guanidine has been researched along with pyridoxal phosphate in 14 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 7 (50.00) | 18.2507 |
| 2000's | 6 (42.86) | 29.6817 |
| 2010's | 1 (7.14) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hage, A; Herold, M; Kirschner, K; Leistler, B; Luger, K | 1 |
| Cook, PF; Schnackerz, KD | 1 |
| Kawata, Y; Mizobata, T | 1 |
| Iriarte, A; Martinez-Carrion, M; Reyes, AM | 1 |
| Manning, JM; Peisach, D; Petsko, G; Pospischil, MA; Ringe, D; Soda, K; Van Ophem, PW | 1 |
| Xiao, GS; Zhou, JM | 1 |
| Rao, KN | 1 |
| Benci, S; Beretta, S; Bettati, S; Campanini, B; Chirico, G; Gratton, E; Hazlett, TL; Mozzarelli, A; Raboni, S; Schnackerz, KD | 1 |
| Bhakuni, V; Bhatt, AN; Prakash, K; Subramanya, HS | 1 |
| Artigues, A; Bengoechea-Alonso, MT; Iriarte, A; Martinez-Carrión, M; Osés-Prieto, JA | 1 |
| Coulter-Mackie, MB; Lian, Q; Wong, SG | 1 |
| Deu, E; Kirsch, JF | 1 |
| Das, AK; Mukherjee, S; Saha, B | 1 |
| Ali, V; Bhakuni, V; Mishra, V; Nozaki, T | 1 |
14 other study(ies) available for guanidine and pyridoxal phosphate
| Article | Year |
|---|---|
Autonomous folding and coenzyme binding of the excised pyridoxal 5'-phosphate binding domain of aspartate aminotransferase from Escherichia coli.
Topics: Apoenzymes; Aspartate Aminotransferases; Base Sequence; Chromatography, Gel; Chromatography, High Pressure Liquid; Cloning, Molecular; Coenzymes; Dialysis; Escherichia coli; Guanidine; Guanidines; Imines; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Conformation; Pyridoxal Phosphate; X-Ray Diffraction | 1991 |
Resolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site.
Topics: Apoenzymes; Binding Sites; Coenzymes; Cysteine Synthase; Dialysis; Guanidine; Guanidines; Magnetic Resonance Spectroscopy; Molecular Probes; Pyridoxal; Pyridoxal Phosphate; Salmonella typhimurium; Schiff Bases; Spectrophotometry | 1995 |
The folding characteristics of tryptophanase from Escherichia coli.
Topics: Apoenzymes; Escherichia coli; Guanidine; Guanidines; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Light; Protein Denaturation; Protein Folding; Pyridoxal Phosphate; Scattering, Radiation; Spectrometry, Fluorescence; Time Factors; Tryptophanase | 1995 |
Refolding of the precursor and mature forms of mitochondrial aspartate aminotransferase after guanidine hydrochloride denaturation.
Topics: Apoenzymes; Aspartate Aminotransferases; Enzyme Precursors; Guanidine; Guanidines; Isoenzymes; Kinetics; Macromolecular Substances; Mathematics; Mitochondria; Protein Conformation; Protein Denaturation; Protein Folding; Pyridoxal Phosphate; Spectrometry, Fluorescence | 1993 |
Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding.
Topics: Alanine; Base Sequence; beta-Alanine; Binding Sites; Catalysis; D-Alanine Transaminase; Enzyme Inhibitors; Enzyme Stability; Guanidine; Guanidines; Hot Temperature; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Pyridoxal Phosphate; Recombinant Proteins; Spectrophotometry; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Compounds; Transaminases; Urea | 1995 |
Conformational changes at the active site of bovine pancreatic RNase A at low concentrations of guanidine hydrochloride probed by pyridoxal 5'-phosphate.
Topics: Animals; Binding Sites; Cattle; Fluorescence Polarization; Guanidine; Guanidines; Kinetics; Molecular Probes; Protein Conformation; Protein Denaturation; Pyridoxal Phosphate; Ribonuclease, Pancreatic; Spectrometry, Fluorescence; Tyrosine | 1996 |
Reversible inhibition by pyridoxal 5'-phosphate and irreversible inactivation by urea and guanidine hydrochloride of thymidylate synthase from Lactobacillus leichmannii.
Topics: Dimerization; Enzyme Inhibitors; Guanidine; Lactobacillus; Protein Conformation; Pyridoxal Phosphate; Thymidylate Synthase; Urea | 1998 |
Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase.
Topics: Cysteine Synthase; Guanidine; Light; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Denaturation; Pyridoxal Phosphate; Scattering, Radiation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2000 |
Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase.
Topics: Amino Acid Sequence; Aspartate Aminotransferases; Bacillus subtilis; Chromatography; Circular Dichroism; Enzyme Stability; Fluorescent Dyes; Glutaral; Glycine Hydroxymethyltransferase; Guanidine; Hot Temperature; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Protein Structure, Tertiary; Pyridoxal Phosphate; Sequence Alignment; Sequence Homology; Urea | 2002 |
The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase.
Topics: Animals; Aspartate Aminotransferases; Cyclophilins; Escherichia coli; Guanidine; Hydrogen-Ion Concentration; Kinetics; Liver; Mass Spectrometry; Microscopy, Fluorescence; Models, Chemical; Peptides; Proline; Protein Binding; Protein Folding; Pyridoxal Phosphate; Rats; Spectrometry, Fluorescence; Temperature; Time Factors; Ultraviolet Rays | 2003 |
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor.
Topics: Base Sequence; DNA, Complementary; Escherichia coli; Gene Expression; Guanidine; Humans; Hyperoxaluria, Primary; Kinetics; Mutagenesis, Site-Directed; Protein Folding; Protein Renaturation; Pyridoxal Phosphate; Recombinant Proteins; Transaminases | 2005 |
Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme.
Topics: Aspartate Aminotransferases; Circular Dichroism; Enzyme Stability; Escherichia coli; Guanidine; Holoenzymes; Protein Denaturation; Protein Folding; Protein Renaturation; Protein Structure, Quaternary; Pyridoxal Phosphate; Pyridoxamine; Spectrometry, Fluorescence; Thermodynamics; Urea | 2007 |
Molecular characterization of Mycobacterium tuberculosis cystathionine gamma synthase--apo- and holoforms.
Topics: Amino Acid Sequence; Apoenzymes; Carbon-Oxygen Lyases; Catalytic Domain; Circular Dichroism; Computational Biology; Guanidine; Holoenzymes; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mycobacterium tuberculosis; Protein Denaturation; Protein Renaturation; Pyridoxal Phosphate; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2009 |
Biophysical characterization of Entamoeba histolytica phosphoserine aminotransferase (EhPSAT): role of cofactor and domains in stability and subunit assembly.
Topics: Amino Acid Sequence; Apoenzymes; Biophysical Phenomena; Coenzymes; Entamoeba histolytica; Enzyme Stability; Guanidine; Holoenzymes; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Pyridoxal Phosphate; Transaminases; Urea | 2011 |