cysteine and farnesyl pyrophosphate

cysteine has been researched along with farnesyl pyrophosphate in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (62.50)18.2507
2000's3 (37.50)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Erdman, RA; Kinsella, BT; Maltese, WA1
Cox, AD1
Casey, PJ; Furfine, ES; Landavazo, A; Leban, JJ; Moomaw, JF1
Cane, DE; Fitzsimons, BC; Hohn, TM; Shim, JH; Xue, Q1
Phillips, ST; Poulter, CD; Rozema, DB1
Ayral-Kaloustian, S; Salaski, EJ1
Andres, DA; Liu, S; Spielmann, HP; Subramanian, T; Troutman, JM1
Cao, L; Grant, DF; Zhang, P1

Reviews

1 review(s) available for cysteine and farnesyl pyrophosphate

ArticleYear
Protein farnesyltransferase inhibitors.
    Current medicinal chemistry, 2002, Volume: 9, Issue:10

    Topics: Alkyl and Aryl Transferases; Angiogenesis Inducing Agents; Animals; Antineoplastic Agents; Apoptosis; Cell Membrane; Clinical Trials as Topic; Cysteine; Enzyme Inhibitors; Farnesyltranstransferase; Humans; Neoplasms; Polyisoprenyl Phosphates; Protein Prenylation; Protein Processing, Post-Translational; ras Proteins; Sesquiterpenes

2002

Other Studies

7 other study(ies) available for cysteine and farnesyl pyrophosphate

ArticleYear
Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid.
    Proceedings of the National Academy of Sciences of the United States of America, 1991, Oct-15, Volume: 88, Issue:20

    Topics: Amino Acid Sequence; Animals; Base Sequence; Cell Line; Cysteine; GTP-Binding Proteins; Mevalonic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotides; Polyisoprenyl Phosphates; Protein Biosynthesis; Protein Processing, Post-Translational; Proto-Oncogene Proteins p21(ras); Sesquiterpenes; Transfection

1991
Mutation and analysis of prenylation signal sequences.
    Methods in enzymology, 1995, Volume: 250

    Topics: Animals; Cells, Cultured; Cloning, Molecular; Cysteine; DNA Mutational Analysis; Indicators and Reagents; Mammals; Methionine; Mevalonic Acid; Polyisoprenyl Phosphates; Polymerase Chain Reaction; Protein Biosynthesis; Protein Prenylation; Protein Sorting Signals; Rabbits; Radioisotope Dilution Technique; Recombinant Proteins; Reticulocytes; Sesquiterpenes; Sulfur Radioisotopes; Tritium

1995
Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release.
    Biochemistry, 1995, May-23, Volume: 34, Issue:20

    Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Binding Sites; Biotin; Catalysis; Cysteine; Kinetics; Molecular Sequence Data; Peptides; Polyisoprenyl Phosphates; Protein Prenylation; Sesquiterpenes; Spectrometry, Fluorescence; Transferases

1995
Trichodiene synthase. Identification of active site residues by site-directed mutagenesis.
    Biochemistry, 1995, Feb-28, Volume: 34, Issue:8

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Carbon-Carbon Lyases; Catalysis; Cloning, Molecular; Cysteine; DNA Primers; DNA, Fungal; Escherichia coli; Fusarium; Kinetics; Lyases; Methyl Methanesulfonate; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Polyisoprenyl Phosphates; Sesquiterpenes; Substrate Specificity

1995
Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues.
    Organic letters, 1999, Sep-09, Volume: 1, Issue:5

    Topics: Alkyl and Aryl Transferases; Alkylation; Cysteine; Peptides; Polyisoprenyl Phosphates; Protein Binding; Saccharomyces cerevisiae; Sesquiterpenes; Spectrometry, Mass, Electrospray Ionization; Thermodynamics

1999
Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity.
    Chembiochem : a European journal of chemical biology, 2008, Nov-24, Volume: 9, Issue:17

    Topics: Alkyl and Aryl Transferases; Catalysis; Crystallography, X-Ray; Cysteine; Hydrophobic and Hydrophilic Interactions; Lipids; Oligopeptides; Oncogene Protein p21(ras); Polyisoprenyl Phosphates; Protein Prenylation; Sesquiterpenes; Substrate Specificity; Terpenes

2008
An insect farnesyl phosphatase homologous to the N-terminal domain of soluble epoxide hydrolase.
    Biochemical and biophysical research communications, 2009, Feb-27, Volume: 380, Issue:1

    Topics: Amino Acid Sequence; Animals; Catalysis; Cysteine; Diterpenes; Drosophila melanogaster; Enzyme Inhibitors; Epoxide Hydrolases; Molecular Sequence Data; Polyisoprenyl Phosphates; Pyrophosphatases; Sequence Homology, Amino Acid; Sesquiterpenes

2009