phenylalanine and tapi-2

phenylalanine has been researched along with tapi-2 in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Buckle, DR; Hooper, NM; Karran, EH; Oppong, SY; Parvathy, S; Turner, AJ	1
Albanell, J; Arribas, J; Baselga, J; Codony-Servat, J; Lopez-Talavera, JC	1

Other Studies

2 other study(ies) available for phenylalanine and tapi-2

Article	Year
Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in a lipid bilayer. The Biochemical journal, 1997, Oct-01, Volume: 327 ( Pt 1) Topics: Affinity Labels; Animals; Azirines; Ceramides; Detergents; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Hydroxamic Acids; Kidney; Lipid Bilayers; Liposomes; Matrix Metalloproteinase Inhibitors; Metalloendopeptidases; Peptidyl-Dipeptidase A; Phenylalanine; Protease Inhibitors; Solubility; Substrate Specificity; Swine; Thiophenes; Trypsin; Zinc	1997
Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells. Cancer research, 1999, Mar-15, Volume: 59, Issue:6 Topics: Breast Neoplasms; Endopeptidases; Humans; Hydroxamic Acids; Metalloendopeptidases; Phenylalanine; Phosphorylation; Protease Inhibitors; Receptor, ErbB-2; Thiophenes; Tissue Inhibitor of Metalloproteinase-1; Tumor Cells, Cultured; Tyrosine; Vanadates	1999

Article

Year

Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in a lipid bilayer.

The Biochemical journal, 1997, Oct-01, Volume: 327 ( Pt 1)

Topics: Affinity Labels; Animals; Azirines; Ceramides; Detergents; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Hydroxamic Acids; Kidney; Lipid Bilayers; Liposomes; Matrix Metalloproteinase Inhibitors; Metalloendopeptidases; Peptidyl-Dipeptidase A; Phenylalanine; Protease Inhibitors; Solubility; Substrate Specificity; Swine; Thiophenes; Trypsin; Zinc

1997

Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells.

Cancer research, 1999, Mar-15, Volume: 59, Issue:6

Topics: Breast Neoplasms; Endopeptidases; Humans; Hydroxamic Acids; Metalloendopeptidases; Phenylalanine; Phosphorylation; Protease Inhibitors; Receptor, ErbB-2; Thiophenes; Tissue Inhibitor of Metalloproteinase-1; Tumor Cells, Cultured; Tyrosine; Vanadates

1999