phenylalanine and dinitrochlorobenzene

phenylalanine has been researched along with dinitrochlorobenzene in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19901 (14.29)18.7374
1990's3 (42.86)18.2507
2000's3 (42.86)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Judd, KP; Reif, AE; Southwick, PL1
Morgenstern, R; Swedmark, S; Weinander, R1
Allardyce, CS; Lian, LY; McDonagh, PD; Roberts, GC; Wolf, CR1
Listowsky, I; Patskovska, LN; Patskovsky, YV1
Armstrong, RN; Codreanu, SG; Gilliland, GL; Hachey, DL; Ladner, JE; Stourman, NV; Xiao, G1
Carletti, E; De Luca, A; Di Ilio, C; Favaloro, B; Sacchetta, P1
Dai, A; Gim, JS; Hardy, SI; Johansson, AS; Kau, IH; Lin, HJ; Mannervik, B; Materi, AM; Park, JM; Parker, MW; Stenberg, G; Zhou, H1

Other Studies

7 other study(ies) available for phenylalanine and dinitrochlorobenzene

ArticleYear
Skin sensitization with the new reagents NOPYE (4-nitro-1-cyclohexyl-3-ethoxy-2-oxo-3-pyrroline) and NOPY-L-phenylalanine.
    Journal of surgical oncology, 1980, Volume: 13, Issue:2

    Topics: Adjuvants, Immunologic; Animals; Cross Reactions; Cyclohexanes; Dinitrochlorobenzene; Female; Guinea Pigs; Hypersensitivity, Delayed; Immunotherapy; Neoplasms; Ovalbumin; Phenylalanine; Pyrroles; Skin; Tuberculin

1980
The mRNA for GST Pi from FRHK rhesus monkey kidney cells codes for an enzyme with activity towards 1-chloro-2,4-dinitrobenzene in spite of an I68F mutation.
    Gene, 1998, Jan-05, Volume: 206, Issue:1

    Topics: Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; Cell Line; Dinitrochlorobenzene; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Glutathione S-Transferase pi; Glutathione Transferase; Humans; Isoenzymes; Isoleucine; Kidney; Macaca mulatta; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Recombinant Fusion Proteins; RNA, Messenger; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate; Substrate Specificity

1998
The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases.
    The Biochemical journal, 1999, Nov-01, Volume: 343 Pt 3

    Topics: Amino Acid Substitution; Binding Sites; Catalysis; Dinitrochlorobenzene; Ethacrynic Acid; Glutathione Transferase; Isoenzymes; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Phenylalanine; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity; Tyrosine

1999
An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases.
    Biochemistry, 1999, Dec-07, Volume: 38, Issue:49

    Topics: Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Catalysis; Crystallography, X-Ray; Dinitrochlorobenzene; Glutathione Transferase; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Recombinant Fusion Proteins

1999
Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase.
    Biochemistry, 2002, Dec-24, Volume: 41, Issue:51

    Topics: Amides; Amino Acid Substitution; Animals; Catalysis; Circular Dichroism; Crystallization; Crystallography, X-Ray; Deuterium Oxide; Dinitrochlorobenzene; Glutathione Transferase; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Protein Conformation; Protons; Rats; Spectrometry, Fluorescence; Structure-Activity Relationship; Substrate Specificity; Thermodynamics; Tyrosine

2002
A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site.
    The Biochemical journal, 2003, Jul-15, Volume: 373, Issue:Pt 2

    Topics: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Dinitrochlorobenzene; Escherichia coli; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Glutathione S-Transferase pi; Glutathione Transferase; Glycine; Humans; Isoenzymes; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Reverse Transcriptase Polymerase Chain Reaction; Substrate Specificity; Tyrosine; Xenopus laevis; Xenopus Proteins

2003
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione transferase P1-1.
    Biochimica et biophysica acta, 2003, Jun-26, Volume: 1649, Issue:1

    Topics: Amino Acid Motifs; Amino Acid Substitution; Black People; Dinitrochlorobenzene; Enzyme Stability; Genetic Variation; Glutathione S-Transferase pi; Glutathione Transferase; Half-Life; Humans; Hydrophobic and Hydrophilic Interactions; Isoenzymes; Kinetics; Leucine; Models, Molecular; Phenylalanine; Polymorphism, Genetic; Protein Folding

2003