Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
about
As a toxin dies a prion comes to life: A tentative natural history of the [Het-s] prionFibrillogenesis of huntingtin and other glutamine containing proteinsThe relationship between amyloid structure and cytotoxicityA proton-detected 4D solid-state NMR experiment for protein structure determinationThe amyloid-Congo red interface at atomic resolutionAntiparallel -sheet architecture in Iowa-mutant -amyloid fibrilsAtomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsMolecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonanceMeasurement of amyloid formation by turbidity assay-seeing through the cloudMolecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel networkSite-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46KUnlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicityStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreA general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymersAtomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.4D solid-state NMR for protein structure determination.The structure of the infectious prion protein: experimental data and molecular models.Hexagonal ice in pure water and biological NMR samples.Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids.VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy.Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomesEfficient modeling of symmetric protein aggregates from NMR data.Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures.Cooperativity among short amyloid stretches in long amyloidogenic sequencesThe Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids.The mechanism of toxicity in HET-S/HET-s prion incompatibility.Physical and structural basis for polymorphism in amyloid fibrilsStructural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopyHigh-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.Structural insights into functional and pathological amyloid.Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid foldStructured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopyStructural studies of truncated forms of the prion protein PrP.Amyloid polymorphism: structural basis and neurobiological relevance.Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studiesCompensated second-order recoupling: application to third spin assisted recoupling.
P2860
Q26825702-99C84214-BFFA-4E1B-A7E8-673E37BB7AE2Q26850062-CF849618-0D05-493A-8839-CB6C1375AE4CQ27012641-F8B5DE0C-49D2-4530-9022-80D7F0DAE829Q27667130-393A49C6-8844-4C8F-8DAD-74FB8BCFC31FQ27667880-9F89A8AF-7FF9-473A-B3DA-50E434B6DCB4Q27677945-807639C6-B1D3-4FBF-BF63-F7511396BB3AQ27714742-9D1A9700-8F88-4DEC-9C41-28D878D2094CQ28066391-CCFC544F-780C-49B4-9700-9D04B750E98FQ28080287-8D2FB8CD-207B-4CAB-9325-8CD11BBBDBEEQ28385938-798DA7B0-66B0-48F2-B130-CD790B5B0B6DQ28487771-D6A19D7A-2ABF-4534-95A0-97E75E609295Q28540502-85A21C35-C8AB-419C-B855-D88E0CA37FEDQ28553950-A737AA74-817E-4022-B675-69A863D24B05Q30010284-5EACB68D-CD19-4B94-8742-07A736D1CA7CQ30391127-3AF40403-4EBE-4989-BE92-454F6C10AF4AQ30414061-0A725B24-CB05-41B3-9747-F92B458E7DB3Q30768165-65F7948C-EC0B-4DBE-8DEB-35078CFD3F27Q31151675-3B673838-2295-47C4-8427-2852A5983B96Q31159621-56B00298-837C-4FB4-97CB-A1240C00F9B1Q33749018-3A51D25B-B68C-493A-A525-85BF5207B18DQ34077837-8505F9CB-AD1C-4137-96D9-318C94913F08Q34106370-8E4ADFE7-1564-48C4-9DE7-D0E0EE8419D0Q34208232-C195A42B-D7C9-456C-A737-102A49C9C906Q34228516-5EB3EFAD-7775-4EC8-8B5C-C4E51B2C0A16Q34288597-DB7F3DE1-E7CD-4CE1-B120-2360CC20A64FQ34307230-583DB064-12A0-4DB6-BD1B-0F3CD16D4F95Q34326067-A25D7300-40B9-4512-95A1-081052BE0DE2Q34482233-5C8763D7-C9F6-445F-9DD0-11105DBC36DFQ34539592-4D348A8B-05EA-492D-86BE-FC5F44EBAF83Q34559641-4EB2E0F3-01FC-42D0-831F-07F7481918DCQ34602521-2217CF69-1DCA-4EAE-91B2-72ADCCF0DB95Q34610814-EA5D0083-FBF4-4C8B-9E7A-563421DECBD5Q34947293-870701F4-3EE9-4AEC-A4FE-BA5BD6D41179Q35130900-58C94C03-3688-4B0D-BE9A-D89C2F13F5D7Q35168339-3E8F19E6-CD26-4447-B238-A40E2571E8D8Q35190046-AA27D27E-B1C1-4294-85CB-BCB0ABF5D915Q35221753-5146A000-D8C9-48AE-96DE-0B4EB6B93BA4Q35586308-F974B81D-7872-4227-831E-10E7AA924FB9Q35596512-1AC8F0C5-C978-4BCA-AB4F-281B285CAB1DQ35633887-9D74E227-F8B5-465B-A3F1-8545528B9E8C
P2860
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@ast
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@en
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@nl
type
label
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@ast
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@en
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@nl
altLabel
Atomic-Resolution Three-Dimens ...... y Solid-State NMR Spectroscopy
@en
prefLabel
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@ast
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@en
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@nl
P50
P3181
P356
P1476
Atomic-resolution three-dimens ...... y solid-state NMR spectroscopy
@en
P2093
Anja Böckmann
Hélène Van Melckebeke
P304
P3181
P356
10.1021/JA104213J
P407
P577
2010-10-06T00:00:00Z