Results 121 to 130 of about 5,604,422 (355)
Prion Protein in Glioblastoma Multiforme [PDF]
International Journal of Molecular Sciences, 2019 The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes ...
Larisa Ryskalin +6 more
openaire +3 more sources
Backbone Protecting Groups for Enhanced Peptide and Protein Synthesis
Angewandte Chemie International Edition, Accepted Article.Solid‐phase peptide synthesis has become an indispensable technique for the routine preparation of linear peptides of up to ~40 amino acids in length. However, the solid‐phase approach is still hampered by chain insolubility and aggregation, which reduces synthetic yields.
Samuel L Paravizzini +3 more
wiley +1 more source
Frontiers in Cellular Neuroscience, 2019 Prion diseases or transmissible spongiform encephalopathies are fatal, progressive, neurodegenerative, protein-misfolding disorders. Prion diseases may arise spontaneously, be inherited genetically or be acquired by infection and affect a variety of ...
Barry M. Bradford +2 more
doaj +1 more source
Glycosylphosphatidylinositols: More than just an anchor? [PDF]
, 2016 There is increasing interest in the role of glycosylphosphatidylinositol (GPI) anchors that attach some proteins to cell membranes. Far from being biologically inert, GPIs influence the targeting, intracellular trafficking and function of the attached ...
Bate, C, Nolan, W, Williams, A
core +1 more source
Physics of Protein Aggregation in Normal and Accelerated Brain Aging
BioEssays, EarlyView.Soluble monomeric proteins precipitate via nucleation into insoluble amyloids in response to age‐related exposures (e.g., microbes, nanoparticles). Persistent soluble‐to‐insoluble phase transition depletes the functional proteins. In normal aging, replacement matches loss; in accelerated aging, it does not.
Alberto J. Espay +9 more
wiley +1 more source
Human stem cell-derived astrocytes replicate human prions in a PRNP genotype-dependent manner. [PDF]
, 2017 Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt-Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades.
Alibhai, James +9 more
core +1 more source
Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases
BioEssays, EarlyView.The energy landscape of Aβ reveals its flexible, “chameleon‐like” behavior, enabling diverse structures from disordered to β‐rich forms. This polymorphism facilitates aggregation, contributing to Alzheimer's disease progression, while the flat landscape also allows disaggregation, potentially slowing disease progression compared to prion proteins with ...
Birgit Strodel
wiley +1 more source
Emerging Infectious Diseases, 2011 Bovine spongiform encephalopathy (BSE) and BSE-related disorders have been associated with a single major prion strain. Recently, 2 atypical, presumably sporadic forms of BSE have been associated with 2 distinct prion strains that are characterized ...
Juan-María Torres +7 more
doaj +1 more source
The Molecular Pathology of Prion Diseases [PDF]
, 2004 Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Herms, Jochen +2 more
core
Neuronal zinc regulation and the prion protein
Prion, 2013 Zinc, the most abundant trace metal in the brain, has numerous functions in health and disease. It is released into the synaptic cleft alongside glutamate and this connection between zinc and glutamatergic neurotransmission allows the ion to modulate ...
N. Watt, Heledd H. Griffiths, N. Hooper
semanticscholar +1 more source