Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates.
Dominic M. Walsh,Dean M. Hartley,Yoko Kusumoto,Youcef Fezoui,Margaret M. Condron,Aleksey Lomakin,Aleksey Lomakin,George B. Benedek,Dennis J. Selkoe,David B. Teplow +9 more
TL;DR: Walsh et al. as discussed by the authors found that amyloid protofibrils are in equilibrium with low molecular weight Abeta (monomeric or dimeric) and have a secondary structure characteristic of Amyloid fibrils.
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About: This article is published in Journal of Biological Chemistry. The article was published on 03 Sep 1999. and is currently open access. The article focuses on the topics: Amyloid beta & P3 peptide.
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Citations
Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer's disease
Marta M. Lipinski,Bin Zheng,Tao Lu,Zhenyu Yan,Bénédicte F. Py,Aylwin Ng,Ramnik J. Xavier,Cheng Li,Bruce A. Yankner,Clemens R. Scherzer,Junying Yuan +10 more
TL;DR: It is shown that reactive oxygen species (ROS) serve as common mediators upstream of the activation of the type III PI3 kinase, which is critical for the initiation of autophagy, and it is demonstrated thatAutophagy is transcriptionally down-regulated during normal aging in the human brain.
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Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies.
TL;DR: A paradigm shift is emerging that necessitates the reevaluation of the relative importance of polymeric (fibrillar) vs. oligomeric assemblies in the pathobiology of AD.
Amyloid β-Protein Assembly and Alzheimer Disease
TL;DR: The discussion that follows seeks to introduce the reader to the complex world of Aβ assembly and biological activity, a goal it hope will provide a conceptual framework upon which further knowledge or experimentation may be built.
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Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases.
TL;DR: This theme of protein aggregation as it relates to the two most common neurodegenerative conditions—Alzheimer's and Parkinson’s diseases is discussed.
567
Semen-Derived Amyloid Fibrils Drastically Enhance HIV Infection
Jan Münch,Elke Rücker,Ludger Ständker,Knut Adermann,Christine Goffinet,Michael Schindler,Steffen Wildum,Raghavan Chinnadurai,Devi Rajan,Anke Specht,Guillermo Giménez-Gallego,Pedro Cuevas Sánchez,Douglas M. Fowler,Atanas V. Koulov,Jeffery W. Kelly,Walther Mothes,Jean-Charles Grivel,Leonid Margolis,Oliver T. Keppler,Wolf-Georg Forssmann,Frank Kirchhoff +20 more
TL;DR: It is shown that naturally occurring fragments of the abundant semen marker prostatic acidic phosphatase form amyloid fibrils, termed Semen-derived Enhancer of Virus Infection (SEVI), capture HIV virions and promote their attachment to target cells, thereby enhancing the infectious virus titer by several orders of magnitude.
564
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Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
Elizabeth H. Corder,Ann M. Saunders,Warren J. Strittmatter,Donald E. Schmechel,P. C. Gaskell,Gary W. Small,A. D. Roses,Jonathan L. Haines,Margaret A. Pericak-Vance +8 more
TL;DR: The APOE-epsilon 4 allele is associated with the common late onset familial and sporadic forms of Alzheimer9s disease (AD) in 42 families with late onset AD.
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TL;DR: A locus segregating with familial Alzheimer's disease (AD) has been mapped to chromosome 21, close to the amyloid precursor protein (APP) gene as discussed by the authors, which suggests that some cases of AD could be caused by mutations in the APP gene.
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TL;DR: It is demonstrated that in this kindred, which shows linkage to chromosome 21 markers, there is a point mutation in the APP gene that causes an amino-acid substitution close to the carboxy terminus of the β-amyloid peptide.
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Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
R. Sherrington,Evgeny I. Rogaev,Yan Liang,Ekaterina Rogaeva,G. Levesque,M. Ikeda,H. Chi,Chih-Ping Lin,Gavin Li,K. Holman,T. Tsuda,L. Mar,J. F. Foncin,Amalia C. Bruni,Mp Montesi,Sandro Sorbi,Innocenzo Rainero,Lorenzo Pinessi,L. Nee,Ilya Chumakov,Daniel A. Pollen,A. Brookes,Philippe Sanseau,R. Polinsky,Wilma Wasco,H. A. R. Da Silva,Jonathan L. Haines,Margaret A. Pericak-Vance,Rudolph E. Tanzi,A. D. Roses,Paul E. Fraser,Johanna M. Rommens,P. St. George-Hyslop +32 more
TL;DR: A minimal cosegregating region containing the AD3 gene is defined, and at least 19 different transcripts encoded within this region corresponds to a novel gene whose product is predicted to contain multiple transmembrane domains and resembles an integral membrane protein.
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Diffusible, nonfibrillar ligands derived from Aβ1–42 are potent central nervous system neurotoxins
Mary P. Lambert,A. K. Barlow,Brett A. Chromy,C. Edwards,R. Freed,M. Liosatos,Todd E. Morgan,Irina Rozovsky,Barbara L. Trommer,Kirsten L. Viola,Pat Wals,Chuan Zhang,Caleb E. Finch,Grant A. Krafft,William L. Klein +14 more
TL;DR: It is hypothesized that impaired synaptic plasticity and associated memory dysfunction during early stage Alzheimer's disease and severe cellular degeneration and dementia during end stage could be caused by the biphasic impact of Abeta-derived diffusible ligands acting upon particular neural signal transduction pathways.
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