Stuart C. Feinstein

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The method of microtubule tracking and dynamics analysis, presented here, improves upon the current means of manual and automated quantification of microtubule behavior. Key contributions are increasing accuracy and data volume, eliminating user bias and providing advanced analysis tools for the discovery of temporal patterns in cellular processes. By(More)
Interest in the microtubule-associated protein tau stems from its critical roles in neural development and maintenance, as well as its role in Alzheimer's, FTDP-17 and related neurodegenerative diseases. Under normal circumstances, tau performs its functions by binding to microtubules and powerfully regulating their stability and growing and shortening(More)
We present an automated method for the tracking and dynamics modeling of microtubules-a major component of the cytoskeleton-which provides researchers with a previously unattainable level of data analysis and quantification capabilities. The proposed method improves upon the manual tracking and analysis techniques by i) increasing accuracy and quantified(More)
Tau is an intrinsically unstructured microtubule (MT)-associated protein capable of binding to and organizing MTs into evenly spaced parallel assemblies known as "MT bundles." How tau achieves MT bundling is enigmatic because each tau molecule possesses only one MT-binding region. To dissect this complex behavior, we have used a surface forces apparatus to(More)
Microtubule (MT) dynamics are traditionally analyzed from time lapse images by manual techniques that are laborious, approximate and often limited. Recently, computer vision techniques have been applied to the problem of automated tracking of MTs in live cell images. Aside of very low signal to noise ratios, live cell images of MTs exhibit severe clutter(More)
The microtubule (MT)-associated protein tau is important in neuronal development and in Alzheimer's and other neurodegenerative diseases. Genetic analyses have established a cause-and-effect relationship between tau dysfunction/misregulation and neuronal cell death and dementia in frontotemporal dementia and parkinsonism associated with chromosome 17;(More)
The microtubule-associated protein tau is implicated in the pathogenesis of many neurodegenerative diseases, including fronto-temporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), in which both RNA splicing and amino acid substitution mutations in tau cause dominantly inherited early onset dementia. RNA-splicing FTDP-17 mutations alter the(More)
A variety of genetic and biochemical evidence suggests that amyloid β (Aβ) oligomers promote downstream errors in Tau action, in turn inducing neuronal dysfunction and cell death in Alzheimer and related dementias. To better understand molecular mechanisms involved in Aβ-mediated neuronal cell death, we have treated primary rat hippocampal cultures with Aβ(More)
The neural microtubule-associated protein tau binds to and stabilizes microtubules. Because of alternative mRNA splicing, tau is expressed with either 3 or 4 C-terminal repeats. Two observations indicate that differences between these tau isoforms are functionally important. First, the pattern of tau isoform expression is tightly regulated during(More)
The neural microtubule-associated protein Tau binds directly to microtubules and regulates their dynamic behavior. In addition to being required for normal development, maintenance, and function of the nervous system, Tau is associated with several neurodegenerative diseases, including Alzheimer disease. One group of neurodegenerative dementias known as(More)