Page last updated: 2024-08-17

aspartic acid and trypsinogen

aspartic acid has been researched along with trypsinogen in 16 studies

Research

Studies (16)

TimeframeStudies, this research(%)All Research%
pre-199010 (62.50)18.7374
1990's2 (12.50)18.2507
2000's3 (18.75)29.6817
2010's1 (6.25)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Craik, CS; Gráf, L; Hegyi, G; Hepp, J; Likó, I; Medzihradszky, K; Rutter, WJ1
Craik, CS; Fletterick, RJ; Graf, L; Patthy, A; Roczniak, S; Rutter, WJ1
Barns, RJ; Elmslie, RG1
Bradshaw, RA; Neurath, H; Tye, RW; Walsh, KA; Winter, WP1
Jacobsen, N; Sönju, T1
Lazdunski, M; Vincent, JP1
Bricteux-Grégoire, S; Florkin, M; Schyns, R1
Neurath, H; Radhakrishnan, TM; Walsh, KA1
Baratti, J; Desnuelle, P; Maroux, S1
Bricas, E; Delaage, M; Desnuelle, P; Lazdunski, M; Savrda, J1
Ichishima, E; Shintani, T1
Hedstrom, L; Lin, TY; Liu, X; Pasternak, A1
Gettins, PG; Gordon, NC; Peterson, FC1
Nemoda, Z; Sahin-Tóth, M1
Bradbury, AR; Destro-Bisol, G; Rickards, O; Rónai, Z; Sahin-Tóth, M; Witt, H1
Dziekonski, ET; Foreman, DJ; McLuckey, SA1

Other Studies

16 other study(ies) available for aspartic acid and trypsinogen

ArticleYear
Structural and functional integrity of specificity and catalytic sites of trypsin.
    International journal of peptide and protein research, 1988, Volume: 32, Issue:6

    Topics: Aspartic Acid; Binding Sites; Escherichia coli; Glutamates; Glutamic Acid; Kinetics; Models, Theoretical; Serine; Trypsin; Trypsinogen

1988
Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin.
    Biochemistry, 1987, May-05, Volume: 26, Issue:9

    Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Binding Sites; Cattle; Computer Graphics; Escherichia coli; Kinetics; Lysine; Models, Molecular; Plasmids; Protein Conformation; Rats; Recombinant Proteins; Substrate Specificity; Trypsin; Trypsinogen

1987
The active site of porcine enteropeptidase. Selective inactivation of the peptidase activity.
    Biochimica et biophysica acta, 1974, Jun-18, Volume: 350, Issue:2

    Topics: Animals; Aspartic Acid; Binding Sites; Calcium; Cattle; Dipeptides; Drug Stability; Enteropeptidase; Glutamine; Hot Temperature; Kinetics; Protease Inhibitors; Protein Binding; Protein Conformation; Protein Denaturation; Swine; Trypsinogen

1974
Comparison of the partial amino-acid sequence of dogfish trypsinogen with bovine trypsinogen.
    Nature, 1970, Apr-18, Volume: 226, Issue:5242

    Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Biological Evolution; Cattle; Chromatography, Ion Exchange; Cystine; Pepsin A; Peptides; Sharks; Species Specificity; Trypsin; Trypsinogen; Valine

1970
Molecular weight and amino acid composition of Macaca irus parotid alpha-amylase.
    Scandinavian journal of dental research, 1971, Volume: 79, Issue:3

    Topics: Albumins; Amino Acids; Amylases; Animals; Aspartic Acid; Chromatography, Gel; Enzyme Activation; Glycine; Haplorhini; Hydrogen-Ion Concentration; Hydrolysis; Macaca; Microscopy, Electron; Molecular Weight; Muramidase; Myoglobin; Ovalbumin; Parotid Gland; Trypsinogen; Ultracentrifugation

1971
Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges.
    Biochemistry, 1972, Aug-01, Volume: 11, Issue:16

    Topics: Acetamides; Alkylation; Aspartic Acid; Binding Sites; Borohydrides; Carbon Isotopes; Chromatography, Gel; Cysteine; Disulfides; Half-Life; Hydrogen-Ion Concentration; Imines; Iodoacetates; Kinetics; Lysine; Mathematics; Models, Chemical; Oxidation-Reduction; Pancreas; Protein Binding; Temperature; Trypsin; Trypsin Inhibitors; Trypsinogen

1972
Phylogeny of trypsinogen activation peptides.
    Comparative biochemistry and physiology. B, Comparative biochemistry, 1972, May-15, Volume: 42, Issue:1

    Topics: Amino Acid Sequence; Amino Acids; Animals; Artiodactyla; Aspartic Acid; Biological Evolution; Camelus; Chromatography, Ion Exchange; Chromatography, Thin Layer; Dansyl Compounds; Deer; Electrophoresis; Enzyme Activation; Goats; Mutation; Oligopeptides; Pancreas; Sheep; Species Specificity; Swine; Trypsinogen

1972
The promotion of activation of bovine trypsinogen by specific modification of aspartyl residues.
    Biochemistry, 1969, Volume: 8, Issue:10

    Topics: Amides; Amino Acids; Animals; Aspartic Acid; Calcium; Cattle; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Enzyme Activation; Isoleucine; Lysine; Peptides; Trypsin; Trypsinogen

1969
Purification and specificity of porcine enterokinase.
    The Journal of biological chemistry, 1971, Aug-25, Volume: 246, Issue:16

    Topics: Aminopeptidases; Animals; Aspartic Acid; Binding Sites; Calcium; Catalysis; Cattle; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Paper; Chymotrypsin; Duodenum; Electrophoresis; Endopeptidases; Enzyme Activation; Enzyme Precursors; Hydrogen-Ion Concentration; Hydrolysis; Isoflurophate; Isoleucine; Kinetics; Lysine; Methylation; Paper; Peptides; Phosphorus Isotopes; Protease Inhibitors; Sulfonic Acids; Swine; Toluene; Trypsin; Trypsin Inhibitors; Trypsinogen

1971
On the activation of trypsinogen. A study of peptide models related to the N-terminal sequence of the zymogen.
    Biochemical and biophysical research communications, 1967, Oct-26, Volume: 29, Issue:2

    Topics: Amino Acid Sequence; Aspartic Acid; Calcium; Catalysis; Chemical Phenomena; Chemistry; Kinetics; Peptides; Trypsinogen

1967
Primary structure of aspergillopepsin I deduced from nucleotide sequence of the gene and aspartic acid-76 is an essential active site of the enzyme for trypsinogen activation.
    Biochimica et biophysica acta, 1994, Feb-16, Volume: 1204, Issue:2

    Topics: Amino Acid Sequence; Aspartic Acid; Aspartic Acid Endopeptidases; Aspergillus; Base Sequence; Binding Sites; Genes, Fungal; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Pepsin A; Serine; Substrate Specificity; Trypsinogen

1994
Activating a zymogen without proteolytic processing: mutation of Lys15 and Asn194 activates trypsinogen.
    Biochemistry, 1998, Nov-17, Volume: 37, Issue:46

    Topics: Animals; Aprotinin; Asparagine; Aspartic Acid; Cattle; Coumarins; Enzyme Activation; Enzyme Stability; Histidine; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Oligopeptides; Peptide Fragments; Phenylalanine; Protein Conformation; Protein Processing, Post-Translational; Rats; Recombinant Fusion Proteins; Substrate Specificity; Trypsin; Trypsinogen

1998
High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.
    Biochemistry, 2001, May-29, Volume: 40, Issue:21

    Topics: Alanine; Animals; Aprotinin; Aspartic Acid; Cattle; Enzyme Activation; Escherichia coli; Macromolecular Substances; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Protons; Serine; Trypsin; Trypsin Inhibitor, Kunitz Soybean; Trypsin Inhibitors; Trypsinogen

2001
The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition.
    The Journal of biological chemistry, 2005, Aug-19, Volume: 280, Issue:33

    Topics: Amino Acid Motifs; Animals; Aspartic Acid; Cattle; Conserved Sequence; Enteropeptidase; Enzyme Activation; Enzyme Precursors; Humans; Trypsin; Trypsinogen

2005
A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).
    The Biochemical journal, 2009, Feb-15, Volume: 418, Issue:1

    Topics: Adolescent; Adult; Africa; Aged; Aged, 80 and over; Aspartic Acid; Cell Line; Child; Child, Preschool; Female; Genotype; Humans; Male; Middle Aged; Mutation; Polymorphism, Genetic; Sulfur; Trypsin; Trypsinogen; Tyrosine

2009
Maximizing Selective Cleavages at Aspartic Acid and Proline Residues for the Identification of Intact Proteins.
    Journal of the American Society for Mass Spectrometry, 2019, Volume: 30, Issue:1

    Topics: Arginine; Aspartic Acid; Carbonic Anhydrases; Databases, Protein; Hydrogen-Ion Concentration; Myoglobin; Proline; Proteins; Proteomics; Software; Spectrometry, Mass, Electrospray Ionization; Trypsinogen; Ubiquitin

2019