heme has been researched along with valine in 81 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 34 (41.98) | 18.7374 |
| 1990's | 24 (29.63) | 18.2507 |
| 2000's | 15 (18.52) | 29.6817 |
| 2010's | 8 (9.88) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cosson, A; Gacon, G; Krishnamoorthy, R; Labie, D; Tapon, J; Wajcman, H | 1 |
| Bechtel, KC; Bonaventura, C; Bonaventura, J; Dunlap, WM; Johnson, MH; Jue, DL; Moo-Penn, WF; Opella, SJ; Schmidt, DE; Schmidt, RM | 1 |
| Gelin, BR; Karplus, M | 1 |
| Glenn, AR; May, BK | 1 |
| Cahn, F; Lubin, M | 1 |
| Cai, M; Timkovich, R | 1 |
| Bray, RR; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN | 1 |
| Bray, RC; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN; Veitch, NC; Williams, RJ | 1 |
| Koshy, TI; Luntz, TL; Margoliash, E; Schejter, A | 1 |
| Boxer, SG; Gray, HB; Varadarajan, R; Zewert, TE | 1 |
| Boxer, SG; Lambright, DG; Varadarajan, R | 1 |
| Dalvit, C; Ho, C | 1 |
| Gurd, FR; Hanania, GI; Shire, SJ | 1 |
| Eastman, PM; Schrier, SL; Schwartz, R | 1 |
| Perutz, MF; TenEyck, LF | 1 |
| Koga, Y; Kusaka, I | 1 |
| Ho, C; Lindstrom, TR | 1 |
| Shaeffer, JR | 1 |
| Goldberg, IH; Kappen, LS | 1 |
| Noble, RW; Ranney, HM; Sharma, VS | 1 |
| Baldwin, TO; Imamura, T; Riggs, A | 1 |
| Charache, S; Ho, C; Lehmann, H; Lindstrom, TR; Norén, IB | 1 |
| Levere, RD; Mizoguchi, H | 2 |
| Glatthaar, B; Winterhalter, KH | 1 |
| Grayzel, AI; Hörchner, P; London, IM | 1 |
| Anderson, WF; Gilbert, JM | 1 |
| Hill, RJ; Macleod, RM | 1 |
| Dus, K; Erbes, DL; Gunsalus, IC; Katagiri, M; Yu, CA | 1 |
| Hillman, K; Krausz, LM; Wainio, WW | 1 |
| Braunitzer, G; Neuwirth, H; Reinhard, F | 1 |
| Lanzerotti, K; Schrier, SL; Waltuch, G | 1 |
| Adamson, SD; Godchaux, W; Herbert, E | 1 |
| Bargellesi, A; Conconi, F; Pontremoli, S | 1 |
| Jobe, A; Schulman, HM | 1 |
| Evans, RF; Shaeffer, JR; Trostle, PK | 1 |
| Cedel, TE; Ho, C; Mims, MP; Miura, S; Olson, JS; Russu, IM | 1 |
| Admiraal, SJ; Dou, Y; George, GN; Ikeda-Saito, M; Krzywda, S; Li, T; Olson, JS; Pickering, IJ; Prince, RC; Wilkinson, AJ | 1 |
| Newmyer, SL; Ortiz de Montellano, PR | 1 |
| Morishima, I; Nagano, S; Tanaka, M; Watanabe, Y | 1 |
| Joshi, AA; McDonald, MJ | 1 |
| Lisowski, M; Picur, B; Poerio, E; Taniuchi, H | 1 |
| Brinigar, WS; Bucci, JL; Chiancone, E; Fronticelli, C; Gattoni, M; Lu, AL | 1 |
| Admiraal, SJ; Dou, Y; Ikeda-Saito, M; La Mar, GN; Qin, J | 1 |
| Brinigar, WS; Bucci, E; Fronticelli, C; Gryczynski, Z; Kowalczyk, J; O'Donnell, JK; Olson, JS | 1 |
| Chiu, ML; La Mar, GN; Qin, J; Rajarathnam, K; Sligar, SG | 1 |
| Boxer, SG; Decatur, SM; DePillis, GD | 1 |
| Daldal, F; Ding, H; Dutton, PL; Saribaş, AS | 1 |
| Boffi, A; Chiancone, E; Colotti, G; Das, TK; Gibson, QH; Guarrera, L; Rousseau, DL | 1 |
| Almo, SC; Ho, C; Ho, NT; Puius, YA; Zou, M | 1 |
| Brinigar, WS; Cupane, A; Fronticelli, C; Karavitis, M; Leone, M; Militello, V; Vasquez, GB | 1 |
| Alzari, PM; Betzel, C; Fita, I; Herzog, C; Koller, F; Maté, MJ; Nykyri, LM; Zamocky, M | 1 |
| Matsuura, K; Nagashima, KV; Osyczka, A; Shimada, K | 1 |
| Bartunik, HD; Kachalova, GS; Popov, AN | 1 |
| Lu, Y; Wang, X | 1 |
| Huang, ZX; Qian, W; Wang, WH; Wang, YH; Wu, J; Xia, ZX; Xie, Y; Xue, LL; Yao, P | 1 |
| Hendrich, MP; Ho, C; Ho, NT; Jeong, ST | 1 |
| Boffi, A; Chiancone, E; Giangiacomo, L; Guarrera, L; Spagnuolo, C | 1 |
| Bemski, G; Flores, M; Wajnberg, E | 1 |
| Morgan, JE; Puustinen, A; Riistama, S; Verkhovsky, MI; Wikström, M | 1 |
| Acharya, AS; Ho, C; Ho, NT; Kumar, R; Malavalli, A; Manjula, BN; Nagel, RL; Prabhakaran, M; Rao, MJ; Sun, DP | 1 |
| Lee, D; Park, S; Shimizu, H; Shiro, Y; Shoun, H | 1 |
| Ishikawa, H; Ishimori, K; Morishima, I; Takahashi, S; Uchida, T | 1 |
| Bollen, A; Ferrari, RP; Ghibaudi, EM; Moguilevsky, N; Suriano, G; Watanabe, S | 1 |
| Heering, HA; Smith, AT; Smulevich, G | 1 |
| Gan, JH; Huang, ZX; Wang, YH; Wang, ZQ; Wu, J; Xia, ZX | 1 |
| Carpena, X; Chelikani, P; Fita, I; Loewen, PC | 1 |
| BRUNS, GP; LONDON, IM | 1 |
| Cao, C; Huang, ZX; Wang, YF; Wang, YH; Wang, ZQ; Wu, H; Zhang, Q | 1 |
| Crane, BR; Pant, K; Sharma, M; Stuehr, DJ; Wang, ZQ; Wei, CC | 1 |
| de Vitry, C; Desbois, A; Redeker, V; Wollman, FA; Zito, F | 1 |
| O'Connor, SE; Vaillancourt, FH; Vosburg, DA; Walsh, CT; Yeh, E | 1 |
| Bendall, DS; Hirst, J; Howe, CJ; Luisi, BF; Marcaida, MJ; Moorlen, RJ; Reda, T; Schlarb-Ridley, BG; Wastl, J; Worrall, JA | 1 |
| Stuehr, DJ; Wang, ZQ; Wei, CC | 1 |
| Hu, T; Li, D; Liang, Y; Ma, G; Su, Y; Su, Z; Wang, J; Wang, Q; Wang, S | 1 |
| Ho, C; Ho, NT; Maillett, DH; Rice, NW; Shen, TJ; Simplaceanu, V; Tam, MF; Tam, TCS | 1 |
| Boeglin, WE; Brash, AR; Mashhadi, Z | 1 |
| Al Haddad, A; Auböck, G; Chergui, M; Monni, R; van Mourik, F | 1 |
| Chen, Y; Einarsdóttir, Ó; Fee, JA; Funatogawa, C; Li, Y; McDonald, W; Stout, CD; Szundi, I | 1 |
| Besley, NA; Hirst, JD; Suess, CJ | 1 |
| Dantas, JM; Duke, NEC; Fernandes, AP; Londer, YY; Pokkuluri, PR; Portela, PC; Salgueiro, CA; Schiffer, M; Yang, X | 1 |
81 other study(ies) available for heme and valine
| Article | Year |
|---|---|
Hemoglobin Djelfa beta98 (FG 5) Val leads to Ala: isolation and functional properties of the heme saturated form.
Topics: Alanine; Diphosphoglyceric Acids; Erythrocytes; Heme; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Oxyhemoglobins; Valine | 1977 |
Hemoglobin Raleigh (beta1 valine replaced by acetylalanine). Structural and functional characterization.
Topics: Adult; Alanine; Amino Acids; Carbon Monoxide; Female; Heme; Hemoglobin A; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Male; Mass Spectrometry; Oxygen; Pedigree; Peptide Fragments; Phytic Acid; Valine | 1977 |
Mechanism of tertiary structural change in hemoglobin.
Topics: Amino Acid Sequence; Globins; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Biological; Models, Molecular; Oxyhemoglobins; Protein Conformation; Thermodynamics; Valine | 1977 |
Effect of haemin on endogenous protein synthesis in oocytes of the Queensland cane toad Bufo marinus.
Topics: Animals; Bufo marinus; Depression, Chemical; Female; Heme; Hemin; Leucine; Oocytes; Ovum; Phenylalanine; Protein Biosynthesis; Valine | 1975 |
Ability of formyl-methionyl-tRNA to initiate globin synthesis in the presence of double-stranded RNA or in the absence of hemin.
Topics: Animals; Escherichia coli; Globins; Heme; Hemin; Leucine; Leucine-tRNA Ligase; Liver; Methionine; Methionine-tRNA Ligase; N-Formylmethionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Rabbits; Reticulocytes; RNA; RNA, Transfer; Valine; Valine-tRNA Ligase | 1975 |
Ionization of the heme propionate substituents in pseudomonad cytochromes c-551.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytochrome c Group; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Pseudomonas; Pseudomonas aeruginosa; Valine | 1992 |
Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligodeoxyribonucleotides; Oxidation-Reduction; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Valine | 1992 |
Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys.
Topics: Arginine; Cyanides; Heme; Horseradish Peroxidase; Hydroxamic Acids; Isoenzymes; Lysine; Magnetic Resonance Spectroscopy; Phenylalanine; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Valine | 1992 |
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.
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 |
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin.
Topics: Asparagine; Aspartic Acid; Glutamates; Glutamic Acid; Heme; Humans; Mutation; Myoglobin; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine | 1989 |
Electrostatic interactions in wild-type and mutant recombinant human myoglobins.
Topics: Codon; Cyanides; Cysteine; Genetic Vectors; Heme; Humans; Kinetics; Molecular Conformation; Mutation; Myoglobin; Protein Binding; Protein Conformation; Recombinant Proteins; Spectrophotometry; Valine | 1989 |
Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms.
Topics: Carboxyhemoglobin; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Oxyhemoglobins; Protein Binding; Protein Conformation; Valine | 1985 |
Electrostatic effects in myoglobin. pH and ionic strength variations of ionization equilibria for individual groups in sperm whale ferrimyoglobin.
Topics: Amino Acid Sequence; Animals; Cetacea; Chemical Phenomena; Chemistry; Evaluation Studies as Topic; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Mathematics; Models, Chemical; Myoglobin; Osmolar Concentration; Protein Conformation; Protein Denaturation; Valine; Water | 1974 |
Distinctions between idiopathic ineffective erythropoiesis and di Guglielmo's disease: clinical and biochemical differences.
Topics: 5-Aminolevulinate Synthetase; Adult; Aged; Anemia, Hemolytic; Blood Cell Count; Blood Platelets; Bone Marrow; Bone Marrow Cells; Carbon Isotopes; Cells, Cultured; Erythrocytes, Abnormal; Erythropoiesis; Female; Globins; Glycine; Hematopoiesis; Heme; Humans; Isoelectric Focusing; Karyotyping; Leukemia, Erythroblastic, Acute; Leukemia, Myeloid, Acute; Levulinic Acids; Male; Middle Aged; Reticulocytes; Valine | 1972 |
Stereochemistry of cooperative effects in hemoglobin.
Topics: Animals; Arginine; Chemical Phenomena; Chemistry; Crystallization; Diphosphoglyceric Acids; Heme; Hemoglobins; Hemoglobins, Abnormal; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Macromolecular Substances; Methemoglobin; Models, Structural; Oxygen; Protein Binding; Protein Conformation; Valine; X-Ray Diffraction | 1972 |
Characterization of autolysed membranes of Bacillus cereus. Characterization in membrane biosynthesis and binding of hemes to proteins of membrane subfraction L10P.
Topics: Apoproteins; Bacillus cereus; Bacteriolysis; Carbon Isotopes; Cell Membrane; Centrifugation, Density Gradient; Cytochromes; Electrophoresis, Disc; Glycerol; Heme; Leucine; Phospholipases; Phospholipids; Protein Binding; Spheroplasts; Valine | 1972 |
Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin.
Topics: Adult; Binding Sites; Carbon Monoxide; Deuterium; Diphosphoglyceric Acids; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Magnetic Resonance Spectroscopy; Oxygen; Phosphates; Potassium Chloride; Protein Binding; Protein Conformation; Sulfates; Tromethamine; Valine | 1973 |
Structure and synthesis of the unstable hemoglobin Sabin (alpha 2 beta 2--91 Leu leads to pro).
Topics: Amino Acid Sequence; Carbon Radioisotopes; Chemical Phenomena; Chemistry; Erythrocytes; Female; Globins; Glycine; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Kinetics; Leucine; Macromolecular Substances; Models, Chemical; Peptides; Structure-Activity Relationship; Tritium; Valine | 1973 |
Inhibition of globin chain initiation in reticulocyte lysates by pactamycin: accumulation of methionyl-valine.
Topics: Animals; Antibiotics, Antineoplastic; Carbon Radioisotopes; Centrifugation, Density Gradient; Electrophoresis; Globins; Heme; In Vitro Techniques; Liver; Methionine; Peptide Chain Elongation, Translational; Peptide Chain Initiation, Translational; Polyribosomes; Protein Binding; Puromycin; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer; Sucrose; Sulfur Radioisotopes; Valine | 1973 |
Structure-function relation in hemoglobin Köln (beta 98 Val leads to Met).
Topics: Carboxyhemoglobin; Diphosphoglyceric Acids; Heme; Hemoglobinometry; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Methionine; Molecular Weight; Oxygen; Oxyhemoglobins; Spectrum Analysis; Ultracentrifugation; Valine | 1974 |
The amino acid sequence of the monomeric hemoglobin component from the bloodworm, Glyat liver.
Topics: Amino Acid Sequence; Amino Acids; Animals; Annelida; Carbon Isotopes; Carboxypeptidases; Cetacea; Chromatography, Ion Exchange; Chromatography, Paper; Chymotrypsin; Cyanogen Bromide; Electrophoresis; Electrophoresis, Paper; Fluoroacetates; Globins; Heme; Hemoglobins; Kinetics; Liver; Macromolecular Substances; Mathematics; Models, Biological; Myoglobin; Peptide Hydrolases; Peptides; Perfusion; Protein Binding; Protein Biosynthesis; Species Specificity; Thiocyanates; Trypsin; Valine | 1972 |
Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin.
Topics: Animals; Australia; Carbon Monoxide; Chloromercuribenzoates; Cytochromes; Deuterium; Fetal Hemoglobin; Heme; Hemoglobins; Hemoglobins, Abnormal; Horses; Humans; Macromolecular Substances; Magnetic Resonance Spectroscopy; Myocardium; Protein Conformation; Switzerland; Umbilical Cord; Valine | 1972 |
Stimulation of alpha and beta polypeptide chain synthesis in cultured human marrow by erythropoietin.
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 |
Enhancement of heme and globin synthesis in cultured human marrow by certain 5 -H steroid metabolites.
Topics: 5-Aminolevulinate Synthetase; Bile Acids and Salts; Bone Marrow; Bone Marrow Cells; Carbon Isotopes; Cells, Cultured; Chromatography; Dactinomycin; Enzyme Induction; Erythropoiesis; Erythropoietin; Etiocholanolone; Globins; Heme; Hemoglobins; Humans; In Vitro Techniques; Iron; Iron Isotopes; Ketones; Ketosteroids; Methylcellulose; Pregnanediol; Pregnanes; Progesterone; Puromycin; Stimulation, Chemical; Testosterone; Valine | 1971 |
Intermediates of hemoglobin and their relation to biosynthesis.
Topics: Amino Acid Sequence; Amino Acids; Animals; Carbon Isotopes; Chromatography, Ion Exchange; Electrophoresis, Disc; Globins; Heme; Hemoglobins; Humans; Iron Isotopes; Leucine; Oxidation-Reduction; Peptide Biosynthesis; Puromycin; Rabbits; Reticulocytes; Ribosomes; RNA, Messenger; Tritium; Ultracentrifugation; Valine | 1971 |
The stimulation of globin synthesis by heme.
Topics: Animals; Fluorides; Globins; Heme; Hemoglobins; In Vitro Techniques; Peptide Biosynthesis; Puromycin; Rabbits; Reticulocytes; Ribosomes; Valine | 1966 |
Translational control of in vitro hemoglobin synthesis.
Topics: Animals; Carbon Isotopes; Cell-Free System; Chromatography, Ion Exchange; Globins; Heme; Hemoglobins; Kinetics; Leucine; Liver; Peptides; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer; Tritium; Valine | 1969 |
Reaction of human CO hemoglobin with p,p'-difluoro-m,m'-dinitrodiphenylsulfone.
Topics: Carbon Monoxide; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Heme; Hemoglobins; Humans; Hydrocarbons, Halogenated; Infrared Rays; Nitrobenzenes; Oxygen; Spectrophotometry; Sulfones; Valine | 1970 |
Chemical characterization of cytochrome P-450cam.
Topics: Amino Acid Sequence; Amino Acids; Asparagine; Aspartic Acid; Autoanalysis; Camphor; Carbohydrates; Carboxypeptidases; Chemical Phenomena; Chemistry; Cytochromes; Formates; Heme; Hydrazines; Hydrogen-Ion Concentration; Isoelectric Focusing; Isoflurophate; Molecular Weight; Nitrobenzenes; Peptides; Porphyrins; Pseudomonas; Valine | 1970 |
Polyamino acid derivatives of mammalian cytochrome c undecapeptide.
Topics: Anhydrides; Animals; Chemical Phenomena; Chemistry; Cytochromes; Glycine; Heme; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Oxidation-Reduction; Peptides; Spectrophotometry; Spectrum Analysis; Valine | 1970 |
[Variants of the haeme complex: the amino acid residues in positions E7, E11 and F8 of an insect haemoglobin (erythrocruorin)].
Topics: Amino Acid Sequence; Animals; Heme; Hemoglobins; Histidine; Insecta; Valine | 1971 |
Marrow defect in idiopathic ineffective erythropoiesis.
Topics: Adult; Aged; Anemia; Bone Marrow; Bone Marrow Cells; Carbon Isotopes; Erythropoiesis; Female; Glycine; Heme; Humans; In Vitro Techniques; Levulinic Acids; Male; Methods; Middle Aged; Time Factors; Valine | 1968 |
Factors affecting the rate of protein synthesis in lysate systems from reticulocytes.
Topics: Adenosine Triphosphate; Animals; Carbon Isotopes; Cell-Free System; Centrifugation, Density Gradient; Chromatography, Gel; Chromatography, Ion Exchange; Deuterium; Female; Heme; Hydrogen-Ion Concentration; Magnesium; Osmotic Fragility; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; Temperature; Time Factors; Valine | 1968 |
Excess of alpha-globin synthesis in homozygous beta-thalassemia. Its cytoplasmic molecular forms.
Topics: Adult; Blood Proteins; Centrifugation, Density Gradient; Child; Child, Preschool; Chromatography, Ion Exchange; Cytoplasm; Erythrocytes; Globins; Heme; Hemoglobins; Hemolysis; Homozygote; Humans; Infant, Newborn; Infant, Premature; Leucine; Lysine; Peptides; Thalassemia; Tritium; Valine | 1968 |
The inhibition of heme and globin synthesis by cobalt in rabbit reticulocytes and bone marrow.
Topics: Amino Acids; Animals; Blood Proteins; Bone Marrow; Bone Marrow Cells; Carbon Isotopes; Chromatography, Gel; Cobalt; Globins; Glycine; Heme; Hemoglobins; In Vitro Techniques; Kinetics; Leucine; Levulinic Acids; Peptide Biosynthesis; Rabbits; Reticulocytes; Valine | 1968 |
Inhibition of the biosynthetic completion of rabbit hemoglobin by isolated human hemoglobin chains.
Topics: Animals; Carbon Isotopes; Cell-Free System; Centrifugation, Density Gradient; Chromatography, Ion Exchange; Depression, Chemical; Electrophoresis; Heme; Hemoglobins; Humans; Leucine; Methods; Peptide Biosynthesis; Peptides; Rabbits; Reticulocytes; Ribosomes; Solubility; Species Specificity; Valine | 1969 |
Proton nuclear magnetic resonance studies of isonitrile-heme protein complexes.
Topics: Animals; Carbon Monoxide; Cyanides; Heme; Hemoglobins; Humans; Macromolecular Substances; Magnetic Resonance Spectroscopy; Myoglobin; Nitriles; Thermodynamics; Valine; Whales | 1983 |
Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant.
Topics: Animals; Carbon Monoxide; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Imidazoles; Ligands; Models, Molecular; Mutation; Myoglobin; Protein Engineering; Spectrophotometry; Spectrum Analysis; Swine; Valine; X-Rays | 1995 |
Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron.
Topics: Alanine; Animals; Catalysis; Cell Line; Heme; Histidine; Horseradish Peroxidase; Imines; Iron; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Spodoptera; Substrate Specificity; Sulfides; Sulfoxides; Valine | 1995 |
Putative hydrogen bond network in the heme distal site of horseradish peroxidase.
Topics: Amino Acid Sequence; Asparagine; Cloning, Molecular; Electron Transport Complex IV; Escherichia coli; Heme; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Spectrophotometry; Valine | 1995 |
Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.
Topics: Amino Acid Sequence; Arginine; Genetic Variation; Glutamates; Glutamic Acid; Heme; Hemoglobin A; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Oxyhemoglobins; Point Mutation; Spectrophotometry; Tyrosine; Valine | 1994 |
Comparison of thermodynamic and kinetic effects between the Leu32-->norvaline and Leu35-->norvaline substitutions of the three-fragment complex of cytochrome c.
Topics: Amino Acid Sequence; Animals; Cytochrome c Group; Heme; Horses; In Vitro Techniques; Kinetics; Leucine; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Protein Structure, Tertiary; Spectrum Analysis; Thermodynamics; Valine | 1994 |
The dimer-tetramer equilibrium of recombinant hemoglobins. Stabilization of the alpha 1 beta 2 interface by the mutation beta(Cys112-->Gly) at the alpha 1 beta 1 interface.
Topics: 2,3-Diphosphoglycerate; Amino Acid Sequence; Base Sequence; Binding Sites; Carboxyhemoglobin; Chromatography, Gel; Cysteine; Diphosphoglyceric Acids; Drug Stability; Globins; Glycine; Heme; Hemoglobin A; Humans; Macromolecular Substances; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Point Mutation; Protein Folding; Recombinant Proteins; Sequence Deletion; Valine | 1994 |
1H NMR study of the solution molecular and electronic structure of engineered distal myoglobin His64(E7) Val/Val68(E11) His double mutant. Coordination of His64(E11) at the sixth position in both low-spin and high-spin states.
Topics: Amino Acid Sequence; Heme; Histidine; Humans; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Metmyoglobin; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Solutions; Structure-Activity Relationship; Temperature; Valine | 1994 |
Recombinant human hemoglobin: modification of the polarity of the beta-heme pocket by a valine67(E11)-->threonine mutation.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Escherichia coli; Heme; Hemoglobins; Humans; Kinetics; Ligands; Macromolecular Substances; Mathematics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotides, Antisense; Recombinant Proteins; Threonine; Valine | 1993 |
Solution structure determination of the heme cavity in the E7 His-->Val cyano-met myoglobin point mutant based on the 1H NMR detected dipolar field of the iron: evidence for contraction of the heme pocket.
Topics: Amino Acid Sequence; Animals; Binding Sites; Heme; Histidine; Hydrogen; Magnetic Resonance Spectroscopy; Mathematics; Metmyoglobin; Point Mutation; Protein Structure, Secondary; Valine; Whales | 1993 |
Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands.
Topics: Animals; Binding Sites; Carbon Monoxide; Cloning, Molecular; Escherichia coli; Heme; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Myoglobin; Point Mutation; Protein Conformation; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Valine; Whales | 1996 |
Substitutions at position 146 of cytochrome b affect drastically the properties of heme bL and the Qo site of Rhodobacter capsulatus cytochrome bc1 complex.
Topics: Alanine; Amino Acid Sequence; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Glycine; Heme; Kinetics; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Rhodobacter capsulatus; Structure-Activity Relationship; Ubiquinone; Valine | 1997 |
The apolar distal histidine mutant (His69-->Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation.
Topics: Amino Acid Substitution; Animals; Bivalvia; Carbon Monoxide; Circular Dichroism; Dimerization; Heme; Hemoglobins; Histidine; Ligands; Mutagenesis, Insertional; Protein Binding; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Valine | 1998 |
Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp).
Topics: Blood Substitutes; Crystallization; Crystallography, X-Ray; Heme; Hemoglobin A; Hemoglobins; Humans; Hydrogen Bonding; Ligands; Models, Molecular; Oxygen; Protein Binding; Protein Conformation; Recombinant Proteins; Tryptophan; Valine; Water | 1998 |
Properties of human hemoglobins with increased polarity in the alpha- or beta-heme pocket. Carbonmonoxy derivatives.
Topics: Carboxyhemoglobin; Globins; Heme; Hemoglobin A; Humans; Macromolecular Substances; Models, Molecular; Point Mutation; Protein Conformation; Spectrophotometry; Temperature; Thermodynamics; Threonine; Valine | 1998 |
Structure of catalase-A from Saccharomyces cerevisiae.
Topics: Alanine; Binding Sites; Catalase; Crystallography, X-Ray; Heme; Models, Molecular; Mutagenesis, Site-Directed; NADP; Protein Conformation; Saccharomyces cerevisiae; Valine | 1999 |
Interaction site for high-potential iron-sulfur protein on the tetraheme cytochrome subunit bound to the photosynthetic reaction center of Rubrivivax gelatinosus.
Topics: Bacterial Proteins; Binding Sites; Cytochromes; Electron Transport; Glutamic Acid; Heme; Iron-Sulfur Proteins; Light-Harvesting Protein Complexes; Lysine; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Photosynthetic Reaction Center Complex Proteins; Rhodospirillaceae; Valine | 1999 |
A steric mechanism for inhibition of CO binding to heme proteins.
Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Hydrogen Bonding; Iron; Ligands; Metmyoglobin; Models, Molecular; Myoglobin; Nitrogen; Protein Conformation; Protein Structure, Secondary; Temperature; Valine | 1999 |
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Topics: Arginine; Aspartic Acid; Binding Sites; Cyanides; Cytochrome-c Peroxidase; Glutamic Acid; Glycine; Heme; Histidine; Leucine; Molecular Mimicry; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Engineering; Protons; Spectrophotometry; Valine | 1999 |
Effect of mutation at valine 61 on the three-dimensional structure, stability, and redox potential of cytochrome b5.
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 |
Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation.
Topics: Amino Acid Substitution; Asparagine; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Kinetics; Leucine; Lysine; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Oxyhemoglobins; Phenylalanine; Protein Binding; Recombinant Proteins; Tryptophan; Valine | 1999 |
Proximal and distal effects on the coordination chemistry of ferric Scapharca homodimeric hemoglobin as revealed by heme pocket mutants.
Topics: Amino Acid Substitution; Animals; Bivalvia; Dimerization; Ferric Compounds; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Leucine; Phenylalanine; Point Mutation; Spectrophotometry; Spectrum Analysis, Raman; Ultracentrifugation; Valine | 2000 |
Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: the role of His-E7 and Val-E11.
Topics: Animals; Biophysical Phenomena; Biophysics; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Models, Molecular; Myocardium; Myoglobin; Protein Conformation; Protons; Valine | 2000 |
Binding of O(2) and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans.
Topics: Amino Acid Substitution; Conserved Sequence; Cytochrome b Group; Cytochromes; Electron Transport Complex IV; Escherichia coli; Escherichia coli Proteins; Heme; Isoleucine; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Paracoccus denitrificans; Photolysis; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Valine | 2000 |
Interspecies hybrid HbS: complete neutralization of Val6(beta)-dependent polymerization of human beta-chain by pig alpha-chains.
Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Anemia, Sickle Cell; Animals; Binding Sites; Dimerization; Genetic Therapy; Globins; Heme; Hemoglobin, Sickle; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Oxygen; Protein Engineering; Protein Structure, Quaternary; Recombinant Fusion Proteins; Static Electricity; Swine; Valine | 2000 |
Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
Topics: Binding Sites; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electrons; Fusarium; Heme; Hydrogen Bonding; Kinetics; Ligands; Models, Molecular; Mutation; Nitric Oxide; Oxidoreductases; Protein Conformation; Protein Structure, Secondary; Protons; Recombinant Proteins; Serine; Spectrophotometry; Temperature; Threonine; Valine; Water | 2000 |
Ligand migration in human myoglobin: steric effects of isoleucine 107(G8) on O(2) and CO binding.
Topics: Alanine; Amino Acid Substitution; Binding Sites; Heme; Humans; Isoleucine; Kinetics; Leucine; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine | 2001 |
Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase.
Topics: Amino Acid Substitution; Animals; Aspartic Acid; Base Sequence; Blotting, Western; Cattle; CHO Cells; Cricetinae; DNA Primers; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Glutamic Acid; Glycine; Heme; Lactoperoxidase; Mutation; Valine | 2001 |
Spectroscopic characterization of mutations at the Phe41 position in the distal haem pocket of horseradish peroxidase C: structural and functional consequences.
Topics: Amino Acid Substitution; Benzothiazoles; Heme; Horseradish Peroxidase; Isoenzymes; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Binding; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Structure-Activity Relationship; Sulfonic Acids; Tryptophan; Valine | 2002 |
Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b5 mutants.
Topics: Binding Sites; Crystallography, X-Ray; Cytochrome c Group; Cytochromes b5; Drug Stability; Electron Transport; Heme; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Valine | 2002 |
An electrical potential in the access channel of catalases enhances catalysis.
Topics: Arginine; Aspartic Acid; Catalase; Catalysis; Electrochemistry; Escherichia coli; Heme; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Valine | 2003 |
THE EFFECT OF HEMIN ON THE SYNTHESIS OF GLOBIN.
Topics: Animals; Carbon Isotopes; Globins; Glycine; Heme; Hemin; Hemoglobins; Levulinic Acids; Rabbits; Radiometry; Research; Reticulocytes; Valine | 1965 |
1H NMR studies of the effect of mutation at Valine45 on heme microenvironment of cytochrome b5.
Topics: Animals; Cattle; Cytochromes b5; Enzyme Stability; Glutamine; Heme; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Microsomes; Molecular Structure; Mutation; Protein Conformation; Temperature; Tyrosine; Valine | 2003 |
A conserved Val to Ile switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles.
Topics: Amino Acid Substitution; Animals; Bacillus subtilis; Bacterial Proteins; Binding Sites; Catalysis; Conserved Sequence; Heme; Iron; Isoleucine; Kinetics; Mice; Models, Chemical; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Valine | 2004 |
Biochemical and spectroscopic characterization of the covalent binding of heme to cytochrome b6.
Topics: Amino Acid Sequence; Animals; Binding Sites; Chlamydomonas reinhardtii; Conserved Sequence; Cysteine; Cytochromes b6; Dimerization; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Heme; Hydrolysis; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Peroxidase; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis, Raman; Valine | 2004 |
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis.
Topics: Acyltransferases; Amino Acids; Bacterial Proteins; Catalysis; Chlorine; Enzymes; Heme; Indenes; Iron; Isoleucine; Pseudomonas syringae; Valine | 2005 |
Modulation of heme redox potential in the cytochrome c6 family.
Topics: Amino Acid Sequence; Crystallography, X-Ray; Cyanobacteria; Cytochromes c6; Electrochemistry; Electron Transport; Glutamine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Valine | 2007 |
How does a valine residue that modulates heme-NO binding kinetics in inducible NO synthase regulate enzyme catalysis?
Topics: Animals; Bacillus subtilis; Binding Sites; Catalysis; Computer Simulation; Heme; Isoenzymes; Mice; Molecular Structure; Mutagenesis, Site-Directed; NADP; Nitrates; Nitric Oxide; Nitric Oxide Synthase Type II; Nitrites; Oxidation-Reduction; Superoxides; Valine | 2010 |
Propylbenzmethylation at Val-1(α) markedly increases the tetramer stability of the PEGylated hemoglobin: a comparison with propylation at Val-1(α).
Topics: Adult; Alkenes; Circular Dichroism; Heme; Hemoglobins; Humans; Methylation; Osmotic Pressure; Oxygen; Polyethylene Glycols; Ultracentrifugation; Valine | 2012 |
Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocket.
Topics: Adult; Amino Acid Substitution; Binding Sites; Female; Heme; Hemoglobins; Humans; Male; Oxidation-Reduction; Recombinant Proteins; Structure-Activity Relationship; Valine | 2013 |
Inhibitory effects of a novel Val to Thr mutation on the distal heme of human catalase.
Topics: Amino Acid Sequence; Biocatalysis; Catalase; Catalytic Domain; Crystallography, X-Ray; Heme; Humans; Hydrogen Bonding; Hydrogen Peroxide; Models, Molecular; Molecular Structure; Mutant Proteins; Mutation, Missense; Peroxides; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Threonine; Valine | 2014 |
Tryptophan-to-heme electron transfer in ferrous myoglobins.
Topics: Algorithms; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Kinetics; Leucine; Models, Chemical; Models, Molecular; Myoglobin; Porphyrins; Protein Structure, Tertiary; Spectrophotometry; Tryptophan; Valine | 2015 |
Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba
Topics: Bacterial Proteins; Binding Sites; Carbon Monoxide; Catalytic Domain; Crystallization; Crystallography, X-Ray; Cytochrome b Group; Electron Transport Complex IV; Heme; Kinetics; Ligands; Molecular Dynamics Simulation; Mutation, Missense; Nitric Oxide; Oxidation-Reduction; Oxygen; Protein Binding; Protein Domains; Spectrophotometry; Thermus thermophilus; Valine | 2017 |
Quantum chemical calculations of tryptophan → heme electron and excitation energy transfer rates in myoglobin.
Topics: Density Functional Theory; Electrons; Energy Transfer; Heme; Hydrogen Bonding; Isoleucine; Microscopy; Myoglobin; Protein Conformation; Spectrophotometry, Ultraviolet; Tryptophan; Valine | 2017 |
Structural and Functional Relevance of the Conserved Residue V13 in the Triheme Cytochrome PpcA from Geobacter sulfurreducens.
Topics: Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Geobacter; Heme; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Valine | 2019 |