Results 51 to 60 of about 97,377 (307)

Absence of single nucleotide polymorphisms (SNPs) in the open reading frame (ORF) of the prion protein gene (PRNP) in a large sampling of various chicken breeds

BMC Genomics, 2019
Background Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP ...
Yong-Chan Kim, Sae-Young Won, Byung-Hoon Jeong   +2 more
doaj   +1 more source

Genetic Factors Contributing to the Susceptibility of Development of Prion Diseases [PDF]

, 2017
This paper won an honorable mention writing flag award in the research category. Claire Culbertson, writing for Katherine Bruner’s BIO 325L class, “Lab Experience in Genetics”.Bruner, KatherineUndergraduate ...
Culbertson, Claire
core   +1 more source

SPG4 and Dementia: Expanding the Clinical Spectrum

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Hereditary spastic paraplegia (HSP) is a group of disorders characterized by progressive spasticity and lower limb weakness, with mutations in SPG4/SPAST being the most common cause. Detailed studies and clinical and molecular comparisons across different populations are missing.
Emanuele Panza, Arun Meyyazhagan, Eliseo Picchi, Gustavo Ribas, Ingrid Faber, Ryosuke Miyamoto, Preethi Basavaraju, Paolo Eusebi, Haripriya Kuchi Bhotla, Mario Stasi, Fabrizio Gaudiello, Francesco Patti, Filippo Maria Santorelli, Marcondes Cavalcante França Jr, José Luiz Pedroso, Orlando Graziani Povoas Barsottini, Hélio Afonso Ghizoni Teive, Peter Henry St George‐Hyslop, Toshitaka Kawarai, Antonio Orlacchio   +19 more
wiley   +1 more source

Multifaceted role of sialylation in prion diseases

Frontiers in Neuroscience, 2016
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrPC. Sialylation of the prion protein N-linked glycans was discovered more than 30 years
Ilia V Baskakov, Ilia V Baskakov, Elizaveta Katorcha, Elizaveta Katorcha   +3 more
doaj   +1 more source

Evolutionary descent of prion genes from a ZIP metal ion transport ancestor [PDF]

, 2009
In the more than 20 years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
David Westaway, Gerold Schmitt-Ulms, Holger Wille, Joel C. Watts, Sepehr Ehsani   +4 more
core   +1 more source

Gerstmann-Sträussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments [PDF]

, 2019
Despite their phenotypic heterogeneity, most human prion diseases belong to two broadly defined groups: Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker disease (GSS).
Cali, Ignazio, Cracco, Laura, Gambetti, Pierluigi, Ghetti, Bernardino, Lavrich, Jody, Nemani, Satish K., Notari, Silvio, Surewicz, Witold K., Xiao, Xiangzhu   +8 more
core   +1 more source

A Systematic Comparison of Alpha‐Synuclein Seed Amplification Assays for Increasing Reproducibility

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Seed amplification assays (SAAs) enable ultrasensitive detection of misfolded α‐synuclein across biofluids and tissues. Yet, heterogeneity in protocols limits cross‐study comparability and clinical translation. Here, we review α‐synuclein SAA methods and their performance across various biological matrices.
Manuela Amaral‐do‐Nascimento, Daniela F. Santos, Tuane C. R. G. Vieira, Tiago F. Outeiro   +3 more
wiley   +1 more source

Enhanced phosphorylation of PERK in primary cultured neurons as an autonomous neuronal response to prion infection.

PLoS ONE, 2020
Conversion of cellular prion protein (PrPC) into the pathogenic isoform of prion protein (PrPSc) in neurons is one of the key pathophysiological events in prion diseases.
Misaki Tanaka, Takeshi Yamasaki, Rie Hasebe, Akio Suzuki, Motohiro Horiuchi   +4 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

Amyloidogenic Peptide Fragments Designed From Bacterial Collagen‐like Proteins Form Hydrogel

Advanced Functional Materials, EarlyView.
This study identified amyloidogenic sequence motifs in bacterial collagen‐like proteins and exploited these to design peptides that self‐assemble into β‐sheet fibers and form hydrogels. One hydrogel supported healthy fibroblast growth, showing promise for biocompatible materials. Our work demonstrates that bacterial sequences can be harnessed to create
Vamika Sagar, Xuen J Ng, Lukas Lechel, Ashish Chand Rajwar, Hendrik Bargel, Abhishek A. Jalan   +5 more
wiley   +1 more source