Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen. - Wikidata - wikimedia - TriplyDB

Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen.

Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen.

http://www.wikidata.org/entity/Q46868630

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Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype Class I Major Histocompatibility Complex, the Trojan Horse for Secretion of Amyloidogenic β 2 -Microglobulin Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequence Systemic amyloidosis: lessons from β2-microglobulin.Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion Calcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architecture Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Hydrophobin Vmh2-glucose complexes self-assemble in nanometric biofilms A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity.beta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Misfolding of amyloidogenic proteins and their interactions with membranes.The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Molecular pathogenesis of human amyloidosis: Lessons from β2 -microglobulin-related amyloidosis.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.Role of parnaparin in atherosclerosis.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity.Sulfated glycosaminoglycans in protein aggregation diseases.beta2-Microglobulin is potentially neurotoxic, but the blood brain barrier is likely to protect the brain from its toxicity.Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin.Heparin binds 8 kDa gelsolin cross-β-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension.Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin.Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Assembly of the fungal SC3 hydrophobin into functional amyloid fibrils depends on its concentration and is promoted by cell wall polysaccharides.Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction.Structure and assembly-disassembly properties of wild-type transthyretin amyloid protofibrils observed with atomic force microscopy.Heparin-induced amyloid fibrillation of β2 -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram.The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

P2860

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P2860

Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen.

http://www.wikidata.org/entity/Q46868630

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2007 nî lūn-bûn

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Heparin strongly enhances the ...... e presence of type I collagen.

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Heparin strongly enhances the ...... e presence of type I collagen.

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Heparin strongly enhances the ...... e presence of type I collagen.

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Heparin strongly enhances the ...... e presence of type I collagen.

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Alessandra Gliozzi

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Annalisa Relini

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Antonio Rossi

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Laura Verga

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Loredana Marchese

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P2860

Confinement as a determinant of macromolecular structure and reactivity. II. Effects of weakly attractive interactions between confined macrosolutes and confining structures.

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

Protein misfolding, functional amyloid, and human disease

1H NMR assignments and secondary structure of human beta 2-microglobulin in solution

Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth

Lysine 58-cleaved beta2-microglobulin is not detectable by 2D electrophoresis in ex vivo amyloid fibrils of two patients affected by dialysis-related amyloidosis.

The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids.

In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis

Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit.

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4912-4920

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10.1074/JBC.M702712200

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