From venom peptides to a potential diabetes treatment
Jazyk angličtina Země Velká Británie, Anglie Médium electronic
Typ dokumentu časopisecké články, komentáře
PubMed
30747103
PubMed Central
PMC6372278
DOI
10.7554/elife.44829
PII: 44829
Knihovny.cz E-zdroje
- Klíčová slova
- biochemistry, chemical biology, cone snail, diabetes, hypoglycemic shock, insulin, receptors, venom,
- MeSH
- diabetes mellitus * MeSH
- jedy měkkýšů MeSH
- ligandy MeSH
- obratlovci MeSH
- peptidy MeSH
- receptor inzulinu MeSH
- živočišné jedy * MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- komentáře MeSH
- Názvy látek
- jedy měkkýšů MeSH
- ligandy MeSH
- peptidy MeSH
- receptor inzulinu MeSH
- živočišné jedy * MeSH
Cone snails have evolved a variety of insulin-like molecules that may help with the development of better treatments for diabetes.
Zobrazit více v PubMed
Ahorukomeye A, Disotuar MM, Gajewiak J, Karanth S, Watkins M, Robinson SD, Salcedo P, Smith NA, Smith BJ, Schlegel A, Forbes BE, Olivera B, Chou DH, Safavi-Hemami H. Fish-hunting cone snail venoms are a rich source of minimized ligands of the vertebrate insulin receptor. eLife. 2019;8:e 41574. doi: 10.7554/eLife.41574. PubMed DOI PMC
Baker EN, Blundell TL, Cutfield JF, Cutfield SM, Dodson EJ, Dodson GG, Hodgkin DM, Hubbard RE, Isaacs NW, Reynolds CD. The structure of 2zn pig insulin crystals at 1.5 Å resolution. Philosophical Transactions of the Royal Society of London B, Biological Sciences. 1988;319:369–456. doi: 10.1098/rstb.1988.0058. PubMed DOI
De Meyts P. Insulin/receptor binding: the last piece of the puzzle? BioEssays. 2015;37:389–397. doi: 10.1002/bies.201400190. PubMed DOI
Herring R, Jones RH, Russell-Jones DL. Hepatoselectivity and the evolution of insulin. Diabetes, Obesity and Metabolism. 2014;16:1–8. doi: 10.1111/dom.12117. PubMed DOI
Herring R, Russell-Jones DDL. Lessons for modern insulin development. Diabetic Medicine. 2018;35:1320–1328. doi: 10.1111/dme.13692. PubMed DOI
Menting JG, Whittaker J, Margetts MB, Whittaker LJ, Kong GK, Smith BJ, Watson CJ, Záková L, Kletvíková E, Jiráček J, Chan SJ, Steiner DF, Dodson GG, Brzozowski AM, Weiss MA, Ward CW, Lawrence MC. How insulin engages its primary binding site on the insulin receptor. Nature. 2013;493:241–245. doi: 10.1038/nature11781. PubMed DOI PMC
Menting JG, Yang Y, Chan SJ, Phillips NB, Smith BJ, Whittaker J, Wickramasinghe NP, Whittaker LJ, Pandyarajan V, Wan Z-l, Yadav SP, Carroll JM, Strokes N, Roberts CT, Ismail-Beigi F, Milewski W, Steiner DF, Chauhan VS, Ward CW, Weiss MA, Lawrence MC. Protective hinge in insulin opens to enable its receptor engagement. PNAS. 2014;111:E3395–E3404. doi: 10.1073/pnas.1412897111. PubMed DOI PMC
Menting JG, Gajewiak J, MacRaild CA, Chou DH, Disotuar MM, Smith NA, Miller C, Erchegyi J, Rivier JE, Olivera BM, Forbes BE, Smith BJ, Norton RS, Safavi-Hemami H, Lawrence MC. A minimized human insulin-receptor-binding motif revealed in a Conus geographus venom insulin. Nature Structural & Molecular Biology. 2016;23:916–920. doi: 10.1038/nsmb.3292. PubMed DOI
Scapin G, Dandey VP, Zhang Z, Prosise W, Hruza A, Kelly T, Mayhood T, Strickland C, Potter CS, Carragher B. Structure of the insulin receptor-insulin complex by single-particle cryo-EM analysis. Nature. 2018;556:122–125. doi: 10.1038/nature26153. PubMed DOI PMC
Weis F, Menting JG, Margetts MB, Chan SJ, Xu Y, Tennagels N, Wohlfart P, Langer T, Müller CW, Dreyer MK, Lawrence MC. The signalling conformation of the insulin receptor ectodomain. Nature Communications. 2018;9:4420. doi: 10.1038/s41467-018-06826-6. PubMed DOI PMC
Zaykov AN, Mayer JP, DiMarchi RD. Pursuit of a perfect insulin. Nature Reviews Drug Discovery. 2016;15:425–439. doi: 10.1038/nrd.2015.36. PubMed DOI