guanidine has been researched along with dithionitrobenzoic acid in 23 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (13.04) | 18.7374 |
| 1990's | 10 (43.48) | 18.2507 |
| 2000's | 9 (39.13) | 29.6817 |
| 2010's | 1 (4.35) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fang, D; Gu, W; Hachiya, K; Hamada, S; Sasa, K; Shigemura, A; Takeda, K | 1 |
| Beharry, S; Bragg, PD | 1 |
| Beckman, SB; Duffy, TH; Huennekens, FM; Peterson, SM; Vitols, KS | 1 |
| Anderson, PM; Little, RM | 1 |
| Hellekant, G; Markley, JL; Ming, D | 1 |
| Aisaka, K; Brandts, JF; Chen, HH; Lin, LN; Mas, MT | 1 |
| Frieden, C; Jiang, N | 1 |
| Li, H; Peterson, CB; Seiffert, D; Wagner, NV; Williams, JG; Zhuang, P | 1 |
| Mullaney, EJ; Ullah, AH | 1 |
| Bedouelle, H; Blondel, A; Nageotte, R | 1 |
| Churchich, JE; Li, W | 1 |
| Abian, J; Caminade, E; Canosa, D; Carrascal, M; Daniel, R; Le Goffic, F; Martel, A | 1 |
| Ginsburg, A; Ruvinov, SB; Sackett, DL; Thompson, J | 1 |
| Kunugi, S; Mitani, D; Tanaka, N | 1 |
| Alam, SL; Butler, MC; Feng, Z; Loh, SN | 1 |
| Sridevi, K; Udgaonkar, JB | 1 |
| Ametani, A; Hattori, M; Hiramatsu, K; Kaminogawa, S; Kurata, T; Nishiura, M; Takahashi, K | 1 |
| Basu, G; Chakrabarti, P; Saha, RP | 1 |
| Kim, HH; Lee, YM; Song, NW; Suh, JK | 1 |
| Dudzik, P; Kuciel, R; Mazurkiewicz, A | 1 |
| Meng, FG; Mu, H; Park, YD; Yang, JM; Zhou, SM | 1 |
| Chen, HM; Chow, CY; Fang, HJ; Hu, CK; Tsong, TY; Wu, MC | 1 |
| Basak, S; Bera, K; Nag, M | 1 |
23 other study(ies) available for guanidine and dithionitrobenzoic acid
| Article | Year |
|---|---|
Dependence of reaction rate of 5,5'-dithiobis-(2-nitrobenzoic acid) to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations.
Topics: Dithionitrobenzoic Acid; Guanidine; Guanidines; Kinetics; Mathematics; Ovalbumin; Protein Conformation; Serum Albumin, Bovine; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds; Urea | 1992 |
Conformational change in beef-heart mitochondrial F1 ATPase to ATP synthesis mode induced by dimethylsulfoxide and ATP revealed by sulfhydryl group labeling.
Topics: Adenosine Triphosphate; Animals; Cattle; Cysteine; Dimethyl Sulfoxide; Dithionitrobenzoic Acid; Guanidine; Guanidines; Mitochondria, Heart; Protein Conformation; Proton-Translocating ATPases | 1989 |
L1210 dihydrofolate reductase. Kinetics and mechanism of activation by various agents.
Topics: Animals; Cell Line; Chloromercuribenzoates; Dithionitrobenzoic Acid; Enzyme Activation; Guanidine; Guanidines; Kinetics; Leukemia L1210; Mice; p-Chloromercuribenzoic Acid; Peptide Hydrolases; Potassium Chloride; Protein Conformation; Sodium Chloride; Spectrometry, Fluorescence; Tetrahydrofolate Dehydrogenase; Urea | 1987 |
Structural properties of cyanase. Denaturation, renaturation, and role of sulfhydryls and oligomeric structure in catalytic activity.
Topics: Aminohydrolases; Bicarbonates; Carbon-Nitrogen Lyases; Circular Dichroism; Dithionitrobenzoic Acid; Escherichia coli; Guanidine; Guanidines; Polymers; Protein Conformation; Protein Denaturation; Sulfhydryl Compounds | 1987 |
Quantification of cysteinyl sulfhydryl residues in peptides and proteins by ESI-MS or MALDI-MS.
Topics: Cysteine; Dithionitrobenzoic Acid; Dithiothreitol; Guanidine; Guanidines; Indicators and Reagents; Mass Spectrometry; Peptides; Plant Proteins; Plants; Pyridines; Sulfhydryl Compounds | 1995 |
Effects of C-terminal deletions on the conformational state and denaturation of phosphoglycerate kinase.
Topics: Calorimetry, Differential Scanning; Circular Dichroism; Dithionitrobenzoic Acid; Enzyme Activation; Guanidine; Guanidines; Hot Temperature; Models, Molecular; Mutagenesis; Phosphoglycerate Kinase; Protein Denaturation; Protein Structure, Tertiary; Sequence Deletion; Spectrometry, Fluorescence; Sulfates | 1995 |
Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues.
Topics: Animals; Carrier Proteins; Cysteine; Disulfides; Dithionitrobenzoic Acid; Drug Stability; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Neoplasm Proteins; Nerve Tissue Proteins; Protein Denaturation; Protein Structure, Secondary; Pyridines; Rats; Spectrometry, Fluorescence; Sulfhydryl Compounds | 1993 |
Characterization of the denaturation and renaturation of human plasma vitronectin. II. Investigation into the mechanism of formation of multimers.
Topics: Amino Acid Sequence; Chromatography, Gel; Disulfides; Dithionitrobenzoic Acid; Glutathione; Glutathione Disulfide; Guanidine; Guanidines; Hot Temperature; Humans; Macromolecular Substances; Models, Theoretical; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Protein Denaturation; Protein Folding; Vitronectin | 1996 |
Disulfide bonds are necessary for structure and activity in Aspergillus ficuum phytase.
Topics: 6-Phytase; Amino Acid Sequence; Aspergillus; Disulfides; Dithionitrobenzoic Acid; Guanidine; Guanidines; Kinetics; Mercaptoethanol; Molecular Sequence Data; Oxidation-Reduction; Protein Denaturation; Protein Folding; Sequence Homology, Amino Acid; Sulfhydryl Compounds | 1996 |
Destabilizing interactions between the partners of a bifunctional fusion protein.
Topics: ATP-Binding Cassette Transporters; Bacteriophage M13; Carrier Proteins; Chromatography, Gel; Cloning, Molecular; Cysteine; Dithionitrobenzoic Acid; DNA-Binding Proteins; Escherichia coli; Escherichia coli Proteins; Guanidine; Guanidines; Kinetics; Maltose-Binding Proteins; Models, Molecular; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Periplasmic Binding Proteins; Protein Denaturation; Recombinant Fusion Proteins; Ultracentrifugation | 1996 |
Activation of partially folded mitochondrial malate dehydrogenase by thioredoxin.
Topics: Anilino Naphthalenesulfonates; Animals; Chromatography, Gel; Circular Dichroism; Dithionitrobenzoic Acid; Dithiothreitol; Enzyme Activation; Escherichia coli; Fluorescent Dyes; Guanidine; Guanidines; Malate Dehydrogenase; Mitochondria, Heart; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Swine; Thioredoxins | 1997 |
Mass spectrometric determination of the cleavage sites in Escherichia coli dihydroorotase induced by a cysteine-specific reagent.
Topics: Binding Sites; Cysteine; Dihydroorotase; Dithionitrobenzoic Acid; Escherichia coli; Guanidine; Kinetics; Macromolecular Substances; Peptide Fragments; Spectrometry, Mass, Secondary Ion; Sulfhydryl Reagents; Thiocyanates | 1997 |
Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine. HCl-induced unfolding and a low temperature requirement for refolding.
Topics: Amino Acid Oxidoreductases; Chromatography, Gel; Cloning, Molecular; Dithionitrobenzoic Acid; Escherichia coli; Guanidine; Hydrogen-Ion Concentration; Kinetics; Lactococcus lactis; Macromolecular Substances; Protein Denaturation; Protein Folding; Protein Renaturation; Recombinant Proteins | 1999 |
Pressure-induced perturbation on the active site of beta-amylase monitored from the sulfhydryl reaction.
Topics: beta-Amylase; Binding Sites; Circular Dichroism; Cysteine; Dithionitrobenzoic Acid; Enzyme Stability; Guanidine; Pressure; Protein Conformation; Protein Folding; Solanaceae; Spectrometry, Fluorescence; Sulfhydryl Reagents; Thermodynamics; Thiocyanates | 2001 |
On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin.
Topics: Amides; Animals; Circular Dichroism; Cysteine; Disulfides; Dithionitrobenzoic Acid; Guanidine; Hydrogen; Kinetics; Methyl Methanesulfonate; Models, Molecular; Mutation; Myoglobin; Protein Conformation; Protein Folding; Sulfhydryl Compounds; Thermodynamics; Whales | 2001 |
Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates.
Topics: Bacterial Proteins; Cysteine; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Enzyme Inhibitors; Guanidine; Kinetics; Protein Denaturation; Protein Folding; Solutions; Spectrometry, Fluorescence; Sulfhydryl Reagents; Urea | 2002 |
Complete refolding of bovine beta-lactoglobulin requires disulfide bond formation under strict conditions.
Topics: Animals; Antibodies, Monoclonal; Cattle; Disulfides; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Guanidine; Lactoglobulins; Models, Molecular; Protein Binding; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence | 2005 |
Cloning, expression, purification, and characterization of Vibrio cholerae transcriptional activator, HlyU.
Topics: Bacterial Proteins; Chromatography, Gel; Circular Dichroism; Cloning, Molecular; Cysteine; Dithionitrobenzoic Acid; Escherichia coli; Guanidine; Models, Genetic; Protein Folding; Solvents; Spectrometry, Fluorescence; Trans-Activators; Transcription Factors; Transcription, Genetic; Vibrio cholerae | 2006 |
Photodegradation mechanism and reaction kinetics of recombinant human interferon-alpha2a.
Topics: Circular Dichroism; Disulfides; Dithionitrobenzoic Acid; Glutathione; Guanidine; Humans; Interferon alpha-2; Interferon-alpha; Kinetics; Microscopy, Fluorescence; Oxygen; Photobleaching; Photolysis; Recombinant Proteins; Sensitivity and Specificity; Spectrophotometry, Ultraviolet; Time Factors; Ultraviolet Rays | 2007 |
Kinetic intermediates of unfolding of dimeric prostatic phosphatase.
Topics: Acid Phosphatase; Anilino Naphthalenesulfonates; Congo Red; Dimerization; Dithionitrobenzoic Acid; Enzyme Inhibitors; Guanidine; Humans; In Vitro Techniques; Kinetics; Male; Prostate; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Protein Tyrosine Phosphatases; Spectrometry, Fluorescence; Sulfhydryl Compounds | 2007 |
Towards creatine kinase aggregation due to the cysteine modification at the flexible active site and refolding pathway.
Topics: Anilino Naphthalenesulfonates; Animals; Binding Sites; Chromatography, Gel; Circular Dichroism; Creatine Kinase; Cysteine; Dimerization; Dithionitrobenzoic Acid; Dithiothreitol; Dose-Response Relationship, Drug; Fluorescent Dyes; Guanidine; Kinetics; Models, Biological; Muscles; Protein Denaturation; Protein Folding; Protein Renaturation; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Spectrophotometry, Ultraviolet | 2007 |
Compact dimension of denatured states of staphylococcal nuclease.
Topics: Animals; Cysteine; Dithionitrobenzoic Acid; Fluorescence; Guanidine; Hydrogen-Ion Concentration; Kinetics; Micrococcal Nuclease; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Salmon; Tryptophan | 2008 |
Intermolecular disulfide bond formation promotes immunoglobulin aggregation: investigation by fluorescence correlation spectroscopy.
Topics: Animals; Cattle; Cysteine; Disulfides; Dithionitrobenzoic Acid; Guanidine; Immunoglobulin G; Kinetics; Organophosphorus Compounds; Protein Aggregates; Protein Denaturation; Spectrometry, Fluorescence | 2015 |