Page last updated: 2024-08-22

angiotensin ii and (4-(n-hydroxyamino)-2r-isobutyl-3s-methylsuccinyl)-l-phenylglycine-n-methylamide

angiotensin ii has been researched along with (4-(n-hydroxyamino)-2r-isobutyl-3s-methylsuccinyl)-l-phenylglycine-n-methylamide in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Asakura, M; Asanuma, H; Beppu, S; Higashiyama, S; Hori, M; Ishiguro, H; Ishikura, F; Kitakaze, M; Liao, Y; Matsumura, Y; Node, K; Ohmoto, H; Sanada, S; Tada, M; Takashima, S; Takeda, H; Yoshinaka, T; Yoshino, K	1
Ichikawa, Y; Miki, T; Miura, T; Nakamura, Y; Nakano, A; Shimamoto, K; Tsuchihashi, K	1

Other Studies

2 other study(ies) available for angiotensin ii and (4-(n-hydroxyamino)-2r-isobutyl-3s-methylsuccinyl)-l-phenylglycine-n-methylamide

Article	Year
Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nature medicine, 2002, Volume: 8, Issue:1 Topics: ADAM Proteins; ADAM12 Protein; Angiotensin II; Animals; Aorta, Thoracic; Cardiomegaly; Disease Models, Animal; Disintegrins; Epidermal Growth Factor; ErbB Receptors; Glycine; GTP-Binding Proteins; Heart Ventricles; Heparin-binding EGF-like Growth Factor; Hydroxamic Acids; Hypertension; Intercellular Signaling Peptides and Proteins; Male; Membrane Proteins; Metalloendopeptidases; Phenylephrine; Protease Inhibitors; Protein Processing, Post-Translational; Rats; Signal Transduction; Systole; Transcriptional Activation	2002
The role of ADAM protease in the tyrosine kinase-mediated trigger mechanism of ischemic preconditioning. Cardiovascular research, 2004, Apr-01, Volume: 62, Issue:1 Topics: ADAM Proteins; ADAM17 Protein; Angiotensin II; Animals; Cyclic AMP-Dependent Protein Kinases; Dose-Response Relationship, Drug; Genistein; Glycine; Hydroxamic Acids; Immunoblotting; Ischemic Preconditioning, Myocardial; Metalloendopeptidases; Myocardial Infarction; Naphthalenes; Perfusion; Phosphorylation; Protein-Tyrosine Kinases; Rabbits; Signal Transduction; Tumor Necrosis Factor-alpha	2004

Article

Year

Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy.

Nature medicine, 2002, Volume: 8, Issue:1

Topics: ADAM Proteins; ADAM12 Protein; Angiotensin II; Animals; Aorta, Thoracic; Cardiomegaly; Disease Models, Animal; Disintegrins; Epidermal Growth Factor; ErbB Receptors; Glycine; GTP-Binding Proteins; Heart Ventricles; Heparin-binding EGF-like Growth Factor; Hydroxamic Acids; Hypertension; Intercellular Signaling Peptides and Proteins; Male; Membrane Proteins; Metalloendopeptidases; Phenylephrine; Protease Inhibitors; Protein Processing, Post-Translational; Rats; Signal Transduction; Systole; Transcriptional Activation

2002

The role of ADAM protease in the tyrosine kinase-mediated trigger mechanism of ischemic preconditioning.

Cardiovascular research, 2004, Apr-01, Volume: 62, Issue:1

Topics: ADAM Proteins; ADAM17 Protein; Angiotensin II; Animals; Cyclic AMP-Dependent Protein Kinases; Dose-Response Relationship, Drug; Genistein; Glycine; Hydroxamic Acids; Immunoblotting; Ischemic Preconditioning, Myocardial; Metalloendopeptidases; Myocardial Infarction; Naphthalenes; Perfusion; Phosphorylation; Protein-Tyrosine Kinases; Rabbits; Signal Transduction; Tumor Necrosis Factor-alpha

2004