Results 11 to 20 of about 649,169 (309)

Molecular Basis and Consequences of the Cytochrome c-tRNA Interaction. [PDF]

open access: yes, 2016
The intrinsic apoptosis pathway occurs through the release of mitochondrial cytochrome c to the cytosol, where it promotes activation of the caspase family of proteases.
Christian, Thomas   +6 more
core   +2 more sources

Cytochrome c 6-like protein as a putative donor of electrons to photosystem I in the cyanobacterium Nostoc sp. PCC 7119 [PDF]

open access: yes, 2011
Most organisms performing oxygenic photosynthesis contain either cytochrome c 6 or plastocyanin, or both, to transfer electrons from cytochrome b 6-f to photosystem I. Even though plastocyanin has superseded cytochrome c 6 along evolution, plants contain
Gil Martínez, Jorge   +2 more
core   +1 more source

Cytochrome c signalosome in mitochondria [PDF]

open access: yes, 2011
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the cytoplasmic adducts of cytochrome
Díaz Moreno, Irene   +3 more
core   +1 more source

Rate variation during molecular evolution: creationism and the cytochrome c molecular clock [PDF]

open access: yes, 2017
Molecular clocks based upon amino acid sequences in proteins have played a major role in the clarification of evolutionary phylogenies. Creationist criticisms of these methods sometimes rely upon data that might initially seem to be paradoxical.
Hofmann James, R.
core   +1 more source

Electron transfer interactome of cytochrome C.

open access: yesPLoS Computational Biology, 2012
Lying at the heart of many vital cellular processes such as photosynthesis and respiration, biological electron transfer (ET) is mediated by transient interactions among proteins that recognize multiple binding partners.
Alexander N Volkov, Nico A J van Nuland
doaj   +1 more source

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

open access: yesmBio, 2023
Heme, an essential molecule for virtually all living organisms, acts primarily as a cofactor in a large number of proteins. However, how heme is mobilized from the site of synthesis to the locations where hemoproteins are assembled remains largely ...
Sirui Han   +4 more
doaj   +1 more source

Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c

open access: yesRedox Biology, 2018
In this work, we measured the effect of cytochrome c on the NADH-dependent superoxide anion production by synaptic plasma membrane vesicles from rat brain.
Alejandro K. Samhan-Arias   +5 more
doaj   +1 more source

The effect of cardiolipin side chain composition on cytochrome c protein conformation and peroxidase activity

open access: yesPhysiological Reports, 2021
Skeletal muscle, a highly active tissue, makes up 40% of the total body weight. This tissue relies on mitochondria for ATP production, calcium homeostasis, and programed cell death.
Jennifer A. Wilkinson   +2 more
doaj   +1 more source

Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c

open access: yesBiosensors, 2023
Cytochrome c (Cytc) is a key redox protein for energy metabolism and apoptosis in cells. The activation of Cytc is composed of several steps, including its transfer to the mitochondrial membrane, binding to cytochrome c heme lyase (CCHL) and covalent ...
Mehmet Yunus Genceroglu   +3 more
doaj   +1 more source

Cytochrome c and superoxide [PDF]

open access: yesJBIC Journal of Biological Inorganic Chemistry, 2013
ISSN:0949 ...
openaire   +3 more sources

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