Results 21 to 30 of about 3,672,982 (262)
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.
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The Protein Folding Network [PDF]
Journal of Molecular Biology, 2004 The conformation space of a 20-residue antiparallel $β$-sheet peptide, sampled by molecular dynamics simulations, is mapped to a network. Conformations are nodes of the network, and the transitions between them are links. The conformation space network describes the significant free energy minima and their dynamic connectivity without projections into ...
Rao F, Caflisch A
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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
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Protein GB1 folding and assembly from structural elements. [PDF]
, 2009 Folding of the Protein G B1 domain (PGB1) shifts with increasing salt concentration from a cooperative assembly of inherently unstructured subdomains to an assembly of partly pre-folded structures.
Xue, Wei-Feng +10 more
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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
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Folding nuclei in proteins [PDF]
FEBS Letters, 2001 When a protein folds or unfolds, it passes through many half‐folded microstates. Only a few of them can accumulate and be seen experimentally, and this happens only when the folding (or unfolding) occurs far from the point of thermodynamic equilibrium between the native and denatured states.
Galzitskaya, Oxana V +2 more
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Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
EMBO Molecular Medicine, 2015 The cellular prion protein (PrPC) comprises a natively unstructured N‐terminal domain, including a metal‐binding octarepeat region (OR) and a linker, followed by a C‐terminal domain that misfolds to form PrPSc in Creutzfeldt‐Jakob disease.
Agnes Lau +19 more
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Without magic bullets: the biological basis for public health interventions against protein folding disorders [PDF]
, 2010 Protein folding disorders of aging like Alzheimer's and Parkinson's diseases currently present intractable medical challenges. 'Small molecule' interventions - drug treatments - often have, at best, palliative impact, failing to alter
Rodrick Wallace
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Movement of Chronic Wasting Disease Prions in Prairie, Boreal and Alpine Soils
Pathogens, 2023 Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy negatively impacting cervids on three continents. Soil can serve as a reservoir for horizontal transmission of CWD by interaction with the infectious prion protein (PrPCWD) shed ...
Alsu Kuznetsova +4 more
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Protein folding on the ribosome studied using NMR spectroscopy [PDF]
, 2013 NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution.
Christodoulou, J +7 more
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