Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. - Wikidata - awgldk - TriplyDB

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

http://www.wikidata.org/entity/Q34788209

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The 3D profile method for identifying fibril-forming segments of proteins Misfolding and amyloid aggregation of apomyoglobin The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent.NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Self-assembly of human latexin into amyloid-like oligomers.Dynamics-stability relationships in apo- and holomyoglobin: a combined neutron scattering and molecular dynamics simulations study Protein structure evolution in liquid DESI as revealed by selective noncovalent adduct protein probing.Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity.Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution.Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Intermediacy of poly(L-proline) II and beta-strand conformations in poly(L-lysine) beta-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy.Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Raft lipids as common components of human extracellular amyloid fibrils.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Protein structural perturbation and aggregation on homogeneous surfaces.The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids.Multivalent protein polymers with controlled chemical and physical properties.Potassium and ionic strength effects on the conformational and thermal stability of two aldehyde dehydrogenases reveal structural and functional roles of K⁺-binding sites.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host protein Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobin Unfolding simulations of holomyoglobin from four mammals: identification of intermediates and β-sheet formation from partially unfolded states.Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.Mid-infrared free-electron laser tuned to the amide I band for converting insoluble amyloid-like protein fibrils into the soluble monomeric form Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin Intermediate Tyrosyl Radical and Amyloid Structure in Peroxide-Activated Cytoglobin.Electrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.The structural biology of protein aggregation diseases: Fundamental questions and some answers Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules Modulation of the intermolecular interaction of myoglobin by removal of the heme.Amino acid position-specific contributions to amyloid beta-protein oligomerization.AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.

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P2860

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

http://www.wikidata.org/entity/Q34788209

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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name

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@ast

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

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Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

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type

label

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@ast

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@en

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@nl

prefLabel

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@ast

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@en

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@nl

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PNAS.0303758100

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

P1476

Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.

@en

P2093

Katrin Buder

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

Marcus Fändrich

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Marlis Kittler

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Stephan Diekmann

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Vincent Forge

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P2860

Investigating protein conformation-based inheritance and disease in yeast

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

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).

Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.

Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices.

From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

Pressure-induced perturbation of apomyoglobin structure: fluorescence studies on native and acidic compact forms.

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10.1073/PNAS.0303758100

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100

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14665689

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307590

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