phenylalanine and cytochrome c-t

phenylalanine has been researched along with cytochrome c-t in 23 studies

Research

Studies (23)

Timeframe	Studies, this research(%)	All Research%
pre-1990	2 (8.70)	18.7374
1990's	6 (26.09)	18.2507
2000's	8 (34.78)	29.6817
2010's	7 (30.43)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Guillemette, JG; Inglis, SC; Johnson, JA; Smith, M	1
Hilgen, SE; Pielak, GJ	1
Brayer, GD; Louie, GV	1
Brayer, GD; Louie, GV; Pielak, GJ; Smith, M	1
Brayer, GD; Guillemette, JG; Lo, TP; Louie, GV; Smith, M	1
Auld, DS; Betz, SF; Doyle, DF; Pielak, GJ; Saunders, AJ; Young, GB	1
Durham, B; Hilgen-Willis, S; Liu, RQ; McLean, M; Millett, F; Pielak, GJ; Saunders, AJ; Sligar, SG; Willie, A	1
Feinberg, BA; Liu, X; Margoliash, E; Ryan, MD; Schejter, A; Zhang, C	1
Döpner, S; Harris, TR; Hildebrand, DP; Hildebrandt, P; Mauk, AG; Rosell, FI	1
Anderson, VE; Nukuna, BN; Sun, G	1
Amato, E; Grasso, D; La Rosa, C; Milardi, D; Pappalardo, M	1
Covian, R; Hellwig, P; Hunte, C; Macmillan, F; Meunier, B; Trumpower, BL; Wenz, T	1
Funahashi, Y; Inomata, T; Masuda, H; Ozawa, T; Takahashi, I	1
Hobbs, HR; Kirke, HM; Poliakoff, M; Thomas, NR	1
Adak, S; Dolai, S; Pal, S; Yadav, RK	1
Guo, L; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D	1
Castro, L; Demicheli, V; Kagan, VE; Kapralov, AA; Klein-Seetharaman, J; Maeda, A; Mylnikov, D; Peterson, J; Radi, R; Samhan-Arias, A; Tortora, V; Tyurina, YY; Vladimirov, YA; Weitz, AA; Yanamala, N	1
Dawson, PE; Romesberg, FE; Seo, YJ; Thielges, MC; Zimmermann, J	1
De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T	1
Hagras, MA; Stuchebrukhov, AA	1
De la Rosa, MA; Del Conte, R; Díaz-Moreno, I; Díaz-Moreno, S; Díaz-Quintana, A; García-Mauriño, SM; González-Arzola, K; Guerra-Castellano, A; Moreno-Beltrán, B; Santos-Ocaña, C; Turano, P; Velázquez-Campoy, A	1
Attar, F; Falahati, M; Mansouri, A; Mousavi, M; Saboury, AA	1
Cong, H; Geng, Z; Song, Q; Yu, B	1

Other Studies

23 other study(ies) available for phenylalanine and cytochrome c-t

Article	Year
Analysis of the invariant Phe82 residue of yeast iso-1-cytochrome c by site-directed mutagenesis using a phagemid yeast shuttle vector. Protein engineering, 1991, Volume: 4, Issue:5 Topics: Amino Acid Sequence; Base Sequence; Codon; Coliphages; Cytochrome c Group; Cytochromes c; Gene Expression; Genetic Vectors; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Plasmids; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins	1991
The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector. Protein engineering, 1991, Volume: 4, Issue:5 Topics: Alleles; Base Sequence; Codon; Coliphages; Cytochrome c Group; Cytochromes c; Gene Amplification; Genes, Fungal; Genetic Variation; Genetic Vectors; Glycerol; Lactates; Lactic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Plasmids; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Temperature; Transformation, Genetic	1991
A polypeptide chain-refolding event occurs in the Gly82 variant of yeast iso-1-cytochrome c. Journal of molecular biology, 1989, Nov-20, Volume: 210, Issue:2 Topics: Amino Acid Sequence; Computer Simulation; Cytochrome c Group; Cytochromes c; Electron Transport; Fungal Proteins; Glycine; Heme; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Water	1989
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position. Biochemistry, 1988, Oct-04, Volume: 27, Issue:20 Topics: Cytochrome c Group; Cytochromes c; Electron Transport; Heme; Mutation; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine	1988
Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c. Biochemistry, 1995, Jan-10, Volume: 34, Issue:1 Topics: Amino Acid Sequence; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Transport; Leucine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship	1995
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
Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c. Biochemistry, 1993, Jul-27, Volume: 32, Issue:29 Topics: Cytochrome c Group; Cytochromes b5; Cytochromes c; Electron Transport; Kinetics; Lasers; Osmolar Concentration; Phenylalanine; Photolysis; Ruthenium; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins	1993
Direct voltammetric observation of redox driven changes in axial coordination and intramolecular rearrangement of the phenylalanine-82-histidine variant of yeast iso-1-cytochrome c. Biochemistry, 1998, Sep-22, Volume: 37, Issue:38 Topics: Amino Acid Substitution; Animals; Cysteine; Cytochrome c Group; Cytochromes c; Electrochemistry; Histidine; Horses; Imidazoles; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine	1998
Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c. Biochemistry, 2000, Aug-01, Volume: 39, Issue:30 Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Enzyme Stability; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Structure-Activity Relationship; Tryptophan	2000
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
Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly. Archives of biochemistry and biophysics, 2005, Mar-01, Volume: 435, Issue:1 Topics: Animals; Binding Sites; Computer Simulation; Cytochromes c; Dipeptides; Enzyme Activation; Enzyme Inhibitors; Glycine; Horses; Models, Chemical; Models, Molecular; Motion; Multiprotein Complexes; Myocardium; Phenylalanine; Protein Binding; Protein Conformation; Protein Folding	2005
Mutational analysis of cytochrome b at the ubiquinol oxidation site of yeast complex III. The Journal of biological chemistry, 2007, Feb-09, Volume: 282, Issue:6 Topics: Aspartic Acid; Binding Sites; Crystallization; Cytochromes b; Cytochromes c; DNA Mutational Analysis; Electron Transport Complex III; Enzyme Activation; Enzyme Stability; Glutamic Acid; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Saccharomyces cerevisiae; Tyrosine; Ubiquinone	2007
Electron-transfer reactions through the associated interaction between cytochrome c and self-assembled monolayers of optically active cobalt(III) complexes: molecular recognition ability induced by the chirality of the cobalt(III) units. Chemistry (Weinheim an der Bergstrasse, Germany), 2007, Volume: 13, Issue:28 Topics: Cobalt; Cytochromes c; Electrodes; Electron Transport; Gold; Isomerism; Oxidation-Reduction; Phenylalanine; Surface Properties	2007
Homogeneous biocatalysis in both fluorous biphasic and supercritical carbon dioxide systems. Angewandte Chemie (International ed. in English), 2007, Volume: 46, Issue:41 Topics: Carbon Dioxide; Catalysis; Cytochromes c; Fluorine; Hydrophobic and Hydrophilic Interactions; Ions; Molecular Structure; Phenylalanine	2007
Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme. Biochimica et biophysica acta, 2008, Volume: 1784, Issue:5 Topics: Amino Acid Sequence; Animals; Ascorbate Peroxidases; Ascorbic Acid; Cytochromes c; Hydrogen Peroxide; Kinetics; Leishmania major; Models, Biological; Molecular Sequence Data; Mutant Proteins; Oxidation-Reduction; Peroxidases; Phenylalanine; Spectrum Analysis; Structure-Activity Relationship; Substrate Specificity; Tryptophan	2008
Ultrafast proteinquake dynamics in cytochrome c. Journal of the American Chemical Society, 2009, Mar-04, Volume: 131, Issue:8 Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan	2009
Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c/cardiolipin peroxidase complexes. Biochimica et biophysica acta, 2011, Volume: 1808, Issue:9 Topics: Animals; Cardiolipins; Computer Simulation; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen Peroxide; Iron; Magnetic Resonance Spectroscopy; Mitochondrial Membranes; Mutation; Myocardium; Oxygen; Oxygenases; Peroxidase; Peroxidases; Phenylalanine; Tyrosine	2011
Cyano groups as probes of protein microenvironments and dynamics. Angewandte Chemie (International ed. in English), 2011, Aug-29, Volume: 50, Issue:36 Topics: Cyanides; Cytochromes c; Kinetics; Molecular Dynamics Simulation; Phenylalanine; Protein Folding; Spectrophotometry, Infrared	2011
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
Internal switches modulating electron tunneling currents in respiratory complex III. Biochimica et biophysica acta, 2016, Volume: 1857, Issue:6 Topics: Crystallography, X-Ray; Cytochromes c; Electron Transport; Electron Transport Complex III; Electrons; Heme; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Phenylalanine; Protein Binding; Protein Conformation	2016
Structural basis of mitochondrial dysfunction in response to cytochrome Proceedings of the National Academy of Sciences of the United States of America, 2017, 04-11, Volume: 114, Issue:15 Topics: Cytochromes c; Humans; Magnetic Resonance Spectroscopy; Mitochondria; Mutation; Oxidative Stress; Peroxidases; Phenylalanine; Phosphorylation; Protein Conformation; Reactive Oxygen Species; Signal Transduction; Tyrosine	2017
Interaction of manganese nanoparticle with cytochrome c: A multi-spectroscopic study. International journal of biological macromolecules, 2018, Volume: 106 Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochromes c; Hydrophobic and Hydrophilic Interactions; Manganese; Metal Nanoparticles; Models, Molecular; Particle Size; Phenylalanine; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrum Analysis; Static Electricity; Temperature; Thermodynamics; Tryptophan; Tyrosine	2018
Using ZIF-8 as stationary phase for capillary electrophoresis separation of proteins. Talanta, 2018, Oct-01, Volume: 188 Topics: Animals; Cattle; Chickens; Cytochromes c; Electrophoresis, Capillary; Green Chemistry Technology; Imidazoles; Metal-Organic Frameworks; Muramidase; Nanoparticles; Phenylalanine; Proteins; Reproducibility of Results; Ribonuclease, Pancreatic; Serum Albumin, Bovine; Stereoisomerism; Zeolites	2018