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Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 5157 - 7
Despite the importance of electron transfer between redox proteins in photosynthesis and respiration, the inter-protein electron transfer rate between redox... 
CYTOCHROME-C | BC COMPLEX | TRANSPORT | INTERFACE | MULTIDISCIPLINARY SCIENCES | ARCHITECTURE | STATE | BINDING | WATER | Proteins | Electrochemical potential | Spectroscopy | Aqueous solutions | Electron transfer | Electrochemistry | Molecular dynamics | Photosynthesis | Electric fields | Electrons
Journal Article
FEBS Letters, ISSN 0014-5793, 11/2019, Volume 593, Issue 22, pp. 3101 - 3119
Cytochrome c (Cc) is a protein that functions as an electron carrier in the mitochondrial respiratory chain. However, Cc has moonlighting roles outside... 
histone chaperones | DNA damage response | double‐strand break | apoptosis | chromatin dynamics | apoptosome | cytochrome c | nuclear import | programmed cell death | caspase
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 07/2018, Volume 115, Issue 31, p. 7955
Respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 in the postischemic brain upon neuroprotective insulin treatment, but how such... 
Cytochrome | Tyrosine | Oxidative stress | Neuroprotection | Brain | Phosphorylation | Reactive oxygen species | Phenylalanine | Therapeutic applications | Heme proteins | Cytochrome-c oxidase | Caspase | Metabolism | Insulin | Caspase-3 | Proteins | Mitochondria | Ischemia | Oxidative phosphorylation | Point mutation | Cytochromes | Hypoxia | tRNA Phe | Structure-function relationships
Journal Article
Chemistry, ISSN 0947-6539, 10/2015, Volume 21, Issue 42, pp. 15004 - 15012
  Phosphorylation of tyrosine48 of cytochromec is related to a wide range of human diseases due to the pleiotropic role of the heme-protein in cell life and... 
Proteins | Phosphorylation | Human | Synthesis | Amino acids | Evolution | Kinases | Diseases
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 04/2017, Volume 114, Issue 15, p. E3041
Regulation of mitochondrial activity allows cells to adapt to changing conditions and to control oxidative stress, and its dysfunction can lead to... 
Cytochrome | Tyrosine | Oxidative stress | Phosphorylation | Reactive oxygen species | Nuclear magnetic resonance--NMR | Phenylalanine | Heme proteins | Caspase | Cells | Cytochrome c | Mitochondria | Ischemia | Hypoxia | Peroxidase | Mutation | Cancer | Apoptosis
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 04/2017, Volume 114, Issue 15, pp. E3041 - E3050
Journal Article
Acta Crystallographica Section A Foundations and Advances, ISSN 2053-2733, 12/2017, Volume 73, Issue a2, pp. C1126 - C1126
Journal Article
Chemistry - A European Journal, ISSN 0947-6539, 10/2015, Volume 21, Issue 42, pp. 15004 - 15012
Journal Article
FEBS Letters, ISSN 0014-5793, 02/2015, Volume 589, Issue 4, pp. 476 - 483
The transient interactions of respiratory cytochrome with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome ,... 
Cytochrome c | Cytochrome c oxidase | Isothermal Titration Calorimetry | Nuclear Magnetic Resonance | Supercomplex | Cytochrome bc1 | human cytochrome c | inner mitochondrial membrane | cytochrome c oxidase | DLS | Luria-Bertani | Cbc 1 | CcO | Cc 1 | CcOred | intermembrane mitochondrial space | electron transfer | plant cytochrome c 1 | reduced human cytochrome c | reduced cytochrome c oxidase | mitochondrial matrix | cytochrome c | equilibrium dissociation constant | Principal Component Analysis | plant cytochrome c | CSP | dynamic light scattering | complex IV | reduced plant cytochrome c 1 | III | IMM | hCc | human cytochrome c 1 | complex III | Heteronuclear Single-Quantum Correlation | IV | K D | IMS | cytochrome bc 1 | PCA | pCc | NMR | pCc1 | cytochrome c 1 | hCc1 | ITC | hCc red | HSQC | Chemical-Shift Perturbations | pCc 1red | Cytochrome bc | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MITOCHONDRIAL ELECTRON-TRANSPORT | SP PCC-7119 FLAVODOXIN | SYNECHOCYSTIS SP PCC-6803 | TRANSIENT COMPLEX | CELL BIOLOGY | PROGRAMMED CELL-DEATH | HYDROPHOBIC INTERACTIONS | BIOPHYSICS | PARAMAGNETIC NMR | PHOTOSYSTEM-I | CORRECT EXPRESSION | Cytochromes c - chemistry | Electron Transport Complex III - chemistry | Animals | Osmolar Concentration | Solutions | Cattle | Humans | Protein Structure, Quaternary | Models, Molecular | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Electron Transport Complex IV - chemistry | Cytochrome oxidase
Journal Article
Computational and Structural Biotechnology Journal, ISSN 2001-0370, 2019, Volume 17, pp. 654 - 660
The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to... 
Cytochrome c | Mitochondria | Phosphorylation | Reactive oxygen species | Respiratory supercomplexes
Journal Article
by Suma, Antonio and Micheletti, Cristian and Ludescher, Josef and Bunde, Armin and Schellnhuber, Hans Joachim and Wu, Grace C and Deshmukh, Ranjit and Ndhlukula, Kudakwashe and Radojicic, Tijana and Reilly-Moman, Jessica and Phadke, Amol and Kammen, Daniel M and Callaway, Duncan S and Morrison, Tiffany H and Vazao, Helena and Rosa, Susana and Barata, Tania and Costa, Ricardo and Pitrez, Patricia R and Honorio, Ines and de Vries, Margreet R and Papatsenko, Dimitri and Benedito, Rui and Saris, Daniel and Khademhosseini, Ali and Quax, Paul H. A and Pereira, Carlos F and Mercader, Nadia and Fernandes, Hugo and Ferreira, Lino and Henderson, Kate L and Felth, Lindsey C and Molzahn, Cristen M and Shkel, Irina and Wang, Si and Chhabra, Munish and Ruff, Emily F and Bieter, Lauren and Kraft, Joseph E and Record Jr., M. Thomas and Moreno-Beltran, Blas and Guerra-Castellano, Alejandra and Diaz-Quintana, Antonio and Del Conte, Rebecca and Garcia-Maurino, Sofia M and Diaz-Moreno, Sofia and Gonzalez-Arzola, Katiuska and Santos-Ocana, Carlos and Velazquez-Campoy, Adrian and De la Rosa, Miguel A and Turano, Paola and Diaz-Moreno, Irene and Lenaeus, Michael J and El-Din, Tamer M. Gamal and Ing, Christopher and Ramanadane, Karthik and Pomes, Regis and Zheng, Ning and Catterall, William A and Eser, Umut and Chandler-Brown, Devon and Ay, Ferhat and Straight, Aaron F and Duan, Zhijun and Noble, William Stafford and Skotheim, Jan M and Luo, Dan and de Morree, Antoine and Boutet, Stephane and Quach, Navaline and Natu, Vanita and Rustagi, Arjun and Rando, Thomas A and Ding, Yi and Ploper, Diego and Sosa, Eric A and Colozza, Gabriele and Moriyama, Yuki and Benitez, Maria D. J and Zhang, Kelvin and Merkurjev, Daria and De Robertis, Edward M and Braakman, Rogier and Follows, Michael J and Chisholm, Sallie W and Chawanthayatham, Supawadee and Valentine III, Charles C and Fedeles, Bogdan I and Fox, Edward J and Loeb, Lawrence A and Levine, Stuart S and Slocum, Stephen L and Wogan, Gerald N and Croy, Robert G and Essigmann, John M and Ali, Moustafa R. K and Rahman, Mohammad Aminur and Wu, Yue and Han, Tiegang and Peng, Xianghong and ...
Proceedings of the National Academy of Sciences of the United States, ISSN 0027-8424, 04/2017, Volume 114, Issue 15, pp. 3801 - 3804
Journal Article