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C N Shrimpton

Showing results (1-10 of 8) with videos related to

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Journal of Peptide Science : an Official Publication of the European Peptide Society|July 27, 2000
Soluble neutral metallopeptidases: physiological regulators of peptide actionC N Shrimpton, A I Smith
Journal of Thrombosis and Haemostasis : JTH|August 17, 2005
Receptors, rafts, and microvesicles in thrombosis and inflammationJ A López, I del Conde, C N Shrimpton
The Biochemical Journal|January 6, 2000
Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15C N Shrimpton, G Abbenante, R A Lew, et al.
Biochemical and Biophysical Research Communications|December 4, 1996
Differential activation of endopeptidase EC 3.4.24.15 toward natural and synthetic substrates by metal ionsA J Wolfson, C N Shrimpton, R A Lew, et al.
Hypertension (Dallas, Tex. : 1979)|February 19, 2000
A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotensionA I Smith, R A Lew, C N Shrimpton, et al.
Biochemical Society Transactions|August 30, 2000
Neuropeptidases regulating gonadal functionA I Smith, C N Shrimpton, U M Norman, et al.
The Journal of Biological Chemistry|July 11, 1997
Thiol activation of endopeptidase EC 3.4.24.15. A novel mechanism for the regulation of catalytic activityC N Shrimpton, M J Glucksman, R A Lew, et al.
The Journal of Biological Chemistry|September 2, 2000
The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylationJ W Tullai, P M Cummins, A Pabon, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Journal of Peptide Science : an Official Publication of the European Peptide Society|July 27, 2000
Soluble neutral metallopeptidases: physiological regulators of peptide actionC N Shrimpton, A I Smith
Journal of Thrombosis and Haemostasis : JTH|August 17, 2005
Receptors, rafts, and microvesicles in thrombosis and inflammationJ A López, I del Conde, C N Shrimpton
The Biochemical Journal|January 6, 2000
Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15C N Shrimpton, G Abbenante, R A Lew, et al.
Biochemical and Biophysical Research Communications|December 4, 1996
Differential activation of endopeptidase EC 3.4.24.15 toward natural and synthetic substrates by metal ionsA J Wolfson, C N Shrimpton, R A Lew, et al.
Hypertension (Dallas, Tex. : 1979)|February 19, 2000
A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotensionA I Smith, R A Lew, C N Shrimpton, et al.
Biochemical Society Transactions|August 30, 2000
Neuropeptidases regulating gonadal functionA I Smith, C N Shrimpton, U M Norman, et al.
The Journal of Biological Chemistry|July 11, 1997
Thiol activation of endopeptidase EC 3.4.24.15. A novel mechanism for the regulation of catalytic activityC N Shrimpton, M J Glucksman, R A Lew, et al.
The Journal of Biological Chemistry|September 2, 2000
The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylationJ W Tullai, P M Cummins, A Pabon, et al.
Pageof 1