Results 141 to 150 of about 164,160 (174)

Recommendations for recognizing and diagnosing Acute Hepatic Porphyria in atypical patient populations. [PDF]

Orphanet J Rare Dis
Schmolly K, Rudrapatna V, Beaven S.
europepmc   +1 more source

Iron and metabolic rewiring in cancer. [PDF]

Oncogenesis
Ciscar M, Rodríguez-Santana C, Santana-Codina N.   +2 more
europepmc   +1 more source

Acute intermittent porphyria: alternative splicing of hydroxymethylbilane synthase mRNA excludes exons 3 and 12

Molecular and Cellular Probes, 1998
The hydroxymethylbilane synthase (HMBS) mRNAs from 44 control individuals and 30 patients suffering from acute intermittent porphyria (AIP), were screened for length differences by reverse transcriptase polymerase chain reaction (RT-PCR) and any abnormalities were characterized by direct sequencing.
Michael Moore, W G Lanyon, J M Connor
exaly   +7 more sources

Biallelic inactivation of protoporphyrinogen oxidase and hydroxymethylbilane synthase is associated with liver cancer in acute porphyrias

Journal of Hepatology, 2015
Variegate porphyria (VP) and acute intermittent porphyria (AIP), the two most common types of acute porphyrias (AHPs), result from a partial deficiency of protoporphyrinogen oxidase (PPOX) and hydroxymethylbilane synthase (HMBS), respectively. A rare but serious complication in the AHPs is hepatocellular carcinoma (HCC).
Jasmin Barman-Aksözen, Peter Bauer, Elisabeth I Minder   +2 more
exaly   +4 more sources

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Network analysis of hydroxymethylbilane synthase dynamics

Journal of Molecular Graphics and Modelling, 2020
Hydroxymethylbilane synthase (HMBS) is one of the key enzymes of the heme biosynthetic pathway that catalyzes porphobilinogen to form the linear tetrapyrrole 1-hydroxymethylbilane through four intermediate steps. Mutations in the human HMBS (hHMBS) can lead to acute intermittent porphyria (AIP), a lethal metabolic disorder.
Arijit Roy, Broto Chakrabarty, Gopalakrishnan Bulusu   +2 more
exaly   +3 more sources

Determination of the structure of selenomethionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion

Acta Crystallographica Section D: Biological Crystallography, 1999
The enzyme hydroxymethylbilane synthase (HMBS, E.C. 4.3.1.8) catalyzes the conversion of porphobilinogen into hydroxymethylbilane, a key intermediate for the biosynthesis of heme, chlorophylls, vitamin Bit and related macrocycles.
John R. Helliwell, Alberto Cassetta, A W Thompson   +2 more
exaly   +2 more sources

Functional studies of rat hydroxymethylbilane synthase

Bioorganic Chemistry, 2008
The structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Hydroxymethylbilane synthase catalyzes a rate-limiting step for the biosyntheses of tetrapyrrolic natural products.
Nan Li, Ding Li, Xiusheng Chu
exaly   +3 more sources

Interaction of 5-hydroxymethyl-furfural with hydroxymethylbilane synthase

Phytochemistry, 1997
Abstract The inhibition of chlorophyll biosynthesis in greening cress seedlings (Lepidium sativum L.) by 5-hydroxymethylfurfural (5-HMF), a natural compound isolated from the bulbs of Gladiolus spp. was investigated in vitro and in vivo. A direct reaction between 5-HMF and the chlorophyll precursor porphobilinogen was observed at pH 1.0 but not at pH
Wolfhart Rüdiger
exaly   +2 more sources

New mutations of the hydroxymethylbilane synthase gene in German patients with acute intermittent porphyria

Molecular and Cellular Probes, 1999
Acute intermittent porphyria (AIP) is a low-penetrant, autosomal dominant disorder caused by decreased activity of hydroxymethylbilane synthase (HMBS; MIM 176 000), the third enzyme in the heme biosynthetic pathway. We report the first molecular analysis of HMBS gene mutations in classical AIP patients of German origin.
Hervé Puy, Y Nordmann, M O Doss
exaly   +3 more sources