|1.||Inestrosa, Nibaldo C: 1 article (11/2014)|
|2.||Johnson, Gail V W: 1 article (11/2014)|
|3.||von Bernhardi, Rommy: 1 article (11/2014)|
|4.||Quintanilla, Rodrigo A: 1 article (11/2014)|
|5.||Godoy, Juan A: 1 article (11/2014)|
|6.||Xiong, Lize: 1 article (07/2014)|
|7.||Shi, Ming: 1 article (07/2014)|
|8.||Zhang, Yunxia: 1 article (07/2014)|
|9.||Zhao, Gang: 1 article (07/2014)|
|10.||Zhang, Guangyun: 1 article (07/2014)|
|1.||Alzheimer Disease (Alzheimer's Disease)
11/01/2014 - "Tau phosphorylated at the PHF-1 epitope (S396/S404) is likely involved in the pathogenesis of Alzheimer's disease (AD). "
04/01/2005 - "Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease."
04/01/1994 - "A phosphorylated tau epitope specific for paired helical filaments in Alzheimer's disease is recognized by monoclonal antibody PHF-1. "
07/04/2012 - "Here we show in human SH-SY5Y cells, in dopaminergic neurons, and in wild-type mice that l-dopa results in a reduced SAM/SAH ratio that is associated with hypomethylation of PP2A and increased phosphorylation of Tau (p-Tau) at the Alzheimer's disease-like PHF-1 phospho-epitope. "
03/01/1993 - "Therefore, expression of PHF-1 immunoreactive proteins in Alzheimer's disease suggests that paired helical filament formation might be triggered by mechanisms related to axon regeneration."
06/01/1995 - "Analogous to its presence in immature neurons, we report here that the PHF-1 tau epitope spontaneously occurs in the human neuroblastoma cell line SHSY5Y, where its level can be regulated by differentiation and by molecules found in the extracellular matrix. "
04/01/1994 - "We have found that proliferating SH-SY5Y human neuroblastoma cells also express PHF-1 tau. "
04/01/1999 - "In the present study, microinjection of MAP kinase into SH-SY-5Y human neuroblastoma cells increased tau immunoreactivity toward the phosphodependent antibodies PHF-1 and AT-8. "
03/15/2003 - "We have found that acrolein, a peroxidation product from arachidonic acid, increases the phosphorylation of tau at the site recognized by PHF-1 both in human neuroblastoma cells and in primary cultures of mouse embryo cortical neurons. "
06/01/1995 - "The effects of retinoic acid on PHF-1 immunofluorescence were modifiable by fibronectin, which can be released by some neuroblastoma cell lines [Ciccarone V. et al. (1989) Cancer Res. 49, 219-225; Yoshihara T. "
|3.||Memory Disorders (Memory Loss)
07/01/2014 - "Ischemic insults increased the levels of phosphorylated tau protein at Ser199/202 and PHF-1 sites and caused animal memory deficits. "
04/01/2012 - "Pearson analysis showed that the memory deficit was only significantly correlated with tau phosphorylation level at PHF-1, pS199/202, pT231 and pS396 epitopes. "
04/01/2012 - "In the present study, we expressed human Val97Leu mutant presenilin-1, which is reported in Chinese pedigrees by our group, in transgenic mice and found that the mutant presenilin-1 induced spatial memory deficit and tau hyperphosphorylation at PHF-1, pS199/202, pT231 and pS396 epitopes, but not at pS214 and pS422 epitopes. "
03/01/1996 - "By 6 h after heat shock, there was progressive hyperphosphorylation of tau in female but not male rats exemplified by (1) upward gel mobility shift recognized by PHF-1, Tau-5, and Tau-46, and by Tau-1 after dephosphorylation; (2) significant increase in the ratio of total tau to nonphosphorylated tau; and (3) rephosphorylation of the Tau-1 epitope in the somatodendritic compartment. "
12/19/2000 - "We have previously shown, by using the phosphate-dependent anti-tau antibodies Tau-1 and PHF-1, that heat shock induces rapid dephosphorylation of tau followed by hyperphosphorylation in female rats. "
03/01/1996 - "At 0 h after heat shock, there was dephosphorylation of tau in both female and male rats as evidenced by (1) accentuation and attenuation of tau isoforms recognized by Tau-1 and PHF-1, respectively, and recognition of additional tau polypeptides by Tau-1, Tau-5, and Tau-46 but not PHF-1; (2) significant increase in the nonphosphorylated Tau-1 epitope with resultant decrease in the ratio of total (phosphorylated plus nonphosphorylated) tau to nonphosphorylated tau; and (3) dephosphorylation of the Tau-1 epitope in the somatodendritic compartment. "
|5.||Proteins (Proteins, Gene)
|9.||Protein Isoforms (Isoforms)
|10.||tau Proteins (tau Protein)