Results 91 to 100 of about 202,201 (346)
Polymorphism of amyloid-ß fibrils and its effects on human erythrocyte catalase binding
The Alzheimer's amyloid-β (Aβ) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule.
Harris, J.R. +3 more
core +1 more source
Nanomechanical properties of single amyloid fibrils [PDF]
Amyloid fibrils are traditionally associated with neurodegenerative diseases like Alzheimer's disease, Parkinson's disease or Creutzfeldt-Jakob disease. However, the ability to form amyloid fibrils appears to be a more generic property of proteins. While
Bennink, Martin L. +5 more
core +1 more source
This study shows that lung adenocarcinomas exploit developmental branching morphogenesis to acquire a therapy resistant basal‐like tumour cell state. This process was found to be regulated by combined TP53 loss‐of‐function and type‐I interferon signalling, identifying a novel axis for biomarker and therapeutic target discovery.
Kamila J Bienkowska +13 more
wiley +1 more source
QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study
Self‐assembly and aggregation of human islet amyloid polypeptide (hIAPP, or amylin) into β‐sheet‐rich oligomers and fibrils have been implicated in pancreatic β‐cell dysfunction and failure, contributing to the pathogenesis of type 2 diabetes (T2D ...
María M. Tejero‐Ojeda +8 more
doaj +1 more source
Structure Damage on Cotton Fiber via Coupling Effect of Moisture Regains and Low Temperature
The most crucial variables that influence the characteristics and quality of cotton fibers during the cotton growth and ginning processes are temperature and moisture regains.
Jiqiang Cao +4 more
doaj +1 more source
Finding novel vulnerabilities of hypomorphic BRCA1 alleles
Synthetic lethality screens performed to identify novel vulnerabilities often model complete gene loss, thereby overlooking patient‐derived hypomorphic mutations. In this study, we have performed genome‐wide CRISPR screens on BRCA1 hypomorphic mutations, showing BRCA1I26A behaves like wild‐type, while BRCA1R1699Q mimics deficiency. Furthermore, we have
Anne Schreuder +10 more
wiley +1 more source
Protein droplets exhibit complex self-assembly and deposition behaviors driven by evaporation, which has attracted increasing attention in recent years.
Xuanyi Zhang +3 more
doaj +1 more source
The microenvironments of tissues or organs are complex architectures comprised of structural proteins including collagen. Particularly, the cornea is organized in a lattice pattern of collagen fibrils which play a significant role in its transparency ...
Hyeonji Kim +8 more
semanticscholar +1 more source
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs
Deposits of amyloid fibrils of α-synuclein are the histological hallmarks of Parkinson’s disease, dementia with Lewy bodies and multiple system atrophy, with hereditary mutations in α-synuclein linked to the first two of these conditions.
D. Boyer +6 more
semanticscholar +1 more source

