Highly Charged Proteins and Their Repulsive Interactions Antagonize Biomolecular Condensation

Autor: Cheng Tan, Ai Niitsu, Yuji Sugita

Publikováno v: JACS Au. 3:834-848

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d56c62a3a616b00fcd0357cb9174d5d6
https://doi.org/10.1021/jacsau.2c00646

Repulsive interaction and secondary structure of highly charged proteins in regulating biomolecular condensation

Autor: Cheng Tan, Ai Niitsu, Yuji Sugita

Biomolecular condensation is involved in various cellular processes both functional and dysfunctional. Regulation of the condensation is thus crucial to avoid pathological protein aggregation and to maintain stable cellular environments. Recently, a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dfed291494a25070cc7e035d13e6f911
https://doi.org/10.1101/2022.11.16.516834

Constructing ion channels from water-soluble α-helical barrels

Autor: Kozhinjampara R. Mahendran, William M. Dawson, Mark I. Wallace, Jason T. Sengel, Adrian J. Mulholland, William F. DeGrado, Hagan Bayley, Lijun Liu, R. Leo Brady, Eric J. M. Lang, Ai Niitsu, Alistair J. Scott, Derek N. Woolfson, Marco Mravic, Andrew R. Thomson, Huong T. Kratochvil

Publikováno v: Scott, A J, Niitsu, A, Lang, E J M, Dawson, W M, Brady, R L, Mulholland, A J & Woolfson, D N 2021, ' Constructing ion channels from water-soluble α-helical barrels ', Nature Chemistry, vol. 13, no. 7, pp. 643-650 . https://doi.org/10.1038/s41557-021-00688-0

The design of peptides that assemble in membranes to form functional ion channels is challenging. Specifically, hydrophobic interactions must be designed between the peptides and at the peptide–lipid interfaces simultaneously. Here, we take a multi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37756b89f736b22f8a11bd297b48bcde
https://doi.org/10.1038/s41557-021-00688-0

Veratridine binding to a transmembrane helix of sodium channel Nav1.4 determined by solid-state NMR

Autor: Keisuke Ikeda, Kazuo Tachibana, Ai Niitsu, Ayako Egawa, Toshimichi Fujiwara

Publikováno v: Bioorganic & Medicinal Chemistry. 26:5644-5653

The multi-step ligand action to a target protein is an important aspect when understanding mechanisms of ligand binding and discovering new drugs. However, structurally capturing such complex mechanisms is challenging. This is particularly true for i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::19f3c54c323998471ac7f4147f931449
https://doi.org/10.1016/j.bmc.2018.10.012

De Novo Prediction of Binders and Nonbinders for T4 Lysozyme by gREST Simulations

Autor: Hiraku Oshima, Motoshi Kamiya, Yuji Sugita, Suyong Re, Ai Niitsu

Publikováno v: Journal of chemical information and modeling. 59(9)

Molecular recognition underpins all specific protein-ligand interactions and is essential for biomolecular functions. The prediction of canonical binding poses and distinguishing binders from nonbinders are much sought after goals. Here, we apply the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46ffcee4750fcb02cdb67a6e88fb29f9
https://pubmed.ncbi.nlm.nih.gov/31390205