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Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc)
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/pro.2270openalex-snapshot
The crystal structure of an octapeptide repeat of the Prion protein in complex with a Fab fragment of the POM2 antibody
inferredcites →https://doi.org/10.1007/978-1-4614-3229-6_9openalex-snapshot
Implications of 3D Domain Swapping for Protein Folding, Misfolding and Function
inferredcites →https://doi.org/10.1016/j.jmb.2010.04.066openalex-snapshot
Horse Prion Protein NMR Structure and Comparisons with Related Variants of the Mouse Prion Protein
inferredcites →https://doi.org/10.1016/j.str.2013.11.009openalex-snapshot
Structural Basis of Prion Inhibition by Phenothiazine Compounds
inferredcites →https://doi.org/10.1016/s0014-5793(97)00920-4openalex-snapshot
NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)
inferredcites →https://doi.org/10.1016/s0092-8674(03)01031-6openalex-snapshot
Mammalian Prion Biology
inferredcites →https://doi.org/10.1016/s0960-9822(01)00147-6openalex-snapshot
Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
inferredcites →https://doi.org/10.1021/bi00245a003openalex-snapshot
Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
inferredcites →https://doi.org/10.1021/ja407527popenalex-snapshot
Probing the N-Terminal β-Sheet Conversion in the Crystal Structure of the Human Prion Protein Bound to a Nanobody
inferredcites →https://doi.org/10.1021/ja511568mopenalex-snapshot
Evolutionary Conserved Tyr169 Stabilizes the β2-α2 Loop of the Prion Protein
inferredcites →https://doi.org/10.1038/370295a0openalex-snapshot
Prion protein is necessary for normal synaptic function
inferredcites →https://doi.org/10.1038/380639a0openalex-snapshot
Altered circadian activity rhythms and sleep in mice devoid of prion protein
inferredcites →https://doi.org/10.1038/382180a0openalex-snapshot
NMR structure of the mouse prion protein domain PrP(121–231)
inferredcites →https://doi.org/10.1038/emboj.2009.333openalex-snapshot
Conformational diversity in prion protein variants influences intermolecular β‐sheet formation
inferredcites →https://doi.org/10.1038/nature12402openalex-snapshot
The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein
inferredcites →https://doi.org/10.1038/nature19312openalex-snapshot
The prion protein is an agonistic ligand of the G protein-coupled receptor Adgrg6
inferredcites →https://doi.org/10.1038/nsb0901-770openalex-snapshot
Crystal structure of the human prion protein reveals a mechanism for oligomerization.
inferredcites →https://doi.org/10.1038/nsmb.2035openalex-snapshot
Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
inferredcites →https://doi.org/10.1042/bst0361272openalex-snapshot
Mechanism of the metal-mediated endocytosis of the prion protein
inferredcites →https://doi.org/10.1051/vetres:2008024openalex-snapshot
Prion agent diversity and species barrier
inferredcites →https://doi.org/10.1073/pnas.0307178101openalex-snapshot
From conversion to aggregation: Protofibril formation of the prion protein
inferredcites →https://doi.org/10.1073/pnas.0400014101openalex-snapshot
Insight into the PrP C → PrP Sc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants
inferredcites →https://doi.org/10.1073/pnas.0402254101openalex-snapshot
Evidence for assembly of prions with left-handed β-helices into trimers
inferredcites →https://doi.org/10.1073/pnas.0408937102openalex-snapshot
Prion protein NMR structures of cats, dogs, pigs, and sheep
inferredcites →https://doi.org/10.1073/pnas.0409008102openalex-snapshot
Prion protein NMR structures of elk and of mouse/elk hybrids
inferredcites →https://doi.org/10.1073/pnas.0706522104openalex-snapshot
Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure
inferredcites →https://doi.org/10.1073/pnas.0809170106openalex-snapshot
Crystal structure of human prion protein bound to a therapeutic antibody
inferredcites →https://doi.org/10.1073/pnas.1005267107openalex-snapshot
Prion disease susceptibility is affected by β-structure folding propensity and local side-chain interactions in PrP
inferredcites →https://doi.org/10.1073/pnas.1009062107openalex-snapshot
Pharmacological chaperone for the structured domain of human prion protein
inferredcites →https://doi.org/10.1073/pnas.1106325108openalex-snapshot
Cellular prion protein conformation and function
inferredcites →https://doi.org/10.1073/pnas.1110789109openalex-snapshot
Aβ neurotoxicity depends on interactions between copper ions, prion protein, and N -methyl- d -aspartate receptors
inferredcites →https://doi.org/10.1073/pnas.1306178110openalex-snapshot
Structural plasticity of the cellular prion protein and implications in health and disease
inferredcites →https://doi.org/10.1073/pnas.89.22.10940openalex-snapshot
Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.
inferredcites →https://doi.org/10.1073/pnas.94.19.10069openalex-snapshot
Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
inferredcites →https://doi.org/10.1073/pnas.97.1.145openalex-snapshot
NMR solution structure of the human prion protein
inferredcites →https://doi.org/10.1074/jbc.273.50.33107openalex-snapshot
Copper Stimulates Endocytosis of the Prion Protein
inferredcites →https://doi.org/10.1074/jbc.m313762200openalex-snapshot
The Residue 129 Polymorphism in Human Prion Protein Does Not Confer Susceptibility to Creutzfeldt-Jakob Disease by Altering the Structure or Global Stability of PrPC
inferredcites →https://doi.org/10.1093/brain/awv356openalex-snapshot
Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer’s disease
inferredcites →https://doi.org/10.1093/emboj/19.17.4425openalex-snapshot
Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease
inferredcites →https://doi.org/10.1107/s0907444912037328openalex-snapshot
Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1
inferredcites →https://doi.org/10.1107/s1744309111026273openalex-snapshot
Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody
inferredcites →https://doi.org/10.1111/febs.14438openalex-snapshot
Structural characterization of POM 6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion
inferredcites →https://doi.org/10.1111/jnc.13071openalex-snapshot
Prion protein regulates glutathione metabolism and neural glutamate and cysteine uptake via excitatory amino acid transporter 3
inferredcites →https://doi.org/10.1126/science.1103932openalex-snapshot
Human Prion Protein with Valine 129 Prevents Expression of Variant CJD Phenotype
inferredcites →https://doi.org/10.1126/science.1138718openalex-snapshot
A General Model of Prion Strains and Their Pathogenicity
inferredcites →https://doi.org/10.1126/science.1675487openalex-snapshot
Molecular Biology of Prion Diseases
inferredcites →https://doi.org/10.1128/jvi.77.19.10288-10294.2003openalex-snapshot
New Inhibitors of Scrapie-Associated Prion Protein Formation in a Library of 2,000 Drugs and Natural Products
inferredcites →https://doi.org/10.1146/annurev.neuro.24.1.519openalex-snapshot
Prion Diseases of Humans and Animals: Their Causes and Molecular Basis
inferredcites →https://doi.org/10.1146/annurev.neuro.31.060407.125620openalex-snapshot
The Prion's Elusive Reason for Being
inferredcites →https://doi.org/10.1172/jci42051openalex-snapshot
A molecular switch controls interspecies prion disease transmission in mice
inferredcites →https://doi.org/10.1186/s12915-017-0375-5openalex-snapshot
The biological function of the cellular prion protein: an update
inferredcites →https://doi.org/10.1212/wnl.0b013e3182a9f3b4openalex-snapshot
Quinacrine treatment trial for sporadic Creutzfeldt-Jakob disease
inferredcites →https://doi.org/10.1371/journal.ppat.1005835openalex-snapshot
The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy
inferredcites →https://doi.org/10.1371/journal.ppat.1006733openalex-snapshot
Inhibition of group-I metabotropic glutamate receptors protects against prion toxicity
inferredcites →https://doi.org/10.1371/journal.ppat.1007864openalex-snapshot
Full atomistic model of prion structure and conversion
inferredcites →https://doi.org/10.3390/pathogens7010020openalex-snapshot
The Structure of PrPSc Prions
inferredcites →https://doi.org/10.4161/pri.1.2.4346openalex-snapshot
The Prion Protein Knockout Mouse
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4820084openalex-extracted
Unraveling the Structural Facets of Prp127-132 Polymorphic Variants Using Combined Molecular Dynamics/Markov Modeling
inferred← citeshttps://doi.org/10.1002/9783527830503.ch1openalex-snapshot
Protein Structure and Conformational Dynamics
inferred← citeshttps://doi.org/10.1002/advs.76118openalex-snapshot
A Phase‐Resolved Geometric Deep Learning Framework Maps Structural Determinants of Disease‐Associated Protein Aggregation and Guides Suppressor Design
inferred← citeshttps://doi.org/10.1002/mco2.70766openalex-snapshot
Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1007/978-1-0716-1546-1_14openalex-snapshot
Aggregates Sealed by Ions
inferred← citeshttps://doi.org/10.1007/978-3-031-10832-7_4openalex-snapshot
Inorganic Complexes and Metal-Based for Biomarkers Sensors
inferred← citeshttps://doi.org/10.1007/978-3-031-77911-4_15openalex-snapshot
Prions: A Mechanistic View
inferred← citeshttps://doi.org/10.1007/978-981-96-6202-9_1openalex-snapshot
Neurodegenerative Disorder: An Overview
inferred← citeshttps://doi.org/10.1007/978-981-97-6822-6_8openalex-snapshot
Role of Enzymes in Prion Disease: A Molecular Mechanism
inferred← citeshttps://doi.org/10.1007/978-981-99-6445-1_11openalex-snapshot
Miscellaneous CNS Viral Infections: Underappreciated Causes of Neurologic Disease
inferred← citeshttps://doi.org/10.1007/s11033-022-07806-2openalex-snapshot
Cellular toxicity of scrapie prions in prion diseases; a biochemical and molecular overview
inferred← citeshttps://doi.org/10.1007/s11033-025-10754-2openalex-snapshot
A review on current theories and potential therapies for prion diseases
inferred← citeshttps://doi.org/10.1007/s11940-024-00821-7openalex-snapshot
The Knowns and Unknowns of Prion Protein in Immune Modulation and the Pathogenesis of Neuroautoimmune Diseases
inferred← citeshttps://doi.org/10.1016/b978-0-443-15702-8.00020-8openalex-snapshot
Molecular genetics of prions
inferred← citeshttps://doi.org/10.1016/j.biosystems.2021.104542openalex-snapshot
Biosemiotics comprehension of PrP code and prion disease
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.01.045openalex-snapshot
Ellagic acid and pentagalloylglucose are potential inhibitors of prion protein fibrillization
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.11.049openalex-snapshot
Molecular insights into the critical role of gallate moiety of green tea catechins in modulating prion fibrillation, cellular internalization, and neuronal toxicity
inferred← citeshttps://doi.org/10.1016/j.jmgm.2024.108927openalex-snapshot
Structural characterization of codon 129 polymorphism in prion peptide segments (PrP127-132) using the Markov State Models
inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.143460openalex-snapshot
Design and synthesis of novel fluorescent amino-chalcones as turn-on probes for prion protein fibril detection
inferred← citeshttps://doi.org/10.1016/j.redox.2024.103133openalex-snapshot
Αnti-prion effects of anthocyanins
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b01114openalex-snapshot
Net Charge and Nonpolar Content Guide the Identification of Folded and Prion Proteins
inferred← citeshttps://doi.org/10.1039/c9tb02669jopenalex-snapshot
Transition metal complexes as imaging or therapeutic agents for neurodegenerative diseases
inferred← citeshttps://doi.org/10.1039/d1ra01891dopenalex-snapshot
The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein
inferred← citeshttps://doi.org/10.1039/d4dt00704bopenalex-snapshot
Modulating the aggregation of human prion protein PrP 106–126 by an indole-based cyclometallated palladium complex
inferred← citeshttps://doi.org/10.1042/bcj20220016openalex-snapshot
A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications
inferred← citeshttps://doi.org/10.1042/bcj20253317openalex-snapshot
AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes
inferred← citeshttps://doi.org/10.1080/19336896.2023.2186767openalex-snapshot
Polymorphism of prion protein gene (PRNP) in Nigerian sheep
inferred← citeshttps://doi.org/10.1093/nar/gkaa822openalex-snapshot
RNA as the stone guest of protein aggregation
inferred← citeshttps://doi.org/10.1186/s13568-025-01932-3openalex-snapshot
Mediators linking gut microbiota and sporadic Creutzfeldt–Jakob disease: a Mendelian randomization study
inferred← citeshttps://doi.org/10.1242/jcs.245605openalex-snapshot
Prion protein and prion disease at a glance
inferred← citeshttps://doi.org/10.1515/tnsci-2022-0315openalex-snapshot
Human prion diseases and the prion protein – what is the current state of knowledge?
inferred← citeshttps://doi.org/10.20960/revmedlab.00125openalex-snapshot
Biomarcadores diagnósticos de la enfermedad de Creutzfeld-Jakob
inferred← citeshttps://doi.org/10.20960/revmedlab.00177openalex-snapshot
Utilidad clínica de la proteína tau total y la ratio con su fracción fosforilada en el diagnóstico de enfermedad de Creutzfeldt-Jakob
inferred← citeshttps://doi.org/10.2174/0115743624353499250630090143openalex-snapshot
Comprehensive Insights into Prion Diseases: Classification, Mechanisms of Action, Detection Methods, and Preventive Strategies
inferred← citeshttps://doi.org/10.3103/s1068367425701162openalex-snapshot
Polymorphisms in the Prion Protein Gene (PRNP) in Goat Populations in Russia
inferred← citeshttps://doi.org/10.3389/fbioe.2020.585896openalex-snapshot
Challenges and Advances in Antemortem Diagnosis of Human Transmissible Spongiform Encephalopathies
inferred← citeshttps://doi.org/10.3389/fcimb.2024.1348279openalex-snapshot
Dysbiosis of the gut microbiota and its effect on α-synuclein and prion protein misfolding: consequences for neurodegeneration
inferred← citeshttps://doi.org/10.3390/ani11030691openalex-snapshot
Classical and Atypical Scrapie in Sheep and Goats. Review on the Etiology, Genetic Factors, Pathogenesis, Diagnosis, and Control Measures of Both Diseases
inferred← citeshttps://doi.org/10.3390/ijms21207763openalex-snapshot
A New Take on Prion Protein Dynamics in Cellular Trafficking
inferred← citeshttps://doi.org/10.3390/ijms22116016openalex-snapshot
Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications
inferred← citeshttps://doi.org/10.3390/ijms22179635openalex-snapshot
Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils
inferred← citeshttps://doi.org/10.3390/md22100456openalex-snapshot
Potential of Marine Sponge Metabolites against Prions: Bromotyrosine Derivatives, a Family of Interest
inferred← citeshttps://doi.org/10.3390/molecules27165123openalex-snapshot
Alteration of Biomolecular Conformation by Aluminum-Implications for Protein Misfolding Disease
inferred← citeshttps://doi.org/10.3390/neurolint16050079openalex-snapshot
A Systematic Review of Sporadic Creutzfeldt-Jakob Disease: Pathogenesis, Diagnosis, and Therapeutic Attempts
inferred← citeshttps://doi.org/10.3390/pathogens10010024openalex-snapshot
Inactivation of Prions by Low-Temperature Sterilization Technology Using Vaporized Gas Derived from a Hydrogen Peroxide–Peracetic Acid Mixture
inferred← citeshttps://doi.org/10.3390/pathogens9100819openalex-snapshot
Effect of Nitrogen Gas Plasma Generated by a Fast-Pulsed Power Supply Using a Static Induction Thyristor on Scrapie Prion
inferred← citeshttps://doi.org/10.3390/vetsci11010013openalex-snapshot
National Prevalence of Caprine Prion Protein Genetic Variability at Codons 146, 211, and 222 in Goat Herds in the United States
inferred← citeshttps://doi.org/10.4103/1673-5374.293137openalex-snapshot
Saccharomyces cerevisiae in neuroscience: how unicellular organism helps to better understand prion protein?
inferred← citeshttps://doi.org/10.53859/02352451_2025_39_3_61openalex-snapshot
Polymorphisms in the prion protein gene (PRNP) in some goat populations raised in Russia
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