Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.

doi:10.1007/s00775-011-0804-9

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Article

Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Dec 2011

García-Heredia José M, Díaz-Quintana Antonio, Salzano Maria, Orzáez Mar, Pérez-Payá Enrique, Teixeira Miguel, De la Rosa Miguel A, Díaz-Moreno Irene

Abstract excerpt

Cytochrome c (Cc) is a key protein in cell life (respiration) and cell death (apoptosis). On the one hand, it serves as a mitochondrial redox carrier, transferring electrons between the membrane-embedded complexes III and IV. On the other hand, it acts as a cytoplasmic apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The...

Topics

Amino Acid Sequence
Amino Acid Substitution
Apoptosis
Apoptotic Protease-Activating Factor 1
Caspase 9
Computer Simulation
Cytochromes c
Humans
Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Phosphorylation

Protein Binding

Protein Conformation

Protein Stability

Tyrosine

Source

Open in PubMed

Identifiers

PMID: 21706253
DOI: 10.1007/s00775-011-0804-9

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