review article | Q7318358 |
scholarly article | Q13442814 |
P50 | author | Bruno Macedo | Q58946735 |
Yraima Cordeiro | Q37838157 | ||
P2860 | cites work | Quadruplex DNA: sequence, topology and structure | Q22065978 |
Base-stacking and base-pairing contributions into thermal stability of the DNA double helix | Q22065979 | ||
Prion hypothesis: the end of the controversy? | Q24599702 | ||
Prions | Q24633319 | ||
Formation of native prions from minimal components in vitro | Q24676353 | ||
Prion diseases: immunotargets and therapy | Q26741258 | ||
Molecular Selection, Modification and Development of Therapeutic Oligonucleotide Aptamers | Q26765458 | ||
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases | Q26996441 | ||
Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins. | Q51728894 | ||
Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world. | Q51757971 | ||
Targeting amyloid-beta peptide (Abeta) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Abeta precursor protein (APP) transgenic mice. | Q51811574 | ||
The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. | Q54014038 | ||
Production and Characterization of RNA Aptamers Specific for Amyloid Fibril Epitopes | Q54806579 | ||
Heparin Binding by Murine Recombinant Prion Protein Leads to Transient Aggregation and Formation of RNA-Resistant Species | Q57084698 | ||
Selection and characterization of DNA aptamers against PrPSc | Q60654526 | ||
RNA and CuCl2 induced conformational changes of the recombinant ovine prion protein | Q79950620 | ||
A large ribonucleoprotein particle induced by cytoplasmic PrP shares striking similarities with the chromatoid body, an RNA granule predicted to function in posttranscriptional gene regulation | Q39915581 | ||
Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin. | Q40558969 | ||
The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. | Q40817022 | ||
Cofactor molecules induce structural transformation during infectious prion formation | Q41820269 | ||
Screening of DNA aptamer against mouse prion protein by competitive selection | Q43189229 | ||
BetaAPP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients | Q44135809 | ||
Concentration and removal of prion proteins from biological solutions | Q44358317 | ||
In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups | Q44393768 | ||
Binding of prion proteins to lipid membranes | Q44707244 | ||
Structural determinants of conformationally selective, prion-binding aptamers. | Q44719244 | ||
Nuclease resistant circular DNAs copurify with infectivity in scrapie and CJD. | Q45134169 | ||
Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids | Q45144712 | ||
Polymerization of murine recombinant prion protein in nucleic acid solution | Q46243624 | ||
Preparation of aggregate-free, low molecular weight amyloid-beta for assembly and toxicity assays. | Q47376910 | ||
Interaction of prion peptide HuPrP106-126 with nucleic acid | Q47808057 | ||
RNA molecules stimulate prion protein conversion | Q48170423 | ||
Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro | Q48214478 | ||
Predominance of neuronal mRNAs in individual Alzheimer's disease senile plaques | Q48283039 | ||
RNA sequestration to pathological lesions of neurodegenerative diseases. | Q48342254 | ||
Monoclonal antibodies that target pathological assemblies of Abeta | Q48363878 | ||
Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution | Q48402933 | ||
Characterization and application of a novel RNA aptamer against the mouse prion protein | Q38314743 | ||
DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity | Q38316301 | ||
Nonspecific prion protein-nucleic acid interactions lead to different aggregates and cytotoxic species | Q38324510 | ||
Analysis of nucleic acid chaperoning by the prion protein and its inhibition by oligonucleotides. | Q38333624 | ||
Sensitive discrimination and detection of prion disease-associated isoform with a dual-aptamer strategy by developing a sandwich structure of magnetic microparticles and quantum dots | Q38339688 | ||
RNA aptamers specifically interact with the prion protein PrP. | Q38342284 | ||
Selection of aptamers for amyloid beta-protein, the causative agent of Alzheimer's disease. | Q38342641 | ||
Prion-protein-specific aptamer reduces PrPSc formation | Q38363420 | ||
New approaches for the selection and evaluation of anti-prion organic compounds | Q38365829 | ||
Prions: what are they good for? | Q38592888 | ||
Cell Biology of Prions and Prionoids: A Status Report | Q38603988 | ||
Trends in the Design and Development of Specific Aptamers Against Peptides and Proteins. | Q38777639 | ||
Therapeutic nucleic acids: current clinical status. | Q38816703 | ||
The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins | Q38861978 | ||
Aptamer and its applications in neurodegenerative diseases | Q38937721 | ||
Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases | Q39310077 | ||
Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells | Q39680285 | ||
Crystal structure of the human prion protein reveals a mechanism for oligomerization | Q27634441 | ||
Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein | Q27656952 | ||
Anti-prion activity of an RNA aptamer and its structural basis | Q27675235 | ||
Binding of an RNA aptamer and a partial peptide of a prion protein: crucial importance of water entropy in molecular recognition | Q27683664 | ||
NMR structure of the mouse prion protein domain PrP(121-231) | Q27733163 | ||
Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase | Q27860794 | ||
In vitro selection of RNA molecules that bind specific ligands | Q27861109 | ||
Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
Prion diseases of humans and animals: their causes and molecular basis | Q28209943 | ||
Cellular prion protein localizes to the nucleus of endocrine and neuronal cells and interacts with structural chromatin components | Q29347112 | ||
Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns | Q29392099 | ||
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis | Q29547501 | ||
Molecular chaperones in protein folding and proteostasis | Q29547715 | ||
Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids. | Q30368863 | ||
Effect of additives on protein aggregation. | Q30377982 | ||
Understanding protein non-folding. | Q30385084 | ||
Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions | Q30492360 | ||
Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs | Q30570683 | ||
The multivesicular body is the major internal site of prion conversion | Q30633753 | ||
Identification and characterization of nuclease-stabilized RNA molecules that bind human prostate cancer cells via the prostate-specific membrane antigen | Q30739257 | ||
RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity | Q30879431 | ||
Selection of RNA aptamers to the Alzheimer's disease amyloid peptide | Q31037042 | ||
Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. | Q31151988 | ||
Thioaptamer interactions with prion proteins: sequence-specific and non-specific binding sites | Q33283775 | ||
Selection of aptamers for molecular recognition and characterization of cancer cells | Q33285855 | ||
Synaptic targeting by Alzheimer's-related amyloid beta oligomers. | Q33288786 | ||
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation | Q33433749 | ||
RNA aptamers selected against amyloid beta-peptide (Abeta) inhibit the aggregation of Abeta | Q33492388 | ||
Aptamers to explore prion protein interactions with nucleic acids | Q33520894 | ||
Conformational Abs recognizing a generic amyloid fibril epitope | Q34009881 | ||
Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding | Q34084209 | ||
A new paradigm for aptamer therapeutic AS1411 action: uptake by macropinocytosis and its stimulation by a nucleolin-dependent mechanism | Q34268342 | ||
The amyloid state and its association with protein misfolding diseases. | Q34421102 | ||
Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res | Q34434726 | ||
Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA. | Q34458035 | ||
CJD and Scrapie Require Agent-Associated Nucleic Acids for Infection | Q34509317 | ||
Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides | Q34509751 | ||
In vivo SELEX for Identification of Brain-penetrating Aptamers. | Q34539526 | ||
Aptamers evolved from live cells as effective molecular probes for cancer study | Q35033059 | ||
Phosphorothioate oligonucleotides reduce PrP levels and prion infectivity in cultured cells | Q35844090 | ||
Identification and characterization of a cell membrane nucleic acid channel | Q35896079 | ||
Antibody to DNA detects scrapie but not normal prion protein | Q36018267 | ||
The hypothesis of the catalytic action of nucleic acid on the conversion of prion protein | Q36074709 | ||
Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity. | Q36078399 | ||
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers | Q36178075 | ||
Bioactive and nuclease-resistant L-DNA ligand of vasopressin | Q36591985 | ||
Conformation-dependent anti-amyloid oligomer antibodies | Q36625938 | ||
Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation | Q36668697 | ||
Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinity | Q37080546 | ||
Identification of an intracellular site of prion conversion | Q37170450 | ||
The emerging concept of functional amyloid | Q37389642 | ||
Aptamer identification of brain tumor-initiating cells | Q37601425 | ||
PrP interactions with nucleic acids and glycosaminoglycans in function and disease | Q37663171 | ||
Aptamer-based molecular recognition for biosensor development. | Q37774275 | ||
Nucleic acid-mediated protein aggregation and assembly | Q37918635 | ||
The amyloid state of proteins in human diseases | Q37994283 | ||
Elucidating the role of cofactors in mammalian prion propagation | Q38173629 | ||
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases | Q38185934 | ||
Dialysis: a characterization method of aggregation tendency. | Q38275238 | ||
Aptamers as targeted therapeutics: current potential and challenges | Q38290290 | ||
Application of a novel in vitro selection technique to isolate and characterise high affinity DNA aptamers binding mammalian prion proteins | Q38291515 | ||
A label-free and cascaded dual-signaling amplified electrochemical aptasensing platform for sensitive prion assay | Q38292391 | ||
DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation | Q38295713 | ||
Aptamer-mediated magnetic and gold-coated magnetic nanoparticles as detection assay for prion protein assessment. | Q38298184 | ||
G-quadruplexes within prion mRNA: the missing link in prion disease? | Q38305734 | ||
In vitro selection of RNA aptamers against cellular and abnormal isoform of mouse prion protein | Q38306813 | ||
Structural insights into the interaction between prion protein and nucleic acid | Q38311203 | ||
P275 | copyright license | Creative Commons Attribution | Q6905323 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 5 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | nucleotide | Q28745 |
membrane protein | Q423042 | ||
transport protein | Q2111029 | ||
prion | Q47051 | ||
prion protein family | Q24724413 | ||
nucleotide aptamers | Q49849144 | ||
P577 | publication date | 2017-05-17 | |
P1433 | published in | International Journal of Molecular Sciences | Q3153277 |
P1476 | title | Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids | |
P478 | volume | 18 |
Q52351526 | Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities. |
Q55007427 | Aptamers Selected for Recognizing Amyloid β-Protein-A Case for Cautious Optimism. |
Q50066811 | Aptamers in HIV research diagnosis and therapy. |
Q92152821 | Characterization of the Prion Protein Binding Properties of Antisense Oligonucleotides |
Q92150816 | Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review |
Q47104247 | Nucleic Acid Aptamers: Emerging Applications in Medical Imaging, Nanotechnology, Neurosciences, and Drug Delivery. |
Q93332846 | Prion Protein PRNP: A New Player in Innate Immunity? The Aβ Connection |
Q89563089 | Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy |
Q46756184 | Prion-Like Domains in Phagobiota |
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