Zobrazeno 1 - 10
of 14
pro vyhledávání: '"William H. Stoothoff"'
Autor:
William H Stoothoff, Bradley T Hyman
Publikováno v:
Amyotrophic Lateral Sclerosis ISBN: 9781003076445
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48205c9df52aa179731f438ded825d33
https://doi.org/10.1201/9781003076445-14
https://doi.org/10.1201/9781003076445-14
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1739(2-3):280-297
The microtubule-associated protein tau, abundant in neurons, has gained notoriety due to the fact that it is deposited in cells as fibrillar lesions in numerous neurodegenerative diseases, and most notably Alzheimer's disease. Regulation of microtubu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9119df44ec426957a5cfc379ba781e8f
Publikováno v:
Journal of Cell Science. 117:5721-5729
Tau is a group of neuronal microtubule-associated proteins that are formed by alternative mRNA splicing and accumulate in neurofibrillary tangles in Alzheimer's disease (AD) brain. Tau plays a key role in regulating microtubule dynamics, axonal trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2866edbb2988fdb57f94543338886d0b
https://doi.org/10.1242/jcs.01558
https://doi.org/10.1242/jcs.01558
Publikováno v:
Journal of Neurochemistry. 83:904-913
Glycogen synthase kinase 3β (GSK3β) is an essential protein kinase that regulates numerous functions within the cell. One critically important substrate of GSK3β is the microtubule-associated protein tau. Phosphorylation of tau by GSK3β decreases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4df4c86981615671c0fa224f2ee43922
https://doi.org/10.1046/j.1471-4159.2002.01197.x
https://doi.org/10.1046/j.1471-4159.2002.01197.x
Autor:
Alix de Calignon, Phillip B. Jones, William H. Stoothoff, Tara L. Spires-Jones, Bradley T. Hyman
Publikováno v:
Trends in neurosciences. 32(3)
Neurodegenerative tauopathies are marked by their common pathologic feature of aggregates formed of hyperphosphorylated tau protein, which are associated with synapse and neuronal loss. Changes in tau conformation result in both loss of normal functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cec14a86ee533f8971111f62c359e73
https://pubmed.ncbi.nlm.nih.gov/19162340
https://pubmed.ncbi.nlm.nih.gov/19162340
Autor:
Dudley K. Strickland, Mirjam Koker, William H. Stoothoff, Bradley T. Hyman, Kathryn K. Bercury, Daniel Joyner, Thomas E. Willnow, Kenneth W. Adams, Anne V. Thomas, Olav M. Andersen, Penelope J. Hallett, Meihua Deng, Robert Spoelgen
Publikováno v:
Neuroscience. 158(4)
In this study, we examined protein-protein interactions between two neuronal receptors, low density lipoprotein receptor-related protein (LRP) and sorLA/LR11, and found that these receptors interact, as indicated by three independent lines of evidenc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c72372b0138e115698d66b205cd6483
https://pubmed.ncbi.nlm.nih.gov/19047013
https://pubmed.ncbi.nlm.nih.gov/19047013
Publikováno v:
The Journal of biological chemistry. 280(1)
Tau is a microtubule-associated protein found primarily in neurons, and its function is regulated by site-specific phosphorylation. Although it is well established that tau is phosphorylated at both primed and unprimed epitopes by glycogen synthase k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::670c4cdd3debc4f63220dc8f93f03470
https://pubmed.ncbi.nlm.nih.gov/15522877
https://pubmed.ncbi.nlm.nih.gov/15522877
Publikováno v:
Journal of neurochemistry. 83(4)
Glycogen synthase kinase 3beta (GSK3beta) is an essential protein kinase that regulates numerous functions within the cell. One critically important substrate of GSK3beta is the microtubule-associated protein tau. Phosphorylation of tau by GSK3beta d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::952dcaabe232008319e24117870fd0ec
https://pubmed.ncbi.nlm.nih.gov/12421363
https://pubmed.ncbi.nlm.nih.gov/12421363
Publikováno v:
Journal of neuroscience research. 65(6)
A characteristic hallmark of Alzheimer's disease brain is the presence of hyperphosphorylated tau; however, the mechanisms responsible for the aberrant tau phosphorylation are unknown. Recently, it has been shown that apoptotic-like processes may be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbe2f56d3b46f52670d36002c781caff
https://pubmed.ncbi.nlm.nih.gov/11550225
https://pubmed.ncbi.nlm.nih.gov/11550225
Autor:
Huisheng Liu, Lisheng Peng, Hongyu Ruan, William H. Stoothoff, William H. Tepp, Wei-Dong Yao, Robert H. Brown, Su-Chun Zhang, Min Dong, Eric A. Johnson
Publikováno v:
Nature communications
Botulinum neurotoxins (BoNT/A-G) act by blocking synaptic vesicle exocytosis. Whether BoNTs disrupt additional neuronal functions has not been addressed. Here we report that cleavage of syntaxin 1 by BoNT/C, and cleavage of SNAP-25 by BoNT/E both ind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f02b7112feb2c3326a5c2098f103bd60
http://europepmc.org/articles/PMC4052923
http://europepmc.org/articles/PMC4052923