ArticleThe Journal of biological chemistry2014
A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- Cellular prion protein gene polymorphisms linked to differential scrapie susceptibility correlate with distinct residue connectivity between secondary structure elements.Journal of biomolecular structure & dynamics · 2021Article
- Predicting the spread-risk potential of chronic wasting disease to sympatric ungulate species.Prion · 2020Article
- Structural effects of the highly protective V127 polymorphism on human prion protein.Communications biology · 2020Article
- Unique Structural Features of Mule Deer Prion Protein Provide Insights into Chronic Wasting Disease.ACS omega · 2019Article
- Insights into the Bidirectional Properties of the Sheep-Deer Prion Transmission Barrier.Molecular neurobiology · 2019Review
- Metabolic profile analysis of free amino acids in experimental autoimmune uveoretinitis rat plasma.International journal of ophthalmology · 2019Article
- Disulfide-crosslink scanning reveals prion-induced conformational changes and prion strain-specific structures of the pathological prion protein PrPThe Journal of biological chemistry · 2018Article
- Article
- Asparagine and glutamine ladders promote cross-species prion conversion.The Journal of biological chemistry · 2017Article
- Prion proteinProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Toward the Atomic Structure of PrPCold Spring Harbor perspectives in biology · 2017Review
- Melanosomal formation of PMEL core amyloid is driven by aromatic residues.Scientific reports · 2017Article
- Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.PloS one · 2017Article
- Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Scientific reports · 2016Article
- Cross-species transmission of CWD prions.Prion · 2016Review
- Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.Scientific reports · 2015Article
- A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.PLoS pathogens · 2015Article
- Generic amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prions.Scientific reports · 2015Article
- Human prion protein sequence elements impede cross-species chronic wasting disease transmission.The Journal of clinical investigation · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The transmission of infectious prions into different host species requires compatible prion protein (PrP) primary structures, and even one heterologous residue at a pivotal position can block prion infection. Mapping the key amino acid positions that govern cross-species prion conversion has not yet been possible, although certain residue positions have been identified as restrictive, including residues in the β2-α2 loop region of PrP. To further define how β2-α2 residues impact conversion, we investigated residue substitutions in PrP(C) using an in vitro prion conversion assay. Within the β2-α2 loop, a tyrosine residue at position 169 is strictly conserved among mammals, and transgenic mice expressing mouse PrP having the Y169G, S170N, and N174T substitutions resist prion infection. To better understand the structural requirements of specific residues for conversion initiated by mouse prions, we substituted a diverse array of amino acids at position 169 of PrP. We found that the substitution of glycine, leucine, or glutamine at position 169 reduced conversion by ∼ 75%. In contrast, replacing tyrosine 169 with either of the bulky, aromatic residues, phenylalanine or tryptophan, supported efficient prion conversion. We propose a model based on a requirement for tightly interdigitating complementary amino acid side chains within specific domains of adjacent PrP molecules, known as "steric zippers," to explain these results. Collectively, these studies suggest that an aromatic residue at position 169 supports efficient prion conversion.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.