Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Michael Weisenhaus"'
Autor:
Brian W Jones, Jennifer Deem, Thomas J Younts, Michael Weisenhaus, Christina A Sanford, Margaret C Slack, Jenesa Chin, Daniela Nachmanson, Alex McKennon, Pablo E Castillo, G Stanley McKnight
Publikováno v:
eLife, Vol 5 (2016)
Protein Kinase A (PKA) mediates synaptic plasticity and is widely implicated in learning and memory. The hippocampal dentate gyrus (DG) is thought to be responsible for processing and encoding distinct contextual associations in response to highly si
Externí odkaz:
https://doaj.org/article/ccb6d67e37424b3596d95ff7b4e0d75b
Autor:
Michael Weisenhaus, Margaret L Allen, Linghai Yang, Yuan Lu, C Blake Nichols, Thomas Su, Johannes W Hell, G Stanley McKnight
Publikováno v:
PLoS ONE, Vol 5, Iss 4, p e10325 (2010)
AKAP5 (also referred to as AKAP150 in rodents and AKAP79 in humans) is a scaffolding protein that is highly expressed in neurons and targets a variety of signaling molecules to dendritic membranes. AKAP5 interacts with PKA holoenzymes containing RIIa
Externí odkaz:
https://doaj.org/article/f5f83e536db14ac4a3ae330247768049
Autor:
Brian W. Jones, Jenesa Chin, Christina A Sanford, Thomas J. Younts, Pablo E. Castillo, Margaret C Slack, Alex McKennon, Daniela Nachmanson, G. Stanley McKnight, Michael Weisenhaus, Jennifer D. Deem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ccd0d8168121101884fe6b87caa6daf
https://doi.org/10.7554/elife.20695.015
https://doi.org/10.7554/elife.20695.015
Autor:
Sara Shum, Michael Weisenhaus, G. Stanley McKnight, Chao Zhang, Bertil Hille, Daniel J. Morgan, Kevan M. Shokat, Ruimao Zheng, Donner F. Babcock, Thomas Su
Publikováno v:
Proceedings of the National Academy of Sciences. 105:20740-20745
Studies on cAMP signaling and protein kinase A (PKA) function in vivo are limited by the lack of highly specific inhibitors that can be used in primary cell culture and whole animals. Previously we reported that a mutation in the ATP binding pocket o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29cc0c969838c9a440afc9dac24d41b7
https://doi.org/10.1073/pnas.0810971105
https://doi.org/10.1073/pnas.0810971105
Autor:
Robert F. Dallapiazza, Amy R Halt, Yuriy M. Usachev, Michael Weisenhaus, Yuan Lu, G. Stanley McKnight, Johannes W. Hell, Duane D. Hall, Margaret D. Allen
Publikováno v:
The EMBO Journal. 26:4879-4890
Association of PKA with the AMPA receptor GluR1 subunit via the A kinase anchor protein AKAP150 is crucial for GluR1 phosphorylation. Mutating the AKAP150 gene to specifically prevent PKA binding reduced PKA within postsynaptic densities (>70%). It a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09702709a956326a4fd85d1486916003
https://doi.org/10.1038/sj.emboj.7601884
https://doi.org/10.1038/sj.emboj.7601884
Autor:
Linghai Yang, Michael Weisenhaus, Margaret L. Allen, Thomas Su, Yuan Lu, G. Stanley McKnight, Johannes W. Hell, C. Blake Nichols
Publikováno v:
PLoS ONE
PLoS ONE, Vol 5, Iss 4, p e10325 (2010)
PLoS ONE, Vol 5, Iss 4, p e10325 (2010)
AKAP5 (also referred to as AKAP150 in rodents and AKAP79 in humans) is a scaffolding protein that is highly expressed in neurons and targets a variety of signaling molecules to dendritic membranes. AKAP5 interacts with PKA holoenzymes containing RIIa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::533211b860654383af815ecb42472838
http://europepmc.org/articles/PMC2859064
http://europepmc.org/articles/PMC2859064
Autor:
G. Stanley McKnight, Johannes W. Hell, Duane D. Hall, Mei Shi, Monika A. Davare, Michael Weisenhaus, Margaret L. Allen
Publikováno v:
Biochemistry. 46(6)
The cAMP-dependent protein kinase (PKA) regulates a wide array of cellular functions. In brain and heart PKA increases the activity of the L-type Ca2+ channel Cav1.2 in response to beta-adrenergic stimulation. Cav1.2 forms a complex with the beta2-ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76362ca0b7613cb1ede6ce78e8cd0f75
https://pubmed.ncbi.nlm.nih.gov/17279627
https://pubmed.ncbi.nlm.nih.gov/17279627