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V Chesneau

Showing results (1-10 of 13) with videos related to

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Protein Expression and Purification|June 2, 2000
Functional human insulin-degrading enzyme can be expressed in bacteriaV Chesneau, M R Rosner
The Biochemical Journal|October 12, 2000
Purified recombinant insulin-degrading enzyme degrades amyloid beta-protein but does not promote its oligomerizationV Chesneau, K Vekrellis, M R Rosner, et al.
Methods in Enzymology|January 1, 1995
N-arginine dibasic convertaseP Cohen, A R Pierotti, V Chesneau, et al.
Annals of the New York Academy of Sciences|March 22, 1996
Two novel metallopeptidases with a specificity for basic residues: functional properties, structure and cellular distributionT Foulon, S Cadel, V Chesneau, et al.
Biochimie|January 1, 1994
N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overviewV Chesneau, A R Pierotti, A Prat, et al.
The Journal of Biological Chemistry|January 21, 1994
Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residuesV Chesneau, A R Pierotti, N Barré, et al.
Endocrinology|August 1, 1997
Insulin-degrading enzyme does not require peroxisomal localization for insulin degradationV Chesneau, R K Perlman, W Li, et al.
Annales D'Endocrinologie|January 1, 1997
NRD convertase and aminopeptidase B: two processing metallopeptidases with a selectivity for basic residuesT Foulon, S Cadel, A Prat, et al.
The Biochemical Journal|July 6, 2000
N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surfaceV Hospital, V Chesneau, A Balogh, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 21, 1994
N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymesA R Pierotti, A Prat, V Chesneau, et al.
Pageof 2

Showing results (1-10 of 13) with videos related to

Sort By:
Pageof 2
Protein Expression and Purification|June 2, 2000
Functional human insulin-degrading enzyme can be expressed in bacteriaV Chesneau, M R Rosner
The Biochemical Journal|October 12, 2000
Purified recombinant insulin-degrading enzyme degrades amyloid beta-protein but does not promote its oligomerizationV Chesneau, K Vekrellis, M R Rosner, et al.
Methods in Enzymology|January 1, 1995
N-arginine dibasic convertaseP Cohen, A R Pierotti, V Chesneau, et al.
Annals of the New York Academy of Sciences|March 22, 1996
Two novel metallopeptidases with a specificity for basic residues: functional properties, structure and cellular distributionT Foulon, S Cadel, V Chesneau, et al.
Biochimie|January 1, 1994
N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overviewV Chesneau, A R Pierotti, A Prat, et al.
The Journal of Biological Chemistry|January 21, 1994
Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residuesV Chesneau, A R Pierotti, N Barré, et al.
Endocrinology|August 1, 1997
Insulin-degrading enzyme does not require peroxisomal localization for insulin degradationV Chesneau, R K Perlman, W Li, et al.
Annales D'Endocrinologie|January 1, 1997
NRD convertase and aminopeptidase B: two processing metallopeptidases with a selectivity for basic residuesT Foulon, S Cadel, A Prat, et al.
The Biochemical Journal|July 6, 2000
N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surfaceV Hospital, V Chesneau, A Balogh, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 21, 1994
N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymesA R Pierotti, A Prat, V Chesneau, et al.
Pageof 2