Results 101 to 110 of about 69,500 (311)
The power of many: when genetics met yeasts and high‐throughput
Biological Reviews, EarlyView.ABSTRACT In recent years, complex technological capabilities have evolved, driven by the need to solve complex and integrative biological questions through global analyses. New equipment allows the scaling up and automation of processes which previously were carried out on a very limited scale.
Víctor A. Tallada, Víctor Carranco
wiley +1 more source
Acta Neuropathologica CommunicationsCultured brain slices rapidly replicate murine prions, exhibit prion pathology, and are amenable towards drug discovery, but have not been infected with human prions.
Jessy A. Slota +9 more
doaj +1 more source
DL-3-n-Butylphthalide Protects Against PrP<sup>106</sup> <sup>-126</sup>-Induced Neurotoxicity Through NRF2 Signaling and OPA1/DRP1-Mediated Mitochondrial Dynamics. [PDF]
CNS Neurosci TherNBP counteracts PrP106‐126‐induced neurotoxicity by activating NRF2 and restoring OPA1/DRP1‐mediated mitochondrial dynamics. It suppresses oxidative stress and preserves mitochondrial function and bioenergetics. These actions support NBP as a promising therapeutic candidate for prion‐related neurodegeneration.
Wu W, Zhang X, Jiang M, Ma N.
europepmc +2 more sources
Aspects of prion protein dynamics in cell culture models.
, 2005 The cell biology of Prion formation and transfer is not well understood. In order to further elucidate the dynamics of PrPc and PrPsc in a cellular context, fusions between Green Fluorescent Protein (GFP) and PrP were constructed and infected/uninfected ...
Landy, Timothy Adam, Landy, T.A.
core
A Systematic Review on Disease‐Modifying Therapies in Parkinsonian Disorders
Clinical Pharmacology &Therapeutics, EarlyView.Parkinsonian disorders, including Parkinson's disease, Lewy body dementia, multiple system atrophy, and progressive supranuclear palsy, are progressive neurodegenerative conditions with no treatment options to slow disease progression. This systematic review provides an overview of evidence of disease‐modifying therapies that have been evaluated in ...
Pepijn P.N.M. Eijsvogel +3 more
wiley +1 more source
Prion degradation pathways: Potential for therapeutic intervention
, 2015 Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
McKinnon, C, Tabrizi, SJ, Goold, R
core
Identifying molecular determinants of prion conversion [PDF]
, 2017 Prion diseases have been widely studied, but despite many great leaps in our knowledge of prion and protein misfolding diseases in general, many gaps remain. One example is the structural triggers or provocators of prion conversion found within the prion
Pischke, Kate Elizabeth
core
, 2011 Transmissible spongiform encephalopathies (TSE), also known as prion diseases, are fatal neurodegenerative disorders present both in human and animals with different aetiology as they can occur genetically, spontaneously or by infection (Prusiner 1998 ...
Marzo, Ludovica
core
Dissection and design of yeast prions. [PDF]
, 2004 Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Cox Brian S +15 more
core +1 more source
Journal of the Chinese Chemical Society, EarlyView.While X‐ray crystallography has been the primary method for determining the structures of metalloproteins, cryoEM has taken over this role, illustrated by [4Fe4S]‐cluster containing proteins deposited in the Protein Data Bank. What will be the role for X‐ray crystallography as cryoEM and machine learning methods dominate the initial structural analysis?
Douglas C. Rees
wiley +1 more source