Results 41 to 50 of about 4,023 (167)
Erythropoietic protoporphyria: case reports for clinical and therapeutic hints
Italian Journal of Pediatrics, 2023 Background Erythropoietic protoporphyria is a rare disorder which represents an important health problem in children, causing painful photosensitivity. Little is known on the correlation between genetic profile and clinical manifestations.
Cristina Tumminelli +8 more
doaj +1 more source
Ultrasonics Sonochemistry, 2021 The enzyme Ferrochelatase (FeCH), which is naturally present in pork liver, catalyses the formation of Zinc-protoporphyrin (ZnPP), a natural pigment responsible for the typical color of dry-cured Italian Parma ham.
B. Abril +4 more
doaj +1 more source
Current Cell/Organoid and Animal Models for Primary Sclerosing Cholangitis
Portal Hypertension &Cirrhosis, EarlyView.Primary sclerosing cholangitis (PSC) is a chronic cholestatic liver disease with limited therapeutic options and a marked risk of progression to biliary fibrosis, cirrhosis, and malignancy. Progress in PSC research has been hindered by the lack of models that faithfully recapitulate the complex biliary microenvironment and disease heterogeneity ...
Qigu Yao +4 more
wiley +1 more source
British Journal of Haematology, EarlyView.Gene therapy is revolutionizing treatment paradigms for haemoglobinopathies, establishing a translational framework for disorders that impact red blood cell development. In their paper, Joshi et al. describe the preclinical and early clinical landscape of gene therapies for non‐haemoglobinopathy erythroid disorders and highlight common thematic ...
Gaurav Joshi +3 more
wiley +1 more source
Molecular and Genetic Characterization of Ferrochelatase.
The Tohoku Journal of Experimental Medicine, 1993 Ferrochelatase (heme synthase, protoheme ferrolyase [EC 4.99.1.1]), the final enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous ion into protoporphyrin IX to produce protoheme IX. The thorough understanding of the enzyme is prerequisite to elucidating the regulation of iron and heme metabolism.
openaire +4 more sources
Metal Ion Substrate Inhibition of Ferrochelatase [PDF]
Journal of Biological Chemistry, 2008 Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form heme. Robust kinetic analyses of the reaction mechanism are complicated by the instability of ferrous iron in aqueous solution, particularly at alkaline pH values. At pH 7.00 the half-life for spontaneous oxidation of ferrous ion is approximately 2 min in the absence ...
Gregory A, Hunter +2 more
openaire +2 more sources
JDDG: Journal der Deutschen Dermatologischen Gesellschaft, EarlyView.Summary Background Erythropoietic protoporphyria (EPP) is a rare genetic disorder characterized by severe phototoxic reactions that occur within minutes of light exposure. In clinical studies, afamelanotide has been shown to prolong pain‐free sun exposure, improve quality of life, and reduce the frequency and severity of phototoxic reactions ...
Magdalena Seidl‐Philipp +9 more
wiley +1 more source
Identification of a bacteria-like ferrochelatase in Strongyloides venezuelensis, an animal parasitic nematode. [PDF]
PLoS ONE, 2013 Heme is an essential molecule for vast majority of organisms serving as a prosthetic group for various hemoproteins. Although most organisms synthesize heme from 5-aminolevulinic acid through a conserved heme biosynthetic pathway composed of seven ...
Eiji Nagayasu +6 more
doaj +1 more source
Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes
The FEBS Journal, EarlyView.During heme biosynthesis in Gram‐positive bacteria, coproheme decarboxylase (ChdC) catalyzes the conversion of four‐propionate substrate coproheme to the two propionate product heme b. Its active site is universally covered by a flexible linking loop. This study identifies an important histidine residue, which stabilizes the loop in a ChdC homolog.
Nikolaus Falb +4 more
wiley +1 more source
The importance of porphyrin distortions for the ferrochelatase reaction [PDF]
JBIC Journal of Biological Inorganic Chemistry, 2003 Ferrochelatase is the terminal enzyme in haem biosynthesis, i.e. the enzyme that inserts a ferrous ion into the porphyrin ring. Suggested reaction mechanisms for this enzyme involve a distortion of the porphyrin ring when it is bound to the enzyme. We have examined the energetics of such distortions using various theoretical calculations.
Sigfridsson, Emma, Ryde, Ulf
openaire +2 more sources