proline has been researched along with cytochrome c-t in 21 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (38.10) | 18.7374 |
| 1990's | 2 (9.52) | 18.2507 |
| 2000's | 6 (28.57) | 29.6817 |
| 2010's | 4 (19.05) | 24.3611 |
| 2020's | 1 (4.76) | 2.80 |
| Authors | Studies |
|---|---|
| Nall, BT; Ramdas, L; White, TB; Wood, LC; Zuniga, EH | 1 |
| Berget, PB; Nall, BT; White, TB | 1 |
| Muthukrishnan, K; Nall, BT; Ramdas, L; White, TB; Wood, LC | 1 |
| Nall, BT; Ramdas, L; White, TB; Wood, LC | 1 |
| Ernst, JF; Goldstein, D; Hampsey, DM; Rackovsky, S; Sherman, F; Stewart, JW | 1 |
| Nall, BT; Ramdas, L; Sherman, F | 1 |
| Nall, BT; Ramdas, L | 1 |
| Nall, BT; Veeraraghavan, S | 1 |
| Begley, TJ; Boose, TL; Fetrow, JS; Gilden, BM; Haas, BJ; Mellender, SJ; Spitzer, JS | 1 |
| Nall, BT; Pierce, MM | 1 |
| Bigotti, MG; Bren, KL; Cutruzzolà, F; Russell, BS; Zhong, L | 1 |
| MARGOLIASH, E | 1 |
| Ko, JH; Lee, SJ; Lim, KT | 1 |
| Baddam, S; Bowler, BE | 1 |
| Donald, SP; Hu, CA; Lin, WW; Liu, Z; Obie, C; Phang, JM; Steel, G; Valle, D; Yu, J | 1 |
| Lee, SJ; Lim, KT | 1 |
| Bowler, BE; Finnegan, ML | 1 |
| Mark, FC; Oellermann, M; Pörtner, HO | 1 |
| Gaviraghi, A; Oliveira, MF; Soares, JB | 1 |
| Durand, G; Giraud, MF; Gonzalez, C; Lascu, I; Légiot, A; Manon, S; Simonyan, L | 1 |
| Adams, HR; Fujii, S; Hough, MA; Igawa, T; Kawahara, K; Ohkubo, T; Oki, H; Sambongi, Y; Ueda, K; Yoshimi, T | 1 |
1 review(s) available for proline and cytochrome c-t
| Article | Year |
|---|---|
THE AMINO ACID SEQUENCE OF CYTOCHROME C IN RELATION TO ITS FUNCTION AND EVOLUTION.
Topics: Amino Acid Sequence; Amino Acids; Animals; Biological Evolution; Chemical Phenomena; Chemistry; Cytochromes; Cytochromes c; Horses; Mutation; Peptides; Physiology, Comparative; Poultry; Proline; Rabbits; Research; Species Specificity; Swine | 1964 |
20 other study(ies) available for proline and cytochrome c-t
| Article | Year |
|---|---|
Replacement of a conserved proline and the alkaline conformational change in iso-2-cytochrome c.
Topics: Cytochrome c Group; Cytochromes c; Hydrogen-Ion Concentration; Kinetics; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae | 1989 |
Changes in conformation and slow refolding kinetics in mutant iso-2-cytochrome c with replacement of a conserved proline residue.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes c; Escherichia coli; Genetic Vectors; Mutation; Proline; Protein Conformation; Protein Denaturation; Spectrophotometry | 1987 |
Construction and characterization of mutant iso-2-cytochromes c with replacement of conserved prolines.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes c; Escherichia coli; Glycine; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; Proline; Saccharomyces cerevisiae; Spectrophotometry; Threonine | 1988 |
Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-2-cytochrome c.
Topics: Cytochrome c Group; Cytochromes c; Glycine; Guanidine; Guanidines; Kinetics; Models, Molecular; Proline; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Fluorescence | 1988 |
Substitutions of proline 76 in yeast iso-1-cytochrome c. Analysis of residues compatible and incompatible with folding requirements.
Topics: Amino Acid Sequence; Base Sequence; Cytochrome c Group; Cytochromes c; DNA, Fungal; DNA, Recombinant; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1985 |
Guanidine hydrochloride induced equilibrium unfolding of mutant forms of iso-1-cytochrome c with replacement of proline-71.
Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 1986 |
Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71.
Topics: Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Kinetics; Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1986 |
Characterization of folding intermediates using prolyl isomerase.
Topics: Amino Acid Isomerases; Carrier Proteins; Catalysis; Cytochrome c Group; Cytochromes c; Guanidine; Guanidines; Models, Chemical; Mutation; Peptidylprolyl Isomerase; Proline; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Time Factors | 1994 |
Structure, function, and temperature sensitivity of directed, random mutants at proline 76 and glycine 77 in omega-loop D of yeast iso-1-cytochrome c.
Topics: Animals; Binding Sites; Circular Dichroism; Cytochrome c Group; Cytochromes c; Eukaryotic Cells; Glycine; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Proline; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Temperature | 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 |
Backbone dynamics and hydrogen exchange of Pseudomonas aeruginosa ferricytochrome c(551).
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 |
Glycine- and proline-rich glycoprotein isolated from Solanum nigrum Linne activates caspase-3 through cytochrome c in HT-29 cells.
Topics: Apoptosis; Blotting, Western; Caspase 3; Caspase 9; Caspase Inhibitors; Caspases; Cell Survival; Cysteine Proteinase Inhibitors; Cytochromes c; DNA Fragmentation; Dose-Response Relationship, Drug; Enzyme Activation; Glycine; Glycoproteins; HT29 Cells; Humans; Intracellular Space; L-Lactate Dehydrogenase; Oligopeptides; Plant Proteins; Poly(ADP-ribose) Polymerases; Proline; Reactive Oxygen Species; Solanum nigrum; Time Factors | 2005 |
Thermodynamics and kinetics of formation of the alkaline state of a Lys 79-->Ala/Lys 73-->His variant of iso-1-cytochrome c.
Topics: Alanine; Cytochromes c; Guanidine; Histidine; Hydrogen-Ion Concentration; Kinetics; Lysine; Mutagenesis, Site-Directed; Proline; Protein Denaturation; Saccharomyces cerevisiae Proteins; Static Electricity; Thermodynamics | 2005 |
Overexpression of proline oxidase induces proline-dependent and mitochondria-mediated apoptosis.
Topics: Apoptosis; Caspase 9; Cell Line, Tumor; Cytochromes c; Enzyme Activation; Enzyme Induction; Flow Cytometry; Gene Expression; Humans; Mitochondria; Models, Biological; Proline; Proline Oxidase; Time Factors | 2007 |
Cell death signal by glycine- and proline-rich plant glycoprotein is transferred from cytochrome c and nuclear factor kappa B to caspase 3 in Hep3B cells.
Topics: Apoptosis; Carcinoma, Hepatocellular; Caspase 3; Caspase 9; Cell Line, Tumor; Cytochromes c; DNA; Enzyme Activation; Glycine; Glycoproteins; Humans; Liver Neoplasms; Mitochondria, Liver; NF-kappa B; Nitric Oxide; Nitric Oxide Synthase Type II; Plant Proteins; Poly(ADP-ribose) Polymerases; Proline; Reactive Oxygen Species; Signal Transduction | 2008 |
Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.
Topics: Amino Acid Substitution; Amino Acids, Aromatic; Cytochromes c; Kinetics; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Proline; Protein Conformation; Protein Denaturation; Protein Engineering; Protein Stability; Recombinant Proteins; Saccharomyces cerevisiae Proteins; Static Electricity; Thermodynamics | 2010 |
Mitochondrial dynamics underlying thermal plasticity of cuttlefish (Sepia officinalis) hearts.
Topics: Acclimatization; Adaptation, Physiological; Animals; Body Temperature; Cell Respiration; Cytochromes c; Decapodiformes; Electron Transport Complex I; Heart; Mitochondria, Heart; Mitochondrial Dynamics; Myocardium; Oxidation-Reduction; Proline; Substrate Specificity | 2012 |
Mitochondrial physiology in the major arbovirus vector Aedes aegypti: substrate preferences and sexual differences define respiratory capacity and superoxide production.
Topics: Aedes; Animals; Arboviruses; Body Size; Cytochromes c; Dengue; Electron Transport Complex I; Female; Glycerolphosphate Dehydrogenase; Glycerophosphates; Humans; Insect Proteins; Insect Vectors; Male; Mitochondria, Muscle; NAD; Oxidation-Reduction; Oxygen Consumption; Proline; Pyruvic Acid; Sex Characteristics; Superoxides | 2015 |
The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria.
Topics: Alanine; Amino Acid Substitution; bcl-2-Associated X Protein; Cloning, Molecular; Cytochromes c; Gene Expression; HCT116 Cells; Humans; Liposomes; Mitochondria; Mutation; Permeability; Proline; Protein Binding; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Unilamellar Liposomes | 2017 |
Crystal structure of thermally stable homodimeric cytochrome c'-β from Thermus thermophilus.
Topics: Amino Acid Sequence; Crystallography, X-Ray; Cytochromes c; Cytochromes c'; Phylogeny; Proline; Thermus thermophilus | 2022 |