Results 11 to 20 of about 259,716 (267)

Medium-throughput zebrafish optogenetic platform identifies deficits in subsequent neural activity following brief early exposure to cannabidiol and Δ9-tetrahydrocannabinol

open access: yesScientific Reports, 2021
In light of legislative changes and the widespread use of cannabis as a recreational and medicinal drug, delayed effects of cannabis upon brief exposure during embryonic development are of high interest as early pregnancies often go undetected.
Richard Kanyo   +6 more
doaj   +1 more source

Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity

open access: yesBioactive Materials, 2021
Evidence suggests that increased level/aggregation of beta-amyloid (Aβ) peptides initiate neurodegeneration and subsequent development of Alzheimer's disease (AD). At present, there is no effective treatment for AD. In this study, we reported the effects
Bibin G. Anand   +6 more
doaj   +1 more source

The CNS in inbred transgenic models of 4-repeat Tauopathy develops consistent tau seeding capacity yet focal and diverse patterns of protein deposition

open access: yesMolecular Neurodegeneration, 2017
Background MAPT mutations cause neurodegenerative diseases such as frontotemporal dementia but, strikingly, patients with the same mutation may have different clinical phenotypes.
Ghazaleh Eskandari-Sedighi   +11 more
doaj   +1 more source

On the kinematics of protein folding [PDF]

open access: yesJournal of Computational Chemistry, 2003
AbstractWe offer simple solutions to three kinematic problems that occur in the folding of proteins. We show how to construct suitably local elementary Monte Carlo moves, how to close a loop, and how to fold a loop without breaking the bond that closes it. © 2003 Wiley Periodicals, Inc.
Sean Cahill   +2 more
openaire   +3 more sources

The Standard Scrapie Cell Assay: Development, Utility and Prospects

open access: yesViruses, 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

The Protein Folding Network [PDF]

open access: yesJournal 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
openaire   +4 more sources

Protein folding by NMR [PDF]

open access: yesProgress 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 ...
Zhuravleva, A, Korzhnev, DM
openaire   +3 more sources

Seizures are a druggable mechanistic link between TBI and subsequent tauopathy

open access: yeseLife, 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 [PDF]

open access: yesJournal 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

Folding nuclei in proteins [PDF]

open access: yesFEBS 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
openaire   +2 more sources

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