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Skaidrite K. Krisans

Researcher at San Diego State University

Publications -  47
Citations -  3053

Skaidrite K. Krisans is an academic researcher from San Diego State University. The author has contributed to research in topics: Peroxisome & Reductase. The author has an hindex of 30, co-authored 47 publications receiving 2958 citations. Previous affiliations of Skaidrite K. Krisans include University of California, Los Angeles.

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Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

Geoff H. Werstuck, +11 more
- 15 May 2001 - 
TL;DR: It is reported here that homocysteine-induced endoplasmic reticulum (ER) stress activates both the unfolded protein response and the sterol regulatory element-binding proteins (SREBPs) in cultured human hepatocytes as well as vascular endothelial and aortic smooth muscle cells.
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3-Hydroxy-3-methylglutaryl coenzyme A reductase localization in rat liver peroxisomes and microsomes of control and cholestyramine-treated animals: quantitative biochemical and immunoelectron microscopical analyses.

Gilbert A. Keller, +2 more
- 01 Sep 1986 - 
TL;DR: A quantitative biochemical and immunoelectron microscopical analysis of HMG-CoA reductase in rat liver peroxisomes and microsomes of normal and cholestyramine-treated animals found that the enzyme is present in the matrix of perxisomes.
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Central role of peroxisomes in isoprenoid biosynthesis

Werner J. Kovacs, +2 more
- 01 Sep 2002 - 
TL;DR: The purpose of this review is to emphasize some of the recent findings related to the localization of cholesterol biosynthetic enzymes in peroxisomes and to discuss the impairment ofolesterol biosynthesis inperoxisomal deficiency diseases.
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Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and mitochondrial-associated membrane

Tal M. Lewin, +3 more
- 15 Aug 2002 - 
TL;DR: It is now appears that ACS4 may also be important in activating fatty acids destined for peroxisomal oxidation, and it is determined that, unlike ACS1 and 5, ACS4 is not an intrinsic membrane protein.
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Antibodies directed against the peroxisomal targeting signal of firefly luciferase recognize multiple mammalian peroxisomal proteins.

Stephen Jay Gould, +3 more
- 01 Jan 1990 - 
TL;DR: Immunofluorescence and immunocryoelectron microscopy revealed that the anti-peptide antibodies specifically detected peroxisomes in mammalian cells, and characterized that the antibodies were primarily directed against the COOH-terminal three amino acids of the peptide.