Výsledky vyhledávání - "Timothy D. Garver"

The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation

Autor: Timothy D. Garver, Vann Bennett, Shmuel Tuvia

Publikováno v: Proceedings of the National Academy of Sciences. 94:12957-12962

Cell–cell recognition and patterning of cell contacts have a critical role in mediating reversible assembly of a variety of transcellular complexes in the nervous system. This study provides evidence for regulation of cell interactions through modu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b70c3b08df4fdccaf95342a53b08bb11
https://doi.org/10.1073/pnas.94.24.12957

Zobrazit plný text záznamu

Tyrosine Phosphorylation at a Site Highly Conserved in the L1 Family of Cell Adhesion Molecules Abolishes Ankyrin Binding and Increases Lateral Mobility of Neurofascin

Autor: Qun Ren, Timothy D. Garver, Vann Bennett, Shmuel Tuvia

Publikováno v: The Journal of Cell Biology

This paper presents evidence that a member of the L1 family of ankyrin-binding cell adhesion molecules is a substrate for protein tyrosine kinase(s) and phosphatase(s), identifies the highly conserved FIGQY tyrosine in the cytoplasmic domain as the p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff8f6bcc724738eed3e5a4f5139f960
https://doi.org/10.1083/jcb.137.3.703

Zobrazit plný text záznamu

Microtubule assembly competence analysis of freshly-biopsied human tau, dephosphorylated tau, and Alzheimer tau

Autor: Ralph A. W. Lehman, Melvin L. Billingsley, Timothy D. Garver

Publikováno v: Journal of Neuroscience Research. 44:12-20

Phosphorylation of the microtubule-associated protein tau regulates its binding to microtubules; highly phosphorylated tau is also a prime component of paired helical filaments (PHFs) of Alzheimer's disease (AD). Tau from freshly biopsied human, monk

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7af9712d1498798985776fa4f1fc2d2d
https://doi.org/10.1002/(sici)1097-4547(19960401)44:1<12::aid-jnr2>3.0.co

Zobrazit plný text záznamu

Tau phosphorylation in human, primate, and rat brain: evidence that a pool of tau is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro

Autor: John Q. Trojanowski, Virginia M.-Y. Lee, Katherine A. Harris, Timothy D. Garver, Ralph A. W. Lehman, Melvin L. Billingsley

Publikováno v: Journal of neurochemistry. 63(6)

The extent of tau phosphorylation is thought to regulate the binding of tau to microtubules: Highly phosphorylated tau does not bind to tubules, whereas dephosphorylated tau can bind to microtubules. It is interesting that the extent of tau phosphory

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8defc19b7a061bb447ffa7a8a0c1ffc
https://pubmed.ncbi.nlm.nih.gov/7964748

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání