Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Rajiah Aldrin Denny"'
Autor:
Rajiv Gandhi Govindaraj, Sundar Thangapandian, Michael Schauperl, Rajiah Aldrin Denny, David J. Diller
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2023)
Interest in exploiting allosteric sites for the development of new therapeutics has grown considerably over the last two decades. The chief driving force behind the interest in allostery for drug discovery stems from the fact that in comparison to or
Externí odkaz:
https://doaj.org/article/48fdad24dd4041ffbd38fe6999da2e79
Autor:
Matthew P. Harrigan, Keri A. McKiernan, Veerabahu Shanmugasundaram, Rajiah Aldrin Denny, Vijay S. Pande
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
Abstract Two-pore domain potassium (K2P) channel ion conductance is regulated by diverse stimuli that directly or indirectly gate the channel selectivity filter (SF). Recent crystal structures for the TREK-2 member of the K2P family reveal distinct
Externí odkaz:
https://doaj.org/article/dd1ffd3260654a00bc7579dd22c01274
Autor:
Michael Schauperl, Rajiah Aldrin Denny
Publikováno v:
Journal of Chemical Information and Modeling. 62:3142-3156
Proteins are the molecular machinery of the human body, and their malfunctioning is often responsible for diseases, making them crucial targets for drug discovery. The three-dimensional structure of a protein determines its biological function, its c
Autor:
Annette N. Chiang, Disha Joshi, Peter Wipf, Mads B. Larsen, Raymond A. Frizzell, Jeffrey L. Brodsky, Clare Hill, Jennifer L. Goeckeler-Fried, Rajiah Aldrin Denny, Eric J. Sorscher
Publikováno v:
Bioorg Med Chem Lett
A growing number of diseases are linked to the misfolding of integral membrane proteins, and many of these proteins are targeted for ubiquitin-proteasome-dependent degradation. One such substrate is a mutant form of the Cystic Fibrosis Transmembrane
Autor:
Dafydd R. Owen, Aiping Dong, Martin James Wythes, Steven Kennedy, Dalia Barsyte-Lovejoy, Matthieu Schapira, Hong Wu, Rajiah Aldrin Denny, Viacheslav V. Trush, Mihir D. Parikh, Agustin Casimiro-Garcia, Renato Ferreira de Freitas, Masoud Vedadi, Magdalena Swewczyk, Hong Zeng, Tatlock John H, Fengling Li, Alexandria P. Taylor, Robert Arnold Kumpf, Peter Brown, Cheryl H. Arrowsmith
Publikováno v:
Journal of medicinal chemistry. 62(17)
The first chemical probe to primarily occupy the co-factor binding site of a Su(var)3-9, enhancer of a zeste, trithorax (SET) domain containing protein lysine methyltransferase (PKMT) is reported. Protein methyltransferases require S-adenosylmethioni
Publikováno v:
Journal of Computational Chemistry. 38:1238-1251
Accurate and rapid estimation of relative binding affinities of ligand-protein complexes is a requirement of computational methods for their effective use in rational ligand design. Of the approaches commonly used, free energy perturbation (FEP) meth
Publikováno v:
Journal of Chemical Information and Modeling. 56:1936-1949
The binding affinities (IC50) reported for diverse structural and chemical classes of human β-secretase 1 (BACE-1) inhibitors in literature were modeled using multiple in silico ligand based modeling approaches and statistical techniques. The descri
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Bruton tyrosine kinase (BTK) is a key enzyme in B-cell development whose improper regulation causes severe immunodeficiency diseases. Design of selective BTK therapeutics would benefit from improved, in-silico structural modeling of the kinase’s so
Autor:
Keri A. McKiernan, Veerabahu Shanmugasundaram, Rajiah Aldrin Denny, Matthew P. Harrigan, Vijay S. Pande
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
Two-pore domain potassium (K2P) channel ion conductance is regulated by diverse stimuli that directly or indirectly gate the channel selectivity filter (SF). Recent crystal structures for the TREK-2 member of the K2P family reveal distinct “up” a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e1908b0affdea1e3d57e5b900dd83a9
https://doi.org/10.1101/092155
https://doi.org/10.1101/092155
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 23(7):1935-1944
Protein misfolding is an emerging field that crosses multiple therapeutic areas and causes many serious diseases. As the biological pathways of protein misfolding become more clearly elucidated, small molecule approaches in this arena are gaining inc