The X-ray interpretation of denaturation and the structure of the seed globulins
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Molecular basis for insulin fibril assemblyStructure-based design of non-natural amino-acid inhibitors of amyloid fibril formationExperimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrilsPrediction of Peptide and Protein Propensity for Amyloid FormationProteins of the Nervous System: Considered in the Light of the Prevailing Hypotheses on Protein Structure.Toxic fibrillar oligomers of amyloid-β have cross-β structure.Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers.Hydration water mobility is enhanced around tau amyloid fibers.An X-ray and electron microscope study of tropomyosinThe polypeptide-chain configuration in hemoglobin and other globular proteinsMolecular basis for amyloid fibril formation and stability.Identifying the amylome, proteins capable of forming amyloid-like fibrilsOn the Structure of Native, Denatured, and Coagulated ProteinsPhage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.Strain-specific morphologies of yeast prion amyloid fibrils.Amyloid structure: conformational diversity and consequences.Multidimensional structure-activity relationship of a protein in its aggregated states.Towards revealing the structure of bacterial inclusion bodies.Looked at life from both sides nowStructural studies of truncated forms of the prion protein PrP.Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid foldTHE SOLUTION PROPERTIES AND CONFIGURATIONS OF A POLYAMPHOLYTIC POLYPEPTIDE: COPOLY-L-LYSINE-L-GLUTAMIC ACIDMOLECULAR WEIGHT, ELECTROCHEMICAL AND BIOLOGICAL PROPERTIES OF TUBERCULIN PROTEIN AND POLYSACCHARIDE MOLECULES.A solenoid design for assessing determinants of parallel β-sheet registration.The role of β-sheets in the structure and assembly of keratins.Natural biomolecules and protein aggregation: emerging strategies against amyloidogenesisThe structural biology of protein aggregation diseases: Fundamental questions and some answersNatural compounds may open new routes to treatment of amyloid diseasesAn amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilThe yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure.Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).Short protein segments can drive a non-fibrillizing protein into the amyloid state.Natural and synthetic prion structure from X-ray fiber diffractionInconvenient facts about pathological amyloid fibrils.Fungal prion HET-s as a model for structural complexity and self-propagation in prions.Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Modular design in natural and biomimetic soft materials.
P2860
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P2860
The X-ray interpretation of denaturation and the structure of the seed globulins
description
1935 nî lūn-bûn
@nan
1935年の論文
@ja
1935年論文
@yue
1935年論文
@zh-hant
1935年論文
@zh-hk
1935年論文
@zh-mo
1935年論文
@zh-tw
1935年论文
@wuu
1935年论文
@zh
1935年论文
@zh-cn
name
The X-ray interpretation of denaturation and the structure of the seed globulins
@en
type
label
The X-ray interpretation of denaturation and the structure of the seed globulins
@en
prefLabel
The X-ray interpretation of denaturation and the structure of the seed globulins
@en
P2093
P356
P1433
P1476
The X-ray interpretation of denaturation and the structure of the seed globulins
@en
P2093
P2860
P304
2351-2360.1
P356
10.1042/BJ0292351
P407
P577
1935-10-01T00:00:00Z