Results 151 to 160 of about 97,942 (322)
Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid–Liquid Phase Separation [PDF]
, 2021 Stella A. Polido +2 more
openalex +1 more source
Formation of Condition‐Dependent Alpha‐Synuclein Fibril Strain in Artificial Cerebrospinal Fluid
Advanced Science, Volume 13, Issue 7, 3 February 2026.α‐synuclein aggregation in artificial cerebrospinal fluid (aCSF) leads to a distinct conformation with an electron density pocket motif found in aggregates from PD and MSA patients. Such fibrils has low stability outside the reaction conditions, hinting about the influence of cerebrospinal fluid components not only on the formation, but also on the ...
Rūta Sniečkutė +7 more
wiley +1 more source
Aggregate, Volume 7, Issue 2, February 2026.Protein aggregation drives diverse degenerative diseases, yet its molecular origins are difficult to predict. SKALE uses interpretable machine learning to link sequence, structure, and dynamics, revealing how local structural weakening triggers aggregation.
Wei Xuan Wilson Loo +7 more
wiley +1 more source
A synergistic small-molecule combination directly eradicates diverse prion strain structures
, 2009 Blake E Roberts +7 more
openalex +1 more source
The extracellular regulated kinase-1 (ERK1) controls regulated α-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein. [PDF]
, 2011 Moustapha Cissé +9 more
openalex +1 more source
Proceedings of the National Academy of Sciences, 1998 D, Westaway, G, Telling, S, Priola
openaire +3 more sources
The Journal of Clinical Pharmacology, Volume 66, Issue 2, February 2026.Abstract Posdinemab, a humanized immunoglobulin G1/κ monoclonal antibody, binds with high affinity to phosphorylated tau protein which is associated with Alzheimer's disease (AD) pathophysiology. Posdinemab reduced tau seeding in murine models and was well tolerated in Phase‐1 clinical studies.
Fangfang Wang +7 more
wiley +1 more source
Heat shock protein 10 as a chaperone modulating α‐synuclein amyloid fibril formation
Protein Science, Volume 35, Issue 2, February 2026.Abstract HSP10 is a well‐known human co‐chaperone that interacts with HSP60 to comprise the HSP60/10 chaperonin complex which upholds mitochondrial proteostasis. HSP10 also demonstrates independent roles in binding to misfolded proteins and interacts with several amyloidogenic client proteins.
Johan N. K. Larsson +5 more
wiley +1 more source
Sex Effects in Mouse Prion Disease Incubation Time
, 2011 Shaheen Akhtar +4 more
openalex +2 more sources