serine and benzamidine

serine has been researched along with benzamidine 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
Antal, J; Gráf, L; Jelinek, B; Venekei, I	1
Abdel-Meguid, SS; Babine, RE; Jin, L; Pandey, P; Strickler, JE; Weaver, DT	1

Other Studies

2 other study(ies) available for serine and benzamidine

Article	Year
Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease. Protein engineering, design & selection : PEDS, 2004, Volume: 17, Issue:2 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartic Acid; Benzamidines; Chymotrypsin; Chymotrypsinogen; Glycine; Kinetics; Molecular Sequence Data; Mutation; Peptide Hydrolases; Protein Conformation; Rats; Serine; Substrate Specificity; Trypsin; Trypsin Inhibitors	2004
Mutation of surface residues to promote crystallization of activated factor XI as a complex with benzamidine: an essential step for the iterative structure-based design of factor XI inhibitors. Acta crystallographica. Section D, Biological crystallography, 2005, Volume: 61, Issue:Pt 10 Topics: Benzamidines; Binding Sites; Blood Coagulation Factors; Catalysis; Catalytic Domain; Crystallography, X-Ray; DNA, Complementary; Factor XI; Factor XIa; Humans; Hydrogen Bonding; Inhibitory Concentration 50; Ligands; Macromolecular Substances; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Peptides; Pichia; Protein Binding; Protein Conformation; Recombinant Proteins; Serine	2005

Article

Year

Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease.

Protein engineering, design & selection : PEDS, 2004, Volume: 17, Issue:2

Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartic Acid; Benzamidines; Chymotrypsin; Chymotrypsinogen; Glycine; Kinetics; Molecular Sequence Data; Mutation; Peptide Hydrolases; Protein Conformation; Rats; Serine; Substrate Specificity; Trypsin; Trypsin Inhibitors

2004

Mutation of surface residues to promote crystallization of activated factor XI as a complex with benzamidine: an essential step for the iterative structure-based design of factor XI inhibitors.

Acta crystallographica. Section D, Biological crystallography, 2005, Volume: 61, Issue:Pt 10

Topics: Benzamidines; Binding Sites; Blood Coagulation Factors; Catalysis; Catalytic Domain; Crystallography, X-Ray; DNA, Complementary; Factor XI; Factor XIa; Humans; Hydrogen Bonding; Inhibitory Concentration 50; Ligands; Macromolecular Substances; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Peptides; Pichia; Protein Binding; Protein Conformation; Recombinant Proteins; Serine

2005