Evidence for assembly of prions with left-handed beta-helices into trimers - Wikidata - wikimedia - TriplyDB

Evidence for assembly of prions with left-handed beta-helices into trimers

Evidence for assembly of prions with left-handed beta-helices into trimers

http://www.wikidata.org/entity/Q34375245

about

β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides Structure of the cross-beta spine of amyloid-like fibrils Hot spots in prion protein for pathogenic conversion Multifaceted Role of Sialylation in Prion Diseases Techniques to elucidate the conformation of prions The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy Crystal structure of human prion protein bound to a therapeutic antibody Prion Fibrillization Is Mediated by a Native Structural Element That Comprises Helices H2 and H3 Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Solid-state NMR as a probe of amyloid structure Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs The bactofilin cytoskeleton protein BacM of Myxococcus xanthus forms an extended β-sheet structure likely mediated by hydrophobic interactions Tetracysteine-tagged prion protein allows discrimination between the native and converted forms Comparative genomic analysis of prion genes Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.A mechanism for copper inhibition of infectious prion conversion Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.How the Sequence of a Gene Specifies Structural Symmetry in Proteins.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?Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.The structure of the infectious prion protein: experimental data and molecular models.Prion protein self-peptides modulate prion interactions and conversion.Water molecules as structural determinants among prions of low sequence identity.Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy Probing structural differences in prion protein isoforms by tyrosine nitration Mapping of possible prion protein self-interaction domains using peptide arrays In vitro and in vivo neurotoxicity of prion protein oligomers.Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy.Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles Heterologous stacking of prion protein peptides reveals structural details of fibrils and facilitates complete inhibition of fibril growth.The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo.Investigating the conformational stability of prion strains through a kinetic replication model.

P2860

Q21558493-F2E706EB-9A79-4C61-B2C3-400B134F2440 Q24548308-342FB011-186C-48FA-85B4-151F449DB431 Q24670553-165AC759-50D7-4AC6-BF0F-795F4AF7BF8D Q26739884-954EF79C-8A79-4A1F-A82A-F242991C1B9A Q26795754-A39496BA-78A3-4841-9130-96EB9E8932A5 Q27312168-889B72E0-F61B-49C9-996E-6C9C8396A93F Q27318382-50071B15-7540-43C6-9003-6949F8820A45 Q27653698-F7CBE9FF-6D0B-4736-9C60-B6CB969CE1CD Q27660444-61A3262D-94A9-433B-A7A7-D6CD793FCE56 Q27665069-A38C4433-2FD1-4A0B-8861-8F030E1D25E7 Q27678836-D0CA12E0-4005-4538-89F0-1C34DFC93D3F Q27679150-669A718E-1AE1-43D2-AABF-FCEB3D8EAF11 Q28388148-FF4DD0AB-99D8-4CD4-8F17-51DA44AC2C84 Q28388671-C5B523FE-6050-4A5E-AB4D-CAC06133847F Q28472742-F42F5A12-6079-4C79-A84C-6771DB4F274F Q28544946-22A1E25C-9353-4FB9-A646-C7B2EC580D91 Q28592095-D4215E57-3869-4CCC-BFD0-D077045BD681 Q28763768-12DB7574-7BEB-4737-82C9-84E0ACD37C1E Q30351368-A450637E-C5F4-4079-ACE5-D6BA81A26F44 Q30354332-95EEAD50-AEF0-4522-899E-35BF86B50FD9 Q30364768-43994993-F7E1-45A1-A504-9A317BF15472 Q30369454-63D26FFD-A744-4AE3-98DE-B977E4F573D3 Q30382223-AF8163F8-B204-4ED3-9FE0-039C4268864E Q30414522-5FA01B1B-C1FB-4839-A167-4C30FDBD3658 Q30424667-330C8DC0-4693-4870-935E-257982467FAA Q30477303-2906DED4-D98E-458F-A509-4E2EE4EBFD53 Q30492360-04B9BFB0-15A5-48FD-A0DA-AED51F5CE5FA Q30768165-8FEC74B0-F768-4717-A150-6F0EF819A17F Q30924592-C871E21C-EF23-4E8C-AE4C-9213150CB19D Q31038011-EA7029B7-8A2F-42A7-B42C-408C8347E540 Q33250429-AFA1322D-2997-438C-BBBB-E5325F7F97BC Q33280623-70C208C2-3AB3-44B5-8821-FA6DB2D4B561 Q33281952-1CA26341-1A2B-4F6E-80E6-33C9663CF308 Q33296885-14F683CA-422F-4233-8017-3B4402F8AB70 Q33341391-37B957A0-81C7-46AB-BC26-9337AE450357 Q33354954-137D1BF7-5208-4D7E-BD44-D5AF9E4DE8F6 Q33420268-7AC1C3D5-E893-45FE-ACB4-492A406030CF Q33433749-3F3A8D02-E180-4ABF-B75E-16C6DE5F3A5D Q33449340-2E7739E7-E360-42BA-9750-5F0A19052E4A Q33478386-D2D48428-A618-4C6D-AEE4-1FA091F1F922

P2860

Evidence for assembly of prions with left-handed beta-helices into trimers

http://www.wikidata.org/entity/Q34375245

description

2004 nî lūn-bûn

@nan

2004 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Evidence for assembly of prions with left-handed beta-helices into trimers

@ast

Evidence for assembly of prions with left-handed beta-helices into trimers

@en

Evidence for assembly of prions with left-handed beta-helices into trimers

@nl

type

label

Evidence for assembly of prions with left-handed beta-helices into trimers

@ast

Evidence for assembly of prions with left-handed beta-helices into trimers

@en

Evidence for assembly of prions with left-handed beta-helices into trimers

@nl

prefLabel

Evidence for assembly of prions with left-handed beta-helices into trimers

@ast

Evidence for assembly of prions with left-handed beta-helices into trimers

@en

Evidence for assembly of prions with left-handed beta-helices into trimers

@nl

P1433

Q34375245-16E59B41-7D31-4F4F-8FFC-70FDCE76CA27

P1476

Q34375245-617111F3-7F74-4F7A-827E-E441B2B6280B

P2093

Q34375245-485DF476-5A0A-4CCA-81E6-FE1DFBC3AFE9

Q34375245-A9E2914E-6847-4D78-9C32-B940F22844AA

P2860

Q34375245-08D23B65-6E47-439B-935E-D2A3328528E9

Q34375245-09E5581D-2840-468B-8C09-853A577C88F6

Q34375245-0BD015AD-CA7D-4527-9EA1-DDCC0BB31466

Q34375245-0F2DBCE1-E1CE-4F1D-86DE-78EDB0562F01

Q34375245-14674C74-0C44-49DF-ABEA-E6D8C4A78BF7

Q34375245-1518FB2F-8990-4DEE-A094-98D42275AFEB

Q34375245-2706D28E-7B7C-4183-9C71-542587DAEA33

Q34375245-289C819E-7F6A-4A42-992C-B5BE21569F68

Q34375245-3041F132-A051-41B5-B4BD-4F7D1BAB9EF7

Q34375245-374BB5BF-4CDF-41DB-93E6-0A0009433C5B

P304

Q34375245-D72FDA44-1B29-4C62-88FF-B582C84D9C8E

P31

Q34375245-B9C4EED8-4296-46C4-991A-8DEAE51A6837

P356

Q34375245-E9B83384-CA87-427B-9FB4-C750DAC7063D

P407

Q34375245-C4841161-170B-41E0-88AF-B233932A3B58

P433

Q34375245-BDE842B1-F5D1-4B95-BC83-7C5B623B8E1A

P478

Q34375245-B3C7DFB8-5B82-4591-95D5-2B9B87017DF1

P50

Q34375245-7489A1E8-C79E-4506-AB0E-64C05ED2AC26

Q34375245-EB8B4DC8-BAB1-4E3F-8E9C-066FB59BE174

P577

Q34375245-F1B5A31A-65D9-4F6A-ACD4-FB17D2F48545

P5875

Q34375245-414CC59A-AEAF-4E45-BD81-E191F8AA04E2

P698

Q34375245-1560334D-D4EF-4757-A59A-D9A4C1B7B81E

P921

Q34375245-D140CBF4-5D28-44FF-BDAE-E9C4C5C9A901

P932

Q34375245-D6D61349-7F9D-4457-82E1-9870E0DC5B54

P356

PNAS.0402254101

P1433

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

P1476

Evidence for assembly of prions with left-handed beta-helices into trimers

@en

P2093

Cédric Govaerts

http://www.w3.org/2001/XMLSchema#string

Holger Wille

http://www.w3.org/2001/XMLSchema#string

P2860

Prion Protein Biology

The structural basis of protein folding and its links with human disease

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.

NMR structures of three single-residue variants of the human prion protein

Crystal structure of beta-helical antifreeze protein points to a general ice binding model

NMR structure of the mouse prion protein domain PrP(121-231)

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes.

Shattuck lecture--neurodegenerative diseases and prions

A method to identify protein sequences that fold into a known three-dimensional structure

Areas, volumes, packing and protein structure

P304

8342-8347

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.0402254101

http://www.w3.org/2001/XMLSchema#string

P407

P433

22

http://www.w3.org/2001/XMLSchema#string

P478

101

http://www.w3.org/2001/XMLSchema#string

P50

Stanley B. Prusiner

P577

2004-05-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8550273

http://www.w3.org/2001/XMLSchema#string

P698

15155909

http://www.w3.org/2001/XMLSchema#string

P921

Prion protein family

P932

420396

http://www.w3.org/2001/XMLSchema#string