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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
A range of human degenerative conditions, including Alzheimer's disease, light-chain amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of proteinaceousExpand
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
Muscle acylphosphatase (AcP) is a small protein that folds very slowly with two-state behavior. The conformational stability and the rates of folding and unfolding have been determined for a numberExpand
Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.
[NiFe]-hydrogenases require a set of complementary and regulatory proteins for correct folding and maturation processes. One of the essential regulatory proteins, HypF (82kDa) contains a N-terminalExpand
Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity*
The intracellular free Ca2+ concentration and redox status of murine fibroblasts exposed to prefibrillar aggregates of the HypF N-terminal domain have been investigated in vitro and in vivo using aExpand
Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms
More than 40 human diseases are associated with fibrillar deposits of specific peptides or proteins in tissue. Amyloid fibrils, or their precursors, can be highly toxic to cells, suggesting their keyExpand
The low M r phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase
The low molecular weight phosphotyrosine protein phosphatase (LMW‐PTP) is phosphorylated by Src and Src‐related kinases both in vitro and in vivo; in Jurkat cells, and in NIH‐3T3 cells, it becomesExpand
Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N‐terminal domain
The HypF N‐terminal domain has been found to convert readily from its native globular conformation into protein aggregates with the characteristics of amyloid fibrils associated with a variety ofExpand
Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon.
Amyloid aggregation starts with the initial misfolding of peptide/protein precursors, with subsequent structural rearrangement into oligomers and protofibrils; the latter eventually organize intoExpand
Dephosphorylation of tyrosine phosphorylated synthetic peptides by rat liver phosphotyrosine protein phosphatase isoenzymes
Five phosphotyrosine‐containing peptides have been synthesized by FMOC solid‐phase peptide synthesis. These peptides correspond to the 411–419 sequence of the Xenopus src oncogene, to the 1191–1220Expand
Mutational analysis of the propensity for amyloid formation by a globular protein
Acylphosphatase can be converted in vitro, by addition of trifluoroethanol (TFE), into amyloid fibrils of the type observed in a range of human diseases. The propensity to form fibrils has beenExpand