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  • Hemin-induced reactive oxygen species triggers autophagy-dependent . . .
    The toxic effect of oxidized-heme, also known as hemin, is implicated in developing adverse clinical outcome in various hematolytic diseases To simulate and reconstruct the molecular events associated with hemin exposure on circulating monocytes, we employed a THP-1 cell line based in vitro model Flow cytometry and Western blot analyses were subsequently applied Hemin-treated THP-1 produced
  • Hemin-induced transient senescence via DNA damage response: a . . . - Nature
    Intracerebral hemorrhage (ICH) poses acute fatality and long-term neurological risks, in part due to hemin and iron accumulation from hemoglobin breakdown We observed that hemin induces DNA
  • Heme oxygenase-2 gene deletion attenuates oxidative stress in neurons . . .
    The present study was designed to test the effect of HO-2 gene deletion on the oxidative neuronal injury produced by extracellular hemin We specifically tested the hypothesis that targeted deletion of the HO-2 gene attenuated oxidative cell injury in a primary cell culture model of hemin toxicity Results
  • BRD4 silencing attenuates hemin-induced neuronal ferroptosis and . . .
    Background Intracerebral hemorrhage (ICH), a subtype of hemorrhagic stroke, is associated with high morbidity and mortality This study aimed to investigate the role and underlying mechanism of bromodomain and extraterminal domain protein 4 (BRD4) in neural injury following ICH Methods An in vitro ICH model was established by treating SH-SY5Y cells with hemin BRD4 and activating
  • Hemin-Induced Death Models Hemorrhagic Stroke and Is a Variant of . . .
    Hemin-induced and hemoglobin-induced death meet all of these criteria (Zille et al , 2017) As expected, we previously showed that U0126 completely abrogated cell death induced by hemoglobin and hemin consistent with the notion that these stimuli induce ferroptosis in hemorrhagic stroke in vitro and in vivo (Zille et al , 2017)
  • Glutathione–Hemin Hematin Adduct Formation to Disintegrate . . . - MDPI
    Hemin, an oxidized form of heme, acts as potent oxidant to regulate glutathione (GSH) content in pro-erythroid K562 nucleated cells, via activation of the KEAP1 NRF2 defensive signaling pathway Moreover, GSH, as an essential metabolite, is involved in the regulation of cell-redox homeostasis and proposed to scavenge cytotoxic free heme, which is released from hemoglobin of damaged red blood
  • Involvement of EGFR-AKT signaling in hemin-induced neurotoxicity
    The secondary injury results from released blood which is degraded to blood derived products, including heme hemin and iron These blood-derived products reportedly induce oxidative injury, neuroinflammation and protein aggregation that lead to cell death [1, 3 – 5]
  • Hemin induces an iron-dependent, oxidative injury to human neuron-like . . .
    These results suggest that hemin is toxic to human neuron-like cells at concentrations that are less than 3% of those observed in intracranial hematomas In this model, its toxicity is iron dependent, oxidative, and predominantly necrotic
  • Hemin as a protective agent in an in vitro model of hypoxia . . .
    In this context, hemin, a breakdown product of hemoglobin present in the serum, has garnered attention for its dual biological roles 8 While serum hemin has been shown to have detrimental effects in cerebral hemorrhage through oxidative stress and pro-inflammatory pathways, 9, 10 it has also been suggested to have protective effects in renal
  • In vitro models of intracerebral hemorrhage - ScienceDirect
    In vitro models, on the other hand, enable ICH study in a simplified culture system, and thus are particularly suited for high-throughput screening and mechanistic research Current in vitro ICH models mainly targets secondary injury associated with ICH, including hematoma expansion, neuronal cell death, oxidative stress, and BBB disruption [2]





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