Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
about
Mechanisms of amyloid formation revealed by solution NMRMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Solid-state NMR studies of metal-free SOD1 fibrillar structures.The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.DNP-enhanced MAS NMR of bovine serum albumin sediments and solutions.The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Topical Developments in High-Field Dynamic Nuclear Polarization.Suppression of problematic compound oligomerization by cosolubilization of nondetergent sulfobetainesHigh-resolution NMR characterization of low abundance oligomers of amyloid-β without purificationCharacterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR"CLASSIC NMR": an in-situ NMR strategy for mapping the time-evolution of crystallization processes by combined liquid-state and solid-state measurements.Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.Real-time monitoring of the aggregation of Alzheimer's amyloid-β via1H magic angle spinning NMR spectroscopy.New applications of solid-state NMR in structural biologySSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detailNMR crystallography on paramagnetic systems: solved and open issuesPractical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins
P2860
Q26797492-E6249906-CEA5-40A8-8BDF-BC133E104F46Q30009502-C2B6F5E3-D787-43B8-8B0C-C94072F7EF13Q30153414-A88ED4DA-503B-4A63-A531-ABAD0CEC573DQ30574532-A021DD73-352E-401E-BA77-D0EDD64A3F10Q30741715-86FAE453-CD81-41AA-82D3-3DDDA8BCD308Q33649356-AA697781-2DF4-4586-85B1-C6C47450BC39Q33893017-6DD7B56F-0788-4FD8-B3A8-ED62A9E3762DQ35596929-B6B9F272-C00F-4D31-AF86-07A5684AF4DBQ35753840-DADE1339-8F37-4B2A-A60F-8C53A5598554Q35813445-406783D4-9C06-4E86-B914-4F436B1E2917Q35963074-A81D32F8-B0FD-4A8B-85FC-45B3C585C7F5Q38204914-7C000499-AFF4-4BD6-BFF9-5C9390285344Q42198100-F8B9786A-FD79-4338-B245-0AA64EE26ABFQ42998418-EFD39B7E-DD25-40F3-B6F2-319CCD4B9E0BQ46259687-64439C31-B6DE-4245-B2E9-8D613173B6C6Q48090714-87388BC4-3F04-47DF-9591-7356A10BB5D8Q57095011-1B2463A5-8ABD-4FB9-A3FD-6F8CE385FA2CQ58619042-D8F7EFB9-9A98-44F1-AE94-C6C85E3FF9B9Q58619052-5B160CD5-86B8-464B-A2AD-EE4A88DC14C6Q58619054-39AE173A-0FC7-4E7F-8EB1-37C7430E6315
P2860
Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh-hant
name
Formation kinetics and structu ...... ates by sedimented solute NMR.
@en
Formation kinetics and structu ...... ates by sedimented solute NMR.
@nl
type
label
Formation kinetics and structu ...... ates by sedimented solute NMR.
@en
Formation kinetics and structu ...... ates by sedimented solute NMR.
@nl
prefLabel
Formation kinetics and structu ...... ates by sedimented solute NMR.
@en
Formation kinetics and structu ...... ates by sedimented solute NMR.
@nl
P2093
P2860
P50
P356
P1433
P1476
Formation kinetics and structu ...... ates by sedimented solute NMR.
@en
P2093
Gianluca Gallo
Jiafei Mao
Magdalena Korsak
P2860
P304
P356
10.1002/CBIC.201300141
P577
2013-07-02T00:00:00Z