J. Roitelman

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Human HRD1 Is an E3 Ubiquitin Ligase Involved in Degradation of Proteins from the Endoplasmic Reticulum*

V. Chau, G. Hassink, M. Kikkert, 2004, Journal of Biological Chemistry.

In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal.

R. Schimke, A. Kung, S. Sherwood, 1993, Proceedings of the National Academy of Sciences of the United States of America.

SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells.

J. Olzmann, R. Wojcikiewicz, Y. Wang, 2009, Biochimica et biophysica acta.

The low-density lipoprotein receptor plays a role in the infection of primary human hepatocytes by hepatitis C virus.

D. Harats, F. Malavasi, C. Fournier-Wirth, 2007, Journal of hepatology.

Interindividual variability in sensitivity to warfarin‐Nature or nurture?

H. Halkin, D. Harats, S. Almog, 2001, Clinical pharmacology and therapeutics.

Metabolically Regulated Endoplasmic Reticulum-associated Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase

D. Harats, R. Avner, J. Roitelman, 2011, The Journal of Biological Chemistry.

Apomine, a Novel Hypocholesterolemic Agent, Accelerates Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase and Stimulates Low Density Lipoprotein Receptor Activity*

C. Ammon-Zufferey, D. Masson, E. Niesor, 2004, Journal of Biological Chemistry.

Direct plasma radioimmunoassay for rat amylin-(1-37): concentrations with acquired and genetic obesity.

Y. Lee, D. Stein, K. Luskey, 1994, The American journal of physiology.

Impaired Regulation of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation in Lovastatin-resistant Cells*

S. Polak‐Charcon, T. Ravid, S. Polak-Charcon, 1999, The Journal of Biological Chemistry.

Lack of correlation between 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and lovastatin resistance in nerve growth factor treated PC-12 cells

Y. Kloog, G. Ben-Baruch, J. Roitelman, 1994, Cellular and Molecular Neurobiology.

Immunological evidence for eight spans in the membrane domain of 3- hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulum

W. Dunn, R. D. Simoni, S. Bar-Nun, 1992, The Journal of cell biology.

Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase.

R. D. Simoni, J. Roitelman, 1992, The Journal of biological chemistry.

Inhibition of degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo by cysteine protease inhibitors.

R. D. Simoni, S. Inoue, S. Bar-Nun, 1991, The Journal of biological chemistry.

Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. Evidence for thiol-dependent allosteric modulation of enzyme activity.

I. Shechter, J. Roitelman, 1984, Journal of Biological Chemistry.

Allosteric and non-allosteric forms of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase: differential inhibition of activity by adenosine 2'-monophospho-5'-diphosphoribose.

I. Shechter, J. Roitelman, 1986, Journal of lipid research.

Allosteric activation of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase by nicotinamide adenine dinucleotides.

I. Shechter, J. Roitelman, 1984, The Journal of biological chemistry.

Structural requirements for allosteric activators of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase.

I. Shechter, J. Roitelman, 1984, Biochemical and biophysical research communications.

Lovastatin and phospholipase Cgamma regulate constitutive and protein kinase C dependent integrin mediated interactions of human T-cells with collagen.

L. Chess, I. Bank, I. Goldstein, 2003, Cellular immunology.

The Ubiquitin-Proteasome Pathway Mediates the Regulated Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase*

D. Harats, T. Ravid, R. Avner, 2000, The Journal of Biological Chemistry.

Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system

R. Wojcikiewicz, A. Weissman, G. L. Wilson, 2012, Molecular biology of the cell.

Peptide transport by the multidrug resistance pump.

R. Schimke, R. Sharma, R. D. Simoni, 1992, The Journal of biological chemistry.

Specific Induction of Tumor Neovasculature Death by Modified Murine PPE-1 Promoter Armed with HSV-TK

I. Barshack, D. Harats, S. Greenberger, 2008, Pathobiology.

Improved PCR amplification/Hhal restriction for unambiguous determination of apolipoprotein E alleles.

J. Roitelman, S. Eisenberg, E. Appel, 1995, Clinical chemistry.

Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation.

D. Harats, R. Avner, J. Roitelman, 2009, Molecular biology of the cell.

Photoactivated aflatoxins are mutagens to Salmonella typhimurium and bind covalently to DNA in vitro.

A. Stark, J. Roitelman, H. Israel-Kalinsky, 1982, Carcinogenesis.

Haploid Mammalian Genetic Screen Identifies UBXD8 as a Key Determinant of HMGCR Degradation and Cholesterol Biosynthesis

M. Raaben, T. Brummelkamp, N. Zelcer, 2017, Arteriosclerosis, thrombosis, and vascular biology.

Ubiquitin Is Conjugated by Membrane Ubiquitin Ligase to Three Sites, including the N Terminus, in Transmembrane Region of Mammalian 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase

R. Avner, R. Doolman, J. Roitelman, 2004, Journal of Biological Chemistry.

Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase.

R. D. Simoni, S. Inoue, S. Bar-Nun, 1991, The Journal of biological chemistry.

Studies on the catalytic site of rat liver HMG-CoA reductase: interaction with CoA-thioesters and inactivation by iodoacetamide.

I. Shechter, J. Roitelman, Ishaiahu Shechter, 1989, Journal of lipid research.

The Ubiquitin-Proteasome Pathway Mediates the Regulated Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase*

D. Harats, T. Ravid, R. Avner, 2000, The Journal of Biological Chemistry.