]pyrimidine derivatives as potent and orally active STAT6 inhibitors.