Natural and synthetic prion structure from X-ray fiber diffraction
about
Recombinant prion protein induces a new transmissible prion disease in wild-type animals.Multifaceted Role of Sialylation in Prion DiseasesTechniques to elucidate the conformation of prionsThe strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of diseaseThe Structural Architecture of an Infectious Mammalian Prion Using Electron CryomicroscopyGenesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion diseasePrion Fibrillization Is Mediated by a Native Structural Element That Comprises Helices H2 and H3Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion DiseaseAtomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion DiseaseDe novo generation of prion strainsGeneric amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prionsThe Priority position paper: Protecting Europe's food chain from prionsStructure-Based Drug Discovery for Prion Disease Using a Novel Binding SimulationProgress towards structural understanding of infectious sheep PrP-amyloid.Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins.Mammalian prions: tolerance to sequence changes-how far?Two amyloid States of the prion protein display significantly different folding patternsLive imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websThe structure of the infectious prion protein: experimental data and molecular models.Glycosylphosphatidylinositol anchoring directs the assembly of Sup35NM protein into non-fibrillar, membrane-bound aggregatesBiology and genetics of prions causing neurodegenerationHigh-resolution structure of infectious prion protein: the final frontierPeptide and glycopeptide dendrimers and analogous dendrimeric structures and their biomedical applications.Amyloid structure: conformational diversity and consequences.Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures.Prions.Structural organization of mammalian prions as probed by limited proteolysis.The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.Two misfolding routes for the prion protein around pH 4.5.The evolution of transmissible prions: the role of deformed templatingStructural studies of truncated forms of the prion protein PrP.Mechanism of scrapie prion precipitation with phosphotungstate anions.Spontaneous generation of anchorless prions in transgenic mice.Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion ProteinTau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation.Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid foldPrion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.A new mechanism for transmissible prion diseasesStructural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.
P2860
Q24645106-D44949F6-E2E9-4CD6-B3A1-91EC4B806B67Q26739884-51A8F0CB-D0E6-47B8-9DC5-92FBD6A4A250Q26795754-34B318C4-7C22-4688-868A-AD2153A1F296Q27312083-2E3D70B8-1D9F-430E-AC94-0119B14A061EQ27312168-268C8FDC-A6B8-4499-AD37-0BEA7C556054Q27348022-3F4A3AA6-B32D-4A35-A37E-F6ADDB8984D1Q27660444-57A00678-7C3F-467F-87FD-C78A64FD0780Q27663878-ED203FD8-39E5-47BE-8F43-CCB9687040AAQ27666974-5EE9F796-BC54-4ADD-8E95-97089C325D8BQ28249136-DB40511B-04F2-48F2-8EFE-95506FE7981FQ28607285-60F43F46-5BF8-4139-8673-D76CB4F83EDAQ28830533-93373FE3-3013-448B-A635-89CB7B3EADC4Q28831416-DF948646-92D8-43A5-8626-CFC0042C6518Q30369454-A0351737-78F8-4F32-AD8C-A020792960F4Q30414522-8A0BA1C3-CC0D-4C36-A3A4-6161F1B20357Q30424667-92B92826-F706-4E0A-B9D4-FD941EDE4F66Q30474752-F2A558BF-707B-41EF-B25C-EF7BBA85788DQ30570683-6939F6A5-5F6B-4107-B286-C0394EB9688EQ30768165-C19FD6D3-7AD2-4638-AC40-7657373AD969Q33556069-8DB0BDDE-184A-4F42-BB31-1FFF5472C042Q33567229-91075DB0-120B-4DDC-B015-F8A65E7C6E19Q33725453-7C89CFDB-B869-4EE7-AD0F-0BF8B6D8B99EQ33740696-2AD7B7FE-DCE1-4411-B487-901EA04BDCD9Q34175001-03FCCA87-2C5C-4A2F-A260-F7314DE97294Q34307230-80DB60C6-A4FD-4D3F-AEBE-40913773B2D9Q34413061-62D99CA7-83B4-49A6-8C87-EF8DEE2BBEC1Q34491072-CF7BBB84-3F14-4C2D-8AA6-542DEC063633Q34512151-F6FEF28A-2F76-4A52-8C25-4378054FBD45Q34733523-19E6A9C5-D5B6-44DE-BBA6-940966C4F600Q35067202-C346D23C-7ECC-43C3-9A7C-F00BC08FAA30Q35221753-620D9F0F-A5D4-49E8-A3B3-D61D1BBB8DC9Q35624254-00D4519B-40EF-4C48-9BB9-64B24DEFBA69Q35641343-DF9BD699-87BC-4EC8-88C7-A9E2919B9D6EQ35668543-85FCF2BE-F484-4E4D-A196-4EF4C05FAD03Q35721664-D9F5AF56-D6F7-49FF-A018-3419BFE79043Q35962928-6A2B68E4-DFA0-4077-9D44-4048A48678CEQ35989584-6EB3F1C6-1AE8-4C3C-A88F-3FDA1BDC7422Q36003628-C6DAC9F7-18F0-49DB-97AB-CA15192395BAQ36011275-147EC383-579C-4357-A890-4577FEF9734DQ36048504-5A3B3840-5B3F-4A05-929A-BA2BCFA590DC
P2860
Natural and synthetic prion structure from X-ray fiber diffraction
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 28 September 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Natural and synthetic prion structure from X-ray fiber diffraction
@en
Natural and synthetic prion structure from X-ray fiber diffraction.
@nl
type
label
Natural and synthetic prion structure from X-ray fiber diffraction
@en
Natural and synthetic prion structure from X-ray fiber diffraction.
@nl
prefLabel
Natural and synthetic prion structure from X-ray fiber diffraction
@en
Natural and synthetic prion structure from X-ray fiber diffraction.
@nl
P2093
P2860
P921
P356
P1476
Natural and synthetic prion structure from X-ray fiber diffraction
@en
P2093
Alexander L Borovinskiy
Amy Kendall
David W Colby
Gerald Stubbs
Holger Wille
Julian Ollesch
Lillian Bloch
Michele McDonald
P2860
P304
16990-16995
P356
10.1073/PNAS.0909006106
P407
P577
2009-09-28T00:00:00Z