Page last updated: 2024-08-17

aspartic acid and 1-anilino-8-naphthalenesulfonate

aspartic acid has been researched along with 1-anilino-8-naphthalenesulfonate in 36 studies

Research

Studies (36)

TimeframeStudies, this research(%)All Research%
pre-19906 (16.67)18.7374
1990's12 (33.33)18.2507
2000's11 (30.56)29.6817
2010's5 (13.89)24.3611
2020's2 (5.56)2.80

Authors

AuthorsStudies
Borgström, B; Erlanson, C; Sternby, B1
Read, CP; Ruff, MD1
Brockerhoff, H1
Camus, J; Christophe, J; Deschodt-Lanckman, M; Kutzner, R; Robberecht, P1
Benzonana, G; Desnuelle, P; Sémériva, M1
Jennens, ML; Lowe, ME1
Cygler, M; de Montigny, C; Recktenwald, A; Schrag, JD; Tessier, DC; Thomas, DY; Vernet, T; Ziomek, E1
Li, Y; Man, WJ; O'Connor, CD; Wilton, DC1
Cleasby, A; Egmond, MR; Frenken, LG; Johnson, LN; Noble, ME1
DiPersio, LP; Hui, DY1
Brumlik, MJ; Buckley, JT1
Lowe, ME1
Laskowski, RA; Thornton, JM; Wallace, AC1
Aisaka, K; Hirano, A; Shinkai, A1
Chahrokh-Zadeh, S; Lohse, P; Seidel, D1
Cordle, RA; Lowe, ME1
Alves dos Santos, CM; Cox, RC; Egmond, MR; Simons, JW; Ubarretxena-Belandia, I; van Kampen, MD; Verheij, HM1
Amada, K; Haruki, M; Hyun-Ju, K; Kanaya, S; Kwon, HJ; Morikawa, M1
Caspar, DL; Guerrero, L; Logan, TM; Parthasarathy, G; Twigg, PD1
Masuda, T; Ohta, H; Shimada, H; Suzuki, T; Takamiya, K; Tsuchiya, T; Yamada, T1
TAKENAKA, T; TASAKI, I1
McAuley, KE; Patkar, SA; Svendsen, A; Wilson, KS1
Cohen, SM; Davis, TC; Golynskiy, MV; Helmann, JD1
Attias, C; Carrière, F; Chahinian, H; Fojan, P; Petersen, SB; Snabe, T1
Carrière, F; Ferrato, F; Freie, AB; Lowe, ME1
Gargouri, Y; Mosbah, H; Sayari, A1
Angelaccio, S; Chiaraluce, R; Consalvi, V; Florio, R; Gianese, G; van der Oost, J; van Lieshout, JF1
Boersma, YL; Cool, RH; Dijkstra, BW; Dröge, MJ; Pijning, T; Quax, WJ; van der Sloot, AM1
Bischoff, R; Cool, RH; Krzeslak, J; Paal, KA; Papaioannou, E; Quax, WJ; van Merkerk, R1
Gopalakrishna, KN; Kumar, PR; Prakash, V1
Gupta, R; Kumari, A1
Andreeva, TV; Ayvazyan, NM; Ghazaryan, NA; Ghulikyan, L; Kishmiryan, A; Lomonte, B; Tsetlin, VI; Utkin, YN1
Barbieri, F; Grandori, R; Martorana, AM; Polissi, A; Santambrogio, C; Sperandeo, P1
Li, Y; Lin, X; Wang, Y; Wu, Q; Xia, B; Zhang, Y1
Carballares, D; Fernandez-Lafuente, R; Gonçalves, LRB; Lopez-Carrobles, N; Lopez-Gallego, F; Rodrigues, S; Souza, PMP1
Capone, M; Daidone, I; Leonzi, I; Spreti, N; Zanetti-Polzi, L1

Other Studies

36 other study(ies) available for aspartic acid and 1-anilino-8-naphthalenesulfonate

ArticleYear
Further characterization of two co-lipases from porcine pancreas.
    Biochemical and biophysical research communications, 1974, Aug-05, Volume: 59, Issue:3

    Topics: Amino Acid Sequence; Amino Acids; Animals; Asparagine; Aspartic Acid; Electrophoresis, Disc; Glutamates; Glutamine; Hydrogen-Ion Concentration; Isoenzymes; Lipase; Molecular Weight; Pancreas; Swine

1974
Inhibition of pancreatic lipase by Hymenolepis diminuta.
    The Journal of parasitology, 1973, Volume: 59, Issue:1

    Topics: Animals; Arginine; Aspartic Acid; Cestoda; Culture Media; Heparin; Hydrogen-Ion Concentration; Lipase; Male; Methods; Pancreas; Peptides; Rats; RNA; Spectrometry, Fluorescence; Time Factors; Trichloroacetic Acid; Triolein

1973
A model of pancreatic lipase and the orientation of enzymes at interfaces.
    Chemistry and physics of lipids, 1973, Volume: 10, Issue:3

    Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry; Histidine; Leucine; Lipase; Models, Chemical; Pancreas; Protein Binding; Protein Conformation; Serine

1973
Amino acid levels in rat pancreas after pilocarpine or pancreozymin.
    The American journal of physiology, 1973, Volume: 224, Issue:6

    Topics: Alanine; Amino Acids; Amylases; Animals; Aspartic Acid; Cholecystokinin; Chymotrypsinogen; Female; Glutamates; Glutamine; Injections, Intraperitoneal; Injections, Intravenous; Intestine, Small; Lipase; Liver; Oxidative Phosphorylation; Pancreas; Pilocarpine; Rats; Secretory Rate

1973
Some properties of a lipase from Rhizopus arrhizus. Separation of a glycopeptide bound to the enzyme.
    Biochimica et biophysica acta, 1969, Volume: 191, Issue:3

    Topics: Amino Acids; Asparagine; Aspartic Acid; Chemical Phenomena; Chemical Precipitation; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Drug Stability; Glycoproteins; Hexosamines; Lipase; Mannose; Molecular Weight; Peptides; Proteins; Rhizopus; Spectrum Analysis; Temperature; Trichloroacetic Acid

1969
C-terminal domain of human pancreatic lipase is required for stability and maximal activity but not colipase reactivation.
    Journal of lipid research, 1995, Volume: 36, Issue:5

    Topics: Amino Acid Sequence; Aspartic Acid; Carboxylic Acids; Colipases; Enzyme Reactivators; Enzyme Stability; Gene Deletion; Humans; Lipase; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Pancreas; Protein Structure, Tertiary; Tyrosine

1995
Cloning and expression of Geotrichum candidum lipase II gene in yeast. Probing of the enzyme active site by site-directed mutagenesis.
    The Journal of biological chemistry, 1993, Dec-15, Volume: 268, Issue:35

    Topics: Aspartic Acid; Base Sequence; Binding Sites; Cloning, Molecular; DNA Mutational Analysis; DNA Primers; Geotrichum; Glutamates; Glutamic Acid; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Saccharomyces cerevisiae

1993
The effect of replacing the conserved active-site residues His-264, Asp-312 and Arg-314 on the binding and catalytic properties of Escherichia coli citrate synthase.
    The Biochemical journal, 1994, Jun-15, Volume: 300 ( Pt 3)

    Topics: Anilino Naphthalenesulfonates; Arginine; Aspartic Acid; Base Sequence; Binding Sites; Catalysis; Citrate (si)-Synthase; Dithionitrobenzoic Acid; Escherichia coli; Histidine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Protein Conformation; Structure-Activity Relationship

1994
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.
    FEBS letters, 1993, Sep-27, Volume: 331, Issue:1-2

    Topics: Amino Acid Sequence; Aspartic Acid; Catalysis; Crystallization; Lipase; Molecular Sequence Data; Protein Conformation; Pseudomonas

1993
Aspartic acid 320 is required for optimal activity of rat pancreatic cholesterol esterase.
    The Journal of biological chemistry, 1993, Jan-05, Volume: 268, Issue:1

    Topics: Acetylcholinesterase; Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Bile Acids and Salts; Cholinesterases; Cloning, Molecular; Geotrichum; Humans; Kinetics; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Pancreas; Rats; Restriction Mapping; RNA, Messenger; Sequence Homology, Amino Acid; Sterol Esterase; Transfection

1993
Identification of the catalytic triad of the lipase/acyltransferase from Aeromonas hydrophila.
    Journal of bacteriology, 1996, Volume: 178, Issue:7

    Topics: Acyltransferases; Aeromonas hydrophila; Amino Acid Sequence; Aspartic Acid; Base Sequence; Binding Sites; Catalysis; DNA, Bacterial; Histidine; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Serine; Structure-Activity Relationship

1996
Mutation of the catalytic site Asp177 to Glu177 in human pancreatic lipase produces an active lipase with increased sensitivity to proteases.
    Biochimica et biophysica acta, 1996, Jul-26, Volume: 1302, Issue:2

    Topics: Amino Acid Sequence; Animals; Aspartic Acid; Baculoviridae; Binding Sites; Cell Line; Endopeptidases; Gene Expression; Glutamic Acid; Humans; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Pancreas; Protein Denaturation; Spodoptera; Transfection; Urea

1996
Derivation of 3D coordinate templates for searching structural databases: application to Ser-His-Asp catalytic triads in the serine proteinases and lipases.
    Protein science : a publication of the Protein Society, 1996, Volume: 5, Issue:6

    Topics: Amino Acid Isomerases; Aspartic Acid; Bacterial Proteins; Binding Sites; Carrier Proteins; Databases, Factual; Histidine; Immunoglobulin G; Lipase; Peptide Fragments; Peptidylprolyl Isomerase; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Proteins; Sequence Analysis; Sequence Homology, Amino Acid; Serine; Serine Endopeptidases; Templates, Genetic

1996
Substitutions of Ser for Asn-163 and Pro for Leu-264 are important for stabilization of lipase from Pseudomonas aeruginosa.
    Journal of biochemistry, 1996, Volume: 120, Issue:5

    Topics: Aspartic Acid; Enzyme Stability; Hydrogen-Ion Concentration; Leucine; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Proline; Protein Conformation; Pseudomonas aeruginosa; Restriction Mapping; Serine

1996
Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: identification of the catalytically active serine, aspartic acid, and histidine residues.
    Journal of lipid research, 1997, Volume: 38, Issue:5

    Topics: Animals; Aspartic Acid; Binding Sites; DNA, Complementary; Histidine; Humans; Hydrolysis; Lipase; Mutagenesis, Site-Directed; Rats; Serine; Substrate Specificity

1997
The hydrophobic surface of colipase influences lipase activity at an oil-water interface.
    Journal of lipid research, 1998, Volume: 39, Issue:9

    Topics: Aspartic Acid; Cell Membrane; Chemical Phenomena; Chemistry, Physical; Colipases; Fat Emulsions, Intravenous; Humans; Lipase; Models, Molecular; Mutagenesis, Site-Directed; Oils; Structure-Activity Relationship; Surface Properties; Triglycerides; Triolein; Tyrosine; Water

1998
Identification of a calcium binding site in Staphylococcus hyicus lipase: generation of calcium-independent variants.
    Biochemistry, 1999, Jan-05, Volume: 38, Issue:1

    Topics: Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Binding Sites; Calcium; Calorimetry; Enzyme Activation; Lipase; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Alignment; Sequence Homology, Amino Acid; Staphylococcus

1999
Identification of the histidine and aspartic acid residues essential for enzymatic activity of a family I.3 lipase by site-directed mutagenesis.
    FEBS letters, 2000, Oct-20, Volume: 483, Issue:2-3

    Topics: Amino Acid Substitution; Aspartic Acid; Binding Sites; Catalytic Domain; Circular Dichroism; Esterases; Histidine; Lipase; Mutagenesis, Site-Directed; Mutation; Pseudomonas

2000
Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Sep-25, Volume: 98, Issue:20

    Topics: Amino Acid Substitution; Anilino Naphthalenesulfonates; Aspartic Acid; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; DNA-Binding Proteins; Escherichia coli; Models, Molecular; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Protein Conformation; Protein Folding; Recombinant Proteins; Thrombin

2001
Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad.
    Plant & cell physiology, 2003, Volume: 44, Issue:1

    Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Carboxylic Ester Hydrolases; Catalysis; Chenopodium album; Enzyme Inhibitors; Histidine; Hydrolysis; Isoflurophate; Lipase; Molecular Sequence Data; Morpholines; Mutagenesis, Site-Directed; Mutation; p-Chloromercuribenzoic Acid; Phenylmethylsulfonyl Fluoride; Sequence Homology, Amino Acid; Serine; Serine Endopeptidases

2003
EFFECTS OF VARIOUS POTASSIUM SALTS AND PROTEASES UPON EXCITABILITY OF INTRACELLULARLY PERFUSED SQUID GIANT AXONS.
    Proceedings of the National Academy of Sciences of the United States of America, 1964, Volume: 52

    Topics: Acetates; Animals; Aspartic Acid; Axons; Bromides; Chlorides; Citrates; Decapodiformes; Electrophysiology; Fluorides; Glutamates; Iodides; Lipase; Mollusca; Neurophysiology; Nitrates; Peptide Hydrolases; Pharmacology; Potassium; Research; Salts; Tartrates; Thiocyanates

1964
Structure of a feruloyl esterase from Aspergillus niger.
    Acta crystallographica. Section D, Biological crystallography, 2004, Volume: 60, Issue:Pt 5

    Topics: Amino Acid Sequence; Aspartic Acid; Aspergillus niger; Bacterial Proteins; Binding Sites; Carboxylic Ester Hydrolases; Catalytic Domain; Coumaric Acids; Crystallography, X-Ray; Fungal Proteins; Histidine; Lipase; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Serine; Structural Homology, Protein

2004
Metal-induced structural organization and stabilization of the metalloregulatory protein MntR.
    Biochemistry, 2005, Mar-08, Volume: 44, Issue:9

    Topics: Anilino Naphthalenesulfonates; Arginine; Aspartic Acid; Bacillus subtilis; Bacterial Proteins; Binding Sites; Circular Dichroism; DNA-Binding Proteins; Fluorescent Dyes; Glutamic Acid; Hot Temperature; Manganese; Metals, Heavy; Methionine; Protein Conformation; Protein Denaturation; Repressor Proteins

2005
How gastric lipase, an interfacial enzyme with a Ser-His-Asp catalytic triad, acts optimally at acidic pH.
    Biochemistry, 2006, Jan-24, Volume: 45, Issue:3

    Topics: Animals; Aspartic Acid; Dogs; Histidine; Hydrogen-Ion Concentration; Kinetics; Lipase; Plants, Genetically Modified; Recombinant Proteins; Serine; Stomach; Zea mays

2006
Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles.
    The Journal of biological chemistry, 2006, Mar-24, Volume: 281, Issue:12

    Topics: Adsorption; Aspartic Acid; Bile Acids and Salts; Caprylates; Colipases; Diglycerides; DNA, Complementary; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Humans; Isoleucine; Kinetics; Leucine; Lipase; Lysine; Micelles; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Pancreas; Phosphatidylcholines; Phospholipids; Pressure; Protein Binding; Protein Conformation; Protein Interaction Mapping; Protein Structure, Secondary; Proteins; Time Factors; Triglycerides; Triolein; Valine

2006
Importance of the residue Asp 290 on chain length selectivity and catalytic efficiency of recombinant Staphylococcus simulans lipase expressed in E. coli.
    Molecular biotechnology, 2007, Volume: 36, Issue:1

    Topics: Aspartic Acid; Calcium; Catalysis; Cloning, Molecular; Detergents; Emulsions; Enzyme Stability; Escherichia coli; Gene Expression; Genes, Bacterial; Hydrogen-Ion Concentration; Kinetics; Lipase; Mutant Proteins; Mutation; Plasmids; Recombinant Proteins; Staphylococcus; Structure-Activity Relationship; Substrate Specificity; Temperature; Triglycerides; Triolein

2007
Tertiary structure in 7.9 M guanidinium chloride--the role of Glu53 and Asp287 in Pyrococcus furiosus endo-beta-1,3-glucanase.
    The FEBS journal, 2007, Volume: 274, Issue:23

    Topics: Anilino Naphthalenesulfonates; Aspartic Acid; Binding Sites; Calcium; Chelating Agents; Dose-Response Relationship, Drug; Egtazic Acid; Enzyme Stability; Escherichia coli; Fluorescent Dyes; Glucan Endo-1,3-beta-D-Glucosidase; Glutamic Acid; Guanidine; Kinetics; Models, Biological; Models, Molecular; Mutation; Protein Binding; Protein Denaturation; Protein Renaturation; Protein Structure, Tertiary; Pyrococcus furiosus; Thermodynamics; Titrimetry

2007
A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A.
    Chembiochem : a European journal of chemical biology, 2008, May-05, Volume: 9, Issue:7

    Topics: Alkenes; Aspartic Acid; Bacillus subtilis; Directed Molecular Evolution; Escherichia coli; Gene Expression Regulation, Bacterial; Gene Library; Glycerol; Hydrolysis; Lipase; Mutation; Periplasm; Stereoisomerism; Substrate Specificity

2008
Lipase A gene transcription in Pseudomonas alcaligenes is under control of RNA polymerase σ54 and response regulator LipR.
    FEMS microbiology letters, 2012, Volume: 329, Issue:2

    Topics: Adenosine Triphosphatases; Aspartic Acid; Bacterial Proteins; DNA-Binding Proteins; Fungal Proteins; Gene Expression Regulation, Bacterial; Lipase; Mutation; Phosphorylation; Pseudomonas alcaligenes; RNA Polymerase Sigma 54; Transcription Factors; Transcription, Genetic

2012
Chemical modification of catalytic site of lipase from wheat germ: altered structure-activity profile.
    Indian journal of biochemistry & biophysics, 2002, Volume: 39, Issue:1

    Topics: Aspartic Acid; Calorimetry, Differential Scanning; Catalytic Domain; Circular Dichroism; Dose-Response Relationship, Drug; Histidine; Hot Temperature; Kinetics; Lipase; Protein Conformation; Protein Structure, Secondary; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Temperature; Triticum

2002
Functional characterization of a novel aspartic acid rich lipase, TALipC, from Trichosporon asahii MSR54: solvent-dependent enantio inversion during esterification of 1-phenylethanol.
    Biotechnology letters, 2015, Volume: 37, Issue:1

    Topics: Amino Acid Sequence; Aspartic Acid; Benzyl Alcohols; Enzyme Stability; Esterification; Fungal Proteins; Lipase; Molecular Sequence Data; Sequence Alignment; Stereoisomerism; Trichosporon

2015
Phospholipases a2 from Viperidae snakes: Differences in membranotropic activity between enzymatically active toxin and its inactive isoforms.
    Biochimica et biophysica acta, 2015, Volume: 1848, Issue:2

    Topics: 2-Naphthylamine; Amino Acid Substitution; Anilino Naphthalenesulfonates; Animals; Aspartic Acid; Biological Transport; Brain Chemistry; Catalytic Domain; Fluorescent Dyes; Laurates; Lipid Bilayers; Lysine; Male; Membrane Fluidity; Phospholipases A2; Rats; Reptilian Proteins; Serine; Snake Venoms; Structure-Activity Relationship; Unilamellar Liposomes; Viperidae; Water

2015
An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands.
    Biochimica et biophysica acta, 2015, Volume: 1854, Issue:10 Pt A

    Topics: Amino Acid Substitution; Anilino Naphthalenesulfonates; Aspartic Acid; Biological Transport; Carbohydrate Sequence; Carrier Proteins; Escherichia coli K12; Escherichia coli Proteins; Gene Expression; Isoleucine; Ligands; Lipopolysaccharides; Molecular Sequence Data; Mutation; Protein Binding; Protein Folding; Recombinant Fusion Proteins; Spectrometry, Fluorescence

2015
Solvent-Free Lipase-Catalyzed Synthesis: Unique Properties of Enantiopure D- and L- Polyaspartates and Their Complexation.
    Biomacromolecules, 2016, Jan-11, Volume: 17, Issue:1

    Topics: Aspartic Acid; Catalysis; Circular Dichroism; Lipase; Nylons; Peptide Hydrolases; Peptides; Polymerization; Polymers; Solvents; X-Ray Diffraction

2016
Enzyme-support interactions and inactivation conditions determine Thermomyces lanuginosus lipase inactivation pathways: Functional and florescence studies.
    International journal of biological macromolecules, 2021, Nov-30, Volume: 191

    Topics: Aspartic Acid; Enzymes, Immobilized; Ethylenediamines; Eurotiales; Fungal Proteins; Glycine; Lipase; Microspheres; Sepharose; Substrate Specificity; Sulfones; Triacetin

2021
Evidence for a high pK
    Journal of biomolecular structure & dynamics, 2023, Volume: 41, Issue:11

    Topics: Aspartic Acid; Catalytic Domain; Fungal Proteins; Lipase

2023