heme has been researched along with proline in 22 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (36.36) | 18.7374 |
| 1990's | 4 (18.18) | 18.2507 |
| 2000's | 5 (22.73) | 29.6817 |
| 2010's | 5 (22.73) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Koshy, TI; Luntz, TL; Margoliash, E; Schejter, A | 1 |
| Detlefsen, DJ; Pecoraro, VL; Thanabal, V; Wagner, G | 1 |
| Morgan, WT | 1 |
| Gnarra, DJ; Green, D; Honig, GR; Mason, RG; Maurer, HS; Shamsuddin, M; Vida, LN | 1 |
| Margoliash, E; Putterman, GJ; Sherman, F | 1 |
| Labie, D; Solal, MC | 1 |
| Hutterer, F; Klion, FM; Popper, H; Schaffner, F; Wengraf, A | 1 |
| Hutner, SH; Tamburro, KM | 1 |
| Craigie, JS; Laycock, MV | 1 |
| Alperin, JB; Brimhall, B; Jones, RT; Schneider, RG; Ueda, S | 1 |
| Bersch, B; Brutscher, B; Marion, D; Meyer, TE | 1 |
| Fisher, MB; Fujii-Kuriyama, Y; Rettie, AE; Yokotani, N; Zheng, YM | 1 |
| Nall, BT; Pierce, MM | 1 |
| Huang, TJ; Maines, MD; McCoubrey, WK | 1 |
| Babcock, GT; Durham, B; Ferguson-Miller, S; Geren, L; Hiser, C; Hoganson, CW; Millett, F; Mills, DA; Qian, J; Schmidt, B; Wang, K | 1 |
| Burstyn, JN; Cherney, MM; Clark, RW; Parks, RB; Roberts, GP; Youn, H | 1 |
| Burstyn, JN; Clark, RW; Pinkert, JC | 1 |
| Barr, I; Burstyn, JN; Chen, Y; Guo, F; Scheidemantle, BD; Senturia, R; Smith, AT | 1 |
| Alderton, W; Angell, AD; Beswick, PJ; Brown, D; Chambers, CL; Crowe, MC; Dawson, J; Hamlett, CC; Hodgson, ST; Kleanthous, S; Knowles, RG; Russell, LJ; Stocker, R; Woolven, JM; Young, RJ | 1 |
| Davidson, VL; Feng, M; Jensen, LM; Liu, A; Wei, X; Wilmot, CM; Yukl, ET | 1 |
| Otzen, D; Schneider, D; Tome, L; Weber, M | 1 |
| Basran, J; Carr, KH; Kwon, H; Lad, L; Moody, PCE; Raven, EL; Turner, DD | 1 |
22 other study(ies) available for heme and proline
| Article | Year |
|---|---|
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 |
Sequential 1H NMR assignments of iron(II) cytochrome c551 from Pseudomonas aeruginosa.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytochrome c Group; Ferrous Compounds; Heme; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Molecular Structure; Proline; Protein Conformation; Pseudomonas aeruginosa; X-Ray Diffraction | 1990 |
The histidine-rich glycoprotein of serum has a domain rich in histidine, proline, and glycine that binds heme and metals.
Topics: Animals; Binding Sites; Circular Dichroism; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Metals; Molecular Weight; Proline; Proteins; Rabbits | 1985 |
Hemoglobin Abraham Lincoln, beta32 (B14) leucine leads to proline. An unstable variant producing severe hemolytic disease.
Topics: Adult; Amino Acids; Anemia, Hemolytic; Carbon Isotopes; Carbon Monoxide; Chemical Precipitation; Chromatography, Ion Exchange; Chromium Isotopes; Electrophoresis; Erythrocytes; Female; Half-Life; Heme; Hemoglobins, Abnormal; Hot Temperature; Humans; Hydroxymercuribenzoates; Inclusion Bodies; Leucine; Methemoglobin; Proline; Reticulocytes; Sulfites | 1973 |
Identification of missense mutants by amino acid replacements in iso-1-cytochrome c from yeast.
Topics: Amino Acid Sequence; Binding Sites; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Thin Layer; Chymotrypsin; Cytochrome c Group; Electrophoresis; Genes; Heme; Hydrolysis; Isoleucine; Mutation; Peptides; Proline; RNA, Messenger; Saccharomyces cerevisiae; Serine; Threonine; Ultraviolet Rays | 1974 |
A new case of hemoglobin Genova 2 2 28(B10) Leu leads to Pro. Further studies on the mechanism of instability and defective synthesis.
Topics: Amino Acids; Blood Protein Electrophoresis; Carbon Isotopes; Child; Chromatography, Ion Exchange; Drug Stability; Electrophoresis, Starch Gel; Genetics, Medical; Heme; Hemoglobins; Hemoglobins, Abnormal; Hot Temperature; Humans; Italy; Leucine; Macromolecular Substances; Male; Mutation; Oxygen; Partial Pressure; Peptides; Proline; Reticulocytes | 1973 |
Hepatocellular adaptation and injury. Structural and biochemical changes following dieldrin and methyl butter yellow.
Topics: Animals; Chemical and Drug Induced Liver Injury; Dieldrin; DNA; Endoplasmic Reticulum; Enzyme Induction; Female; Heme; Histocytochemistry; Hypertrophy; Liver; Microscopy, Electron; Microsomes; Mitochondria, Liver; Mixed Function Oxygenases; Oxidative Phosphorylation; Oxidoreductases; p-Dimethylaminoazobenzene; Proline; Proteins; Rats | 1969 |
Carbohydrate-free media for Crithidia.
Topics: Animals; Anopheles; Arginine; Carbohydrates; Culex; Culture Media; Eukaryota; Glutamates; Glycerol; Heme; Hydrogen-Ion Concentration; Proline; Sorbitol; Succinates; Sucrose | 1971 |
Purification and characterization of cytochrome 553 from the chrysophycean alga Monochrysis lutheri.
Topics: Amino Acids; Arginine; Autoanalysis; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cytochromes; Dialysis; Electron Transport; Electrophoresis, Disc; Eukaryota; Freeze Drying; Heme; Histidine; Iron; Isoelectric Focusing; Methionine; Methods; Molecular Weight; Oxidation-Reduction; Photosynthesis; Proline; Quaternary Ammonium Compounds; Spectrophotometry; Sulfates; Tryptophan; Ultracentrifugation; Ultraviolet Rays | 1971 |
Hemoglobin sabine beta 91 (F 7) leu → pro. An unstable variant causing severe anemia with inclusion bodies.
Topics: Adolescent; Amino Acid Sequence; Anemia, Hemolytic; Blood Protein Electrophoresis; Chromatography; Chromium Isotopes; Erythrocyte Aging; Erythrocyte Count; Erythrocytes; Female; Fetal Hemoglobin; Globins; Heinz Bodies; Heme; Hemoglobinometry; Hemoglobins, Abnormal; Hemolysin Proteins; Histocytochemistry; Humans; Leucine; Methemoglobin; Microscopy, Fluorescence; Proline; Protein Binding; Reticulocytes; Splenectomy | 1969 |
1H and 13C NMR assignments and structural aspects of a ferrocytochrome c-551 from the purple phototrophic bacterium Ectothiorhodospira halophila.
Topics: Amino Acid Sequence; Bacterial Proteins; Carbon Isotopes; Cytochrome c Group; Heme; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides; Proline; Protein Structure, Secondary; Protons; Rhodospirillales; Sequence Homology, Amino Acid | 1995 |
Identification of a meander region proline residue critical for heme binding to cytochrome P450: implications for the catalytic function of human CYP4B1.
Topics: Animals; Aryl Hydrocarbon Hydroxylases; Binding Sites; Catalysis; Cytochrome P-450 Enzyme System; Heme; Humans; Hydroxylation; Insecta; Lauric Acids; Mutagenesis, Site-Directed; Proline; Rabbits; Rats; Serine; Steroid Hydroxylases; Testosterone | 1998 |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochrome c Group; Cytochromes c; Enzyme Stability; Fluorescence; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Proline; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae; Sequence Alignment; Thermodynamics | 2000 |
Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs.
Topics: Amino Acid Motifs; Amino Acid Substitution; Catalytic Domain; Circular Dichroism; Cysteine; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen-Ion Concentration; Metalloporphyrins; Peptide Fragments; Proline; Protein Binding; Protoporphyrins; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfhydryl Reagents | 2001 |
Role of the conserved arginine pair in proton and electron transfer in cytochrome C oxidase.
Topics: Alanine; Arginine; Catalysis; Conserved Sequence; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Kinetics; Lysine; Magnesium; Mutagenesis, Site-Directed; Photolysis; Proline; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet | 2004 |
Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA.
Topics: Amino Acid Substitution; Bacterial Proteins; Carbon Monoxide; Circular Dichroism; DNA-Binding Proteins; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins; Ferric Compounds; Ferrous Compounds; Fimbriae Proteins; Heme; Hemeproteins; Ligands; Oxidation-Reduction; Peptide Fragments; Proline; Protein Binding; Spectrophotometry; Trans-Activators | 2004 |
Modeling proline ligation in the heme-dependent CO sensor, CooA, using small-molecule analogs.
Topics: Bacterial Proteins; Carbon Monoxide; Computational Biology; Crystallography, X-Ray; Heme; Hemeproteins; Histidine; Imidazoles; Iron; Ligands; Models, Molecular; Molecular Structure; Proline; Pyrrolidines; Trans-Activators | 2006 |
DiGeorge critical region 8 (DGCR8) is a double-cysteine-ligated heme protein.
Topics: Animals; Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Horses; Humans; MicroRNAs; Muscle, Skeletal; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Porphyrins; Proline; Proteins; RNA-Binding Proteins; Selenomethionine; Spectrophotometry; Xenopus laevis | 2011 |
Heteroalicyclic carboxamidines as inhibitors of inducible nitric oxide synthase; the identification of (2R)-2-pyrrolidinecarboxamidine as a potent and selective haem-co-ordinating inhibitor.
Topics: Amidines; Enzyme Activation; Enzyme Inhibitors; Heme; Heterocyclic Compounds; Humans; Inhibitory Concentration 50; Models, Molecular; Molecular Structure; Nitric Oxide Synthase Type II; Proline | 2011 |
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Topics: Bacterial Proteins; Catalysis; Crystallography, X-Ray; Heme; Hemeproteins; Indolequinones; Kinetics; Ligands; Mass Spectrometry; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Proline; Tryptophan | 2012 |
A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer.
Topics: Cell Membrane; Cytochrome b Group; Dimerization; Heme; Hydrogen Bonding; Models, Molecular; Molecular Conformation; Mutation; Oxygen; Photosystem II Protein Complex; Proline; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Spectrophotometry | 2012 |
The role of Ala134 in controlling substrate binding and reactivity in ascorbate peroxidase.
Topics: Alanine; Ascorbate Peroxidases; Ascorbic Acid; Catalysis; Chromatography, High Pressure Liquid; Guaiacol; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Proline; Substrate Specificity | 2018 |