Results 21 to 30 of about 399 (144)

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase [PDF]

open access: yesInternational Journal of Cancer, 2007
AbstracthBVR functions in the cell as a reductase and as a kinase. In the first capacity, it reduces biliverdin, the product of HO activity, to the effective intracellular antioxidant, bilirubin; as a dual‐specificity kinase (S/T/Y) it activates the MAPK and IGF/IRK receptor signal transduction pathways. NF‐κB and the MAPK pathway are activated by ROS,
Peter E M, Gibbs, Mahin D, Maines
openaire   +2 more sources

Biliverdin–copper complex at physiological pH [PDF]

open access: yesDalton Transactions, 2019
In physiological settings, biliverdin and Cu2+build a paramagnetic complex with formal structure: radical cation/Cu1+or radical anion/Cu3+.
Milena S. Dimitrijević   +8 more
openaire   +10 more sources

High-level expression of Myrothecium verrucaria bilirubin oxidase in Pichia pastoris, and its facile purification and characterization

open access: yes, 2005
Bilirubin oxidase (BO) from Myrothecium verrucaria (authentic BO) catalyzing the oxidation of bilirubin to biliverdine was overexpressed in the methylotrophic yeast, Pichia pastoris. The cDNA encoding BO was cloned into the P.
15131   +10 more
core   +1 more source

Eggshell Biliverdin as an Antioxidant Maternal Effect [PDF]

open access: yesBioEssays, 2020
AbstractIn this essay, the hypothesis that biliverdin pigment plays an antioxidant role in the avian eggshell is proposed. Due to its ability to scavenge free radical species and to reduce mutation, biliverdin potentially counteracts the oxidative action of pathogens that penetrate the eggshell and/or protects the shell membrane from oxidation, thus ...
openaire   +3 more sources

Study of thiol addition to biliverdine, the synthesis of labelled bilirubine [PDF]

open access: yes, 2011
Biliverdin and bilirubin are bile pigments which are degradation products of heme. Biliverdin (BV) is greenish-blue pigment and is reduction product of tetrapyrrolic core of heme by influence of the hemoxygenase (HO).
Felklová, Veronika
core  

Theoretische Studien zur Entwicklung eines besseren Verständnisses von Kofaktorstrukturen und Mechanismen von Fotorezeptoren und metallhaltigen Enzymen mittels quantenchemischer und moleküldynamischer Ansätze

open access: yes, 2020
In this work two phytochromes, namely Cyanobacterial phytochrome Cph1 and Agrobacterium tumefaciens phytochrome Agp2, as well as formate dehydrogenase of Rhodobacter Capsulatus (RcFDH), are investigated. Part III shows the development and its application
Belger, Dennis Heinz
core   +1 more source

Direct Antioxidant Properties of Bilirubin and Biliverdin. Is there a Role for Biliverdin Reductase? [PDF]

open access: yesFrontiers in Pharmacology, 2012
Reactive oxygen species (ROS) and signaling events are involved in the pathogenesis of endothelial dysfunction and represent a major contribution to vascular regulation. Molecular signaling is highly dependent on ROS. But depending on the amount of ROS production it might have toxic or protective effects.
Jansen, Thomas, Daiber, Andreas
openaire   +3 more sources

Study of fluorescent labelled bilirubine preparation [PDF]

open access: yes, 2013
Heme is a prosthetic group containing iron atom at the center of the tetrapyrrole cycle, which is the part of hemoglobin. Heme is metabolized by heme oxygenase to linear tetrapyrrolic pigment - biliverdine.
Felklová, Veronika
core  

Biliverdin as a Pigment in a Fish [PDF]

open access: yesNature, 1945
IN Belone belone, the garfish, the bones, scales and fin rays are of a bright green colour. The chemical nature of this well-known colouring matter has long remained unknown. It cannot be extracted from the tissues in which it occurs by any organic, or neutral, weak acid or alkaline inorganic solvent.
openaire   +1 more source

Home - About - Disclaimer - Privacy