Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases.
Explore this paper's citation graph
Summary
This work will show successful approaches that have been used recently and will illustrate some of the results that have contributed to elucidate important structural aspects of amyloid formation in vivo.
- Type
- review
- Published
- 2008-12-01
- Cited by
- 116
- References
- 69
- OpenAlex
- https://openalex.org/W1997666386
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:35214490
Keywords
Amyloid fibril, Protein folding, Protein aggregation, Amyloid (mycology), Mechanism (biology)
References
- Watching amyloid fibrils grow by time-lapse atomic force microscopy.
- Glycosaminoglycan and proteoglycan inhibit the depolymerization of beta2-microglobulin amyloid fibrils in vitro.
- A close ultrastructural relationship between sulfated proteoglycans and AA amyloid fibrils.
- Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth.
- Metalloendoprotease cleavage triggers gelsolin amyloidogenesis
- Distribution pattern of matrix metalloproteinases 1, 2, 3, and 9, tissue inhibitors of matrix metalloproteinases 1 and 2, and α2-macroglobulin in cases of generalized AA- and AL amyloidosis
- Increased matrix metalloproteinases as possible cause of osseoarticular tissue destruction in long-term haemodialysis and β2-microglobulin amyloidosis
- Molecular recycling within amyloid fibrils
- Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2+ stabilization
- Gelsolin–derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187
- The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light‐chain protein
- Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils.
- Nucleation of protein fibrillation by nanoparticles
- Misfolding of the cystic fibrosis transmembrane conductance regulator and disease.
- Beta 2-microglobulin amyloid deposit in HLA-B27 transgenic rats
- The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis
- Long term effect of renal transplantation on dialysis-related amyloid deposits and symptomatology.
- Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin.
- Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes.
- Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes.
Cited by
- Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms
- Chronische Entzündung und AA-Amyloidose
- Untangling fibrillogenesis : investigations of the mechanisms of amyloid formation
- Characterizing the Role of HspB2 in Cardiac Metabolism and Muscle Structure Using Yeast and Mammalian Systems
- Engineering and characterization of a binder to inhibit in vivo α-synuclein aggregation
- Amiloidosis asociada a la hemodiálisis
- Amyloid in skin and brain: What′s the link?
- Serum Amyloid A (SAA): Proinflammatory functions and their regulation by serum lipoproteins
- Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones
- From Protein to Fiber: The Characterization and Spectral Analysis of A Model Peptide for Amyloidosis
- Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions
- Transthyretin Aggregate-Specific Antibodies Recognize Cryptic Epitopes on Patient-Derived Amyloid Fibrils
- Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes
- Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism.
- Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose
- Heparin Induces Harmless Fibril Formation in Amyloidogenic W7FW14F Apomyoglobin and Amyloid Aggregation in Wild-Type Protein In Vitro
- Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates.
- Cerato-Populin and Cerato-Platanin, Two Non-Catalytic Proteins from Phytopathogenic Fungi, Interact with Hydrophobic Inanimate Surfaces and Leaves
- Intermolecular β-Strand Networks Avoid Hub Residues and Favor Low Interconnectedness: A Potential Protection Mechanism against Chain Dissociation upon Mutation
- Structure, Folding Dynamics, and Amyloidogenesis of D76N β2-Microglobulin
Related papers
- A generic class of amyloid fibril inhibitors.
- Structural models of amyloid-like fibrils.
- Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology
- Formation of amyloid fibrils from β‐amylase
- Two-step nucleation of amyloid fibrils: omnipresent or not?
- Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
- Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids.
- Protein amyloidose misfolding: mechanisms, detection, and pathological implications.