guanidine and adenosine 5'-o-(3-thiotriphosphate)

guanidine has been researched along with adenosine 5'-o-(3-thiotriphosphate) in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (40.00)18.2507
2000's3 (60.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cashikar, AG; Rao, NM1
Bera, AK; Bernhardt, R1
Hoskins, JR; Kim, SY; Wickner, S1
Bisaillon, M; Bougie, I1
Ferry, JG; Gorrell, A; Lawrence, SH1

Other Studies

5 other study(ies) available for guanidine and adenosine 5'-o-(3-thiotriphosphate)

ArticleYear
Unfolding pathway in red kidney bean acid phosphatase is dependent on ligand binding.
    The Journal of biological chemistry, 1996, Mar-01, Volume: 271, Issue:9

    Topics: Acid Phosphatase; Adenosine Triphosphate; Circular Dichroism; Fabaceae; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Ligands; Mercaptoethanol; Phosphates; Plants, Medicinal; Potassium Iodide; Protein Conformation; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Tryptophan

1996
GroEL-assisted and -unassisted refolding of mature and precursor adrenodoxin: the role of the precursor sequence.
    Archives of biochemistry and biophysics, 1999, Jul-01, Volume: 367, Issue:1

    Topics: Adenosine Triphosphate; Adrenodoxin; Animals; Cattle; Chaperonin 10; Chaperonin 60; Dithiothreitol; Electron Transport; Escherichia coli; Guanidine; Holoenzymes; Inclusion Bodies; Kinetics; Protein Binding; Protein Denaturation; Protein Folding; Protein Precursors; Recombinant Proteins; Solubility; Thermodynamics

1999
Substrate recognition by the ClpA chaperone component of ClpAP protease.
    The Journal of biological chemistry, 2000, Nov-10, Volume: 275, Issue:45

    Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acids; DNA; DNA Helicases; DNA-Binding Proteins; Dose-Response Relationship, Drug; Endopeptidase Clp; Enzyme Activation; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Green Fluorescent Proteins; Guanidine; Kinetics; Luminescent Proteins; Molecular Chaperones; Peptides; Plasmids; Protein Binding; Protein Conformation; Protein Folding; Proteins; Recombinant Fusion Proteins; Serine Endopeptidases; Substrate Specificity; Time Factors; Trans-Activators

2000
Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase.
    The Journal of biological chemistry, 2003, Sep-05, Volume: 278, Issue:36

    Topics: Acid Anhydride Hydrolases; Adenosine Triphosphate; Binding Sites; Catalysis; Catalytic Domain; Circular Dichroism; Cobalt; Dose-Response Relationship, Drug; Guanidine; Hydrogen-Ion Concentration; Ions; Kinetics; Ligands; Magnesium; Manganese; Phosphoric Monoester Hydrolases; Plasmids; Protein Binding; Protein Denaturation; Protein Folding; RNA; RNA, Messenger; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Ultraviolet Rays

2003
Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.
    The Journal of biological chemistry, 2005, Mar-18, Volume: 280, Issue:11

    Topics: Acetate Kinase; Acetates; Adenosine Diphosphate; Adenosine Triphosphate; Arginine; Binding Sites; Catalysis; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electrons; Guanidine; Hydrogen-Ion Concentration; Hydroxylamine; Kinetics; Methanosarcina; Models, Chemical; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Stereoisomerism; Threonine

2005