Fah1p, a Saccharomyces cerevisiae Cytochromeb 5 Fusion Protein, and ItsArabidopsis thaliana Homolog That Lacks the Cytochromeb 5 Domain Both Function in the α-Hydroxylation of Sphingolipid-associated Very Long Chain Fatty Acids-Reference-Cited by-同舟云学术

Fah1p, a Saccharomyces cerevisiae Cytochromeb 5 Fusion Protein, and ItsArabidopsis thaliana Homolog That Lacks the Cytochromeb 5 Domain Both Function in the α-Hydroxylation of Sphingolipid-associated Very Long Chain Fatty Acids

Published:1997-11 Issue:45 Volume:272 Page:28281-28288
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mitchell Andrew G.,Martin Charles E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Structural and functional properties of the membrane binding segment of cytochrome b5.

2. Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase.

3. The fatty acid chain elongation system of mammalian endoplasmic reticulum

4. Localization of the synthesis of very-long-chain fatty acid in mitochondria from Saccharomyces cerevisiae

5. Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerophospholipids that mimic sphingolipid structures.

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