Results 141 to 150 of about 41,016 (180)

Survivin can alter mitochondrial architecture by regulating phosphatidylethanolamine synthesis. [PDF]

open access: yesJ Cell Sci
Dunajová L   +5 more
europepmc   +1 more source

GLP-1 receptor and Mitochondria-ER Contact Sites: an emerging mechanism of metabolic regulation. [PDF]

open access: yesFront Physiol
Cruz P   +5 more
europepmc   +1 more source

Regulation of phosphatidylserine decarboxylase abundance in the ER and mitochondria

open access: yesRegulation of phosphatidylserine decarboxylase abundance in the ER and mitochondria
openaire   +1 more source

Phosphatidylserine Decarboxylase Is Located on the External Side of the Inner Mitochondrial Membrane

open access: yesFEBS Letters, 1983
It is shown that the trypsin-treatment of rat liver mitochondria, depleted of the outer membrane, causes a strong inactivation of phosphatidylserine decarboxylase.
Lech Wojtczak   +2 more
exaly   +4 more sources

Structural Basis for Phosphatidylethanolamine Biosynthesis by Bacterial Phosphatidylserine Decarboxylase [PDF]

open access: yesStructure, 2020
In both prokaryotes and eukaryotes, phosphatidylethanolamine (PE), one of the most abundant membrane phospholipids, plays important roles in various membrane functions and is synthesized through the decarboxylation of phosphatidylserine (PS) by PS decarboxylases (PSDs). However, the catalysis and substrate recognition mechanisms of PSDs remain unclear.
Seiya Watanabe   +2 more
exaly   +3 more sources

Phosphatidylserine Decarboxylases, Key Enzymes of Lipid Metabolism [PDF]

open access: yesIUBMB Life, 2009
AbstractPhosphatidylserine decarboxylases (PSDs) (E.C. 4.1.1.65) are enzymes which catalyze the formation of phosphatidylethanolamine (PtdEtn) by decarboxylation of phosphatidylserine (PtdSer). This enzymatic activity has been identified in both prokaryotic and eukaryotic organisms.
Günther Daum
exaly   +3 more sources

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