scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M311300200 |
P698 | PubMed publication ID | 14752113 |
P2093 | author name string | Per Westermark | |
Ronald Wetzel | |||
Brian O'Nuallain | |||
Angela D Williams | |||
P2860 | cites work | Solubilization and disaggregation of polyglutamine peptides | Q28361593 |
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Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange | Q28394786 | ||
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Specificity in intracellular protein aggregation and inclusion body formation | Q33949081 | ||
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Conformational Abs recognizing a generic amyloid fibril epitope | Q34009881 | ||
Transmissibility of systemic amyloidosis by a prion-like mechanism | Q34068073 | ||
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation | Q34088689 | ||
Rationalization of the effects of mutations on peptide and protein aggregation rates. | Q34222395 | ||
Missense mutation of amylin gene (S20G) in Japanese NIDDM patients | Q34393899 | ||
Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease | Q34729047 | ||
Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers | Q35750568 | ||
S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin | Q35829725 | ||
Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence | Q36831406 | ||
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The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus | Q40992063 | ||
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Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide | Q43854800 | ||
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Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity | Q45303479 | ||
Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling. | Q45941938 | ||
Conformational diversity in a yeast prion dictates its seeding specificity | Q46425975 | ||
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Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. | Q46492867 | ||
Prion domain initiation of amyloid formation in vitro from native Ure2p | Q46625178 | ||
Seeding of A beta fibril formation is inhibited by all three isotypes of apolipoprotein E. | Q46722154 | ||
Abeta protofibrils possess a stable core structure resistant to hydrogen exchange | Q47361751 | ||
Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides | Q48406520 | ||
A beta deposition inhibitor screen using synthetic amyloid. | Q48790396 | ||
In vitro growth of Alzheimer's disease beta-amyloid plaques displays first-order kinetics. | Q49161050 | ||
Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin). | Q50864761 | ||
Insulin and Alzheimer's disease: an amyloid connection. | Q52007101 | ||
Analysis of protein aggregation kinetics. | Q52143609 | ||
Interaction between A beta(1-42) and A beta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro. | Q53231526 | ||
Diabetes mellitus and the risk of dementia: The Rotterdam Study. | Q53231897 | ||
Effects of sequential proline substitutions on amyloid formation by human amylin20-29. | Q54128400 | ||
Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB | Q54131245 | ||
Thioflavine T interaction with amyloid β-sheet structures | Q58258322 | ||
P433 | issue | 17 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 17490-17499 | |
P577 | publication date | 2004-01-29 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Seeding specificity in amyloid growth induced by heterologous fibrils | |
P478 | volume | 279 |
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Q96431669 | Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils |
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Q38831388 | Current and future treatment of amyloid diseases |
Q89963670 | Cynomolgus Monkeys With Spontaneous Type-2-Diabetes-Mellitus-Like Pathology Develop Alpha-Synuclein Alterations Reminiscent of Prodromal Parkinson's Disease and Related Diseases |
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Q41845860 | Eighty years of research on islet amyloidosis in Uppsala |
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Q33479158 | Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model |
Q45016854 | Full length amylin oligomer aggregation: insights from molecular dynamics simulations and implications for design of aggregation inhibitors. |
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