Results 31 to 40 of about 42,954 (256)
RIPK3 dampens mitochondrial bioenergetics and lipid droplet dynamics in metabolic liver disease
RIPK3 dampens mitochondrial bioenergetics and lipid droplet dynamics in metabolic liver disease. Abstract Background and Aims Receptor‐interacting protein kinase 3 (RIPK3) mediates NAFLD progression, but its metabolic function is unclear. Here, we aimed to investigate the role of RIPK3 in modulating mitochondria function, coupled with lipid droplet (LD)
Marta B. Afonso +16 more
wiley +1 more source
Rcf1 Modulates Cytochrome c Oxidase Activity Especially Under Energy-Demanding Conditions
The mitochondrial respiratory chain is assembled into supercomplexes. Previously, two respiratory supercomplex-associated proteins, Rcf1 and Rcf2, were identified in Saccharomyces cerevisiae, which were initially suggested to mediate supercomplex ...
Hannah Dawitz +5 more
doaj +1 more source
HEME Trafficking by the Cytochrome C Biogenesis Pathways [PDF]
Cytochromes function in electron transport chains to perform critical cellular functions, such as respiration and photosynthesis. Cytochromes c are unique due to their requirement for the covalent attachment of heme via two thioether bonds at a conserved CXXCH motif. Three pathways have been identified for cytochrome c maturation: System I (prokaryotes)
Molly C. Sutherland +2 more
openaire +2 more sources
Yeast cytochrome c oxidase: a model system to study mitochondrial forms of the haem-copper oxidase superfamily. [PDF]
The known subunits of yeast mitochondrial cytochrome c oxidase are reviewed. The structures of all eleven of its subunits are explored by building homology models based on the published structures of the homologous bovine subunits and similarities and ...
Maréchal, A +14 more
core +1 more source
Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome
Although intracellular heme trafficking must occur for heme protein assembly, only a few heme transporters have been unequivocally discovered and nothing is known about their structure or mechanisms.
Molly C. Sutherland +5 more
doaj +1 more source
Biogenesis of mitochondrialc-type cytochromes
Cytochromes c and c1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space; cytochrome c is loosely attached to the surface of the inner mitochondrial membrane, whereas ...
Gonzales, Daniel H., Neupert, Walter
openaire +3 more sources
Early steps in mitochondrial protein import [PDF]
The process of insertion of precursor proteins into mitochondrial membranes was investigated using a hybrid protein (pSc1-c) that contains dual targeting information and, at the same time, membrane insertion activity.
Stuart, Rosemary A. +2 more
core +1 more source
Biogenesis of eukaryotic cytochrome c oxidase
Eukaryotic cytochrome c oxidase (CcO), the terminal component of the mitochondrial electron transport chain is a heterooligomeric complex that belongs to the superfamily of heme-copper containing terminal oxidases. The enzyme, composed of both mitochondrially and nuclear encoded subunits, is embedded in the inner mitochondrial membrane, where it ...
L, Stiburek +4 more
openaire +2 more sources
Cytochrome c oxidase, the terminal enzyme of the respiratory chain, is assembled from mitochondria- and nuclear-encoded subunits. The MITRAC complex represents the central assembly intermediate during this process as it receives imported subunits and ...
Sven Dennerlein +8 more
doaj +1 more source
A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria [PDF]
The novel genetic method of "sheltered RIP" (repeat induced point mutation) was used to generate a Neurospora crassa mutant in which MOM19, a component of the protein import machinery of the mitochondrial outer membrane, can be depleted.
W Neupert +16 more
core +1 more source

