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porphyrias/nicotine

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A case of porphyria cutanea tarda in the setting of hepatitis C infection and tobacco usage.

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Porphyria cutanea tarda (PCT) is the most common type of porphyria, presenting in middle-aged patients with a photodistributed vesiculobullous eruption, milia, and scars. Porphyria cutanea tarda occurs in relation to inhibition of uroporphyrinogen decarboxylase, a key enzyme in the heme biosynthesis

Functional definition of the tobacco protoporphyrinogen IX oxidase substrate-binding site.

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PPO (protoporphyrinogen IX oxidase) catalyses the flavin-dependent six-electron oxidation of protogen (protoporphyrinogen IX) to form proto (protoporphyrin IX), a crucial step in haem and chlorophyll biosynthesis. The apparent K(m) value for wild-type tobacco PPO2 (mitochondrial PPO) was 1.17 muM,

[Friedrich Wilhelm I and porphyria].

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Historical evidence has been collected attempting to diagnose members of royal houses, perhaps most publicized by Macalpine and Hunter (1969) for George III and his assumed porphyria, claiming that his insanity was a classic case of thereof. This rare metabolic disease presents with a variety of

CYP1A2*1F and GSTM1 alleles are associated with susceptibility to porphyria cutanea tarda.

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Porphyria cutanea tarda (PCT) is a cutaneous porphyria with sporadic (type 1) and familial (type 2) subtypes, both resulting from decreased hepatic uroporphyrinogen decarboxylase (UROD) activity. Environmental and genetic factors are involved in the development of PCT, and genetic variants in the

Non-viral factors contributing to hepatocellular carcinoma.

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Hepatocellular carcinoma (HCC) is a major cause of cancer death worldwide, accounting for over half a million deaths per year. The geographic pattern of HCC incidence is parallel to exposure to viral etiologic factors. Its incidence is increasing, ranging between 3% and 9% annually depending on the

Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis.

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Protoporphyrinogen IX oxidase (PPO), the last common enzyme of haem and chlorophyll biosynthesis, catalyses the oxidation of protoporphyrinogen IX to protoporphyrin IX. The membrane-embedded flavoprotein is the target of a large class of herbicides. In humans, a defect in PPO is responsible for the

Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen.

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Protoporphyrinogen IX oxidase, a monotopic membrane protein, which catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX in the heme/chlorophyll biosynthetic pathway, is distributed widely throughout nature. Here we present the structure of protoporphyrinogen IX oxidase from

[Risks factors for pediatric malignant liver tumors].

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OBJECTIVE Pediatric Hepatic Malignancies (PHMs) are the result of the interaction between constitutional and environmental risk factors (RFs). We review the evidence on the main RFs associated to PHMs. METHODS Systematic review of the literature published in the last 25 years on Medline, Embase,
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