Zobrazeno 1 - 10
of 101
pro vyhledávání: '"metabolism [Membrane Proteins]"'
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 2; Pages: 912
International journal of molecular sciences 24(2), 912 (2023). doi:10.3390/ijms24020912
International journal of molecular sciences 24(2), 912 (2023). doi:10.3390/ijms24020912
It has been hypothesised that inhalational anaesthetics such as isoflurane (Iso) may trigger the pathogenesis of Alzheimer’s disease (AD), while the gaseous anaesthetic xenon (Xe) exhibits many features of a putative neuroprotective agent. Loss of
Autor:
Alkmini A, Papadopoulou, Walter, Stelzer, Mara, Silber, Christine, Schlosser, Charlotte, Spitz, Martina, Haug-Kröper, Tobias, Straub, Stephan A, Müller, Stefan F, Lichtenthaler, Claudia, Muhle-Goll, Dieter, Langosch, Regina, Fluhrer
Publikováno v:
Scientific Reports, 12 (1), Art.-Nr.: 20987
Scientific reports 12(1), 20987 (2022). doi:10.1038/s41598-022-24772-8
Scientific reports 12(1), 20987 (2022). doi:10.1038/s41598-022-24772-8
Signal-Peptide Peptidase Like-3 (SPPL3) is an intramembrane cleaving aspartyl protease that causes secretion of extracellular domains from type-II transmembrane proteins. Numerous Golgi-localized glycosidases and glucosyltransferases have been identi
Autor:
Jolien Perneel, Manuela Neumann, Bavo Heeman, Simon Cheung, Marleen Van den Broeck, Sarah Wynants, Matt Baker, Cristina T. Vicente, Júlia Faura, Rosa Rademakers, Ian R. A. Mackenzie
Publikováno v:
Acta neuropathologica
Acta neuropathologica 145, 285–302 (2023). doi:10.1007/s00401-022-02531-3
Acta neuropathologica 145, 285–302 (2023). doi:10.1007/s00401-022-02531-3
Several studies using cryogenic electron microscopy (cryo-EM) techniques recently reported the isolation and characterization of novel protein filaments, composed of a C-terminal fragment (CTF) of the endolysosomal transmembrane protein 106B (TMEM106
Autor:
Georg Jocher, Vincent Grass, Sarah K Tschirner, Lydia Riepler, Stephan Breimann, Tuğberk Kaya, Madlen Oelsner, M Sabri Hamad, Laura I Hofmann, Carl P Blobel, Carsten B Schmidt‐Weber, Ozgun Gokce, Constanze A Jakwerth, Jakob Trimpert, Janine Kimpel, Andreas Pichlmair, Stefan F Lichtenthaler
Publikováno v:
EMBO Rep. 23:e54305 (2022)
EMBO reports 23(6), e54305 (2022). doi:10.15252/embr.202154305
EMBO reports 23(6), e54305 (2022). doi:10.15252/embr.202154305
The severe‐acute‐respiratory‐syndrome‐coronavirus‐2 (SARS‐CoV‐2) is the causative agent of COVID‐19, but host cell factors contributing to COVID‐19 pathogenesis remain only partly understood. We identify the host metalloprotease ADA
Autor:
Markus Zweckstetter, King Faisal Yambire, Niels Denkert, Claudia Steinem, Nelli Teske, Daryna Tarasenko, Michael Meinecke, Ira Milosevic, Indrani Mukherjee, Garima Jaipuria, Benjamin Kroppen
Publikováno v:
Cellular and Molecular Life Sciences
Cellular and molecular life sciences 78(5), 2355-2370 (2021). doi:10.1007/s00018-020-03647-z
Cellular and molecular life sciences 78(5), 2355-2370 (2021). doi:10.1007/s00018-020-03647-z
Membrane remodeling is a critical process for many membrane trafficking events, including clathrin-mediated endocytosis. Several molecular mechanisms for protein-induced membrane curvature have been described in some detail. Contrary, the effect that
Autor:
Lena Wischhof, Aasha Adhikari, Mrityunjoy Mondal, Anaïs Marsal-Cots, Jacek Biernat, Eva Maria Mandelkow, Eckhard Mandelkow, Dan Ehninger, Pierluigi Nicotera, Daniele Bano
Publikováno v:
The journal of biological chemistry 298(4), 101774 (2022). doi:10.1016/j.jbc.2022.101774
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Microtubule-associated protein tau is a naturally unfolded protein that can modulate a vast array of physiological processes through direct or indirect binding with molecular partners. Aberrant tau homeostasis has been implicated in the pathogenesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9afa5e92eaa371e963a4b0f7e6dd11ef
https://pub.dzne.de/record/163729
https://pub.dzne.de/record/163729
Autor:
Schlosser, Pascal, Tin, Adrienne, Matias-Garcia, Pamela R., Thio, Chris H. L., Joehanes, Roby, Liu, Hongbo, Weihs, Antoine, Yu, Zhi, Hoppmann, Anselm, Grundner-Culemann, Franziska, Min, Josine L., Adeyemo, Adebowale A., Agyemang, Charles, Ärnlöv, Johan, Aziz, Nasir A., Baccarelli, Andrea, Bochud, Murielle, Brenner, Hermann, Breteler, Monique M. B., Carmeli, Cristian, Chaker, Layal, Chambers, John C., Cole, Shelley A., Coresh, Josef, Corre, Tanguy, Correa, Adolfo, Cox, Simon R., de Klein, Niek, Delgado, Graciela E., Domingo-Relloso, Arce, Eckardt, Kai-Uwe, Ekici, Arif B., Endlich, Karlhans, Evans, Kathryn L., Floyd, James S., Fornage, Myriam, Franke, Lude, Fraszczyk, Eliza, Gao, Xu, Gào, Xīn, Ghanbari, Mohsen, Ghasemi, Sahar, Gieger, Christian, Greenland, Philip, Grove, Megan L., Harris, Sarah E., Hemani, Gibran, Henneman, Peter, Herder, Christian, Horvath, Steve, Hou, Lifang, Hurme, Mikko A., Hwang, Shih-Jen, Jarvelin, Marjo-Riitta, Kardia, Sharon L. R., Kasela, Silva, Kleber, Marcus E., Koenig, Wolfgang, Kooner, Jaspal S., Kramer, Holly, Kronenberg, Florian, Kühnel, Brigitte, Lehtimäki, Terho, Lind, Lars, Liu, Dan, Liu, Yongmei, Lloyd-Jones, Donald M., Lohman, Kurt, Lorkowski, Stefan, Lu, Ake T., Marioni, Riccardo E., März, Winfried, McCartney, Daniel L., Meeks, Karlijn A. C., Milani, Lili, Mishra, Pashupati P., Nauck, Matthias, Navas-Acien, Ana, Nowak, Christoph, Peters, Annette, Prokisch, Holger, Psaty, Bruce M., Raitakari, Olli T., Ratliff, Scott M., Reiner, Alex P., Rosas, Sylvia E., Schöttker, Ben, Schwartz, Joel, Sedaghat, Sanaz, Smith, Jennifer A., Sotoodehnia, Nona, Stocker, Hannah R., Stringhini, Silvia, Sundström, Johan, Swenson, Brenton R., Tellez-Plaza, Maria, van Meurs, Joyce B. J., van Vliet-Ostaptchouk, Jana V., Venema, Andrea, Verweij, Niek, Walker, Rosie M., Wielscher, Matthias, Winkelmann, Juliane, Wolffenbuttel, Bruce H. R., Zhao, Wei, Zheng, Yinan, Esko, Tõnu, Metspalu, Andres, Mägi, Reedik, Nelis, Mari, Loh, Marie, Snieder, Harold, Levy, Daniel, Waldenberger, Melanie, Susztak, Katalin, Köttgen, Anna, Teumer, Alexander
Publikováno v:
Nature communications, 12(1):7174. Nature Publishing Group
Nature Communications, 12:7174. Nature Publishing Group
Nature communications, vol. 12, no. 1, pp. 7174
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Repisalud
Instituto de Salud Carlos III (ISCIII)
Nature Communications
Nat. Commun. 12:7174 (2021)
Nature Communications, 12(1):7174. Nature Publishing Group
et al. 2021, ' Meta-analyses identify DNA methylation associated with kidney function and damage ', Nature Communications, vol. 12, 7174 (2021) . https://doi.org/10.1038/s41467-021-27234-3
Schlosser, P, Tin, A, Matias-garcia, P R, Thio, C H L, Joehanes, R, Liu, H, Weihs, A, Yu, Z, Hoppmann, A, Grundner-culemann, F, Min, J L, Adeyemo, A A, Agyemang, C, Ärnlöv, J, Aziz, N A, Baccarelli, A, Bochud, M, Brenner, H, Breteler, M M B, Carmeli, C, Chaker, L, Chambers, J C, Cole, S A, Coresh, J, Corre, T, Correa, A, Cox, S R, De Klein, N, Delgado, G E, Domingo-relloso, A, Eckardt, K, Ekici, A B, Endlich, K, Evans, K L, Floyd, J S, Fornage, M, Franke, L, Fraszczyk, E, Gao, X, Gào, X, Ghanbari, M, Ghasemi, S, Gieger, C, Greenland, P, Grove, M L, Harris, S E, Hemani, G, Henneman, P, Herder, C, Horvath, S, Hou, L, Hurme, M A, Hwang, S, Jarvelin, M, Kardia, S L R, Kasela, S, Kleber, M E, Koenig, W, Kooner, J S, Kramer, H, Kronenberg, F, Kühnel, B, Lehtimäki, T, Lind, L, Liu, D, Liu, Y, Lloyd-jones, D M, Lohman, K, Lorkowski, S, Lu, A T, Marioni, R E, März, W, Mccartney, D L, Meeks, K A C, Milani, L, Mishra, P P, Nauck, M, Navas-acien, A, Nowak, C, Peters, A, Prokisch, H, Psaty, B M, Raitakari, O T, Ratliff, S M, Reiner, A P, Rosas, S E, Schöttker, B, Schwartz, J, Sedaghat, S, Smith, J A, Sotoodehnia, N, Stocker, H R, Stringhini, S, Sundström, J, Swenson, B R, Tellez-plaza, M, Van Meurs, J B J, Van Vliet-ostaptchouk, J V, Venema, A, Verweij, N, Walker, R M, Wielscher, M, Winkelmann, J, Wolffenbuttel, B H R, Zhao, W, Zheng, Y, Milani, L, Loh, M, Snieder, H, Levy, D, Waldenberger, M, Susztak, K, Köttgen, A & Teumer, A 2021, ' Meta-analyses identify DNA methylation associated with kidney function and damage ', Nature Communications, vol. 12, no. 1, 7174 . https://doi.org/10.1038/s41467-021-27234-3
Nature Communications 12(1), 7174 (2021). doi:10.1038/s41467-021-27234-3
Nature Communications, 12:7174. Nature Publishing Group
Nature communications, vol. 12, no. 1, pp. 7174
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Repisalud
Instituto de Salud Carlos III (ISCIII)
Nature Communications
Nat. Commun. 12:7174 (2021)
Nature Communications, 12(1):7174. Nature Publishing Group
et al. 2021, ' Meta-analyses identify DNA methylation associated with kidney function and damage ', Nature Communications, vol. 12, 7174 (2021) . https://doi.org/10.1038/s41467-021-27234-3
Schlosser, P, Tin, A, Matias-garcia, P R, Thio, C H L, Joehanes, R, Liu, H, Weihs, A, Yu, Z, Hoppmann, A, Grundner-culemann, F, Min, J L, Adeyemo, A A, Agyemang, C, Ärnlöv, J, Aziz, N A, Baccarelli, A, Bochud, M, Brenner, H, Breteler, M M B, Carmeli, C, Chaker, L, Chambers, J C, Cole, S A, Coresh, J, Corre, T, Correa, A, Cox, S R, De Klein, N, Delgado, G E, Domingo-relloso, A, Eckardt, K, Ekici, A B, Endlich, K, Evans, K L, Floyd, J S, Fornage, M, Franke, L, Fraszczyk, E, Gao, X, Gào, X, Ghanbari, M, Ghasemi, S, Gieger, C, Greenland, P, Grove, M L, Harris, S E, Hemani, G, Henneman, P, Herder, C, Horvath, S, Hou, L, Hurme, M A, Hwang, S, Jarvelin, M, Kardia, S L R, Kasela, S, Kleber, M E, Koenig, W, Kooner, J S, Kramer, H, Kronenberg, F, Kühnel, B, Lehtimäki, T, Lind, L, Liu, D, Liu, Y, Lloyd-jones, D M, Lohman, K, Lorkowski, S, Lu, A T, Marioni, R E, März, W, Mccartney, D L, Meeks, K A C, Milani, L, Mishra, P P, Nauck, M, Navas-acien, A, Nowak, C, Peters, A, Prokisch, H, Psaty, B M, Raitakari, O T, Ratliff, S M, Reiner, A P, Rosas, S E, Schöttker, B, Schwartz, J, Sedaghat, S, Smith, J A, Sotoodehnia, N, Stocker, H R, Stringhini, S, Sundström, J, Swenson, B R, Tellez-plaza, M, Van Meurs, J B J, Van Vliet-ostaptchouk, J V, Venema, A, Verweij, N, Walker, R M, Wielscher, M, Winkelmann, J, Wolffenbuttel, B H R, Zhao, W, Zheng, Y, Milani, L, Loh, M, Snieder, H, Levy, D, Waldenberger, M, Susztak, K, Köttgen, A & Teumer, A 2021, ' Meta-analyses identify DNA methylation associated with kidney function and damage ', Nature Communications, vol. 12, no. 1, 7174 . https://doi.org/10.1038/s41467-021-27234-3
Nature Communications 12(1), 7174 (2021). doi:10.1038/s41467-021-27234-3
Chronic kidney disease is a major public health burden. Elevated urinary albumin-to-creatinine ratio is a measure of kidney damage, and used to diagnose and stage chronic kidney disease. To extend the knowledge on regulatory mechanisms related to kid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a666ac8780ee854739b2d4005651ff27
https://pure.amc.nl/en/publications/metaanalyses-identify-dna-methylation-associated-with-kidney-function-and-damage(0b3d0490-c103-42d9-a83e-999de439d3e1).html
https://pure.amc.nl/en/publications/metaanalyses-identify-dna-methylation-associated-with-kidney-function-and-damage(0b3d0490-c103-42d9-a83e-999de439d3e1).html
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:
Mikael Simons, Nikolaus Plesnila, Joshua Shrouder, Carl P. Blobel, Stephan A. Müller, Stefan F. Lichtenthaler, Johanna Tüshaus, Martina Arends
Publikováno v:
The FASEB journal 35(11), e21962 (2021). doi:10.1096/fj.202100936R
FASEB J
FASEB J
Proteolytic ectodomain shedding of membrane proteins is a fundamental mechanism to control the communication between cells and their environment. A key protease for membrane protein shedding is ADAM17, which requires a non-proteolytic subunit, either
Autor:
Simone Bonelli, Veronica M. Pravata, Stefan F. Lichtenthaler, Elisa Monaca, Matteo Calligaris, Danilo D'Apolito, Stephan A. Müller, Anna Paola Carreca, Simone D. Scilabra
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 5
International Journal of Molecular Sciences, Vol 22, Iss 2392, p 2392 (2021)
International journal of molecular sciences 22(5), 2392-(2021). doi:10.3390/ijms22052392
Volume 22
Issue 5
International Journal of Molecular Sciences, Vol 22, Iss 2392, p 2392 (2021)
International journal of molecular sciences 22(5), 2392-(2021). doi:10.3390/ijms22052392
Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane