Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers.
about
Probing structural differences in prion protein isoforms by tyrosine nitrationN-terminal domain of prion protein directs its oligomeric association.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrilsPartially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Rheologic behavior of osteoarthritic synovial fluid after addition of hyaluronic acid: a pilot study.Thermodynamic characterization of the unfolding of the prion protein.Prions and manganese: A maddening beast.Complement protein C1q forms a complex with cytotoxic prion protein oligomersNMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility.Interaction of prion protein with small highly structured RNAs: detection and characterization of PrP-oligomers.Conformational changes and development of proteinase K resistance in surface-immobilized PrP.Activation of classical pathway of complement cascade by soluble oligomers of prion.
P2860
Q33280623-E12BACCE-989D-4771-A8F9-B0C132E9F063Q34170632-510526C7-1DB8-4ACE-B763-C99945C98C85Q34414446-8B4DFCCB-3291-4FCF-88E9-F8BF3E99728AQ34416296-7C157EA3-35F9-46F7-9AA9-D85D80698EA5Q36283277-C744D4CD-73EA-475F-8D56-AFE52565EFACQ36954090-9BBB47AE-3095-49A8-82DD-89BB763EC7FDQ37380193-4A41BCDF-D245-41F5-80FE-CBD800CF6752Q37533502-44CE6566-7BAB-4AB5-AAA9-53BD4DD61E9FQ37851367-708C5CF0-D336-4D7C-99E8-7991ED790703Q41048016-639B24FC-1722-4992-85B2-9606BA9E0058Q42924468-783CFD6D-C91D-48A0-AFA9-3908AA6FF788Q48498733-AAFA4AE7-9F29-4B80-B67B-F53036B5518BQ51575226-7FBB6AD5-54C7-4F9D-828A-7C9BBC5BCE9DQ51577199-3274537B-9B38-4DCA-852F-494F51E4D677
P2860
Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Assembly of the full-length re ...... ormation of soluble oligomers.
@ast
Assembly of the full-length re ...... ormation of soluble oligomers.
@en
type
label
Assembly of the full-length re ...... ormation of soluble oligomers.
@ast
Assembly of the full-length re ...... ormation of soluble oligomers.
@en
prefLabel
Assembly of the full-length re ...... ormation of soluble oligomers.
@ast
Assembly of the full-length re ...... ormation of soluble oligomers.
@en
P2093
P1476
Assembly of the full-length re ...... Formation of soluble oligomers
@en
P2093
Charlotte Vendrely
Hélène Valadié
Jéremy Cappadoro
Laurent Cardin
Lucie Bednarova
Marc Jamin
Marguerite Rinaudo
Marielle Pasdeloup
P304
P356
10.1016/J.BBAGEN.2005.05.017
P407
P50
P577
2005-08-01T00:00:00Z