Results 31 to 40 of about 6,813,928 (408)
The Standard Scrapie Cell Assay: Development, Utility and Prospects
Viruses, 2015 Prion diseases are a family of fatal neurodegenerative diseases that involve the misfolding of a host protein, PrPC. Measuring prion infectivity is necessary for determining efficacy of a treatment or infectivity of a prion purification procedure; animal
Jacques van der Merwe +3 more
doaj +1 more source
Seizures are a druggable mechanistic link between TBI and subsequent tauopathy
eLife, 2021 Traumatic brain injury (TBI) is a prominent risk factor for dementias including tauopathies like chronic traumatic encephalopathy (CTE). The mechanisms that promote prion-like spreading of Tau aggregates after TBI are not fully understood, in part due to
Hadeel Alyenbaawi +8 more
doaj +1 more source
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis [PDF]
, 1989 Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides.
Hartl, Franz-Ulrich +3 more
core +1 more source
Journal of Nanobiotechnology, 2023 Evidence suggests that increased level/aggregation of β-amyloid (Aβ) peptide, together with enhanced phosphorylation/aggregation of tau protein, play a critical role in the development of Alzheimer’s disease (AD), the leading cause of dementia in the ...
Karthivashan Govindarajan +1 more
doaj +1 more source
Effect of protein structure on evolution of cotranslational folding [PDF]
, 2020 Cotranslational folding depends on the folding speed and stability of the nascent protein. It remains difficult, however, to predict which proteins cotranslationally fold. Here, we simulate evolution of model proteins to investigate how native structure influences evolution of cotranslational folding.
arxiv +1 more source
Journal of Cellular and Molecular Medicine, 2003 AbstractThe problem of protein folding is that how proteins acquire their native unique three‐dimensional structure in the physiological milieu. To solve the problem, the following key questions should be answered: do proteins fold co‐ or post‐translationally, i.e.
openaire +2 more sources
Progress in Nuclear Magnetic Resonance Spectroscopy, 2017 Protein folding is a highly complex process proceeding through a number of disordered and partially folded nonnative states with various degrees of structural organization. These transiently and sparsely populated species on the protein folding energy landscape play crucial roles in driving folding toward the native conformation, yet some of these ...
Anastasia Zhuravleva, Dmitry M. Korzhnev
openaire +2 more sources
Friends in need: how chaperonins recognize and remodel proteins that require folding assistance [PDF]
Front. Mol. Biosci. (2022) 9:1071168, 2022 Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the bacterial proteome.
arxiv +1 more source
, 2020 The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE, respectively). The Hsp70 system prevents protein aggregation and increases folding yields.
Balchin, D. +3 more
core +1 more source
Highly accurate protein structure prediction with AlphaFold
Nature, 2021 Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function. Through an enormous experimental effort1–4, the structures of around 100,000 unique proteins have been determined5, but this ...
J. Jumper +33 more
semanticscholar +1 more source