Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Tyler L, Perfitt"'
Autor:
Claudia Huichalaf, Tyler L. Perfitt, Anna Kuperman, Renea Gooch, Ramesh C. Kovi, Karrie A. Brenneman, Xian Chen, Dinesh Hirenallur-Shanthappa, Tiffany Ma, Basel T. Assaf, Ingrid Pardo, Tania Franks, Laura Monarski, Ting-Wen Cheng, Kevin Le, Chunyan Su, Suryanarayan Somanathan, Laurence O. Whiteley, Christine Bulawa, Marko J. Pregel, Alain Martelli
Publikováno v:
Molecular Therapy: Methods & Clinical Development, Vol 24, Iss , Pp 367-378 (2022)
Friedreich's ataxia is a rare disorder resulting from deficiency of frataxin, a mitochondrial protein implicated in the synthesis of iron-sulfur clusters. Preclinical studies in mice have shown that gene therapy is a promising approach to treat indiv
Externí odkaz:
https://doaj.org/article/46b5bb7ac72846398fc35f753653a2fa
Autor:
Tyler L. Perfitt, Alain Martelli
Publikováno v:
Inorganics, Vol 10, Iss 3, p 31 (2022)
Iron–sulfur clusters (Fe–S or ISC) are essential cofactors that function in a wide range of biological pathways. In mammalian cells, Fe–S biosynthesis primarily relies on mitochondria and involves a concerted group of evolutionary-conserved pro
Externí odkaz:
https://doaj.org/article/3605f0fae5334e229cba5e4f935d4359
Clustering of neuronal L-type voltage-gated Ca2+channels (LTCC) in the plasma membrane is increasingly implicated in creating highly localized Ca2+signaling nanodomains. For example, LTCC activation can increase phosphorylation of the nuclear CREB tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0d3ae785061ba8dd0faeb84779405a1
https://doi.org/10.1101/2022.10.21.513252
https://doi.org/10.1101/2022.10.21.513252
Publikováno v:
Biochem Biophys Res Commun
Protein-protein interactions can be modulated by phosphorylation of either binding partner, thereby altering subcellular localization and/or physiological function. Shank3, a master postsynaptic scaffolding protein that controls the developmental mat
Neuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction
Autor:
Terunaga Nakagawa, Tyler L. Perfitt, Jason R. Stephenson, Xiaohan Wang, David A. Jacobson, Matthew T. Dickerson, Roger J. Colbran
Publikováno v:
J Neurosci
The activation of neuronal plasma membrane Ca2+channels stimulates many intracellular responses. Scaffolding proteins can preferentially couple specific Ca2+channels to distinct downstream outputs, such as increased gene expression, but the molecular
Autor:
James S. Sutcliffe, Tyler L. Perfitt, Roger J. Colbran, Xiaohan Wang, Walker P. Parrish, Brian C. Shonesy, Douglas P. Mortlock, Christian R. Marks, Jason R. Stephenson, Terunaga Nakagawa
Publikováno v:
The Journal of Neuroscience. 37:2216-2233
Characterizing the functional impact of novel mutations linked to autism spectrum disorder (ASD) provides a deeper mechanistic understanding of the underlying pathophysiological mechanisms. Here we show that ade novoGlu183 to Val (E183V) mutation in
Neuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction
The molecular mechanisms that couple plasma membrane receptors/channels to specific intracellular responses, such as increased gene expression, are incompletely understood. The postsynaptic scaffolding protein Shank3 associates with Ca2+ permeable re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::baafdc20311ef8f156c8220a817d7d43
Autor:
Christian R. Marks, Roger J. Colbran, Amy S. Lee, David A. Jacobson, Xiaohan Wang, Tyler L. Perfitt, Terunaga Nakagawa
Neuronal excitation can induce new mRNA transcription, a phenomenon called excitation-transcription (E-T) coupling. Among several pathways implicated in E-T coupling, activation of voltage-gated L-type Ca2+ channels (LTCCs) in the plasma membrane can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11ee25424b1207728a2727b2de092521
https://europepmc.org/articles/PMC5655510/
https://europepmc.org/articles/PMC5655510/
Autor:
Jason R, Stephenson, Xiaohan, Wang, Tyler L, Perfitt, Walker P, Parrish, Brian C, Shonesy, Christian R, Marks, Douglas P, Mortlock, Terunaga, Nakagawa, James S, Sutcliffe, Roger J, Colbran
Publikováno v:
The Journal of neuroscience : the official journal of the Society for Neuroscience. 37(8)
Characterizing the functional impact of novel mutations linked to autism spectrum disorder (ASD) provides a deeper mechanistic understanding of the underlying pathophysiological mechanisms. Here we show that a de novo Glu183 to Val (E183V) mutation i