Dr SHAILESH MISTRY's Outputs (6)

Positive allosteric modulation of the muscarinic M1 receptor improves efficacy of antipsychotics in mouse glutamatergic deficit models of behavior (2016)
Journal Article
Choy, K. H., Shackleford, D. M., Malone, D. T., Mistry, S. N., Patil, R. T., Scammells, P. J., …Christopoulos, A. (2016). Positive allosteric modulation of the muscarinic M1 receptor improves efficacy of antipsychotics in mouse glutamatergic deficit models of behavior. Journal of Pharmacology and Experimental Therapeutics, 359(2), https://doi.org/10.1124/jpet.116.235788

Current antipsychotics are effective in treating the positive symptoms associated with schizophrenia, but they remain suboptimal in targeting cognitive dysfunction. Recent studies have suggested that positive allosteric modulation of the M1 muscarini... Read More about Positive allosteric modulation of the muscarinic M1 receptor improves efficacy of antipsychotics in mouse glutamatergic deficit models of behavior.

GPCRs through the keyhole: the role of protein flexibility in ligand binding to β-adrenoceptors (2016)
Journal Article
Emtage, A. L., Mistry, S. N., Fischer, P. M., Kellam, B., & Laughton, C. A. (2017). GPCRs through the keyhole: the role of protein flexibility in ligand binding to β-adrenoceptors. Journal of Biomolecular Structure and Dynamics, 35(12), 2604-2619. https://doi.org/10.1080/07391102.2016.1226197

© 2016 Informa UK Limited, trading as Taylor & Francis Group. G protein-coupled receptors (GPCRs) are proteins of pharmaceutical importance, with over 30% of all drugs in clinical use targeting them. Increasing numbers of X-ray crystal (XRC) struct... Read More about GPCRs through the keyhole: the role of protein flexibility in ligand binding to β-adrenoceptors.

The composite influence of the imidazolone moiety of CGP 12177 on its affinity and efficacy at the two conformations of the human β1-adrenoceptor (2016)
Presentation / Conference Contribution
Mistry, S. N., & Baker, J. G. (2016). The composite influence of the imidazolone moiety of CGP 12177 on its affinity and efficacy at the two conformations of the human β1-adrenoceptor.

The effect of the N-alkyl moiety on the interaction of pindolol analogues with the two agonist conformations of the human β1-adrenoceptor (2016)
Presentation / Conference Contribution
Mistry, S. N., & Baker, J. G. (2016). The effect of the N-alkyl moiety on the interaction of pindolol analogues with the two agonist conformations of the human β1-adrenoceptor.

Novel Fused Arylpyrimidinone Based Allosteric Modulators of the M1 Muscarinic Acetylcholine Receptor. (2016)
Journal Article
Scammells, P. J., Lane, J. R., Mistry, S. N., Lim, H., Jörg, M., Capuano, B., …Scammells, P. J. (2016). Novel Fused Arylpyrimidinone Based Allosteric Modulators of the M1 Muscarinic Acetylcholine Receptor. ACS Chemical Neuroscience, 7(5), 647-661. https://doi.org/10.1021/acschemneuro.6b00018

Benzoquinazolinone 1 is a positive allosteric modulator (PAM) of the M1 muscarinic acetylcholine receptor (mAChR), which is significantly more potent than the prototypical PAM, 1-(4-methoxybenzyl)-4-oxo-1,4-dihydroquinoline-3-carboxylic acid (BQCA).... Read More about Novel Fused Arylpyrimidinone Based Allosteric Modulators of the M1 Muscarinic Acetylcholine Receptor..

Potent dual inhibitors of Plasmodium falciparum M1 and M17 aminopeptidases through optimization of S1 pocket interactions (2016)
Journal Article
Drinkwater, N., Vinh, N. B., Mistry, S. N., Bamert, R. S., Ruggeri, C., Holleran, J. P., …Scammells, P. J. (2016). Potent dual inhibitors of Plasmodium falciparum M1 and M17 aminopeptidases through optimization of S1 pocket interactions. European Journal of Medicinal Chemistry, 110, 43-64. https://doi.org/10.1016/j.ejmech.2016.01.015

© 2016 Elsevier Masson SAS. Malaria remains a global health problem, and though international efforts for treatment and eradication have made some headway, the emergence of drug-resistant parasites threatens this progress. Antimalarial therapeutics a... Read More about Potent dual inhibitors of Plasmodium falciparum M1 and M17 aminopeptidases through optimization of S1 pocket interactions.