Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Claudia B. Caputo"'
Publikováno v:
Biochemical and Biophysical Research Communications. 221:248-253
The protein tau was degraded to distinct products by a DNA-stimulated protease isolated from human leukemia HL-60 cell extracts. The enzyme partially purified by sequential chromatography on GTP-agarose, DEAE-cellulose, and TSK 3000 (0.6 X 60 mm) col
Publikováno v:
Molecular Brain Research. 20:221-228
The tau protein of Alzheimer paired helical filaments (PHFs) is aberrantly phosphorylated, as evidenced by its reactivity with several phosphate-dependent antibodies. We sought to identify whether this unusual phosphorylation state exists in tau expr
Publikováno v:
Brain Research. 611:237-242
Tau protein was evaluated as a substrate for a proline-directed protein kinase (p34cdc2/p58cyclin A) which recognizes the phosphorylation site motif X-Ser/Thr-Pro-X. The shortest human tau isoform, expressed as a recombinant protein, was phosphorylat
Publikováno v:
Journal of Biological Chemistry. 268:1166-1173
Tau protein is an integral component of paired helical filaments, a pathological feature of Alzheimer's disease. tau extracted from these filaments displays decreased electrophoretic mobility due to aberrant phosphorylation. Here we show that recombi
Publikováno v:
Brain Research. 597:227-232
The composition of paired helical filaments (PHFs), the intracellular amyloid fibrils that accumulate in the brains of Alzheimer patients, is not completely known. We investigated whether synthetic peptides from β-amyloid precursor protein (APP) can
Publikováno v:
Archives of Biochemistry and Biophysics. 292:199-205
A synthetic peptide whose sequence corresponds to the 20 carboxy-terminal amino acids of beta-amyloid protein precursor (APP) was found to form fibrils in vitro. These fibrils showed birefringence in polarized light when stained with Congo red, fluor
Publikováno v:
Journal of Neuroscience Research. 30:154-162
Three isoforms of human tau protein were compared for their abilities to induce microtubule assembly. The three isoforms, tau 3 (tau containing three microtubule-binding domains), tau 4 (tau containing four microtubule-binding domains) and tau 4L (ta
Publikováno v:
Brain research. 628(1-2)
Aluminum has been detected in Alzheimer neurofibrillary tangles, but the significance of its presence is unknown. The principal component of tangles is the paired helical filament (PHF), comprised of tau protein. We investigated whether aluminum coul
Autor:
Ann W. Fieles, Michel Goedert, Tyrrell Norris, Virginia M.-Y. Lee, Claudia B. Caputo, Clay W Scott, Mathew M.S. Lo, Pauline G. Dargis
Publikováno v:
Brain research. Molecular brain research. 20(3)
Tau protein is a neuronal microtubule-associated protein that promotes the assembly and stability of microtubules. To evaluate the biological significance of tau isoform diversity, NIH-3T3 cells were stably transfected with cDNAs encoding each of the
Publikováno v:
Archives of biochemistry and biophysics. 306(2)
C-APP, a synthetic peptide corresponding to the C-terminal 20 amino acids of β-amyloid precursor protein, forms amyloid fibrils in vitro . We investigated the effect of altering the C-APP sequence or deleting part of it on its ability to form amyloi