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G Isaya

Showing results (11-20 of 29) with videos related to

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Human Molecular Genetics|May 20, 1999
Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiaeS S Branda, Z Y Yang, A Chew, et al.
Biochemical and Biophysical Research Communications|September 24, 1996
Mutations in a putative zinc-binding domain inactivate the mitochondrial intermediate peptidaseA Chew, R A Rollins, W R Sakati, et al.
Clinical Biochemistry|February 1, 1987
Clinical varieties of carnitine and carnitine palmitoyltransferase deficiencyC Angelini, C Trevisan, G Isaya, et al.
The Journal of Biological Chemistry|October 6, 2000
Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different ratesP Cavadini, J Adamec, F Taroni, et al.
The Journal of Cell Biology|April 1, 1991
Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptideG Isaya, F Kalousek, W A Fenton, et al.
Neurology|March 1, 1984
Myoglobinuria and carnitine palmityltransferase (CPT) deficiency: studies with malonyl-CoA suggest absence of only CPT-IIC P Trevisan, C Angelini, L Freddo, et al.
European Neurology|January 1, 1986
Malonyl-CoA abnormal inhibition of residual enzyme activity in carnitine palmitoyltransferase deficiencyC P Trevisan, C Angelini, L A Fiorellini, et al.
Genomics|March 15, 1997
Cloning, expression, and chromosomal assignment of the human mitochondrial intermediate peptidase gene (MIPEP)A Chew, E A Buck, S Peretz, et al.
The Journal of Biological Chemistry|July 31, 1999
Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidaseS S Branda, P Cavadini, J Adamec, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1991
Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutationP E Purdue, J Allsop, G Isaya, et al.
Pageof 3

Showing results (11-20 of 29) with videos related to

Sort By:
Pageof 3
Human Molecular Genetics|May 20, 1999
Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiaeS S Branda, Z Y Yang, A Chew, et al.
Biochemical and Biophysical Research Communications|September 24, 1996
Mutations in a putative zinc-binding domain inactivate the mitochondrial intermediate peptidaseA Chew, R A Rollins, W R Sakati, et al.
Clinical Biochemistry|February 1, 1987
Clinical varieties of carnitine and carnitine palmitoyltransferase deficiencyC Angelini, C Trevisan, G Isaya, et al.
The Journal of Biological Chemistry|October 6, 2000
Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different ratesP Cavadini, J Adamec, F Taroni, et al.
The Journal of Cell Biology|April 1, 1991
Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptideG Isaya, F Kalousek, W A Fenton, et al.
Neurology|March 1, 1984
Myoglobinuria and carnitine palmityltransferase (CPT) deficiency: studies with malonyl-CoA suggest absence of only CPT-IIC P Trevisan, C Angelini, L Freddo, et al.
European Neurology|January 1, 1986
Malonyl-CoA abnormal inhibition of residual enzyme activity in carnitine palmitoyltransferase deficiencyC P Trevisan, C Angelini, L A Fiorellini, et al.
Genomics|March 15, 1997
Cloning, expression, and chromosomal assignment of the human mitochondrial intermediate peptidase gene (MIPEP)A Chew, E A Buck, S Peretz, et al.
The Journal of Biological Chemistry|July 31, 1999
Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidaseS S Branda, P Cavadini, J Adamec, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1991
Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutationP E Purdue, J Allsop, G Isaya, et al.
Pageof 3