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The pharmacology of amyloid precursor protein processing [PDF]

open access: possibleExperimental Gerontology, 2003
The possibility to understand the causes and treat the symptoms of Alzheimer's disease patients is still a great challenge. The triggering events leading to the selective neurodegeneration observed in Alzheimer's brains are not completely understood.
RACCHI, MARCO, GOVONI, STEFANO
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Processing of precursor proteins by plant mitochondria

Archives of Biochemistry and Biophysics, 1990
Precursor proteins from Neurospora crassa were correctly processed by a matrix extract from Vicia faba and cauliflower mitochondria. Processing yielded mature protein of the same molecular mass as mature Neurospora protein. The processing activity has two components.
Matthew A. Harmey   +2 more
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Processing of pro-hormone precursor proteins

Archives of Biochemistry and Biophysics, 1989
Peptide-hormones and other biologically active peptides are synthesized as higher molecular weight precursor proteins (pro-proteins) which must undergo post-translational modification to yield the bioactive peptide(s). These post-translational enzymatic events include limited endoproteolysis and may include other modifications of the generated peptide ...
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Amyloid beta protein precursor is a mitogen

Biochemical and Biophysical Research Communications, 1989
The form of the secreted amyloid beta-protein precursor which contains the protease inhibitor sequence is mitogenic for Swiss 3T3 cells, while the precursor molecule lacking the protease inhibitor domain is not. A ten-fold stimulation of DNA synthesis occurs at 8 x 10(-9) M protein.
Tsunao Saitoh   +3 more
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Eukaryotic protein processing: endoproteolysis of precursor proteins

Current Opinion in Biotechnology, 1997
Limited endoproteolysis of biologically inactive polypeptide precursors is a general mechanism generating a diversity of biologically active peptides and proteins in all eukaryotic phyla. One of the major recognition motifs involves cleavage at either specific single or pairs of basic residues of the general formula (R/K) - Xn - (R/K) decreases, where ...
Michel Chrétien, Nabil G. Seidah
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Identification of microRNA Precursor-Associated Proteins

2018
MicroRNA (miRNA) biogenesis is regulated intricately at multiple levels. In addition to transcriptional control of pri-miRNA loci, sequence as well as structural features of the pri-miRNA-stem loop determine its processing efficiency by the endonucleases Drosha and Dicer.
Nora Treiber   +2 more
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Amyloid Precursor Protein Is Found in Lysosomes

Gerontology, 1993
The major component of Alzheimer's disease amyloid is a small polypeptide referred as the amyloid beta protein, which is derived from a larger precursor, amyloid precursor protein (APP). Cell fractionation and immunological studies on the APP molecule indicate that APP is localized either in the neuron and astrocyte and that the molecule is recovered ...
Shoichi Ishiura   +7 more
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Function of amyloid and amyloid protein precursor

Clinical Neurology and Neurosurgery, 1992
A short review is given of the functions of amyloid (beta/A4) and its precursor protein (APP). The possible relationship between amyloid deposition and dementia is discussed.
Joost Haan, Raymund A.C. Roos
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Genetics of the Alzheimer Amyloid Protein Precursor

1990
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder characterized by gradual loss of memory, reasoning, orientation, and judgment (Katzman, 1983). AD generally occurs as a sporadic disorder of unknown cause. However, a proportion of cases, which have been termed familial Alzheimer’s disease (FAD), are caused by a genetic defect that is
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The Functions of the Amyloid Precursor Protein Gene

Reviews in the Neurosciences, 2001
The amyloid precursor protein (APP) gene and its protein products have multiple functions in the central nervous system and fulfil criteria as neuractive peptides: presence, release and identity of action. There is increased understanding of the role of secretases (proteases) in the metabolism of APP and the production of its peptide fragments. The APP
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