Predicting protein targets for drug-like compounds using transcriptomics.

Autor: Nicolas A Pabon, Yan Xia, Samuel K Estabrooks, Zhaofeng Ye, Amanda K Herbrand, Evelyn Süß, Ricardo M Biondi, Victoria A Assimon, Jason E Gestwicki, Jeffrey L Brodsky, Carlos J Camacho, Ziv Bar-Joseph

Publikováno v: PLoS Computational Biology, Vol 14, Iss 12, p e1006651 (2018)

An expanded chemical space is essential for improved identification of small molecules for emerging therapeutic targets. However, the identification of targets for novel compounds is biased towards the synthesis of known scaffolds that bind familiar

Externí odkaz: https://doaj.org/article/34634c75dc7c43d1b7435c229390e398

Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells

Autor: Silvia Rinaldi, Victoria A. Assimon, Szu Yu Kuo, Giulia Morra, Giorgio Colombo, Hao Shao, Keith D. Green, Zapporah T. Young, Sylvie Garneau-Tsodikova, Isabelle R. Taylor, Xiaokai Li, Jason E. Gestwicki, Daniel Nguyen

Publikováno v: Chemical science (Camb. 2010. Print) 11 (2020): 1892–1904. doi:10.1039/c9sc04284a
info:cnr-pdr/source/autori:Taylor I.R.; Assimon V.A.; Kuo S.Y.; Rinaldi S.; Li X.; Young Z.T.; Morra G.; Green K.; Nguyen D.; Shao H.; Garneau-Tsodikova S.; Colombo G.; Gestwicki J.E./titolo:Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells/doi:10.1039%2Fc9sc04284a/rivista:Chemical science (Camb. 2010. Print)/anno:2020/pagina_da:1892/pagina_a:1904/intervallo_pagine:1892–1904/volume:11
Chemical science, vol 11, iss 7
Chemical Science

Understanding the selectivity of a small molecule for its target(s) in cells is an important goal in chemical biology and drug discovery. One powerful way to address this question is with dominant negative (DN) mutants, in which an active site residu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57760f8b903fe9bfc56ae9186f307a38
https://publications.cnr.it/doc/437271

Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy

Autor: Atta Ahmad, Bryan M. Dunyak, Misol Ahn, Chad A. Dickey, Jennifer N. Rauch, Victoria A. Assimon, Umesh K. Jinwal, Erik R. P. Zuiderweg, Sharan R. Srinivasan, George A. Carlson, Zapporah T. Young, Xiaokai Li, Jason E. Gestwicki

Publikováno v: Cell chemical biology, vol 23, iss 8

Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates the turnover of some proteins (termed “clients”) by linking them to the degradation pathways. This activity is critical to normal protein homeostasis, yet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e38cfa03e80d43361d88f38e0f7265
https://doi.org/10.1016/j.chembiol.2016.04.014

High-throughput screen for inhibitors of protein–protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex

Autor: Tomoko Komiyama, Isabelle R. Taylor, Hao Shao, Xu Ran, Chakrapani Kalyanaraman, Bryan M. Dunyak, Jennifer N. Rauch, Jason E. Gestwicki, Victoria A. Assimon, Erik R. P. Zuiderweg, Matthew P. Jacobson

Publikováno v: The Journal of biological chemistry, vol 293, iss 11

Protein-protein interactions (PPIs) are an important category of putative drug targets. Improvements in high-throughput screening (HTS) have significantly accelerated the discovery of inhibitors for some categories of PPIs. However, methods suitable

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::049e20459c02218650c0740e8072ffe5
https://europepmc.org/articles/PMC5857975/

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation

Autor: Daniel R. Southworth, Jason E. Gestwicki, Victoria A. Assimon

Publikováno v: Biochemistry, vol 54, iss 48

Heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) require the help of tetratricopeptide repeat (TPR) domain-containing cochaperones for many of their functions. Each monomer of Hsp70 or Hsp90 can interact with only a single TPR cochaper

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12eee7c412391b5b9ecbb09c549c7fe5
https://pubmed.ncbi.nlm.nih.gov/26565746