Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc - Wikidata - awgldk - TriplyDB

Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc

Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc

http://www.wikidata.org/entity/Q36672125

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Novel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and scrapie Selective incorporation of polyanionic molecules into hamster prions.Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity Advances in Antibody Design Two amyloid States of the prion protein display significantly different folding patterns Scrapie-induced defects in learning and memory of transgenic mice expressing anchorless prion protein are associated with alterations in the gamma aminobutyric acid-ergic pathway.The structure of the infectious prion protein: experimental data and molecular models.Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.Prion protein self-peptides modulate prion interactions and conversion.The expanding universe of prion diseases.Antibody binding loop insertions as diversity elements Mapping of possible prion protein self-interaction domains using peptide arrays Anti-idiotypic antibodies: a new approach in prion research.Prion protein expression and processing in human mononuclear cells: the impact of the codon 129 prion gene polymorphism.Tracing conformational transition of abnormal prion proteins during interspecies transmission by using novel antibodies.Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice.Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Conformation-dependent high-affinity monoclonal antibodies to prion proteins.Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systems The N-terminal sequence of prion protein consists an epitope specific to the abnormal isoform of prion protein (PrP(Sc))High titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo.Superparamagnetic nanoparticle capture of prions for amplification.Human prions and plasma lipoproteins.Biological effects and use of PrPSc- and PrP-specific antibodies generated by immunization with purified full-length native mouse prions.Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.Epitope Specificity Determines Pathogenicity and Detectability of Anti-Platelet-Derived Growth Factor Receptor α Autoantibodies in Systemic Sclerosis.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Structure-based design of conformation- and sequence-specific antibodies against amyloid β.Characterization of prion protein (PrP)-derived peptides that discriminate full-length PrPSc from PrPC.Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.Progress in prion vaccines and immunotherapies.The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).Generation of inhibitory monoclonal antibodies targeting matrix metalloproteinase-14 by motif grafting and CDR optimization.Mutated but Not Deleted Ovine PrP(C) N-Terminal Polybasic Region Strongly Interferes with Prion Propagation in Transgenic Mice Design and Optimization of Anti-amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid Polypeptide The reconstitution of mammalian prion infectivity de novo.PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains.Therapeutic approaches for prion disorders.PrP antibody binding-induced epitope modulation evokes immunocooperativity The region approximately between amino acids 81 and 137 of proteinase K-resistant PrPSc is critical for the infectivity of the Chandler prion strain.

P2860

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P2860

Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc

http://www.wikidata.org/entity/Q36672125

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

@ast

Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

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type

label

Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

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Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

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prefLabel

Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

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Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Motif-grafted antibodies conta ...... lar PrP are specific for PrPSc

@en

P2093

Dennis R Burton

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Gil Abalos

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Glenn C Telling

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Laura Solforosi

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Nnennaya Kanu

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R Anthony Williamson

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P2860

Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design

The binding of prion proteins to serum components is affected by detergent extraction conditions

Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody

Ebola virus can be effectively neutralized by antibody produced in natural human infection.

Mapping the prion protein using recombinant antibodies.

Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein

Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence.

Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody.

A prion protein epitope selective for the pathologically misfolded conformation.

P304

10404-10409

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10.1073/PNAS.0403522101

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28

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101

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Gianluca Moroncini

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2004-07-06T00:00:00Z

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8468137

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15240877

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478584

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