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Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology.
Alzheimer's disease (AD) is a protein misfolding disease characterized by a buildup of β-amyloid (Aβ) peptide as senile plaques, uncontrolled neurodegeneration, and memory loss. AD pathology isExpand
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GTP-Dependent K-Ras Dimerization.
Ras proteins recruit and activate effectors, including Raf, that transmit receptor-initiated signals. Monomeric Ras can bind Raf; however, activation of Raf requires its dimerization. It has beenExpand
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Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer’s Disease and Down syndrome
  • H. Jang, F. Arce, +5 authors R. Lal
  • Medicine, Chemistry
  • Proceedings of the National Academy of Sciences
  • 22 March 2010
Full-length amyloid beta peptides (Aβ1–40/42) form neuritic amyloid plaques in Alzheimer’s disease (AD) patients and are implicated in AD pathology. However, recent transgenic animal models castExpand
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Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.
Antimicrobial peptides (AMPs) induce cytotoxicity by altering membrane permeability. The electrical properties of membrane-associated AMPs as well as their cellular effects have been extensivelyExpand
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Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies.
Antimicrobial peptides (AMPs) are an emerging class of antibiotics for controlling health effects of antibiotic-resistant microbial strains. Protegrin-1 (PG-1) is a model antibiotic among beta-sheetExpand
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Mutations in LZTR1 drive human disease by dysregulating RAS ubiquitination
Regulation of RAS by ubiquitination The protein LZTR1 is mutated in human cancers and developmental diseases. Work from two groups now converges to implicate the protein in regulating signaling byExpand
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GTP-dependent K-Ras dimerization
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Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process.
Here we model the Alzheimer beta-peptide ion channel with the goal of obtaining insight into the mechanism of amyloid toxicity. The models are built based on NMR data of the oligomers, with theExpand
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Ras Conformational Ensembles, Allostery, and Signaling.
Ras proteins are classical members of small GTPases that function as molecular switches by alternating between inactive GDP-bound and active GTP-bound states. Ras activation is regulated by guanineExpand
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Antimicrobial properties of amyloid peptides.
More than two dozen clinical syndromes known as amyloid diseases are characterized by the buildup of extended insoluble fibrillar deposits in tissues. These amorphous Congo red staining depositsExpand
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