alanine and mci 9038

alanine has been researched along with mci 9038 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
Ambler, J; Baettig, U; Brown, L; Brundish, D; Cockcroft, X; Dell, C; Furzer, A; Garman, S; Janus, D; Kane, PD; Mitchelson, A; Smith, G; Talbot, MD; Tweed, M; Walker, CV; Wills, N	1
de Bosch, N; Ebisawa, K; Iwahana, H; Matsudai, M; Ruiz-Sáez, A; Sekine, O; Sugo, T; Umeyama, H	1

Other Studies

2 other study(ies) available for alanine and mci 9038

Article	Year
The design and synthesis of thrombin inhibitors: analogues of MD805 containing non-polar surrogates for arginine at the P1 position. Bioorganic & medicinal chemistry letters, 2000, Jul-17, Volume: 10, Issue:14 Topics: Alanine; Antithrombins; Arginine; Chymotrypsin; Drug Design; Factor Xa Inhibitors; Fibrinolysin; Kallikreins; Models, Molecular; Molecular Structure; Pipecolic Acids; Serine Proteinase Inhibitors; Structure-Activity Relationship; Sulfonamides; Thiazoles; Thrombin; Trypsin	2000
Substitution of Gly-548 to Ala in the substrate binding pocket of prothrombin Perijá leads to the loss of thrombin proteolytic activity. Thrombosis and haemostasis, 2002, Volume: 87, Issue:2 Topics: Alanine; Amino Acid Substitution; Antithrombin III; Arginine; Binding Sites; Catalytic Domain; Codon; DNA Mutational Analysis; Enzyme Activation; Enzyme Inhibitors; Exons; Factor V; Factor Xa; Glycine; Humans; Models, Molecular; Pipecolic Acids; Polymorphism, Single-Stranded Conformational; Protein Conformation; Prothrombin; Serine; Structure-Activity Relationship; Sulfonamides; Thrombin	2002

Article

Year

The design and synthesis of thrombin inhibitors: analogues of MD805 containing non-polar surrogates for arginine at the P1 position.

Bioorganic & medicinal chemistry letters, 2000, Jul-17, Volume: 10, Issue:14

Topics: Alanine; Antithrombins; Arginine; Chymotrypsin; Drug Design; Factor Xa Inhibitors; Fibrinolysin; Kallikreins; Models, Molecular; Molecular Structure; Pipecolic Acids; Serine Proteinase Inhibitors; Structure-Activity Relationship; Sulfonamides; Thiazoles; Thrombin; Trypsin

2000

Substitution of Gly-548 to Ala in the substrate binding pocket of prothrombin Perijá leads to the loss of thrombin proteolytic activity.

Thrombosis and haemostasis, 2002, Volume: 87, Issue:2

Topics: Alanine; Amino Acid Substitution; Antithrombin III; Arginine; Binding Sites; Catalytic Domain; Codon; DNA Mutational Analysis; Enzyme Activation; Enzyme Inhibitors; Exons; Factor V; Factor Xa; Glycine; Humans; Models, Molecular; Pipecolic Acids; Polymorphism, Single-Stranded Conformational; Protein Conformation; Prothrombin; Serine; Structure-Activity Relationship; Sulfonamides; Thrombin

2002