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Background A survey was developed to characterize disease incidence, common pathology lesions, environmental characteristics, and nutrition programs within captive research marmoset colonies. Methods Seventeen research facilities completed the electronic survey. Results Nutritional management programs varied amongst research institutions housing marmosets; eight primary base diets were reported. The most common clinical syndromes reported were gastrointestinal disease (i.e. inflammatory bowel disease like disease, chronic lymphocytic enteritis, chronic malabsorption, chronic diarrhea), metabolic bone disease or fracture, infectious diarrhea, and oral disease (tooth root abscesses, gingivitis, tooth root resorption). The five most common pathology morphologic diagnoses were colitis, nephropathy/nephritis, enteritis, chronic lymphoplasmacytic enteritis, and cholecystitis. Obesity was more common (average 20% of a reporting institution's population) than thin body condition (average 5%). Conclusions Through review of current practices, we aim to inspire development of evidence‐based practices to standardize husbandry and nutrition practices for marmoset research colonies.

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PTHs) as potent lead structure. Here we report the comparison of PTHs to selected curcumin derivatives and approved tetracyclines for their tau antiaggregatory properties and their affinity to fibrillar beta-amyloid in several assays and cellular models. The most potent fluorescent compounds were evaluated for beta-amyloid/tau PHF selectivity by fluorescence microscopy of human AD probes. Methods: Lead Optimization of PTHs. Several diverse PTH analogues were obtained by variation of the substituents R1-R4 to explore a preliminary SAR. Fluorescent substituents were incorporated without significantly compromising in vitro activity. Results: Tau-biased ligands with enhanced affinity to tau paired helical filaments over beta-amyloid were identified by a panel of protein aggregation assays and fluorescence microscopy of human AD preparations. Conclusions: Phenylthiazolylhydrazides are potent inhibitors of tau-aggregation. The fluorescence microscopy of human AD preparation suggests a binding to growth-relevant sites of tau aggregates.Background: Tau is the major microtubule-associated protein in neurones, which functions in the formation and maintenance of axons by influencing microtubule organization. Increased tau phosphorylation is also a salient feature of Alzheimer's disease (AD) and tauopathies such as frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17). In these neurodegenerative disorders, normally soluble tau is present as paired-helical filaments (PHFs), which in turn aggregate to form neurofibrillary tangles (NFTs). p53 and p73 are tumor suppressor proteins, which induces cell cycle arrest or apoptosis. Methods: Here we explore the effects of p53 family members (p53 and p73␣) on tau phosphorylation in a mammalian cell culture model by western blotting. We also investigate the expression levels of p53 and p73 in human post-mortem samples from AD and control cases. Results: Normally, p53 and p73 are maintained at low levels inside cells. However, we and others have reported an increase in p53 immunoreactivity, but not p73 immunoreactivity in AD. Furthermore, p53 -/mice display a reduction in tau phosphorylation. Consistent with this, we have demonstrated that p53 induces tau (human 2N4R) phosphorylation at the AT8/tau-1 epitope in HEK293a cells and that p73␣, a related p53 homologue, also induces tau (human 2N4R) phosphorylation at the AT-8/tau-1 epitope as well as the PHF-1 epitope in HEK293a cells. In contrast, we find that the N-terminally truncated transcriptionally inactive or ⌬N isoform of p73␣ fails to induce tau (human 2N4R) phosphorylation. Conclusions: These results suggest that p53 and indeed p73 induce tau phosphorylation in a cell culture model of neurodegeneration and that the effects of p73 and perhaps p53 on tau are dependent on the transcriptional activity of these proteins. Interestingly, p53, but not p73 was upregulated in AD. However, p73 has been reported to be aberrantly expressed in the nucleus of hippocampal neurons in AD -p73 expression co-localizing with NFTs....