Results 21 to 30 of about 467,569 (310)

Exercise training-induced PPARβ increases PGC-1α protein stability and improves insulin-induced glucose uptake in rodent muscles [PDF]

open access: yes, 2020
This study aimed to investigate the long-term effects of training intervention and resting on protein expression and stability of peroxisome proliferator-activated receptor β/δ (PPARβ), peroxisome proliferator-activated receptor gamma coactivator 1-α ...
Holloszy, John O   +3 more
core   +2 more sources

c-Type cytochrome-dependent formation of U(IV) nanoparticles by Shewanella oneidensis. [PDF]

open access: yesPLoS Biology, 2006
Modern approaches for bioremediation of radionuclide contaminated environments are based on the ability of microorganisms to effectively catalyze changes in the oxidation states of metals that in turn influence their solubility.
Matthew J Marshall   +17 more
doaj   +1 more source

Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation. [PDF]

open access: yes, 2019
Gasdermin E (GSDME/DFNA5) cleavage by caspase-3 liberates the GSDME-N domain, which mediates pyroptosis by forming pores in the plasma membrane.
Alnemri, Emad S.   +5 more
core   +3 more sources

Perturbation of Cytochrome c Maturation Reveals Adaptability of the Respiratory Chain in Mycobacterium tuberculosis

open access: yesmBio, 2013
Mycobacterium tuberculosis depends on aerobic respiration for growth and utilizes an aa3-type cytochrome c oxidase for terminal electron transfer. Cytochrome c maturation in bacteria requires covalent attachment of heme to apocytochrome c, which occurs ...
Jennifer L. Small   +5 more
doaj   +1 more source

Q-band electron nuclear double resonance (ENDOR) and X-band EPR of the sulfobetaine 12 heat-treated cytochrome c oxidase complex [PDF]

open access: yes, 1997
Heat treatment of the bovine cytochrome c oxidase complex in the zwitterionic detergent sulfobetaine 12 (SB-12) results in loss of subunit III and the appearance of a type II copper center as characterized by electron paramagnetic resonance (EPR ...
Chan, Sunney I.   +4 more
core   +1 more source

Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature

open access: yesScientific Reports, 2017
Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane.
Rebecka Andersson   +15 more
doaj   +1 more source

A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding [PDF]

open access: yes, 2007
In bacterial c-type cytochromes, the haem cofactor is covalently attached via two cysteine residues organized in a haem c-binding motif. Here, a novel octa-haem c protein, MccA, is described that contains only seven conventional haem c-binding motifs ...
Allen J.W.A.   +17 more
core   +1 more source

Selective Enzymatic Oxidation of Silanes to Silanols [PDF]

open access: yes, 2020
Compared to the biological world's rich chemistry for functionalizing carbon, enzymatic transformations of the heavier homologue silicon are rare. We report that a wild‐type cytochrome P450 monooxygenase (P450_(BM3) from Bacillus megaterium, CYP102A1 ...
Dimitris E. Katsoulis   +8 more
core   +2 more sources

Studies on the Cytochrome C Oxidase Activities and Analysis of the Glycolysis and High Energy Phosphorus Compounds in the Normal Bacteria and those Fast to the Antibacterial Com­pounds. [PDF]

open access: yes, 1952
The following results were obtained through the experiments on the cytochrome c oxidase activities and the analysis of the glycolysis and high energy phosphorus compounds in the normal bacteria and those fast to penicillin, sulfathiazol, 2.4 ...
Kanehisa, Teiki
core   +1 more source

Biogenesis of mitochondrialc-type cytochromes

open access: yesJournal of Bioenergetics and Biomembranes, 1990
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

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