Compounds > methionine
Page last updated: 2024-08-17

methionine and cytochrome c-t

methionine has been researched along with cytochrome c-t in 62 studies

Research

Studies (62)

TimeframeStudies, this research(%)All Research%
pre-19901 (1.61)18.7374
1990's7 (11.29)18.2507
2000's24 (38.71)29.6817
2010's28 (45.16)24.3611
2020's2 (3.23)2.80

Authors

AuthorsStudies
Hosokawa, Y; Moerschell, RP; Sherman, F; Tsunasawa, S1
Sherman, F; Stewart, JW; Tsunasawa, S1
Banci, L; Bertini, I; Bren, KL; Gray, HB; Sompornpisut, P; Turano, P1
Bren, KL; Casimiro, DR; Gray, HB; Lu, Y; Richards, JH1
Auld, DS; Betz, SF; Doyle, DF; Pielak, GJ; Saunders, AJ; Young, GB1
Silkstone, G; Stanway, G; Wilson, MT1
Attfield, K; Bowler, BE; Clayton, D; Dec, E; Dong, A; Hammack, B; Sarisky, C1
Baxter, SM; Fetrow, JS1
Blouin, C; Guillemette, JG; Wallace, CJ1
Bigotti, MG; Bren, KL; Cutruzzolà, F; Russell, BS; Zhong, L1
Dutca, LM; Kostić, NM; Milović, NM1
Kawachi, R; Kume, T; Nagasawa, N; Nishio, T; Oku, T; Satoh, T; Suruga, K; Yamada, S1
Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Lushington, GH; Rodgers, KR; Silchenko, S1
Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Rodgers, KR1
Bowler, BE; Martinez, RE1
Bartalesi, I; Bertini, I; Di Rocco, G; Ranieri, A; Rosato, A; Vanarotti, M; Vasos, PR; Viezzoli, MS1
Hasegawa, J; Hemmi, H; Mita, H; Sambongi, Y; Tachiiri, N; Takayama, SJ; Yamamoto, Y1
Dohmae, N; Iizuka, T; Ishida, M; Isogai, Y; Oku, T; Shiro, Y1
Anderson, VE; Nukuna, BN; Sun, G1
Cianetti, S; Kruglik, SG; Martin, JL; Négrerie, M; Vos, MH1
Dai, Y; Dent, P; Grant, S; Li, W; Pei, XY; Rahmani, M1
Clementi, ME; Misiti, F1
Hoshino, K; Igarashi, K; Kashiwagi, K; Momiyama, E; Nishimura, K; Sakai, S; Toida, T; Yoshida, K1
Cremeens, ME; Dawson, PE; Fujisaki, H; Matsuda, S; Romesberg, FE; Sagle, LB; Straub, JE; Zhang, Y; Zimmermann, J1
Battistuzzi, G; Borsari, M; Bortolotti, CA; Casalini, S; Ranieri, A; Sola, M1
Anderson, VE; Guo, M; Kenney, ME; Kim, J; Oleinick, NL; Rodriguez, ME1
Hou, Y; Li, L; Liu, G; Tong, Y; Wei, H; Wu, L; Wu, S1
Bren, KL; Elliott, SJ; Kaur, R; Michel, LV; Senguen, FT; Ye, T1
Ferguson, SJ; Harvat, EM; Redfield, C; Stevens, JM1
King, FL; Zhao, T1
Back, J; Baskin, JM; Bertozzi, CR; de Jong, L; de Koning, LJ; de Koster, CG; Hiemstra, H; Kramer, G; Nessen, MA; Smeenk, LE; van Maarseveen, JH1
Brennan, LA; Cowell, T; Giblin, F; Kantorow, M; Lee, W1
Brennan, LA; Kantorow, M; Lee, W1
Clement, MH; Gralla, EB; Longo, VD; Martins, J; Sehati, S; Valentine, JS; Xu, L1
Bowman, SE; Bren, KL; Can, M; Elliott, SJ; Levin, BD1
Adak, S; Dolai, S; Pal, S; Yadav, RK1
Małolepsza, E; Straub, JE; Zhang, P1
De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T1
Battistuzzi, G; Bellei, M; Bortolotti, CA; Di Rocco, G; Hildebrandt, P; Salewski, J; Sola, M1
Dantas, JM; Londer, YY; Morgado, L; Pokkuluri, PR; Salgueiro, CA; Simões, T1
Bren, KL; Hughes, G; Josephs, TM; Ledgerwood, EC; Liptak, MD; Lo, A; Smith, RM; Wilbanks, SM1
Callizot, N; Combes, M; Poindron, P; Steinschneider, R1
Hirota, S; Nagao, S; Nugraheni, AD; Ogura, T; Yanagisawa, S1
Ahn, SW; Straub, JE; Zhang, P1
Fitzgerald, MC; Strickland, EC; Xu, Y1
Ando, Y; Hirota, S; Nagao, S; Nugraheni, AD; Ren, C; Wang, Z1
Alonso-Mori, R; Casa, D; Hadt, RG; Hedman, B; Hodgson, KO; Kroll, T; Lundberg, M; Sokaras, D; Solomon, EI; Upton, MH; Weng, TC; Wilson, SA; Yan, JJ1
Bren, KL; Elliott, SJ; Levin, BD; Sullivan, KK; Walsh, KA1
Bandi, S; Bowler, BE1
Sharma, GS; Singh, LR1
Castegna, A; Cianciulli, A; Iacobazzi, V; Infantino, V; Mazzone, M; Menga, A; Palmieri, EM; Palmieri, F; Scilimati, A1
Battista, T; Cervelli, M; Ciaccio, C; Coletta, M; Fiorucci, L; Howes, BD; Mariottini, P; Santucci, R; Smulevich, G; Tognaccini, L1
Hirota, S; Nagao, S; Wang, Z; Yamashiro, N1
Baratto, MC; Fittipaldi, M; Howes, BD; Milazzo, L; Piro, MC; Pogni, R; Santucci, R; Sinibaldi, F; Smulevich, G; Tognaccini, L1
Hirota, S; Matsumoto, Y; Nagao, S; Nugraheni, AD; Ren, C; Yamanaka, M1
Pletneva, EV; Zhong, F1
Benabbas, A; Champion, PM1
Al-Refaie, W; Hoffman, RM; Miki, K; Tan, Y; Xu, M1
Nesterova, AM; Remenshchikov, VE; Vladimirov, GK; Vladimirov, YA; Volkov, VV1
Deng, Y; Hoke, KR; Pletneva, EV; Weaver, ML1
Alonso-Mori, R; Bergmann, U; Biasin, E; Chollet, M; Driel, TBV; Gaffney, KJ; Gee, LB; Glownia, JM; Hadt, RG; Hartsock, RW; Hedman, B; Hodgson, KO; Kjaer, KS; Kroll, T; Kunnus, K; Lim, H; Mara, MW; Nelson, S; Reinhard, ME; Sokaras, D; Solomon, EI; Weninger, C1
Ben Aoun, S; Ibrahim, SM1

Other Studies

62 other study(ies) available for methionine and cytochrome c-t

ArticleYear
The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation.
    The Journal of biological chemistry, 1990, Nov-15, Volume: 265, Issue:32

    Topics: Acetylation; Amino Acid Sequence; Aminopeptidases; Base Sequence; Chromatography, High Pressure Liquid; Cytochrome c Group; Cytochromes c; Methionine; Methionyl Aminopeptidases; Molecular Sequence Data; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity; Transformation, Genetic

1990
Methionine or not methionine at the beginning of a protein.
    BioEssays : news and reviews in molecular, cellular and developmental biology, 1985, Volume: 3, Issue:1

    Topics: Amino Acid Sequence; Base Sequence; Cytochrome c Group; Cytochromes c; Methionine; Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

1985
Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity.
    Biochemistry, 1995, Sep-12, Volume: 34, Issue:36

    Topics: Alanine; Amino Acid Sequence; Animals; Crystallography, X-Ray; Cyanides; Cytochrome c Group; Cytochromes c; Heme; Horses; Ligands; Magnetic Resonance Spectroscopy; Methionine; Molecular Sequence Data; Myocardium; Protein Conformation; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions

1995
Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met-80-->Ala iso-1-cytochrome c.
    Proceedings of the National Academy of Sciences of the United States of America, 1993, Dec-15, Volume: 90, Issue:24

    Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; Cytochromes; Cytochromes c; Escherichia coli; Heme; Horses; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Protein Engineering; Recombinant Proteins; Restriction Mapping; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription, Genetic

1993
Probing weakly polar interactions in cytochrome c.
    Protein science : a publication of the Protein Society, 1993, Volume: 2, Issue:12

    Topics: Cysteine; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Tyrosine

1993
Yeast iso-1-cytochrome c met80X mutants: the pKa of the spin state transition as a probe for haem pocket flexibility.
    Biochemical Society transactions, 1998, Volume: 26, Issue:4

    Topics: Cytochrome c Group; Cytochromes c; Heme; Hydrogen-Ion Concentration; Methionine; Molecular Probes; Mutation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

1998
The magnitude of changes in guanidine-HCl unfolding m-values in the protein, iso-1-cytochrome c, depends upon the substructure containing the mutation.
    Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:8

    Topics: Circular Dichroism; Cytochrome c Group; Cytochromes c; Guanidine; Hydrochloric Acid; Methionine; Models, Molecular; Molecular Structure; Mutagenesis; Protein Folding; Saccharomyces cerevisiae Proteins; Solvents; Spectrum Analysis; Static Electricity; Thermodynamics

1998
Hydrogen exchange behavior of [U-15N]-labeled oxidized and reduced iso-1-cytochrome c.
    Biochemistry, 1999, Apr-06, Volume: 38, Issue:14

    Topics: Cysteine; Cytochrome c Group; Cytochromes c; Enzyme Stability; Iron; Kinetics; Methionine; Models, Molecular; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Denaturation; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions; Threonine

1999
Resolving the individual components of a pH-induced conformational change.
    Biophysical journal, 2001, Volume: 81, Issue:4

    Topics: Animals; Arginine; Colon, Sigmoid; Cytochrome c Group; Cytochromes c; Horses; Hydrogen-Ion Concentration; Iron; Isomerism; Kinetics; Lysine; Methionine; Mitochondria; Mutagenesis, Site-Directed; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Titrimetry

2001
Backbone dynamics and hydrogen exchange of Pseudomonas aeruginosa ferricytochrome c(551).
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2003, Volume: 8, Issue:1-2

    Topics: Amino Acid Sequence; Bacterial Proteins; Cytochrome c Group; Cytochromes c; Deuterium; Hydrogen; Hydrogen Bonding; Kinetics; Methionine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Proline; Pseudomonas aeruginosa; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship

2003
Transition-metal complexes as enzyme-like reagents for protein cleavage: complex cis-[Pt(en)(H2O)2]2+ as a new methionine-specific protease.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2003, Oct-17, Volume: 9, Issue:20

    Topics: Amino Acid Sequence; Animals; Caseins; Cattle; Cyanogen Bromide; Cytochromes c; Endopeptidases; Horses; Indicators and Reagents; Kinetics; Methionine; Models, Chemical; Molecular Sequence Data; Molecular Structure; Molecular Weight; Palladium; Platinum Compounds; Proteins; Substrate Specificity

2003
Radiation-induced enhancement of nitrite reducing activity of cytochrome c.
    Journal of agricultural and food chemistry, 2003, Nov-05, Volume: 51, Issue:23

    Topics: Circular Dichroism; Cytochromes c; Drug Stability; Gamma Rays; Heme; Methionine; Nitrite Reductases; Nitrites; Oxidation-Reduction; Protein Folding

2003
Comparison of thioethers and sulfoxides as axial ligands for N-acetylmicroperoxidase-8: implications for oxidation of methionine-80 in cytochrome c.
    Inorganic chemistry, 2003, Nov-17, Volume: 42, Issue:23

    Topics: Animals; Choline; Cytochromes c; Dimethyl Sulfoxide; Ferric Compounds; Ferrous Compounds; Hemeproteins; Horses; Ligands; Methionine; Models, Molecular; Myocardium; Oxidation-Reduction; Peptide Fragments; Spectrophotometry; Spectrum Analysis, Raman; Thermodynamics

2003
A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.
    Biochemistry, 2004, Feb-17, Volume: 43, Issue:6

    Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship

2004
Proton-mediated dynamics of the alkaline conformational transition of yeast iso-1-cytochrome c.
    Journal of the American Chemical Society, 2004, Jun-02, Volume: 126, Issue:21

    Topics: Amino Acid Substitution; Cytochromes c; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Lysine; Methionine; Protein Conformation; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry

2004
Protein stability and mutations in the axial methionine loop of a minimal cytochrome c.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2004, Volume: 9, Issue:5

    Topics: Amino Acids; Bacillus; Cytochromes c; Enzyme Stability; Guanidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Protein Denaturation; Protein Folding; Thermodynamics; Water

2004
Effects of axial methionine coordination on the in-plane asymmetry of the heme electronic structure of cytochrome c.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2004, Volume: 9, Issue:6

    Topics: Cytochromes c; Magnetic Resonance Spectroscopy; Methionine; Models, Chemical; Models, Molecular; Oxidation-Reduction; Protein Conformation

2004
Design and synthesis of de novo cytochromes c.
    Biochemistry, 2004, Aug-03, Volume: 43, Issue:30

    Topics: Amino Acid Sequence; Animals; Cattle; Cytochromes b; Cytochromes c; Genes, Synthetic; Helix-Loop-Helix Motifs; Heme; Histidine; Methionine; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfides

2004
Hydroxyl radical oxidation of cytochrome c by aerobic radiolysis.
    Free radical biology & medicine, 2004, Oct-15, Volume: 37, Issue:8

    Topics: Aerobiosis; Amino Acid Sequence; Animals; Cytochromes c; Dose-Response Relationship, Radiation; Electrons; Heme; Horses; Hydroxyl Radical; Hydroxylation; Intracellular Membranes; Methionine; Mitochondria, Heart; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Conformation; Pulse Radiolysis; Rats; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet; Tyrosine

2004
Photodissociation of heme distal methionine in ferrous cytochrome C revealed by subpicosecond time-resolved resonance Raman spectroscopy.
    Journal of the American Chemical Society, 2004, Nov-03, Volume: 126, Issue:43

    Topics: Cytochromes c; Heme; Kinetics; Methionine; Photochemistry; Spectrum Analysis, Raman

2004
The farnesyltransferase inhibitor L744832 potentiates UCN-01-induced apoptosis in human multiple myeloma cells.
    Clinical cancer research : an official journal of the American Association for Cancer Research, 2005, Jun-15, Volume: 11, Issue:12

    Topics: Alkyl and Aryl Transferases; Antineoplastic Agents; Apoptosis; Blotting, Western; CDC2 Protein Kinase; Cell Line, Tumor; Cytochromes c; DNA-Binding Proteins; Dose-Response Relationship, Drug; Drug Synergism; Farnesyltranstransferase; Glycogen Synthase Kinase 3; Humans; JNK Mitogen-Activated Protein Kinases; Methionine; Multiple Myeloma; Phosphorylation; Ribosomal Protein S6 Kinases, 70-kDa; STAT3 Transcription Factor; Staurosporine; Trans-Activators

2005
Substitution of methionine 35 inhibits apoptotic effects of Abeta(31-35) and Abeta(25-35) fragments of amyloid-beta protein in PC12 cells.
    Medical science monitor : international medical journal of experimental and clinical research, 2005, Volume: 11, Issue:11

    Topics: Amino Acid Substitution; Amyloid beta-Peptides; Animals; Apoptosis; Caspases; Cytochromes c; Humans; Methionine; Neurons; Norleucine; PC12 Cells; Peptide Fragments; Rats

2005
Polyamine transport by mammalian cells and mitochondria: role of antizyme and glycosaminoglycans.
    The Journal of biological chemistry, 2005, Dec-30, Volume: 280, Issue:52

    Topics: Amino Acid Sequence; Animals; Blotting, Western; Calcium; Cell Line; Codon, Initiator; Cytochromes c; Dose-Response Relationship, Drug; Fibroblasts; Glycosaminoglycans; Heparitin Sulfate; Humans; Kinetics; Liver; Lung; Magnesium; Methionine; Mice; Mitochondria; Mitochondria, Liver; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; NIH 3T3 Cells; Plasmids; Polyamines; Protein Isoforms; Protein Structure, Tertiary; Proteins; Rats; RNA, Messenger; Spermine; Time Factors; Transfection

2005
Efforts toward developing direct probes of protein dynamics.
    Journal of the American Chemical Society, 2006, May-10, Volume: 128, Issue:18

    Topics: Animals; Cytochromes c; Deuterium; Horses; Methionine; Models, Molecular; Protein Conformation; Quantum Theory; Spectrophotometry, Infrared; Thermodynamics

2006
Electron transfer and electrocatalytic properties of the immobilized methionine80alanine cytochrome c variant.
    The journal of physical chemistry. B, 2008, Feb-07, Volume: 112, Issue:5

    Topics: Alanine; Amino Acid Substitution; Catalysis; Cytochromes c; Electrochemistry; Electron Transport; Enzymes, Immobilized; Hydrogen-Ion Concentration; Indicators and Reagents; Methionine; Oxygen; Protein Conformation; Saccharomyces cerevisiae; Thermodynamics

2008
Oxidative modification of cytochrome c by singlet oxygen.
    Free radical biology & medicine, 2008, May-01, Volume: 44, Issue:9

    Topics: Animals; Apoptosis; Cytochromes c; Histidine; Horses; Hydrogen-Ion Concentration; Methionine; Mitochondria; Models, Biological; Models, Chemical; Myocardium; Oxygen; Photochemotherapy; Reactive Oxygen Species; Tryptophan

2008
Protection by bicyclol derivatives against acetaminophen-induced acute liver failure in mice and its active mechanism.
    Liver international : official journal of the International Association for the Study of the Liver, 2008, Volume: 28, Issue:9

    Topics: Acetaminophen; Adenosine Triphosphate; Analgesics, Non-Narcotic; Animals; Apoptosis; Apoptosis Inducing Factor; Benzodioxoles; Biphenyl Compounds; Cytochromes c; Glutathione; Liver; Liver Failure, Acute; Male; Membrane Potential, Mitochondrial; Methionine; Mice; Mitochondria, Liver; Mitochondrial Swelling; Necrosis

2008
Methionine ligand lability of type I cytochromes c: detection of ligand loss using protein film voltammetry.
    Journal of the American Chemical Society, 2008, May-28, Volume: 130, Issue:21

    Topics: Animals; Cytochromes c; Electrochemistry; Electrodes; Graphite; Ligands; Methionine; Pseudomonas aeruginosa

2008
Probing the heme-binding site of the cytochrome c maturation protein CcmE.
    Biochemistry, 2009, Mar-03, Volume: 48, Issue:8

    Topics: Amino Acid Substitution; Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mutant Proteins; Mutation; Oxidation-Reduction; Potentiometry; Protein Structure, Secondary; Tyrosine

2009
Direct determination of the primary binding site of cisplatin on cytochrome C by mass spectrometry.
    Journal of the American Society for Mass Spectrometry, 2009, Volume: 20, Issue:6

    Topics: Animals; Binding Sites; Cisplatin; Cytochromes c; Fourier Analysis; Horses; Mass Spectrometry; Methionine; Trypsin

2009
Selective enrichment of azide-containing peptides from complex mixtures.
    Journal of proteome research, 2009, Volume: 8, Issue:7

    Topics: Alanine; Amino Acid Sequence; Azides; Cations; Chromatography, Ion Exchange; Cross-Linking Reagents; Cytochromes c; Glutarates; Kinetics; Mass Spectrometry; Methionine; Molecular Sequence Data; Peptides; Proteome; Proteomics

2009
Deletion of mouse MsrA results in HBO-induced cataract: MsrA repairs mitochondrial cytochrome c.
    Molecular vision, 2009, May-15, Volume: 15

    Topics: Animals; Cataract; Cell Line; Cytochromes c; Disease Models, Animal; Gene Deletion; Humans; Hyperbaric Oxygenation; Lens, Crystalline; Light; Methionine; Methionine Sulfoxide Reductases; Mice; Mice, Knockout; Mitochondrial Proteins; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Scattering, Radiation; Spectrometry, Mass, Electrospray Ionization

2009
TXNL6 is a novel oxidative stress-induced reducing system for methionine sulfoxide reductase a repair of α-crystallin and cytochrome C in the eye lens.
    PloS one, 2010, Nov-04, Volume: 5, Issue:11

    Topics: alpha-Crystallins; Blotting, Western; Cell Line; Cytochromes c; Cytosol; Gene Expression Profiling; Humans; Hydrogen Peroxide; Kidney; Lens, Crystalline; Methionine; Methionine Sulfoxide Reductases; Mitochondria; Oxidants; Oxidation-Reduction; Oxidative Stress; Retina; Reverse Transcriptase Polymerase Chain Reaction; Thioredoxins

2010
Metabolic alterations in yeast lacking copper-zinc superoxide dismutase.
    Free radical biology & medicine, 2011, Jun-01, Volume: 50, Issue:11

    Topics: Cell Growth Processes; Cell Respiration; Cytochromes c; Ethanol; Glucose; Lysine; Methionine; Mitochondria; Mutation; Oxidative Stress; Oxygen; Oxygen Consumption; Saccharomyces cerevisiae Proteins; Superoxide Dismutase; Yeasts

2011
Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study.
    The journal of physical chemistry. B, 2011, Oct-13, Volume: 115, Issue:40

    Topics: Bacteria; Cytochromes c; Electrochemical Techniques; Electrodes; Graphite; Ligands; Methionine; Mutation; Oxidation-Reduction; Protein Folding; Temperature; Thermodynamics

2011
Role of proximal methionine residues in Leishmania major peroxidase.
    Archives of biochemistry and biophysics, 2011, Volume: 515, Issue:1-2

    Topics: Animals; Base Sequence; Cytochromes c; DNA Primers; Kinetics; Leishmania; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Peroxidases; Spectrophotometry, Ultraviolet

2011
Dynamics of methionine ligand rebinding in cytochrome c.
    The journal of physical chemistry. B, 2012, Jun-14, Volume: 116, Issue:23

    Topics: Binding Sites; Cytochromes c; Ligands; Methionine; Models, Molecular; Molecular Dynamics Simulation

2012
Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.
    The journal of physical chemistry. B, 2012, May-17, Volume: 116, Issue:19

    Topics: Cytochromes c; Fatty Acids; Heme; Humans; Iron; Kinetics; Lysine; Methionine; Mutation; Nitro Compounds; Oxidation-Reduction; Phenylalanine; Protein Stability; Protein Structure, Quaternary; Recombinant Proteins; Silver Compounds; Static Electricity; Sulfhydryl Compounds; Tyrosine; Water

2012
Role of Met80 and Tyr67 in the low-pH conformational equilibria of cytochrome c.
    Biochemistry, 2012, Jul-31, Volume: 51, Issue:30

    Topics: Cytochromes c; Hydrogen-Ion Concentration; Methionine; Protein Conformation; Protein Unfolding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Tyrosine

2012
Role of Met(58) in the regulation of electron/proton transfer in trihaem cytochrome PpcA from Geobacter sulfurreducens.
    Bioscience reports, 2012, Nov-30, Volume: 33, Issue:1

    Topics: Bacterial Proteins; Cytochromes c; Electron Transport; Escherichia coli; Geobacter; Heme; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Solutions; Thermodynamics

2012
Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013, Volume: 18, Issue:3

    Topics: Amino Acid Substitution; Apoptosis; Caspases; Cell Line, Tumor; Cytochromes c; Enzyme Activation; Glycine; Humans; Iron; Methionine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Point Mutation; Protein Conformation

2013
Operational dissection of β-amyloid cytopathic effects on cultured neurons.
    Journal of neuroscience research, 2013, Volume: 91, Issue:5

    Topics: Amyloid beta-Peptides; Animals; Apoptosis; Catalase; Cells, Cultured; Cerebral Cortex; Cytochromes c; Embryo, Mammalian; Female; Hippocampus; Methionine; Nerve Net; Neurons; Organ Culture Techniques; Oxidative Stress; Peptide Fragments; Pregnancy; Rats; Rats, Wistar; Synapses

2013
Interaction of dimeric horse cytochrome c with cyanide ion.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013, Volume: 18, Issue:3

    Topics: Animals; Cyanides; Cytochromes c; Horses; Iron; Methionine; Models, Molecular; Protein Binding; Protein Multimerization; Protein Stability; Protein Structure, Secondary; Temperature

2013
"Strange kinetics" in the temperature dependence of methionine ligand rebinding dynamics in cytochrome c.
    The journal of physical chemistry. B, 2013, Jun-20, Volume: 117, Issue:24

    Topics: Cytochromes c; Kinetics; Ligands; Methionine; Models, Molecular; Molecular Dynamics Simulation; Temperature

2013
Thermodynamic analysis of protein folding and stability using a tryptophan modification protocol.
    Analytical chemistry, 2014, Jul-15, Volume: 86, Issue:14

    Topics: Amino Acid Sequence; Cytochromes c; Methionine; Molecular Sequence Data; Muramidase; Protein Folding; Protein Stability; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfonium Compounds; Thermodynamics; Tryptophan

2014
Self-oxidation of cytochrome c at methionine80 with molecular oxygen induced by cleavage of the Met-heme iron bond.
    Molecular bioSystems, 2014, Volume: 10, Issue:12

    Topics: Cytochromes c; Dithiothreitol; Heme; Humans; Iron; Liposomes; Methionine; Oxidation-Reduction; Oxygen; Protein Conformation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2014
Resonant inelastic X-ray scattering on ferrous and ferric bis-imidazole porphyrin and cytochrome c: nature and role of the axial methionine-Fe bond.
    Journal of the American Chemical Society, 2014, Dec-31, Volume: 136, Issue:52

    Topics: Cytochromes c; Electron Transport; Imidazoles; Iron; Metalloporphyrins; Methionine; Quantum Theory; X-Ray Diffraction

2014
Methionine ligand lability of homologous monoheme cytochromes c.
    Inorganic chemistry, 2015, Jan-05, Volume: 54, Issue:1

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cytochromes c; Electrochemical Techniques; Electrodes; Escherichia coli; Gene Expression; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Sequence Data; Nitrosomonas europaea; Oxidation-Reduction; Protein Folding; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Shewanella; Temperature; Thermodynamics

2015
Effect of an Ala81His mutation on the Met80 loop dynamics of iso-1-cytochrome c.
    Biochemistry, 2015, Mar-10, Volume: 54, Issue:9

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Cytochromes c; Histidine; Hydrogen-Ion Concentration; Methionine; Models, Molecular; Molecular Sequence Data; Mutation, Missense; Protein Folding; Protein Stability; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Temperature

2015
Conformational status of cytochrome c upon N-homocysteinylation: Implications to cytochrome c release.
    Archives of biochemistry and biophysics, 2017, Jan-15, Volume: 614

    Topics: Animals; Apoptosis; Cardiolipins; Cattle; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Homocysteine; Iron; Ligands; Methionine; Myocardium; Oxygen; Peroxidase; Peroxidases; Protein Conformation; Protein Processing, Post-Translational; Spectrophotometry, Ultraviolet

2017
SLC25A26 overexpression impairs cell function via mtDNA hypermethylation and rewiring of methyl metabolism.
    The FEBS journal, 2017, Volume: 284, Issue:6

    Topics: Adenosine Triphosphate; Amino Acid Transport Systems; Apoptosis; Calcium-Binding Proteins; Cell Cycle; Cell Line, Tumor; Cell Proliferation; Cisplatin; Cytochromes c; DNA Methylation; DNA, Mitochondrial; Drug Resistance, Neoplasm; Female; Gene Expression Regulation, Neoplastic; Glutathione; Humans; Methionine; Mitochondria; Promoter Regions, Genetic; S-Adenosylmethionine; Uterine Cervical Neoplasms

2017
The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.
    Journal of inorganic biochemistry, 2017, Volume: 169

    Topics: Alanine; Circular Dichroism; Cytochromes c; Heme; Histamine; Humans; Kinetics; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Recombinant Proteins; Structure-Activity Relationship; Tyrosine

2017
Effect of methionine80 heme coordination on domain swapping of cytochrome c.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017, Volume: 22, Issue:5

    Topics: Calorimetry; Cytochromes c; Heme; Humans; Kinetics; Methionine

2017
Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only.
    Biochemistry, 2017, 04-04, Volume: 56, Issue:13

    Topics: Animals; Carbon Monoxide; Cardiolipins; Cloning, Molecular; Cytochromes c; Escherichia coli; Gene Expression; Genes, Synthetic; Histidine; Horses; Hydrogen Bonding; Methionine; Myocardium; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Unfolding; Recombinant Proteins; Temperature

2017
Oxidative modification of methionine80 in cytochrome c by reaction with peroxides.
    Journal of inorganic biochemistry, 2018, Volume: 182

    Topics: Cardiolipins; Cytochromes c; Liposomes; Methionine; Oxidation-Reduction; Peroxidase; Peroxides; Phosphatidylcholines; Tandem Mass Spectrometry

2018
Ligation and Reactivity of Methionine-Oxidized Cytochrome c.
    Inorganic chemistry, 2018, May-21, Volume: 57, Issue:10

    Topics: Amino Acid Sequence; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Imidazoles; Iron; Ligands; Methionine; Models, Biological; Oxidation-Reduction; Spectrum Analysis, Raman; Sulfoxides; Yeasts

2018
Adiabatic Ligand Binding in Heme Proteins: Ultrafast Kinetics of Methionine Rebinding in Ferrous Cytochrome c.
    The journal of physical chemistry. B, 2018, 12-13, Volume: 122, Issue:49

    Topics: Animals; Binding Sites; Cytochromes c; Ferrous Compounds; Heart; Horses; Kinetics; Ligands; Methionine; Thermodynamics

2018
Methioninase Gene Therapy.
    Methods in molecular biology (Clifton, N.J.), 2019, Volume: 1866

    Topics: Adenoviridae; Animals; Apoptosis; Bystander Effect; Carbon-Sulfur Lyases; Cell Line, Tumor; Cytochromes c; Genetic Therapy; Green Fluorescent Proteins; Humans; Methionine; Mice, Nude; Mitochondria; Permeability; Plasmids; Proto-Oncogene Proteins c-bcl-2; Rats; Recombinant Proteins; Selenomethionine; Tumor Burden

2019
Comparison of the Size and Properties of the Cytochrome c/Cardiolipin Nanospheres in a Sediment and Non-polar Medium.
    Biochemistry. Biokhimiia, 2019, Volume: 84, Issue:8

    Topics: Animals; Apoptosis; Cardiolipins; Crystallization; Cytochromes c; Dynamic Light Scattering; Fluorescence Resonance Energy Transfer; Heme; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Lipid Bilayers; Lipid Peroxidation; Methanol; Methionine; Mitochondria, Heart; Mitochondrial Membranes; Nanospheres; Protein Conformation; Protein Unfolding

2019
A Heme Propionate Staples the Structure of Cytochrome
    Inorganic chemistry, 2019, Oct-21, Volume: 58, Issue:20

    Topics: Coordination Complexes; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Propionates

2019
Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.
    Nature communications, 2021, 02-17, Volume: 12, Issue:1

    Topics: Cytochromes c; Electron Transport; Ferrous Compounds; Heme; Iron; Metals; Methionine; Molecular Dynamics Simulation; Photolysis; Spectrometry, X-Ray Emission

2021
An engineered thermally tolerant apo-cytochrome scaffold for metal-less incorporation of heme derivative.
    PloS one, 2023, Volume: 18, Issue:11

    Topics: Alanine; Cytochromes c; Heme; Ligands; Methionine; Molecular Docking Simulation; Oxidation-Reduction

2023