Výsledky vyhledávání - "H. Eric Feinstein"

Long-Term Stability of a Vaccine Formulated with the Amphipol-Trapped Major Outer Membrane Protein from Chlamydia trachomatis

Autor: Delia F. Tifrea, Melanie J. Cocco, Guifeng Sun, Luis M. de la Maza, H. Eric Feinstein, Jean-Luc Popot

Publikováno v: The Journal of membrane biology, vol 247, iss 9-10

Chlamydia trachomatis is a major bacterial pathogen throughout the world. Although antibiotic therapy can be implemented in the case of early detection, a majority of the infections are asymptomatic, requiring the development of preventive measures.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7891efd403f1f6423fd0bc168706a61d
https://doi.org/10.1007/s00232-014-9693-5

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Direct force measurements reveal that protein Tau confers short-range attractions and isoform-dependent steric stabilization to microtubules

Autor: Cyrus R. Safinya, Youli Li, Herbert P. Miller, Uri Raviv, H. Eric Feinstein, Stuart C. Feinstein, Peter J. Chung, Leslie Wilson, Myung Chul Choi

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 112, iss 47

Microtubules (MTs) are hollow cytoskeletal filaments assembled from αβ-tubulin heterodimers. Tau, an unstructured protein found in neuronal axons, binds to MTs and regulates their dynamics. Aberrant Tau behavior is associated with neurodegenerative

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5619396561917dd059dadeb030f6b0c6
https://europepmc.org/articles/PMC4664379/

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Oligomerization of the microtubule-associated protein tau is mediated by its N-terminal sequences: implications for normal and pathological tau action

Autor: Stuart C. Feinstein, Sarah J. Benbow, Nichole E. LaPointe, Nicolette Dressler, Srinivasan Ramachandran, Thanh D. Do, Noelle E. Huskey, Megan Korff, Ratnesh Lal, Michelle R. Gaylord, H. Eric Feinstein, Michael T. Bowers, Kristi Lazar Cantrell, Nirav Patel, Brady Quon

Publikováno v: Journal of neurochemistry. 137(6)

Despite extensive structure-function analyses, the molecular mechanisms of normal and pathological tau action remain poorly understood. How does the C-terminal microtubule-binding region regulate microtubule dynamics and bundling? In what biophysical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a7a87a2dea0d271ee2d90abfd0a6ad4
https://pubmed.ncbi.nlm.nih.gov/26953146

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Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis

Autor: Jennifer L. Ross, Stuart C. Feinstein, H. Eric Feinstein, Kenneth J. Rosenberg, Jacob N. Israelachvili

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 po

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1acd6036d8281ea4813cb245cdc07e
https://europepmc.org/articles/PMC2396711/

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The Functional Dependence of the Intrinsically Disordered Domains of Tau

Autor: Joanna Deek, Myung Chul Choi, H. Eric Feinstein, Cyrus R. Safinya, Stuart C. Feinstein, Peter J. Chung, Leslie Wilson

Publikováno v: Biophysical Journal. (2):56a

Hyperphosphorylated tau is the precursor to neurofibrillary tangles, one of the hallmark symptoms of Alzheimer's disease [1]. In its non-diseased state, the microtubule-associated protein tau promotes the assembly of tubulin into microtubules and reg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c29ad3a939503097f8e25374f0acfe1

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