Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Edwin Aoraha"'
Publikováno v:
Chemical communications (Cambridge, England). 54(49)
Self-assembly of amyloid polypeptides (1) imparts biological effects depending on the size in over 20 amyloid diseases and (2) produces useful yet relatively untapped biomaterials. Unfortunately, our understanding of amyloid polypeptides, as related
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48f4cec055f2a166710b6120d711ec8a
https://pubmed.ncbi.nlm.nih.gov/29872774
https://pubmed.ncbi.nlm.nih.gov/29872774
Autor:
Brennal Pierre, Edwin Aoraha, Jin Ryoun Kim, Asher Williams, Edward Chau, Jeffrey J. Gray, Tina Xiong, Jason W. Labonte, Kazi Yasin Helal, Vandan Shah
Publikováno v:
ChemBioChem. 16:2392-2402
A universal method that improves protein stability and evolution has thus far eluded discovery. Recently, however, studies have shown that insertional fusion to a protein chaperone stabilized various target proteins with minimal negative effects. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10f8d3eec47c7f078e63d1c4299f6c2a
https://doi.org/10.1002/cbic.201500310
https://doi.org/10.1002/cbic.201500310
Publikováno v:
Molecular BioSystems. 11:2281-2289
Aggregation of β-amyloid (Aβ) is central to the pathogenesis of Alzheimer's disease (AD). Aβ aggregation produces amyloid assemblies, such as oligomers and fibrils. In contrast to non-toxic Aβ monomers, Aβ oligomers and fibrils can act directly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b974932d2f6b4d92f73ef6ff1bcba1c8
https://doi.org/10.1039/c5mb00280j
https://doi.org/10.1039/c5mb00280j