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In ORX-KO mice, the ultradian episodic changes in locomotor activity, EEG arousal indices and body temperature were significantly attenuated, but the ultradian patterning was preserved. Findings suggest that the ultradian pattern is common across species and that orexin contributes to driving ultradian episodic changes, however, this neuropeptide is not essential for ultradian pattern generation.
OXA and OX1R (zeige HCRTR1 Proteine) are expressed in the testis and that they may help in proliferation and development of germ cells, Leydig cells and Sertoli cells, and in the spermatogenic process and steroidogenesis.
Results thus suggest that type 1 diabetes mellitus impairs testicular steroidogenesis and glucose homeostasis through inhibition of orexin A/OX1R (zeige HCRTR1 Proteine) signaling cascade due to decreased OX1R (zeige HCRTR1 Proteine) expression in adult mice, thereby affecting germ cell survival and their proliferation in the testis.
Binding of OXA to OX1R (zeige HCRTR1 Proteine) is important for the development of the testis.
Results suggest that orexin A bidirectionally modulates hippocampal CA1 (zeige CA1 Proteine) synaptic plasticity, inhibiting long-term potentiation via OX1Rs at moderate concentrations while inducing re-potentiation via OX1Rs and OX2Rs, possibly through phospholipase C (zeige PLC Proteine) and adenylyl cyclase-protein kinase A signaling at sub-nanomolar concentrations
DYN-A(2-17) interacts with orexin A in the paraventricular hypothalamic nucleus to modulate food intake in mice.
Awake dynamics and brain-wide direct inputs of hypothalamic MCH and orexin/hypocretin networks have been discovered.
Histamine Transmission Modulates the Phenotype of Murine Narcolepsy Caused by Orexin Neuron Deficiency
observation that inhibition of the Orexin-1 receptor signaling blunted binge-like Ethanol, and saccharin drinking suggests that reward-related Orexin circuits participate in the consumption of salient reinforcers regardless of calories.
Results suggest that exercise produces antidepressant effects via suppression of Hcrt/Orx and melanin-concentrating hormone (zeige PMCH Proteine) neural systems in the basolateral amygdala
GAPDH (zeige GAPDH Proteine) and protoporphyrinogen oxidase were shown to have higher expression in faster growing cell lines and primary tumors. Pharmacologic inhibition of GAPDH (zeige GAPDH Proteine) or PPOX reduced the growth of colon cancer cells in vitro
Variegate porphyria is the result of decreased protoporphyrinogen oxidase activity. Diet supplementation with vitamins E and C restores PPOX gene expression in lymphocytes of variegate porphyria patients.
in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX and HMBS (zeige HMBS Proteine)
The c.851G>T and the c.1013C>G of PPOX gene were found in two and four unrelated families respectively. 1 experienced only photosensitivity, 1 only neurological symptoms and the 2 both clinical manifestations.
The mutation 1082-1083insC(1 base pair insertion at position 1082) in exon 10 of the PPOX gene was prevalent in the Swiss population.
findings emphasize the usefulness of MLPA analysis as a complement to PPOX gene sequencing analysis for comprehensive genetic diagnostics in patients with variegate prophyria
Information required for targeting to the mitochondria is contained within the first 250 amino acid residues of human PPOX.
Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using PPOX.
Protoporphyrinogen oxidase targeting mechanism to the mitochondrion.
Mutation in protoporphyrinogen oxidase is associated with variegate porphyria
The tetrapyrrole biosynthetic enzyme PPO1 is required for plastid RNA editing.
This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. Mutations in this gene cause variegate porphyria, an autosomal dominant disorder of heme metabolism resulting from a deficiency in protoporphyrinogen oxidase, an enzyme located on the inner mitochondrial membrane. Alternatively spliced transcript variants encoding the same protein have been identified.
, orexin A
, orexin B
, protoporhyrinogen oxidase