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M Bourdi

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Annals of the New York Academy of Sciences|June 23, 1993
Autoantibodies against cytochromes P-450 in drug-induced autoimmune hepatitisP H Beaune, M Bourdi
Molecular Pharmacology|June 1, 1994
Interactions of dihydralazine with cytochromes P4501A: a possible explanation for the appearance of anti-cytochrome P4501A2 autoantibodiesM Bourdi, M Tinel, P H Beaune, et al.
Chemical Research in Toxicology|April 17, 2001
Halothane-induced liver injury in outbred guinea pigs: role of trifluoroacetylated protein adducts in animal susceptibilityM Bourdi, H R Amouzadeh, T H Rushmore, et al.
Toxicology|October 5, 1993
Immunotoxicology and expression of human cytochrome P450 in microorganismsP Beaune, M Bourdi, C Belloc, et al.
Chemical Research in Toxicology|January 1, 1997
UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothaneH R Amouzadeh, M Bourdi, J L Martin, et al.
European Journal of Haematology. Supplementum|January 1, 1996
Anti-cytochrome P450 autoantibodies in drug-induced diseaseP H Beaune, S Lecoeur, M Bourdi, et al.
Molecular Pharmacology|August 1, 1992
Anti-liver microsomes autoantibodies and dihydralazine-induced hepatitis: specificity of autoantibodies and inductive capacity of the drugM Bourdi, J C Gautier, J Mircheva, et al.
The Journal of Clinical Investigation|June 1, 1990
Anti-liver endoplasmic reticulum autoantibodies are directed against human cytochrome P-450IA2. A specific marker of dihydralazine-induced hepatitisM Bourdi, D Larrey, J Nataf, et al.
Chemical Research in Toxicology|October 1, 1996
Human cytochrome P450 2E1 is a major autoantigen associated with halothane hepatitisM Bourdi, W Chen, R M Peter, et al.
Archives of Biochemistry and Biophysics|November 10, 1995
cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferaseM Bourdi, D Demady, J L Martin, et al.
Pageof 2

Showing results (1-10 of 14) with videos related to

Sort By:
Pageof 2
Annals of the New York Academy of Sciences|June 23, 1993
Autoantibodies against cytochromes P-450 in drug-induced autoimmune hepatitisP H Beaune, M Bourdi
Molecular Pharmacology|June 1, 1994
Interactions of dihydralazine with cytochromes P4501A: a possible explanation for the appearance of anti-cytochrome P4501A2 autoantibodiesM Bourdi, M Tinel, P H Beaune, et al.
Chemical Research in Toxicology|April 17, 2001
Halothane-induced liver injury in outbred guinea pigs: role of trifluoroacetylated protein adducts in animal susceptibilityM Bourdi, H R Amouzadeh, T H Rushmore, et al.
Toxicology|October 5, 1993
Immunotoxicology and expression of human cytochrome P450 in microorganismsP Beaune, M Bourdi, C Belloc, et al.
Chemical Research in Toxicology|January 1, 1997
UDP-glucose:glycoprotein glucosyltransferase associates with endoplasmic reticulum chaperones and its activity is decreased in vivo by the inhalation anesthetic halothaneH R Amouzadeh, M Bourdi, J L Martin, et al.
European Journal of Haematology. Supplementum|January 1, 1996
Anti-cytochrome P450 autoantibodies in drug-induced diseaseP H Beaune, S Lecoeur, M Bourdi, et al.
Molecular Pharmacology|August 1, 1992
Anti-liver microsomes autoantibodies and dihydralazine-induced hepatitis: specificity of autoantibodies and inductive capacity of the drugM Bourdi, J C Gautier, J Mircheva, et al.
The Journal of Clinical Investigation|June 1, 1990
Anti-liver endoplasmic reticulum autoantibodies are directed against human cytochrome P-450IA2. A specific marker of dihydralazine-induced hepatitisM Bourdi, D Larrey, J Nataf, et al.
Chemical Research in Toxicology|October 1, 1996
Human cytochrome P450 2E1 is a major autoantigen associated with halothane hepatitisM Bourdi, W Chen, R M Peter, et al.
Archives of Biochemistry and Biophysics|November 10, 1995
cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferaseM Bourdi, D Demady, J L Martin, et al.
Pageof 2