Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Sarah A. Shoichet"'
Publikováno v:
FEBS Open Bio, Vol 7, Iss 9, Pp 1234-1245 (2017)
Synaptic α‐amino‐3‐hydroxyl‐5‐methyl‐4‐isoxazole‐propionate (AMPA) receptors are essential mediators of neurotransmission in the central nervous system. Shisa9/cysteine‐knot AMPAR modulating protein 44 (CKAMP44) is a transmembrane
Externí odkaz:
https://doaj.org/article/229fbf70d9be4ae89a3629d250eb6e70
Autor:
Bettina Schmerl, Niclas Gimber, Benno Kuropka, Alexander Stumpf, Jakob Rentsch, Stella-Amrei Kunde, Judith von Sivers, Helge Ewers, Dietmar Schmitz, Christian Freund, Jan Schmoranzer, Nils Rademacher, Sarah A Shoichet
Publikováno v:
PLoS Biology, Vol 20, Iss 3, p e3001503 (2022)
Recent advances in imaging technology have highlighted that scaffold proteins and receptors are arranged in subsynaptic nanodomains. The synaptic membrane-associated guanylate kinase (MAGUK) scaffold protein membrane protein palmitoylated 2 (MPP2) is
Externí odkaz:
https://doaj.org/article/1fdddd98c68b4e5c87d67fe3221885b3
Autor:
Nils Rademacher, Benno Kuropka, Stella-Amrei Kunde, Markus C Wahl, Christian Freund, Sarah A Shoichet
Publikováno v:
eLife, Vol 8 (2019)
PSD-95 MAGUK family scaffold proteins are multi-domain organisers of synaptic transmission that contain three PDZ domains followed by an SH3-GK domain tandem. This domain architecture allows coordinated assembly of protein complexes composed of neuro
Externí odkaz:
https://doaj.org/article/657b32974df34aa090966829cedbd2aa
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
Scientific reports 10(1), 5709 (2020). doi:10.1038/s41598-020-62207-4
Scientific Reports
Scientific reports 10(1), 5709 (2020). doi:10.1038/s41598-020-62207-4
Scientific Reports
Scaffold proteins are responsible for structural organisation within cells; they form complexes with other proteins to facilitate signalling pathways and catalytic reactions. The scaffold protein connector enhancer of kinase suppressor of Ras 2 (CNK2
Autor:
Bettina Schmerl, Niclas Gimber, Benno Kuropka, Alexander Stumpf, Jakob Rentsch, Stella-Amrei Kunde, Judith von Sivers, Helge Ewers, Dietmar Schmitz, Christian Freund, Jan Schmoranzer, Nils Rademacher, Sarah A. Shoichet
Publikováno v:
PLoS biology 20(3), e3001503 (2022). doi:10.1371/journal.pbio.3001503
Recent advances in imaging technology have highlighted that scaffold proteins and receptors are arranged in subsynaptic nanodomains. The synaptic membrane-associated guanylate kinase (MAGUK) scaffold protein membrane protein palmitoylated 2 (MPP2) is
Autor:
Ahmadyar E, Bettina Schmerl, Nils Rademacher, Hanna L. Zieger, Stella-Amrei Kunde, Sarah A. Shoichet
We show here that the dynamics of the synaptic scaffold molecule SAP102 are negatively regulated by JNK inhibition, that SAP102 is a direct phosphorylation target of JNK3, and that SAP102 regulation by JNK is restricted to neurons that harbour mature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec93967343662e180f5223ad6cf3cff9
https://doi.org/10.1101/2021.04.30.442109
https://doi.org/10.1101/2021.04.30.442109
Publikováno v:
FEBS Open Bio
Synaptic α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate (AMPA) receptors are essential mediators of neurotransmission in the central nervous system. Shisa9/cysteine-knot AMPAR modulating protein 44 (CKAMP44) is a transmembrane protein recently f
Scaffold proteins are responsible for structural organisation within cells; they form complexes with other proteins to facilitate signalling pathways and catalytic reactions. The scaffold protein connector enhancer of kinase suppressor of Ras 2 (CNK2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f023db65e0816e62924669d787b0aa4b
https://doi.org/10.1101/532374
https://doi.org/10.1101/532374
Autor:
Sarah A. Shoichet, Christian Freund, Markus C. Wahl, Benno Kuropka, Nils Rademacher, Stella-Amrei Kunde
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
PSD-95 MAGUK family scaffold proteins are multi-domain organisers of synaptic transmission that contain three PDZ domains followed by an SH3-GK domain tandem. This domain architecture allows coordinated assembly of protein complexes composed of neuro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed47dc7910b9ee0632acd1a2d3d2087a
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=101018
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=101018