The structure of the infectious prion protein: experimental data and molecular models.
about
Multifaceted Role of Sialylation in Prion DiseasesDisease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central DogmaTechniques to elucidate the conformation of prionsPrion strains and amyloid polymorphism influence phenotypic variationThe Structural Architecture of an Infectious Mammalian Prion Using Electron CryomicroscopyProgress towards structural understanding of infectious sheep PrP-amyloid.A novel and rapid method for obtaining high titre intact prion strains from mammalian brain.Secondary-structure prediction revisited: Theoretical β-sheet propensity and coil propensity represent structures of amyloids and aid in elucidating phenomena involved in interspecies transmission of prions.Sialylation of the prion protein glycans controls prion replication rate and glycoform ratioDisrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.N(ε)-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms.Generating Bona Fide Mammalian Prions with Internal DeletionsPrions: Beyond a Single Protein.Guinea Pig Prion Protein Supports Rapid Propagation of Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease Prions.The diversity and relationship of prion protein self-replicating states.The structure of human prions: from biology to structural models-considerations and pitfalls.The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.Mammalian prions and their wider relevance in neurodegenerative diseases.In silico strategies on prion pathogenic conversion and inhibition from PrPC -PrPSc.The N Terminus of the Prion Protein Mediates Functional Interactions with the Neuronal Cell Adhesion Molecule (NCAM) Fibronectin Domain.A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity.Transmissibility of Gerstmann-Sträussler-Scheinker syndrome in rodent models: New insights into the molecular underpinnings of prion infectivity.Virtual drug screening for prion diseases: A valuable step?Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.A novel Gerstmann-Sträussler-Scheinker disease mutation defines a precursor for amyloidogenic 8 kDa PrP fragments and reveals N-terminal structural changes shared by other GSS alleles.Left-handed polyproline-II helix revisited: proteins causing proteopathies.Mammalian amyloidogenic proteins promote prion nucleation in yeast.The Structure of PrPSc Prions.Comparing the Folds of Prions and Other Pathogenic Amyloids.Synthetic Prions Provide Clues for Understanding Prion Diseases.
P2860
Q26739884-2D2EEA90-B36D-4CF1-BC67-4C09629214A8Q26770266-F5B72583-F068-4A05-A921-8E37038CD35EQ26795754-7CD49FDD-FCB1-47A0-A2DE-4A833234E830Q26827209-805E2CF4-A772-42C7-AC50-2AB7BC5C0B7FQ27312168-F0216E0C-F137-4B61-A9AF-4C3D28C64BD5Q30369454-8FA4EF72-D677-4A67-8134-8EC8BBD60B08Q35580105-801AB6F6-A4D1-44D5-8150-E501D3E0EC95Q36281251-EAC1E0AD-88E6-4506-9188-747762042474Q36291321-CEA5190A-58BC-45DB-96A7-1605FEEB741BQ36331735-0D008DE5-A4DE-41B4-B8F6-79399932F664Q36994289-430D3443-6107-432F-9D05-9CC0F13DF8B5Q37093469-FB43CEE4-9A99-4CD6-89BD-E584DE1D1F60Q37162363-61EBFC30-8B16-416D-A58A-C9F7AB6D5ABCQ37347272-0E9A8513-A78F-4EE2-878C-D0435EA90F9AQ38259891-5128A32A-FA7C-4551-9942-4CF51FE3F107Q38261710-D32CB45B-E7DD-451E-BE43-A86447A91739Q38826643-21701774-CA7D-4BC6-A0D1-007C89F54E5EQ39004344-812D1F29-2358-4D9C-A304-8EA85B0A21C6Q39101358-76607891-47DE-4F4D-BBDB-42E9A769E4A7Q39480254-74A11EB6-7730-425D-9D05-22832E803B42Q40299414-7B84FF61-7758-4ABD-85DB-1C9B66532C95Q41888735-B397FC43-C1A2-4686-880E-59C414AA2C6DQ42382334-33016554-A86B-4B20-9F1E-8A833D24D815Q47829166-315EB05B-11CF-4691-9BA2-960BF12A067CQ47862323-FCDECFA7-AD6D-4ADC-B455-79CA17DF0B60Q48094432-435E5297-6EAD-49E0-8402-2B14CADFC4DFQ48251902-9F33393C-AF0C-4C1E-9268-ECD444BED0A1Q50133889-0DD7D4F0-06EF-462D-8B4F-0AF99E1E1534Q53397941-29CB16A9-BEE1-429F-AE43-2783D8FA209BQ55263233-6C693E5F-4552-49E8-8A8F-7783D6B21548
P2860
The structure of the infectious prion protein: experimental data and molecular models.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The structure of the infectious prion protein: experimental data and molecular models.
@ast
The structure of the infectious prion protein: experimental data and molecular models.
@en
type
label
The structure of the infectious prion protein: experimental data and molecular models.
@ast
The structure of the infectious prion protein: experimental data and molecular models.
@en
prefLabel
The structure of the infectious prion protein: experimental data and molecular models.
@ast
The structure of the infectious prion protein: experimental data and molecular models.
@en
P2860
P356
P1433
P1476
The structure of the infectious prion protein: experimental data and molecular models.
@en
P2093
Jesús R Requena
P2860
P356
10.4161/PRI.28368
P50
P577
2014-01-01T00:00:00Z