Associated Papers
Lipin phosphatidic acid phosphatases: Structure, function, regulation, and disease association.
Welcome FS et al.
Advances in Biological Regulation, 2025
Crystal structure of a lipin/Pah phosphatidic acid phosphatase.
Khayyo VI et al.
Nature Communications, 2020
Conserved residues in the N terminus of lipin-1 are required for binding to protein phosphatase-1c, nuclear translocation, and phosphatidate phosphatase activity.
Kok BPC et al.
The Journal of Biological Chemistry, 2014
The lipin family: mutations and metabolism.
Reue K
Current Opinion in Lipidology, 2009
Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood.
Zeharia A et al.
American Journal of Human Genetics, 2008
The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity.
Han GS et al.
The Journal of Biological Chemistry, 2007
Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin.
Péterfy M et al.
Nature Genetics, 2001
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