期刊
DISEASE MODELS & MECHANISMS
卷 14, 期 5, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/dmm.048983
关键词
Disaggregase; Neurodegeneration; Phase transition
资金
- National Institutes of Health (NIH) [T32GM008275, F31 NS111870]
- Target ALS
- Amyotrophic Lateral Sclerosis Association
- Office of the Assistant Secretary of Defense for Health Affairs through the Amyotrophic Lateral Sclerosis Research Program [W81XWH2010242]
- G. Harold and Leila Y. Mathers Foundation
- Sanofi
- NIH [R01GM099836, R21AG061784, R21AG065854]
- U.S. Department of Defense (DOD) [W81XWH2010242] Funding Source: U.S. Department of Defense (DOD)
Neurodegenerative diseases and other protein-misfolding disorders pose a longstanding biomedical challenge, with effective therapies still largely elusive. Recent research has found that many aggregation-prone proteins can undergo liquid-liquid phase separation, forming dense condensates with liquid properties distinct from the cellular environment. Current efforts focus on utilizing proteostasis machinery to prevent and reverse pathological protein conformations.
Neurodegenerative diseases and other protein-misfolding disorders represent a longstanding biomedical challenge, and effective therapies remain largely elusive. This failure is due, in part, to the recalcitrant and diverse nature of misfolded protein conformers. Recent work has uncovered that many aggregation-prone proteins can also undergo liquid-liquid phase separation, a process by which macromolecules self-associate to form dense condensates with liquid properties that are compositionally distinct from the bulk cellular milieu. Efforts to combat diseases caused by toxic protein states focus on exploiting or enhancing the proteostasis machinery to prevent and reverse pathological protein conformations. Here, we discuss recent advances in elucidating and engineering therapeutic agents to combat the diverse aberrant protein states that underlie protein-misfolding disorders.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据