User profiles for Gail V.W. Johnson
Gail Johnsonprofessor, department of anesthesiology and perioperative medicine,university of Rochester Verified email at urmc.rochester.edu Cited by 38130 |
The glamour and gloom of glycogen synthase kinase-3
RS Jope, GVW Johnson - Trends in biochemical sciences, 2004 - cell.com
Glycogen synthase kinase-3 (GSK3) is now recognized as a key component of a surprisingly
large number of cellular processes and diseases. Several mechanisms play a part in …
large number of cellular processes and diseases. Several mechanisms play a part in …
Tau phosphorylation in neuronal cell function and dysfunction
GVW Johnson, WH Stoothoff - Journal of cell science, 2004 - journals.biologists.com
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. …
mRNA splicing and accumulate in neurofibrillary tangles in Alzheimer's disease (AD) brain. …
[HTML][HTML] Tau phosphorylation: physiological and pathological consequences
WH Stoothoff, GVW Johnson - … et Biophysica Acta (BBA)-Molecular Basis of …, 2005 - Elsevier
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…
fact that it is deposited in cells as fibrillar lesions in numerous neurodegenerative diseases…
Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
YS Choo, GVW Johnson, M MacDonald… - Human molecular …, 2004 - academic.oup.com
Huntington's disease (HD) is initiated by an abnormally expanded polyglutamine stretch in
the huntingtin protein, conferring a novel property on the protein that leads to the loss of …
the huntingtin protein, conferring a novel property on the protein that leads to the loss of …
p38 kinase is activated in the Alzheimer's disease brain
…, WR Markesbery, E Patel, GVW Johnson… - Journal of …, 1999 - Wiley Online Library
The p38 mitogen‐activated protein kinase is a stress‐activated enzyme responsible for
transducing inflammatory signals and initiating apoptosis. In the Alzheimer's disease (AD) brain, …
transducing inflammatory signals and initiating apoptosis. In the Alzheimer's disease (AD) brain, …
Transglutaminase regulation of cell function
…, AM Belkin, G Colak, GVW Johnson… - Physiological …, 2014 - journals.physiology.org
Transglutaminases (TGs) are multifunctional proteins having enzymatic and scaffolding
functions that participate in regulation of cell fate in a wide range of cellular systems and are …
functions that participate in regulation of cell fate in a wide range of cellular systems and are …
Histone deacetylase 6 interacts with the microtubule‐associated protein tau
H Ding, PJ Dolan, GVW Johnson - Journal of neurochemistry, 2008 - Wiley Online Library
Histone deacetylase 6 (HDAC6), a unique cytoplasmic deacetylase, likely plays a role in
neurodegeneration by coordinating cell responses to abnormal protein aggregation. Here, we …
neurodegeneration by coordinating cell responses to abnormal protein aggregation. Here, we …
[HTML][HTML] Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau (∗)
…, R Barbour, R Jakes, M Goedert, GVW Johnson… - Journal of Biological …, 1995 - ASBMB
Paired helical filaments (PHFs) are the major structural elements of Alzheimer's disease
neurofibrillary lesions, and these filaments are formed from hyperphosphorylated brain tau …
neurofibrillary lesions, and these filaments are formed from hyperphosphorylated brain tau …
[HTML][HTML] Glycogen synthase kinase 3β phosphorylates tau at both primed and unprimed sites: differential impact on microtubule binding
JH Cho, GVW Johnson - Journal of Biological Chemistry, 2003 - ASBMB
Glycogen synthase kinase 3β (GSK3β) phosphorylates substrates, including the microtubule-associated
protein tau, at both primed and unprimed epitopes. GSK3β phosphorylation of …
protein tau, at both primed and unprimed epitopes. GSK3β phosphorylation of …
Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules
JH Cho, GVW Johnson - Journal of neurochemistry, 2004 - Wiley Online Library
Site‐specific phosphorylation of tau negatively regulates its ability to bind and stabilize
microtubule structure. Although tau is a substrate of glycogen synthase kinase 3β (GSK3β), the …
microtubule structure. Although tau is a substrate of glycogen synthase kinase 3β (GSK3β), the …