Zobrazeno 1 - 10
of 11
pro vyhledávání: '"James R. Gaut"'
Publikováno v:
Journal of Neurochemistry. 80:1019-1028
Limiting beta amyloid (Abeta) production could become an important therapeutic target in Alzheimer's disease (AD). Abeta is derived by the sequential cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases. A double missense mutatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5359ef6eeb1d02cfebd0a45720aebf8
https://doi.org/10.1046/j.0022-3042.2002.00764.x
https://doi.org/10.1046/j.0022-3042.2002.00764.x
Publikováno v:
Journal of Biological Chemistry. 273:25552-25555
Recent studies of cellular amyloid precursor protein (APP) metabolism demonstrate a beta-/gamma-secretase pathway resident to the endoplasmic reticulum (ER)/Golgi resulting in intracellular generation of soluble APP (APPsbeta) and Abeta42 peptide. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3b87912cf2d8b718c06e251a5c87994
https://doi.org/10.1074/jbc.273.40.25552
https://doi.org/10.1074/jbc.273.40.25552
Publikováno v:
Proceedings of the National Academy of Sciences. 93:5269-5274
A group of resident ER proteins have been identified that are proposed to function as molecular chaperones. The best characterized of these is BiP/GRP78, an hsp70 homologue that binds peptides containing hydrophobic residues in vitro and unfolded or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d2c3c565666eb120a5489816777db2a
https://doi.org/10.1073/pnas.93.11.5269
https://doi.org/10.1073/pnas.93.11.5269
Publikováno v:
Journal of Biological Chemistry. 270:26677-26682
In the present study, we produced single point mutations in the ATP binding site of hamster BiP, isolated recombinant proteins, and characterized them in terms of their affinity for ATP and ADP, their ability to undergo a conformational change upon n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2d0745eb69004bdf94abd857246cb5c
https://doi.org/10.1074/jbc.270.44.26677
https://doi.org/10.1074/jbc.270.44.26677
Autor:
Linda M. Hendershot, James R. Gaut
Publikováno v:
Current Opinion in Cell Biology. 5:589-595
Proteins fold and assemble in the endoplasmic reticulum in an environment that is very different from the cytosol. The presence of relatively high concentrations of calcium, an oxidizing state, ATP and lumenal proteins are all important in mediating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb498e376931ba5e930d6eebdb337e9b
https://doi.org/10.1016/0955-0674(93)90127-c
https://doi.org/10.1016/0955-0674(93)90127-c
Autor:
James R. Gaut, Edward L. Stuenkel, Chi S. Ho, R. Scott Turner, Michelle L. Steinhilb, Vlad Marinescu
Publikováno v:
The Journal of biological chemistry. 277(30)
X11 proteins have been shown to modulate metabolism of the amyloid precursor protein (APP) and to reduce the secretion of beta-amyloid peptides (Abeta) that are associated with Alzheimer's disease. Whereas X11alpha interacts with APP via its phosphot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e289ea06cfadca9e1c6560a3ba9ce488
https://pubmed.ncbi.nlm.nih.gov/12016213
https://pubmed.ncbi.nlm.nih.gov/12016213
Autor:
R. Scott Turner, Jen Tzer Gau, Kirk A. Frey, Constance J. D'Amato, Tzu Cheg Kao, James R. Gaut, Michelle L. Steinhilb
We examined presynaptic cholinergic markers and β-secretase activity during progressive central nervous system amyloidogenesis in Tg2576 Alzheimer mice (transgenic for human amyloid precursor protein Swedish mutation; hAPPswe). At 14, 18, and 23 mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1fd2f496cd17e1bf2143ff49ddd3500
https://europepmc.org/articles/PMC1850661/
https://europepmc.org/articles/PMC1850661/
Publikováno v:
The Journal of biological chemistry. 276(6)
Amyloid (Abeta) peptides found aggregated into plaques in Alzheimer's disease are derived from the sequential cleavage of the amyloid precursor protein (APP) first by beta- and then by gamma-secretases. Peptide aldehydes, which inhibit cysteine prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1605ff30b0663f1062c0ce63b32aa67
https://pubmed.ncbi.nlm.nih.gov/11084038
https://pubmed.ncbi.nlm.nih.gov/11084038
Publikováno v:
Neurobiology of Aging. 21:115
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22db8bd989765745352d31c192243547
https://doi.org/10.1016/s0197-4580(00)82317-9
https://doi.org/10.1016/s0197-4580(00)82317-9
Autor:
James R. Gaut
Publikováno v:
Cell Stress & Chaperones. 2:252
Immunoglobin binding protein (BiP) molecules exist as both monomers and oligomers and phosphorylated BiP is restricted to the oligomeric pool. Modified BiP is not bound to proteins such as immunoglobulin heavy chain and consequently, may constitute a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::443f900a767313c29095209ea370aeb2
https://doi.org/10.1379/1466-1268(1997)002<0252:ivtpoi>2.3.co
https://doi.org/10.1379/1466-1268(1997)002<0252:ivtpoi>2.3.co