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Amyloid

Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously…

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Overview

Definition

Biological functions

Amyloid toxicity

Molecular biology

Histological staining

Advanced semantic analysis

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Map overview Semantic statistics

Amyloid

Nodes146
Edges145
Triples117
Avg. degree1.99
Density0.013699
Components1

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Amyloid

Top relations

related to Biological functions · 39
Amyloid → Aplysia, CPEB, Csg, Curli, Cyc8p, Enterobacteriales, Fragments, Functional, Gas, GvpA, Homo, Hydrophobins, Intralumenal, Many, Methanosaeta, Neurospora, OCT8, PIN, PMELPeptide/protein, Podospora
related to Amyloid toxicity · 13
Amyloid → Also, AMPA, An, Calcium, Channel, Huntington's, In, NMDA, ROS, Studies, The, There, These
related to Effect of amino acid sequence on polymerization · 10
Amyloid → For, Glutamine-rich, Huntington's, II, In, Studies, The, There, When, Yeast
related to Structure · 10
Amyloid → AFM, Amyloids, Congo, Each, FTIR, Such, TEM, The, There, X-ray
related to Definition · 8
Amyloid → Ancient Greek, For, Latin, Microbiologists, Recently, Rudolf Virchow, The, These
related to External links · 7
Amyloid → Alzheimer's, Amyloid-Like Structure, Bacterial Inclusion Bodies Contain, Journal, Molecular, Protein Folding Disorders, SciVeeAmyloid Cascade HypothesisAmyloid
related to Histological staining · 6
Amyloid → Congo Red, In, Modern, NIAD-4, Recently, To
related to Proteins forming amyloids in human diseases · 5
Amyloid → Amyloidosis, ATTR, The International Society, To, TTR
related to Formation by polymerization · 3
Amyloid → Fibrils, In, When
is a · 2
Amyloid → extracellular, presence of a fibrillar morphology with the expected diameter

Important terminology Word statistics

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Important terminology

fibrils proteins structure diseases amyloids secondary form formation protein may β-sheet fibril various also nucleation aggregates cross-β associated structures different

Entity relationships Subject–Predicate–Object triples

SubjectPredicateObjectConfidenceSrc
Amyloidcausesdiseases are unclear0.90text
Amyloidis aextracellular0.90text
Amyloidis apresence of a fibrillar morphology with the expected diameter0.90text
serum amyloid P componentinstance ofThese deposits often recruit various sugars and other components0.80text
resulting in complexinstance ofThese deposits often recruit various sugars and other components0.80text
and sometimes inhomogeneous structuresinstance ofThese deposits often recruit various sugars and other components0.80text
amylininstance ofwith analogous findings in a C. elegans model system with engineered polyglutamine peptides.Other polypeptides and proteins0.80text
the β amyloid peptide do not have a simple consensus sequenceinstance ofwith analogous findings in a C. elegans model system with engineered polyglutamine peptides.Other polypeptides and proteins0.80text
are thought to aggregate through the sequence segments enriched with hydrophobic residuesinstance ofwith analogous findings in a C. elegans model system with engineered polyglutamine peptides.Other polypeptides and proteins0.80text
or residues with high propensity to form β-sheet structureinstance ofwith analogous findings in a C. elegans model system with engineered polyglutamine peptides.Other polypeptides and proteins0.80text
thioflavin Tinstance ofamyloid diseases are typically identified by a change in the spectroscopic properties of planar aromatic dyes0.80text
congo red or NIAD-4instance ofamyloid diseases are typically identified by a change in the spectroscopic properties of planar aromatic dyes0.80text

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