urea and heme

urea has been researched along with heme in 96 studies

Research

Studies (96)

TimeframeStudies, this research(%)All Research%
pre-199061 (63.54)18.7374
1990's14 (14.58)18.2507
2000's14 (14.58)29.6817
2010's5 (5.21)24.3611
2020's2 (2.08)2.80

Authors

AuthorsStudies
Tsong, TY1
Ahlquist, DA; Schwartz, S1
Aviram, I; Lanir, A1
Buhl, K; Seppelt, U1
Lyman, G; Preisler, HD1
Christoff, G; Preisler, HD; Taylor, E1
Johnston, A; Rentsch, G1
Kappas, A; Maines, MD2
Alfrey, AC; Kurnick, JE; Vautrin, R; Wallner, SF; Ward, HP1
Chan, E; Desforges, JF1
Koshy, TI; Luntz, TL; Margoliash, E; Schejter, A1
Bray, RC; Burke, JF; Dacey, S; Edwards, M; Santama, N; Smith, AT; Thorneley, RN1
Garber, EA; Luntz, TL; Margoliash, E; Schejter, A1
Bonaventura, C; Bonaventura, J; Fushitani, K1
Léonis, J; Peiffer, S1
Ichikawa, Y; Yamano, T1
Rachmilewitz, EA1
Blumberg, WE; Peisach, J; Rachmilewitz, EA1
Williams, GR; Zamudio, I1
Bruschi-Heriaud, M; DerVartanian, DV; Le Gall, J1
Marler, HR; Shakespeare, PG1
Annaev, B; Reichman, LM; Rozantzev, EG1
Morgan, WT; Riehm, JP1
Singh, J; Wharton, DC1
McDonald, CC; Phillips, WD1
Cabral, F; Love, B1
Garewal, HS; Wasserman, AR1
Byrne, MJ; Davison, AJ; Kaminsky, LS1
Hutner, SH1
Barnes, R; Jones, OT; Porra, RJ1
Clegg, JB; Weatherall, DJ1
Feinstein, RN; Howard, JB; Jaroslow, BN1
Miki, K; Okunuki, K1
Huntley, TE; Strittmatter, P2
Levere, RD; Mizoguchi, H1
Scott, RB1
Bensinger, TA; Conrad, ME; Mahmood, L; Maisels, MJ; McCurdy, PR1
Lederer, F; Tarin, J1
Babul, J; Stellwagen, E1
Eriksson, CE; Olsson, PA; Svensson, SG1
Creighton, JM; Marks, GS; Racz, WJ; Schneck, DW; Tyrrell, DL1
Nakamura, Y; Nakaya, K; Onozawa, M; Yamada, K1
Cann, JR1
Nakaya, K; Shibata, K; Suzuki, T; Takenaka, O1
Callahan, EW; Landaw, SA; Schmid, R1
Grizzuti, K; Muller-Eberhard, U1
Singh, J; Wasserman, AR1
Stellwagen, E2
Kita, M; Samejima, T1
Herskovits, TT1
Deisseroth, AB; Dounce, AL1
Sturtevant, JM; Tsong, TY1
Baudras, A; Di Franco, A; Iwatsubo, M; Labeyrie, F1
Janick, PA; Siegel, LM1
Cavill, I; Jacobs, A; Kaaba, S; May, A; Smith, S; Ting, WC; Whittaker, JA1
Abu-Soud, HM; Loftus, M; Stuehr, DJ1
Hager, LP; Osmulski, PA; Zong, Q1
Harrington, JP; Keaton, L1
Admiraal, SJ; Fee, JA; Felsch, JS; Fujiwara, T; Goudreau, PN; Gursky, S; Hobaugh, MR; Horvath, MP; Ikeda-Saito, M; Morgan, WT1
Glick, BS; Reid, GA; Schatz, G; Wachter, C1
Chen, DY; Vergères, G; Waskell, L; Wu, FF1
Lecomte, JT; Moore, CD1
Barrientos, A; Coronel, F; de Salamanca, RE; Fontanellas, A; Herrero, JA; Morán, MJ; Trobo, JI1
Huang, ZX; Qian, W; Sun, YL; Wang, YH; Xie, Y; Zhuang, JH1
Basak, S; Chakrabarti, A; Debnath, D; Haque, E1
Atkins, WM; Daggett, V; Storch, EM1
Huang, ZX; Qian, W; Wang, WH; Wang, YH; Wu, J; Xia, ZX; Xie, Y; Xue, LL; Yao, P1
Chance, MR1
Chen, Y; Panda, K; Stuehr, DJ1
Bren, KL; Russell, BS1
Banci, L; Bartalesi, I; Ciofi-Baffoni, S; Tien, M1
Ghosh, S; Mukherjee, S; Regulski, M; Sahoo, R; Sengupta, R; Stuehr, DJ; Tully, T1
FIGEN, JF; SCHMID, R; SCHWARTZ, S1
DANIELI, G; MASETTI, GP; SANGIORGI, F1
OZOLS, J; STRITTMATTER, P1
TZAGOLOFF, A; WHARTON, DC1
HORIE, S; MORRISON, M1
Bigotti, MG; Brunori, M; Cutruzzolà, F; Musto, R; Travaglini-Allocatelli, C1
Lecomte, JT; Mukhopadhyay, K1
Antalík, M; Augustynski, J; Bánó, M; Dawson, JH; Fedurco, M; Glascock, MC; Indiani, C; Sedlák, E; Smulevich, G1
Banci, L; Barker, PD; Bruix, M; Ciofi-Baffoni, S; de Lumley Woodyear, T; Fersht, AR; Garcia, P; Johnson, CM; Ramachandra Shastry, MC; Rico, M; Roder, H1
Dasgupta, A; Dutta, T; Ghosh, S; Ray, SS; Sahoo, R; Sengupta, R1
Deng, H; Hayden, EY; Li, D; Panda, K; Rousseau, DL; Stuehr, DJ; Yeh, SR1
Knappenberger, JA; Kuriakose, SA; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA1
Antalík, M; Dawson, JH; Droghetti, E; Fedurco, M; Smulevich, G; Sono, M; Sumithran, S1
De Filippis, V; Dewilde, S; Fago, A; Fontana, A; Hundahl, C; Moens, L; Picotti, P1
Alves, FR; Carvalho, FA; Carvalho, JW; Tabak, M1
Battistuzzi, G; Borsari, M; Bortolotti, CA; Di Rocco, G; Paltrinieri, L; Ranieri, A; Sola, M1
Cha, HJ; Choi, KY; Jang, DS; Jin, KS1
Aktas, BH; Dias-Teixeira, KL; Dos Santos Neto, JV; Franco, CH; Lopes, UG; Machado, FC; Moraes, CB; Schenkman, S1
Chen, C; Chen, J; Guo, C; Luo, S; Tong, L; Tong, Y; Xiang, S; Xu, K1
Aktas, BH; Bohm, A; Chorev, M; Du, R; Halperin, J; Reis Monteiro Dos Santos, GR; Yefidoff-Freedman, R; Zhang, Q1
Ahmad, F; Ahmed, A; Hassan, MI; Islam, A; Lakhrm, NA; Malik, A; Nasreen, K; Parray, ZA; Shamsi, A1

Reviews

2 review(s) available for urea and heme

ArticleYear
Inorganic nutrition.
    Annual review of microbiology, 1972, Volume: 26

    Topics: Bacteria; Blood Proteins; Carbon Dioxide; Cells, Cultured; Chelating Agents; Culture Media; Culture Techniques; Eukaryota; Fungi; Growth Substances; Heme; Histidine; Hydrogen-Ion Concentration; Hydroxamic Acids; Iron; Metals; Phenols; Phosphates; Sulfates; Trace Elements; Urea

1972
In vitro hemoglobin synthesis in the thalassemia syndromes.
    International review of experimental pathology, 1974, Volume: 13, Issue:0

    Topics: Amino Acids; Animals; Bone Marrow; Cell-Free System; Chromatography; Chromatography, Gel; Female; Fetal Diseases; Genes; Globins; Heme; Hemoglobin H; Hemoglobins; Hemoglobins, Abnormal; Heterozygote; Homozygote; Humans; In Vitro Techniques; Models, Structural; Pedigree; Pregnancy; RNA, Messenger; Thalassemia; Urea

1974

Other Studies

94 other study(ies) available for urea and heme

ArticleYear
Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.
    Biochemistry, 1976, Dec-14, Volume: 15, Issue:25

    Topics: Cytochrome c Group; Energy Transfer; Fluorescence; Guanidines; Heme; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Temperature; Tryptophan; Tyrosine; Urea

1976
Use of leuco-dyes in the quantitative colorimetric microdetermination of hemoglobin and other heme compounds.
    Clinical chemistry, 1975, Volume: 21, Issue:3

    Topics: Colorimetry; Drug Stability; Evaluation Studies as Topic; Heme; Hemoglobinometry; Humans; Hydrogen-Ion Concentration; Indicators and Reagents; Iron; Methods; Microchemistry; Oxidation-Reduction; Spectrophotometry; Urea

1975
Proton magnetic relaxation and anion effect in solutions of acid ferricytochrome c.
    Archives of biochemistry and biophysics, 1975, Volume: 166, Issue:2

    Topics: Animals; Binding Sites; Cytochrome c Group; Heme; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Magnetic Resonance Spectroscopy; Mathematics; Myocardium; Protein Binding; Protein Conformation; Temperature; Urea; X-Ray Diffraction

1975
[Radiogenic cystitis; endoscopic diagnosis, classification and therapy].
    Fortschritte der Medizin, 1978, Jan-19, Volume: 96, Issue:3

    Topics: Cystitis; Drug Combinations; Heme; Humans; Neomycin; Radiation Injuries; Radiotherapy; Sulfanilamides; Urea; Urinary Bladder

1978
Differentiation of erythroleukemia cells in vitro: properties of chemical inducers.
    Cell differentiation, 1975, Volume: 4, Issue:3

    Topics: Acetamides; Acetone; Animals; Blood; Cell Differentiation; Cell Line; Cryoprotective Agents; Culture Media; Dialysis; Dimethyl Sulfoxide; Drug Interactions; Drug Synergism; Ethylene Glycols; Formamides; Heme; Leukemia, Erythroblastic, Acute; Mice; Molecular Weight; Pharmaceutical Preparations; Pyridines; Urea

1975
Cryoprotective agents as inducers of erythroleukemic cell differentiation in vitro.
    Blood, 1976, Volume: 47, Issue:3

    Topics: Acetamides; Animals; Cell Differentiation; Cell Line; Dimethyl Sulfoxide; Heme; Leukemia, Erythroblastic, Acute; Leukemia, Experimental; Urea

1976
2-Allyl-2-isopropylacetylurea and its influence on the haematopoetic syxtem.
    Experientia, 1975, Feb-15, Volume: 31, Issue:2

    Topics: Allyl Compounds; Animals; Cytochrome P-450 Enzyme System; Dose-Response Relationship, Drug; Half-Life; Hematopoietic Stem Cells; Hematopoietic System; Heme; Hemeproteins; Liver; Male; Protein Denaturation; Rats; Urea

1975
Cobalt stimulation of heme degradation in the liver. Dissociation of microsomal oxidation of heme from cytochrome P-450.
    The Journal of biological chemistry, 1975, Jun-10, Volume: 250, Issue:11

    Topics: 5-Aminolevulinate Synthetase; Allylisopropylacetamide; Animals; Bilirubin; Cobalt; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Dactinomycin; Ethylmorphine-N-Demethylase; Heme; Iodides; Liver; Microsomes, Liver; Oxygen Consumption; Porphyrins; Puromycin; Rats; Thiocyanates; Time Factors; Triazoles; Urea

1975
The anemia of chronic renal failure and chronic diseases: in vitro studies of erythropoiesis.
    Blood, 1976, Volume: 47, Issue:4

    Topics: Adolescent; Adult; Aged; Anemia; Animals; Bone Marrow Cells; Chronic Disease; Creatinine; Dogs; Erythropoiesis; Female; Guanidines; Heme; Humans; In Vitro Techniques; Iron Radioisotopes; Kidney Failure, Chronic; Male; Middle Aged; Urea

1976
The role of disulphide bonds in Heinz body attachment to membranes.
    British journal of haematology, 1976, Volume: 33, Issue:3

    Topics: Binding Sites; Cell Fractionation; Cell Membrane; Disulfides; Dithiothreitol; Erythrocytes; Heinz Bodies; Heme; Humans; Mercaptoethanol; Urea

1976
Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation.
    Proceedings of the National Academy of Sciences of the United States of America, 1990, Volume: 87, Issue:22

    Topics: Alanine; Animals; Binding Sites; Cloning, Molecular; Cytochrome c Group; Drosophila melanogaster; Heme; Hot Temperature; Proline; Protein Conformation; Rats; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Urea; Valine

1990
Expression of a synthetic gene for horseradish peroxidase C in Escherichia coli and folding and activation of the recombinant enzyme with Ca2+ and heme.
    The Journal of biological chemistry, 1990, Aug-05, Volume: 265, Issue:22

    Topics: Amino Acid Sequence; Apoenzymes; Base Sequence; Calcium; Cloning, Molecular; Enzyme Activation; Escherichia coli; Gene Expression; Genes, Synthetic; Heme; Horseradish Peroxidase; Kinetics; Molecular Sequence Data; Peroxidases; Protein Conformation; Recombinant Proteins; Restriction Mapping; Sequence Homology, Nucleic Acid; Spectrophotometry; Urea

1990
Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c.
    Proceedings of the National Academy of Sciences of the United States of America, 1989, Volume: 86, Issue:10

    Topics: Animals; Cytochrome c Group; DNA Mutational Analysis; Heme; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Molecular; Phenylalanine; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea; Water

1989
Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida).
    Comparative biochemistry and physiology. B, Comparative biochemistry, 1986, Volume: 84, Issue:1

    Topics: Animals; Electrophoresis, Polyacrylamide Gel; Heme; Hemoglobins; History, 20th Century; Macromolecular Substances; Polychaeta; Urea

1986
[Myoglobin in solution; preliminary studies].
    Archives internationales de physiologie et de biochimie, 1965, Volume: 73, Issue:1

    Topics: Chemical Phenomena; Chemistry; Heme; Hydrogen-Ion Concentration; Myoglobin; Protein Denaturation; Solutions; Urea

1965
The role of the hydrophobic bonding in P-450 and the effect of organic compounds on the conversion of P-450 to P-420.
    Biochimica et biophysica acta, 1967, Dec-12, Volume: 147, Issue:3

    Topics: Amides; Aniline Compounds; Animals; Chemical Phenomena; Chemistry, Physical; Electron Spin Resonance Spectroscopy; Heme; Liver; Male; Microsomes; Models, Chemical; Oxidation-Reduction; Phenols; Pigments, Biological; Protein Binding; Rabbits; Spectrophotometry; Temperature; Ultracentrifugation; Urea

1967
Formation of hemichromes from oxidized hemoglobin subunits.
    Annals of the New York Academy of Sciences, 1969, Nov-20, Volume: 165, Issue:1

    Topics: Chromatography; Chromatography, Gel; Crystallization; Cytoplasmic Granules; Electron Spin Resonance Spectroscopy; Electrophoresis; Ferricyanides; Globins; Heme; Hemoglobins; Humans; Mercaptoethanol; Pyridines; Sodium Salicylate; Spectrophotometry; Starch; Urea

1969
Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives.
    The Journal of biological chemistry, 1971, May-25, Volume: 246, Issue:10

    Topics: Benzoates; Carbon Monoxide; Chemical Phenomena; Chemistry; Cyanides; Dialysis; Drug Stability; Electron Spin Resonance Spectroscopy; Ferricyanides; Globins; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Iron; Mercury; Methemoglobin; Organometallic Compounds; Oxidation-Reduction; Oxygen; Peptides; Photolysis; Protein Denaturation; Salicylates; Spectrophotometry; Urea

1971
Molecular state of cy tochrome c oxidase on polyacrylamide gel electrophoresis.
    Archives of biochemistry and biophysics, 1971, Volume: 143, Issue:1

    Topics: Acetates; Animals; Cattle; Detergents; Electron Transport Complex IV; Electrophoresis, Disc; Heme; Isoenzymes; Macromolecular Substances; Mitochondria, Muscle; Myocardium; Phenols; Spectrophotometry; Sulfuric Acids; Urea

1971
Electron paramagnetic resonance and light absorption studies on c-type cytochromes of the anaerobic sulfate reducer Desulfovibrio.
    Biochimica et biophysica acta, 1971, Jun-15, Volume: 234, Issue:3

    Topics: Aluminum; Ammonium Chloride; Animals; Chemical Phenomena; Chemistry; Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Cytochromes; Desulfovibrio; Drug Stability; Electron Spin Resonance Spectroscopy; Electrophoresis; Gels; Helium; Heme; Horses; Hydroxides; Ion Exchange Resins; Myocardium; Oxidation-Reduction; Potassium; Protein Conformation; Silicon Dioxide; Spectrophotometry; Sulfites; Ultraviolet Rays; Urea

1971
Purification and some properties of cytochrome c oxidase from the yeast Saccharomyces cerevisiae.
    The Journal of biological chemistry, 1971, Dec-25, Volume: 246, Issue:24

    Topics: Ammonium Sulfate; Animals; Carbon Monoxide; Cattle; Centrifugation, Density Gradient; Chemical Precipitation; Chromatography, Gel; Cyanides; Detergents; Electron Transport Complex IV; Electrophoresis; Heme; Hydrogen Peroxide; Kinetics; Macromolecular Substances; Molecular Weight; Myocardium; Oxidation-Reduction; Saccharomyces; Saccharomyces cerevisiae; Spectrophotometry; Sulfites; Sulfuric Acids; Urea

1971
Studies of microsomal cytochrome P-450 with isocyanide spin label.
    Biochimica et biophysica acta, 1972, Mar-15, Volume: 263, Issue:1

    Topics: Animals; Bile Acids and Salts; Binding Sites; Chloromercuribenzoates; Cyanides; Cyclic N-Oxides; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Male; Microsomes, Liver; Models, Chemical; Osmolar Concentration; Protein Binding; Protein Conformation; Rats; Spectrophotometry; Structure-Activity Relationship; Temperature; Ultraviolet Rays; Urea

1972
Proteins of the thermophilic fungus Humicola lanuginosa. II. Some physicochemical properties of a cytochrome c.
    Archives of biochemistry and biophysics, 1973, Volume: 154, Issue:1

    Topics: Animals; Circular Dichroism; Cytochrome c Group; Fungal Proteins; Heme; Horses; Hydrogen-Ion Concentration; Mitosporic Fungi; Myocardium; Optical Rotatory Dispersion; Peptides; Solvents; Spectrophotometry, Ultraviolet; Tyrosine; Urea

1973
Cytochrome c-556, a di-heme protein from Pseudomonas aeruginosa.
    Biochimica et biophysica acta, 1973, Feb-22, Volume: 292, Issue:2

    Topics: Amino Acids; Ammonium Sulfate; Chemical Precipitation; Chromatography, Ion Exchange; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Electrophoresis, Disc; Electrophoresis, Polyacrylamide Gel; Heme; Iron; Macromolecular Substances; Molecular Weight; Oxidation-Reduction; Pseudomonas aeruginosa; Sodium Dodecyl Sulfate; Spectrophotometry; Ultracentrifugation; Urea

1973
Proton magnetic resonance studies of horse cytochrome c.
    Biochemistry, 1973, Aug-14, Volume: 12, Issue:17

    Topics: Amino Acid Sequence; Amino Acids; Animals; Chemical Phenomena; Chemistry; Cytochrome c Group; Deuterium; Fluoroacetates; Heme; Horses; Hydrogen-Ion Concentration; Iron; Ligands; Magnetic Resonance Spectroscopy; Myocardium; Protein Conformation; Protons; Species Specificity; Temperature; Urea

1973
The heme environment in ferric and ferrous cytochrome c oxidase.
    Biochemistry, 1974, May-07, Volume: 13, Issue:10

    Topics: Animals; Chemical Phenomena; Chemistry; Chymotrypsin; Circular Dichroism; Cytochrome c Group; Electron Transport Complex IV; Ethylenes; Glycerol; Glycols; Heme; Horses; Iron; Myocardium; Oxidation-Reduction; Peptide Fragments; Protein Conformation; Spectrophotometry; Sucrose; Surface-Active Agents; Ultracentrifugation; Urea

1974
Triton X-100-4 M urea as an extraction medium for membrane proteins. II. Molecular properties of pure cytochrome b559: a lipoprotein containing small polypeptide chains and a limited lipid composition.
    Biochemistry, 1974, Sep-24, Volume: 13, Issue:20

    Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Carotenoids; Cell Membrane; Chemical Phenomena; Chemistry, Physical; Chlorophyll; Chloroplasts; Chromatography, Thin Layer; Cytochromes; Deuterium; Electrophoresis, Disc; Heme; Iron; Lipids; Macromolecular Substances; Molecular Weight; Plants; Polyethylene Glycols; Protein Binding; Protein Conformation; Spectrophotometry; Surface-Active Agents; Urea

1974
Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity.
    Proceedings of the National Academy of Sciences of the United States of America, 1974, Volume: 71, Issue:11

    Topics: Animals; Bilirubin; Cobalt; Cytochrome P-450 Enzyme System; Enzyme Induction; Heme; Male; Microsomes, Liver; Mixed Function Oxygenases; Morphine Derivatives; Rats; Urea

1974
Iron ligands in different forms of ferricytochrome c: the 620-nm band as a probe.
    Archives of biochemistry and biophysics, 1972, Volume: 150, Issue:2

    Topics: 1-Propanol; Animals; Chromatography, Gel; Cytochromes; Ethanol; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Mathematics; Methionine; Myocardium; Osmolar Concentration; Pepsin A; Peptides; Protein Binding; Protein Conformation; Protein Denaturation; Spectrophotometry; Temperature; Thermodynamics; Trypsin; Urea; Water

1972
The over-production of porphyrins by semi-anaerobic yeast.
    Enzyme, 1973, Volume: 16, Issue:1

    Topics: 5-Aminolevulinate Synthetase; Ammonium Sulfate; Anaerobiosis; Cell-Free System; Detergents; Ergosterol; Glucose; Heme; Iron; Oleic Acids; Porphyrins; Saccharomyces cerevisiae; Sucrose; Urea

1973
Molecular location of the genetic lesion in the acatalasemic mouse.
    Biochemical genetics, 1972, Volume: 6, Issue:4

    Topics: Animals; Azides; Catalase; Chromatography, Ion Exchange; Drug Stability; Goats; Guanidines; Heme; Hydroxylamines; Immune Sera; Liver; Mice; Mutation; Protein Conformation; Protein Denaturation; Rabbits; Triazoles; Trypsin; Urea

1972
Cytochromes of Bacillus subtilis. II. Purification and spectral properties of cytochromes c-550 and c-554.
    Journal of biochemistry, 1969, Volume: 66, Issue:6

    Topics: Azides; Bacillus subtilis; Chromatography, DEAE-Cellulose; Chromatography, Ion Exchange; Cyanides; Cytochromes; Heme; Hydrogen-Ion Concentration; Imidazoles; Oxidation-Reduction; Spectrophotometry; Temperature; Urea

1969
The effect of heme binding on the tryptophan residue and the protein conformation of cytochrome b 5 .
    The Journal of biological chemistry, 1972, Jul-25, Volume: 247, Issue:14

    Topics: 1-Propanol; Acetates; Acylation; Anhydrides; Animals; Apoproteins; Cattle; Circular Dichroism; Cytochromes; Ethanol; Heme; Mathematics; Protein Binding; Protein Conformation; Protein Denaturation; Rabbits; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan; Ultracentrifugation; Ultraviolet Rays; Urea

1972
The reactivity of the tyrosyl residues of cytochrome b 5 .
    The Journal of biological chemistry, 1972, Jul-25, Volume: 247, Issue:14

    Topics: 1-Propanol; Acetates; Acylation; Anhydrides; Animals; Apoproteins; Cattle; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Circular Dichroism; Cytochromes; Heme; Hydrogen-Ion Concentration; Iodine; Mathematics; Peptides; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Spectrophotometry; Trypsin; Tyrosine; Ultraviolet Rays; Urea

1972
Stimulation of alpha and beta polypeptide chain synthesis in cultured human marrow by erythropoietin.
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), 1972, Volume: 141, Issue:1

    Topics: Bone Marrow; Bone Marrow Cells; Carbon Isotopes; Cells, Cultured; Chromatography, Ion Exchange; Erythropoietin; Globins; Heme; Hemoglobins; Humans; Iron; Iron Isotopes; Macromolecular Substances; Peptide Biosynthesis; Peptides; Stimulation, Chemical; Urea; Valine

1972
Urea therapy in sickle-cell anemia.
    The New England journal of medicine, 1971, Oct-28, Volume: 285, Issue:18

    Topics: Anemia, Sickle Cell; Cyanates; Heme; Hemolysis; Humans; Pain; Urea

1971
Effect of intravenous urea in invert sugar on heme catabolism in sickle-cell anemia.
    The New England journal of medicine, 1971, Oct-28, Volume: 285, Issue:18

    Topics: Anemia, Sickle Cell; Bilirubin; Blood Urea Nitrogen; Carbon Monoxide; Erythrocyte Count; Female; Fructose; Glucose; Hematocrit; Heme; Hemoglobins; Humans; Injections, Intravenous; Male; Reticulocytes; Solutions; Urea

1971
Chemical modification of the thioether bridges in cytochrome c. A novel method for heme cleavage.
    European journal of biochemistry, 1971, Jun-29, Volume: 20, Issue:4

    Topics: Acetates; Animals; Binding Sites; Chemical Phenomena; Chemistry; Cytochromes; Ethers; Heme; Horses; Hydrogen-Ion Concentration; Iodine; Iodine Isotopes; Oxidation-Reduction; Peptides; Sulfur; Urea

1971
The existence of heme-protein coordinate-covalent bonds in denaturing solvents.
    Biopolymers, 1971, Volume: 10, Issue:11

    Topics: Cytochromes; Heme; Protein Binding; Protein Denaturation; Solvents; Spectrum Analysis; Urea

1971
Denatured hemoproteins as catalysts in lipid oxidation.
    Journal of the American Oil Chemists' Society, 1971, Volume: 48, Issue:9

    Topics: Blood Proteins; Catalase; Catalysis; Fatty Acids; Heme; Hot Temperature; Hydrogen-Ion Concentration; Lipids; Oxidation-Reduction; Peroxidases; Protein Denaturation; Urea

1971
Experimental porphyria. II. Drug-induced porphyrin biosynthesis.
    South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde, 1971, Sep-25

    Topics: 5-Aminolevulinate Synthetase; Acetamides; Alkenes; Allyl Compounds; Amides; Animals; Barbiturates; Chemical Phenomena; Chemistry; Chick Embryo; Cytochromes; Enzyme Induction; Esters; Female; Heme; Hydrolysis; Hypnotics and Sedatives; Liver; Male; Porphyrias; Porphyrins; Pregnanes; Pyridines; Sterols; Urea

1971
Interaction of cetylpuridinium chloride with oxymyoglobin.
    Biochimica et biophysica acta, 1971, Volume: 251, Issue:1

    Topics: Aldehydes; Animals; Cetacea; Chemical Phenomena; Chemistry; Detergents; Glyoxylates; Heme; Mathematics; Myoglobin; Optical Rotatory Dispersion; Oxygen; Protein Binding; Protein Conformation; Pyridinium Compounds; Spectrophotometry; Structure-Activity Relationship; Sulfuric Acids; Ultracentrifugation; Urea; Zinc

1971
Contribution of aromatic residue interactions to the stability of myoglobin. IV. Delineation of binding forces between aromatic compounds and myoglobin.
    Biochemistry, 1969, Volume: 8, Issue:10

    Topics: Binding Sites; Butyrates; Chemical Phenomena; Chemistry; Heme; Indoleacetic Acids; Indoles; Kinetics; Myoglobin; Naphthalenes; Protein Denaturation; Spectrum Analysis; Urea

1969
States of amino acid residues in proteins. XIX. Modification of arginine residues in myoglobin.
    Biochimica et biophysica acta, 1969, Nov-11, Volume: 194, Issue:1

    Topics: Acrylates; Aldehydes; Animals; Arginine; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Cyanides; Dextrans; Electrophoresis; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iodoacetates; Lysine; Methemoglobin; Methods; Methylcellulose; Myocardium; Myoglobin; Spectrophotometry; Time Factors; Ultracentrifugation; Urea

1969
Catabolism of heme in vivo: comparison of the simultaneous production of bilirubin and carbon monoxide.
    The Journal of clinical investigation, 1970, Volume: 49, Issue:5

    Topics: Animals; Bile; Bilirubin; Carbon Isotopes; Carbon Monoxide; Feces; Glycine; Heme; Injections, Intravenous; Liver; Phenobarbital; Rats; Respiration; Urea

1970
Conformational studies on human and rabbit plasma hemopexin and on the effect of ligands on the rabbit heme-hemopexin complex.
    Biochemistry, 1971, May-25, Volume: 10, Issue:11

    Topics: Animals; Blood Proteins; Carbon Monoxide; Chemical Phenomena; Chemistry; Circular Dichroism; Cyanides; Formates; Glycoproteins; Heme; Humans; Hydrogen-Ion Concentration; Optical Rotatory Dispersion; Osmolar Concentration; Oxidation-Reduction; Oxygen; Potassium; Protein Binding; Rabbits; Species Specificity; Sulfites; Ultraviolet Rays; Urea

1971
The use of disc gel electrophoresis with nonionic detergent in the purification of cytochrome f from spinach grana membranes.
    The Journal of biological chemistry, 1971, Jun-10, Volume: 246, Issue:11

    Topics: Acrylates; Carbon Monoxide; Chloroplasts; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cold Temperature; Cytochromes; Detergents; Electrophoresis, Disc; Gels; Guanidines; Heme; Iron; Membranes; Methods; Molecular Weight; Oxidation-Reduction; Plant Cells; Solubility; Spectrophotometry; Sulfuric Acids; Surface-Active Agents; Ultracentrifugation; Urea

1971
The reversible unfolding of horse heart ferricytochrome c.
    Biochemistry, 1968, Volume: 7, Issue:8

    Topics: Alkylation; Animals; Chemical Phenomena; Chemistry; Cytochromes; Dialysis; Glycols; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Spectrum Analysis; Tyrosine; Ultracentrifugation; Urea; Viscosity

1968
The conformational changes of catalase molecule caused by ligand molecules.
    Biochimica et biophysica acta, 1969, Feb-04, Volume: 175, Issue:1

    Topics: Azides; Catalase; Cyanides; Heme; Hydrogen-Ion Concentration; Optical Rotatory Dispersion; Potassium; Protein Denaturation; Spectrum Analysis; Ultraviolet Rays; Urea

1969
Solvent perturbation studies of heme proteins and other colored proteins.
    Archives of biochemistry and biophysics, 1969, Volume: 130, Issue:1

    Topics: Animals; Catalase; Cattle; Cetacea; Cytochromes; Deuterium; Glycerol; Glycols; Heme; Hemoglobins; Horses; Hydrogen-Ion Concentration; Liver; Myoglobin; Optical Rotatory Dispersion; Solvents; Spectrum Analysis; Sucrose; Tryptophan; Tyrosine; Ultraviolet Rays; Urea; Water

1969
Comparison of the catalytic and physical properties of the components of lyophilized beef erythrocyte catalase with those of lyophilized beef liver catalase components.
    Archives of biochemistry and biophysics, 1969, Volume: 131, Issue:1

    Topics: Animals; Catalase; Cattle; Chemical Phenomena; Chemistry; Crystallography; Erythrocytes; Freeze Drying; Heme; Liver; Models, Structural; Molecular Weight; Protein Denaturation; Solubility; Spectrum Analysis; Sulfites; Ultracentrifugation; Ultraviolet Rays; Urea

1969
Investigations of yeast L-lactate dehydrogenase (cytochrome b2). VI. Circular dichroism of the holoenzyme.
    The Journal of biological chemistry, 1969, Sep-25, Volume: 244, Issue:18

    Topics: Ascomycota; Chemical Phenomena; Chemistry; Crystallization; Cytochromes; DNA; Flavin Mononucleotide; Heme; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Mathematics; Optical Rotatory Dispersion; Peptides; Saccharomyces; Spectrophotometry; Spectrum Analysis; Urea

1969
Location of the heme moiety of cytochrome c by solvent perturbation.
    The Journal of biological chemistry, 1967, Feb-25, Volume: 242, Issue:4

    Topics: Chymotrypsin; Cytochromes; Glycols; Heme; Models, Theoretical; Solvents; Spectrophotometry; Urea; Viscosity

1967
Fluorometric and spectrophotometric study of heme binding on the apoprotein from a cytochrome b-2-derivative.
    Biochemistry, 1967, Volume: 6, Issue:6

    Topics: Coenzymes; Cytochromes; Flavins; Fluorometry; Heme; L-Lactate Dehydrogenase; Protein Binding; Spectrophotometry; Trypsin; Tryptophan; Tyrosine; Urea

1967
Electron paramagnetic resonance and optical evidence for interaction between siroheme and Fe4S4 prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands.
    Biochemistry, 1983, Jan-18, Volume: 22, Issue:2

    Topics: Arsenic; Arsenites; Carbon Monoxide; Cyanides; Dimethyl Sulfoxide; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferrous Compounds; Guanidines; Heme; Iron; Ligands; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Spectrophotometry; Sulfides; Sulfite Reductase (NADPH); Sulfur; Urea

1983
Anaemia in patients with myelomatosis.
    British journal of cancer, 1982, Volume: 45, Issue:6

    Topics: Adult; Aged; Anemia; Blood Volume; Bone Marrow; Creatinine; Erythrocytes; Erythropoietin; Female; Heme; Hemoglobinometry; Humans; Immunoglobulins; Iron; Male; Middle Aged; Multiple Myeloma; Paraproteins; Urea

1982
Subunit dissociation and unfolding of macrophage NO synthase: relationship between enzyme structure, prosthetic group binding, and catalytic function.
    Biochemistry, 1995, Sep-05, Volume: 34, Issue:35

    Topics: Amino Acid Oxidoreductases; Animals; Binding Sites; Catalysis; Heme; In Vitro Techniques; Kinetics; Macrophages; Mice; Molecular Structure; Nitric Oxide Synthase; Protein Conformation; Protein Denaturation; Protein Folding; Urea

1995
High-pressure-assisted reconstitution of recombinant chloroperoxidase.
    Biochemistry, 1995, Sep-26, Volume: 34, Issue:38

    Topics: Apoenzymes; Chloride Peroxidase; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Fungal Proteins; Heme; Hydrostatic Pressure; Mitosporic Fungi; Plasmids; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry; Urea

1995
Unfolding and release of heme from human hemoglobins A, S and F.
    The International journal of biochemistry, 1993, Volume: 25, Issue:5

    Topics: Fetal Hemoglobin; Heme; Hemoglobin A; Hemoglobin, Sickle; Humans; Methemoglobin; Oxidation-Reduction; Oxyhemoglobins; Protein Denaturation; Protein Folding; Urea

1993
Probing protein-cofactor interactions in the terminal oxidases by second derivative spectroscopy: study of bacterial enzymes with cofactor substitutions and heme A model compounds.
    Protein science : a publication of the Protein Society, 1994, Volume: 3, Issue:11

    Topics: Animals; Apoproteins; Cattle; Cytochrome a Group; Electron Transport; Electron Transport Complex IV; Heme; Hemopexin; Mitochondria, Heart; Myoglobin; Proteins; Spectrophotometry; Spectrum Analysis, Raman; Urea

1994
Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.
    Protein science : a publication of the Protein Society, 1993, Volume: 2, Issue:11

    Topics: Adenosine Triphosphate; Binding Sites; Biological Transport, Active; Cell Compartmentation; Heme; Intracellular Membranes; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mitochondria; Models, Biological; Peptide Fragments; Protein Denaturation; Protein Folding; Protein Precursors; Recombinant Fusion Proteins; Saccharomyces cerevisiae; Tetrahydrofolate Dehydrogenase; Urea

1993
The function of tyrosine 74 of cytochrome b5.
    Archives of biochemistry and biophysics, 1993, Volume: 305, Issue:2

    Topics: Animals; Cytochromes b5; Heme; Hot Temperature; In Vitro Techniques; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea

1993
Characterization of an independent structural unit in apocytochrome b5.
    Biochemistry, 1993, Jan-12, Volume: 32, Issue:1

    Topics: Amino Acid Sequence; Animals; Apoproteins; Binding Sites; Cyclic N-Oxides; Cytochrome b Group; Cytochromes b; Heme; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Molecular Structure; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rats; Spectrometry, Fluorescence; Spin Labels; Urea

1993
Abnormalities of heme biosynthesis in experimental acute renal failure.
    Journal of the American Society of Nephrology : JASN, 1996, Volume: 7, Issue:4

    Topics: Acute Kidney Injury; Anemia, Hemolytic; Animals; Creatinine; Dogs; Erythrocytes; Female; Heme; Male; Porphobilinogen Synthase; Porphyrins; Renal Dialysis; Urea; Uremia; Ureter

1996
The influence of mutation at Glu44 and Glu56 of cytochrome b5 on the protein's stabilization and interaction between cytochrome c and cytochrome b5.
    Biochemistry, 1998, Oct-06, Volume: 37, Issue:40

    Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes b5; Electrochemistry; Energy Transfer; Entropy; Enzyme Stability; Glutamic Acid; Heme; Horses; Hot Temperature; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Solutions; Temperature; Urea

1998
Structural changes of horseradish peroxidase in presence of low concentrations of urea.
    European journal of biochemistry, 1999, Volume: 259, Issue:1-2

    Topics: Anilino Naphthalenesulfonates; Circular Dichroism; Heme; Horseradish Peroxidase; Protein Denaturation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Urea

1999
Engineering out motion: introduction of a de novo disulfide bond and a salt bridge designed to close a dynamic cleft on the surface of cytochrome b5.
    Biochemistry, 1999, Apr-20, Volume: 38, Issue:16

    Topics: Animals; Cytochromes b5; Disulfides; Heme; Hot Temperature; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding; Protein Denaturation; Protein Engineering; Rats; Salts; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Urea

1999
Effect of mutation at valine 61 on the three-dimensional structure, stability, and redox potential of cytochrome b5.
    Biochemistry, 1999, Sep-14, Volume: 38, Issue:37

    Topics: Animals; Cattle; Crystallization; Crystallography, X-Ray; Cytochromes b5; Enzyme Stability; Heme; Hot Temperature; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Denaturation; Protein Engineering; Recombinant Proteins; Urea; Valine

1999
Unfolding of apomyoglobin examined by synchrotron footprinting.
    Biochemical and biophysical research communications, 2001, Sep-28, Volume: 287, Issue:3

    Topics: Amino Acid Sequence; Amino Acids; Apoproteins; Biochemistry; Biophysical Phenomena; Biophysics; Heme; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Myoglobin; Oxygen; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Urea; X-Rays

2001
Control of nitric oxide synthase dimer assembly by a heme-NO-dependent mechanism.
    Biochemistry, 2002, Apr-09, Volume: 41, Issue:14

    Topics: Anaerobiosis; Dimerization; Escherichia coli; Heme; Kinetics; Nitric Oxide; Nitric Oxide Donors; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Recombinant Proteins; S-Nitroso-N-Acetylpenicillamine; Spectrophotometry; Urea

2002
Denaturant dependence of equilibrium unfolding intermediates and denatured state structure of horse ferricytochrome c.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2002, Volume: 7, Issue:7-8

    Topics: Amino Acid Substitution; Animals; Circular Dichroism; Cytochrome c Group; Heme; Horses; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; Protein Denaturation; Protein Folding; Thermodynamics; Urea

2002
Unfolding and pH studies on manganese peroxidase: role of heme and calcium on secondary structure stability.
    Biopolymers, 2003, Volume: 72, Issue:1

    Topics: Apoproteins; Calcium; Circular Dichroism; Dithiothreitol; Enzyme Stability; Heme; Holoenzymes; Hydrogen-Ion Concentration; Models, Molecular; Oxidation-Reduction; Peroxidases; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Urea

2003
Characterization of Drosophila nitric oxide synthase: a biochemical study.
    Biochemical and biophysical research communications, 2003, Jun-27, Volume: 306, Issue:2

    Topics: Animals; Arginine; Biopterins; Dose-Response Relationship, Drug; Drosophila; Electrons; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Hydrogen Peroxide; Hydrolysis; NADP; Nitrates; Nitric Oxide; Nitric Oxide Synthase; Nitrites; Open Reading Frames; Protein Structure, Tertiary; Spectrophotometry; Time Factors; Trypsin; Ultraviolet Rays; Urea

2003
Experimental porphyria. IV. Studies of liver catalase and other heme enzymes in sedormid porphyria.
    The Journal of biological chemistry, 1955, Volume: 217, Issue:1

    Topics: Catalase; Heme; Humans; Hypnotics and Sedatives; Liver; Porphyrias; Urea

1955
[Action of various aromatic substances and nitrogen metabolites on heme synthesis in vitro].
    Bollettino della Societa italiana di biologia sperimentale, 1963, Mar-15, Volume: 39

    Topics: Creatine; Creatinine; Guanidine; Guanidines; Heme; In Vitro Techniques; Indoles; Nitrogen; Phenols; Urea; Uric Acid

1963
THE INTERACTION OF PORPHYRINS AND METALLOPORHYRINS WITH APOCYTOCHROME BETA-5.
    The Journal of biological chemistry, 1964, Volume: 239

    Topics: Chemical Phenomena; Chemistry; Chromatography; Cobalt; Copper; Cytochromes; Deuterium; Heme; Hydrogen-Ion Concentration; Magnesium; Nickel; Porphyrins; Pyrroles; Research; Spectrophotometry; Trypsin; Urea

1964
STUDIES OF THE ELECTRON TRANSPORT SYSTEM. LV. THE INFLUENCE OF PH AND OF PROTEIN-DEPOLYMERIZING REAGENTS ON THE REACTION OF CYTOCHROME A WITH BOROHYDRIDE.
    The Journal of biological chemistry, 1964, Volume: 239

    Topics: Borates; Borohydrides; Carbon Monoxide; Cyanides; Cytochromes; Cytochromes a; Dialysis; Electron Transport; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Indicators and Reagents; Renal Dialysis; Research; Spectrophotometry; Surface-Active Agents; Urea

1964
CYTOCHROME C OXIDASE COMPONENTS. IV. CHEMICAL DISTINCTION BETWEEN CYTOCHROMES ALPHA- AND ALPHA-3.
    The Journal of biological chemistry, 1964, Volume: 239

    Topics: Borates; Chemical Phenomena; Chemistry; Chromatography; Cyanides; Cytochromes; Electron Transport Complex IV; Heme; Research; Spectrophotometry; Sulfites; Urea

1964
Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins.
    Biochemistry, 2004, Jan-13, Volume: 43, Issue:1

    Topics: Amino Acid Substitution; Animals; Aplysia; Apoproteins; Evolution, Molecular; Globins; Heme; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Tyrosine; Urea; Whales

2004
A relationship between heme binding and protein stability in cytochrome b5.
    Biochemistry, 2004, Sep-28, Volume: 43, Issue:38

    Topics: Animals; Aspartic Acid; Cytochromes b5; Heme; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Rats; Temperature; Thermodynamics; Urea

2004
The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies.
    Biochimica et biophysica acta, 2004, Dec-01, Volume: 1703, Issue:1

    Topics: Animals; Circular Dichroism; Cytochrome c Group; Electrochemistry; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Oxidation-Reduction; Protein Denaturation; Solutions; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Urea; Water

2004
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
    Journal of molecular biology, 2005, Feb-11, Volume: 346, Issue:1

    Topics: Amino Acid Sequence; Apoproteins; Circular Dichroism; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Thermodynamics; Tryptophan; Urea

2005
Dissociation and unfolding of inducible nitric oxide synthase oxygenase domain identifies structural role of tetrahydrobiopterin in modulating the heme environment.
    Molecular and cellular biochemistry, 2006, Volume: 284, Issue:1-2

    Topics: Animals; Biopterins; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Indicators and Reagents; Light; Mice; Nitric Oxide Synthase Type II; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Scattering, Radiation; Spectrophotometry, Ultraviolet; Urea

2006
Regulation of the monomer-dimer equilibrium in inducible nitric-oxide synthase by nitric oxide.
    The Journal of biological chemistry, 2006, Mar-24, Volume: 281, Issue:12

    Topics: Amino Acid Motifs; Animals; Arginine; Biopterins; Chelating Agents; Chromatography; Cysteine; Dimerization; Disulfides; Escherichia coli; Heme; Iron; Mass Spectrometry; Mice; Models, Chemical; Models, Molecular; Molecular Conformation; Nitric Oxide; Nitric Oxide Synthase Type II; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrophotometry; Spectrum Analysis, Raman; Structure-Activity Relationship; Sulfhydryl Compounds; Time Factors; Urea; Zinc

2006
Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobin.
    Biochemistry, 2006, Sep-26, Volume: 45, Issue:38

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Cyanides; Ferric Compounds; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Denaturation; Recombinant Proteins; Serine; Sperm Whale; Structure-Activity Relationship; Synechocystis; Temperature; Urea

2006
Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.
    Archives of biochemistry and biophysics, 2009, Volume: 489, Issue:1-2

    Topics: Acetic Acid; Animals; Cattle; Heme; Horses; Hydrogen-Ion Concentration; Iron; Molecular Structure; Myoglobin; Protein Denaturation; Urea

2009
Unusual stability of human neuroglobin at low pH--molecular mechanisms and biological significance.
    The FEBS journal, 2009, Volume: 276, Issue:23

    Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Crystallography, X-Ray; Globins; Heme; Humans; Hydrogen-Ion Concentration; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Conformation; Protein Denaturation; Protein Folding; Protein Stability; Urea

2009
pH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies.
    International journal of biological macromolecules, 2013, Volume: 59

    Topics: Animals; Heme; Hemoglobins; Hydrogen-Ion Concentration; Iron; Kinetics; Light; Molecular Weight; Oligochaeta; Oxidation-Reduction; Protein Multimerization; Protein Stability; Protein Subunits; Protein Unfolding; Scattering, Radiation; Ultracentrifugation; Urea

2013
Effect of motional restriction on the unfolding properties of a cytochrome c featuring a His/Met-His/His ligation switch.
    Metallomics : integrated biometal science, 2014, Volume: 6, Issue:4

    Topics: Cytochromes c; Fungal Proteins; Heme; Immobilized Proteins; Kinetics; Models, Molecular; Motion; Protein Conformation; Protein Unfolding; Solutions; Static Electricity; Urea; Yeasts

2014
Structural analyses combined with small-angle X-ray scattering reveals that the retention of heme is critical for maintaining the structure of horseradish peroxidase under denaturing conditions.
    Amino acids, 2017, Volume: 49, Issue:4

    Topics: Circular Dichroism; Guanidine; Heme; Horseradish Peroxidase; Models, Molecular; Protein Denaturation; Protein Structure, Tertiary; Protein Unfolding; Temperature; Urea; X-Ray Diffraction

2017
Identification of di-substituted ureas that prevent growth of trypanosomes through inhibition of translation initiation.
    Scientific reports, 2018, 03-20, Volume: 8, Issue:1

    Topics: Animals; Cell Line, Tumor; Cell Proliferation; Chagas Disease; eIF-2 Kinase; Eukaryotic Initiation Factor-2; G1 Phase; Heme; Humans; Myoblasts; Parasitic Sensitivity Tests; Phosphorylation; Protozoan Proteins; Rats; Trypanosoma brucei brucei; Trypanosoma cruzi; Urea

2018
High-resolution structures of inhibitor complexes of human indoleamine 2,3-dioxygenase 1 in a new crystal form.
    Acta crystallographica. Section F, Structural biology communications, 2018, Nov-01, Volume: 74, Issue:Pt 11

    Topics: Catalytic Domain; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Mutation; Tryptophan; Urea

2018
New activators of eIF2α Kinase Heme-Regulated Inhibitor (HRI) with improved biophysical properties.
    European journal of medicinal chemistry, 2020, Feb-01, Volume: 187

    Topics: Antineoplastic Agents; Cell Line, Tumor; Cell Proliferation; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Eukaryotic Initiation Factor-2; Heme; Humans; Models, Molecular; Molecular Structure; Phosphorylation; Structure-Activity Relationship; Urea

2020
Crowding Milleu stabilizes apo-myoglobin against chemical-induced denaturation: Dominance of hardcore repulsions in the heme devoid protein.
    International journal of biological macromolecules, 2021, Jun-30, Volume: 181

    Topics: Animals; Apoproteins; Dextrans; Ficoll; Guanidine; Heme; Horses; Macromolecular Substances; Myoglobin; Protein Conformation; Protein Denaturation; Protein Stability; Spectrophotometry, Ultraviolet; Thermodynamics; Urea

2021