Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Magdalena Topolska"'
Autor:
Fernando Martínez-Montañés, Albert Casanovas, Richard R. Sprenger, Magdalena Topolska, David L. Marshall, Marta Moreno-Torres, Berwyck L.J. Poad, Stephen J. Blanksby, Martin Hermansson, Ole N. Jensen, Christer S. Ejsing
Publikováno v:
Cell Reports, Vol 32, Iss 6, Pp 108024- (2020)
Summary: The ability to remodel lipid metabolism under changing conditions is pivotal for cellular functionality and homeostasis. Here, we characterize the regulatory landscape of phosphorylation-based signaling events across the life cycle of Saccha
Externí odkaz:
https://doaj.org/article/c5ea7ca592024eb0a1b9cd19cf2ab979
Publikováno v:
Biomolecules, Vol 10, Iss 12, p 1598 (2020)
Membrane-tethered sterol-binding Lam/Ltc proteins localize at junctions between the endoplasmic reticulum (ER) membrane and other organelles. Two of the six family members—Lam2/Ltc4 (initially Ysp2) and paralog Lam4/Ltc3—localize to ER-plasma mem
Externí odkaz:
https://doaj.org/article/ff4c3bd5e92141efafd49ac79228e654
Publikováno v:
Biomolecules, Vol 10, Iss 1, p 118 (2020)
De novo fatty acid synthesis is a pivotal enzymatic process in all eukaryotic organisms. It is involved in the conversion of glucose and other nutrients to fatty acyl (FA) chains, that cells use as building blocks for membranes, energy storage, and s
Externí odkaz:
https://doaj.org/article/539e3e4f986649ffb555bb3c237c676b
Publikováno v:
Biomolecules; Volume 10; Issue 12; Pages: 1598
Biomolecules
Topolska, M, Roelants, F M, Si, E P & Thorner, J 2020, ' TORC2-Dependent Ypk1-Mediated Phosphorylation of Lam2/Ltc4 Disrupts Its Association with the β-Propeller Protein Laf1 at Endoplasmic Reticulum-Plasma Membrane Contact Sites in the Yeast Saccharomyces cerevisiae ', Biomolecules, vol. 10, no. 12, 1598 . https://doi.org/10.3390/biom10121598
Biomolecules, vol 10, iss 12
Biomolecules, Vol 10, Iss 1598, p 1598 (2020)
Biomolecules
Topolska, M, Roelants, F M, Si, E P & Thorner, J 2020, ' TORC2-Dependent Ypk1-Mediated Phosphorylation of Lam2/Ltc4 Disrupts Its Association with the β-Propeller Protein Laf1 at Endoplasmic Reticulum-Plasma Membrane Contact Sites in the Yeast Saccharomyces cerevisiae ', Biomolecules, vol. 10, no. 12, 1598 . https://doi.org/10.3390/biom10121598
Biomolecules, vol 10, iss 12
Biomolecules, Vol 10, Iss 1598, p 1598 (2020)
Membrane-tethered sterol-binding Lam/Ltc proteins localize at junctions between the endoplasmic reticulum (ER) membrane and other organelles. Two of the six family members—Lam2/Ltc4 (initially Ysp2) and paralog Lam4/Ltc3—localize to ER-plasma mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54dab3c862c64e79309cd526496f87fc
Autor:
Ole N. Jensen, Albert Casanovas, Magdalena Topolska, Christer S. Ejsing, Martin Hermansson, Richard R. Sprenger, David L. Marshall, Stephen J. Blanksby, Berwyck L. J. Poad, Marta Moreno-Torres, Fernando Martínez-Montañés
Publikováno v:
Martínez-Montañés, F, Casanovas, A, Sprenger, R R, Topolska, M, Marshall, D L, Moreno-Torres, M, Poad, B L J, Blanksby, S J, Hermansson, M, Jensen, O N & Ejsing, C S 2020, ' Phosphoproteomic Analysis across the Yeast Life Cycle Reveals Control of Fatty Acyl Chain Length by Phosphorylation of the Fatty Acid Synthase Complex ', Cell Reports, vol. 32, no. 6, 108024 . https://doi.org/10.1016/j.celrep.2020.108024
Cell Reports, Vol 32, Iss 6, Pp 108024-(2020)
Cell Reports, Vol 32, Iss 6, Pp 108024-(2020)
Summary: The ability to remodel lipid metabolism under changing conditions is pivotal for cellular functionality and homeostasis. Here, we characterize the regulatory landscape of phosphorylation-based signaling events across the life cycle of Saccha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe5896e4bd2bdb7b567d7222f3df10a7
https://findresearcher.sdu.dk:8443/ws/files/172075491/1_s2.0_S2211124720310093_main.pdf
https://findresearcher.sdu.dk:8443/ws/files/172075491/1_s2.0_S2211124720310093_main.pdf
Publikováno v:
Biomolecules
Biomolecules, Vol 10, Iss 1, p 118 (2020)
Volume 10
Issue 1
Topolska, M, Martínez-Montañés, F & Ejsing, C S 2020, ' A Simple and Direct Assay for Monitoring Fatty Acid Synthase Activity and Product-Specificity by High-Resolution Mass Spectrometry ', Biomolecules, vol. 10, no. 1, 118 . https://doi.org/10.3390/biom10010118
Biomolecules, Vol 10, Iss 1, p 118 (2020)
Volume 10
Issue 1
Topolska, M, Martínez-Montañés, F & Ejsing, C S 2020, ' A Simple and Direct Assay for Monitoring Fatty Acid Synthase Activity and Product-Specificity by High-Resolution Mass Spectrometry ', Biomolecules, vol. 10, no. 1, 118 . https://doi.org/10.3390/biom10010118
De novo fatty acid synthesis is a pivotal enzymatic process in all eukaryotic organisms. It is involved in the conversion of glucose and other nutrients to fatty acyl (FA) chains, that cells use as building blocks for membranes, energy storage, and s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e03821b1332786d464c7bdadf1916b35
https://pubmed.ncbi.nlm.nih.gov/31936797
https://pubmed.ncbi.nlm.nih.gov/31936797