phenylalanine and hymecromone

phenylalanine has been researched along with hymecromone in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (50.00)18.2507
2000's2 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Kokriakov, VN; Kraeva, LN; Morozov, VI; Pozdnev, VF; Usova, AA1
Barr, BK; Claeyssens, M; Piens, K; Wilson, DB; Wolfgang, DE1
Alam, M; Gilham, D; Lehner, R; Vance, DE1
Battaglia, E; Bernardi, D; Bratton, S; Drake, RR; Finel, M; Radominska-Pandya, A; Ward, MD; Xiong, Y1

Other Studies

4 other study(ies) available for phenylalanine and hymecromone

ArticleYear
[Determination of esterase activity of human and animal serine proteinases using fluorogenic esters of amino acids as substrates].
    Biulleten' eksperimental'noi biologii i meditsiny, 1992, Volume: 113, Issue:6

    Topics: Animals; Cathepsin G; Cathepsins; Esterases; Humans; Hydrolysis; Hymecromone; Neutrophils; Phenylalanine; Rats; Serine Endopeptidases; Spectrometry, Fluorescence; Swine

1992
Active-site binding of glycosides by Thermomonospora fusca endocellulase E2.
    Biochemistry, 1998, Jun-30, Volume: 37, Issue:26

    Topics: Actinomycetales; Bacterial Proteins; Binding Sites; Calorimetry; Cellobiose; Cellulase; Glucose; Glucosides; Glycosides; Hydrogen-Ion Concentration; Hymecromone; Kinetics; Ligands; Mutagenesis, Site-Directed; Phenylalanine; Serine; Spectrometry, Fluorescence; Thermodynamics; Titrimetry; Tyrosine

1998
Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.
    Journal of lipid research, 2006, Volume: 47, Issue:2

    Topics: Acylation; Amino Acid Sequence; Animals; Binding Sites; Butyrates; Catalysis; Cell Line; Chlorocebus aethiops; COS Cells; Cysteine; Gene Deletion; Gene Expression; Humans; Hymecromone; Iodoacetamide; Lipase; Mercaptoethanol; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Sequence Homology, Amino Acid; Spodoptera; Substrate Specificity; Transfection

2006
Phenylalanine 90 and 93 are localized within the phenol binding site of human UDP-glucuronosyltransferase 1A10 as determined by photoaffinity labeling, mass spectrometry, and site-directed mutagenesis.
    Biochemistry, 2006, Feb-21, Volume: 45, Issue:7

    Topics: Amino Acid Sequence; Azides; Binding Sites; Chromatography, Liquid; Glucuronosyltransferase; Humans; Hymecromone; Kinetics; Mass Spectrometry; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrophenols; Phenol; Phenylalanine; Photoaffinity Labels; Recombinant Proteins; Salicylates; Sequence Alignment; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2006