Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Salomé Calado Botelho"'
Autor:
Thomas C. Südhof, Chen Zhang, Fredrik H. Sterky, ChangHui Pak, Salomé Calado Botelho, Sung-Jin Lee, Mengping Wei, Justin H. Trotter, Stephan Maxeiner
Publikováno v:
The Journal of Neuroscience. 37:1062-1080
Three neuronal pentraxins are expressed in brain, the membrane-bound “neuronal pentraxin receptor” (NPR) and the secreted proteins NP1 and NARP (i.e., NP2). Neuronal pentraxins bind to AMPARs at excitatory synapses and play important, well-docume
Publikováno v:
Protein Science. 24:2063-2069
Resistance to sodium carbonate extraction is regarded as a canonical way to distinguish integral membrane proteins (MPs) from other membrane‐associated proteins. However, it has been observed that carbonate extraction releases some mitochondrial in
Autor:
Manuchehr Abedi-Valugerdi, Svetlana Pavlova, Joseph W. DePierre, Moustapha Hassan, Maryam Saghafian, Salomé Calado Botelho
Publikováno v:
Chemosphere. 129:225-231
High-dose exposure of mice to perfluorooctanoate (PFOA) induces both hepatotoxicity and immunotoxicity. Here, we characterized the effects of 10-day dietary treatment with PFOA (0.002-0.02%, w/w) on the liver and complement system of male C57BL/6 mic
Publikováno v:
Journal of Molecular Biology. 425(15):2813-2822
Most integral membrane proteins, both in prokaryotic and eukaryotic cells, are co-translationally inserted into the membrane via Sec-type translocons: the SecYEG complex in prokaryotes and the Sec61 complex in eukaryotes. The contributions of individ
Publikováno v:
Journal of Biological Chemistry. 288:1521-1532
Mitochondrial inner membrane proteins that carry an N-terminal presequence are sorted by one of two pathways: stop transfer or conservative sorting. However, the sorting pathway is known for only a small number of proteins, in part due to the lack of
Autor:
Fei Yi, Tamas Danko, Marius Wernig, Christopher Patzke, ChangHui Pak, Thomas C. Südhof, Salomé Calado Botelho
Publikováno v:
Science. 352
Faulty channels, not faulty synapses SHANK3 is a widely expressed scaffolding protein that is enriched in postsynaptic specializations. In mutant mice, SHANK3 mutations cause autism-like behavioral changes and exhibit alterations in synaptic transmis
Publikováno v:
FEBS Letters. 585:1238-1242
Mgm1p is a nuclearly encoded GTPase important for mitochondrial fusion. Long and short isoforms of the protein are generated in a unique “alternative topogenesis” process in which the most N-terminal of two hydrophobic segments in the protein is
Autor:
Salomé Calado Botelho, Patrik Björkholm, Andreas S. Reichert, Koji Yamano, Hyuntae Kim, Toshiya Endo, Marie Österberg, Gunnar von Heijne
Publikováno v:
The EMBO Journal. 30:1003-1011
While overall hydrophobicity is generally recognized as the main characteristic of transmembrane (TM) α-helices, the only membrane system for which there are detailed quantitative data on how different amino acids contribute to the overall efficienc
Sorting of mitochondrial inner membrane proteins is a complex process in which translocons and proteases function in a concerted way. Many inner membrane proteins insert into the membrane via the TIM23 translocon, and some are then further acted upon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fedd9145cb312baab6363e213a9b4a2
https://europepmc.org/articles/PMC3576084/
https://europepmc.org/articles/PMC3576084/
Publikováno v:
Biochimica et biophysica acta. Bioenergetics, 2015, Vol.1848(2), pp.615-621 [Peer Reviewed Journal]
Botelho, S C, Enquist, K, Von Heijne, G & Draheim, R R 2015, ' Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues ', Biochimica et Biophysica Acta (BBA)-Biomembranes, vol. 1848, no. 2, pp. 615-621 . https://doi.org/10.1016/j.bbamem.2014.11.017
Botelho, S C, Enquist, K, Von Heijne, G & Draheim, R R 2015, ' Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues ', Biochimica et Biophysica Acta (BBA)-Biomembranes, vol. 1848, no. 2, pp. 615-621 . https://doi.org/10.1016/j.bbamem.2014.11.017
Aromatic tuning, i.e. repositioning aromatic residues found at the cytoplasmic end of transmembrane (TM) domains within bacterial receptors, has been previously shown to be an efficient way to modulate signal output from the aspartate chemoreceptor (