- 4.8Impact Factor
- 9.2CiteScore
- 20 daysTime to First Decision
Biomolecules, Volume 14, Issue 7
July 2024 - 150 articles
Cover Story: DMD4B-HYDRA simulations of oligomer formation by naturally occurring Aβ1−38, Aβ1−40, Aβ1−42, and Aβ1−43 reveal that they assemble through distinct oligomer formation pathways. Oligomers of different sizes exhibit self-similarity, yet their structure is isoform specific. While Aβ1−38 and Aβ1−40 hexamers adopt dumb-bell shapes, Aβ1−42 hexamers have a compact C-terminally stabilized core with flexible, solvent-exposed N-termini. Aβ1−42 and Aβ1−43, reported to be neurotoxic, form on average larger oligomers than presumably neuroprotective Aβ1−38 and Aβ1−40. Because larger oligomers are expected to possess an increased affinity to form water-permeable pores in a bilayer, these findings suggest that therapeutic strategies targeting oligomer size reduction will mitigate Aβ-mediated toxicity. View this paper
- Issues are regarded as officially published after their release is announced to the table of contents alert mailing list .
- You may sign up for email alerts to receive table of contents of newly released issues.
- PDF is the official format for papers published in both, html and pdf forms. To view the papers in pdf format, click on the "PDF Full-text" link, and use the free Adobe Reader to open them.
Articles
There are no articles in this issue yet.
Get Alerted
Add your email address to receive forthcoming issues of this journal.
Biomolecules - ISSN 2218-273X