Results 51 to 60 of about 414,627 (398)

A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria [PDF]

open access: yes, 1988
The nuclear cyt-2-1 mutant of Neurospora crassa is characterized by a gross deficiency of cytochrome c (Bertrand, H., and Collins, R. A. (1978) Mol. Gen. Genet. 166, 1-13).
Drygas, Mariola E.   +4 more
core   +1 more source

Could Heme Oxygenase-1 Be a New Target for Therapeutic Intervention in Malaria-Associated Acute Lung Injury/Acute Respiratory Distress Syndrome?

open access: yesFrontiers in Cellular and Infection Microbiology, 2018
Malaria is a serious disease and was responsible for 429,000 deaths in 2015. Acute lung injury/acute respiratory distress syndrome (ALI/ARDS) is one of the main clinical complications of severe malaria; it is characterized by a high mortality rate and ...
Marcelo L. M. Pereira   +2 more
doaj   +1 more source

Preliminary studies of biosynthesis of heme O and heme A in intraerythrocytic stages of P. falciparum [PDF]

open access: yes, 2014
Intermediates of the isoprenoid metabolism can bind to heme groups. Heme is critical and its derivatives, heme O and heme A, are the main compounds of aerobic respiration. They are synthesized by farnesylation of heme groups by ?heme O synthase?
Cirulli, Brenda Analía   +5 more
core   +2 more sources

Heme Catabolism and Heme Oxygenase in Neurodegenerative Disease

open access: yesAntioxidants & Redox Signaling, 2004
Heme oxygenase, the rate-limiting step in heme catabolism, appears to play an important role in a number of neurodegenerative disorders, such as Alzheimer disease. Interestingly, the spatial distribution of heme oxygenase-1 expression in diseased brain is essentially identical to that of the pathological expression of tau, suggesting a key role for ...
Takeda, Atsushi   +7 more
openaire   +4 more sources

Heme b (protoheme IX) is a precursor of heme a and heme d in Bacillus subtilis [PDF]

open access: yesFEMS Microbiology Letters, 1993
Bacillus subtilis can synthesise cytochromes containing a-, b-, c- and d-type heme. The biosynthetic pathways of these heme prosthetic groups were investigated by using strains blocked in uroporphyrinogen III synthesis from porphobilinogen or in heme b (protoheme IX) synthesis from uroporphyrinogen III. The results strongly suggest that heme a and heme
Mats Hansson, Claes von Wachenfeldt
openaire   +3 more sources

Heme-Derived Metabolic Signals Dictate Immune Responses

open access: yesFrontiers in Immunology, 2020
Heme is one of the most abundant molecules in the body acting as the functional core of hemoglobin/myoglobin involved in the O2/CO2 carrying in the blood and tissues, redox enzymes and cytochromes in mitochondria.
Giacomo Canesin   +3 more
doaj   +1 more source

Human Heme Oxygenase Oxidation of 5- and 15-Phenylhemes [PDF]

open access: yes, 2004
Human heme oxygenase-1 (hHO-1) catalyzes the O2- dependent oxidation of heme to biliverdin, CO, and free iron. Previous work indicated that electrophilic addition of the terminal oxygen of the ferric hydroperoxo complex to the -meso-carbon gives 5 ...
Alvarez, Diego Ezequiel   +7 more
core   +1 more source

Iron Induces Anti-tumor Activity in Tumor-Associated Macrophages

open access: yesFrontiers in Immunology, 2017
Tumor-associated macrophages (TAMs) frequently help to sustain tumor growth and mediate immune suppression in the tumor microenvironment (TME). Here, we identified a subset of iron-loaded, pro-inflammatory TAMs localized in hemorrhagic areas of the TME ...
Milene Costa da Silva   +26 more
doaj   +1 more source

Convenient Heme Nanorod Modified Electrode for Quercetin Sensing by Two Common Electrochemical Methods

open access: yesMicromachines, 2021
Quercetin (Qu) is one of the most abundant flavonoids in the human diet. High concentrations of Qu can easily cause adverse effects and induce inflammation, joint pain and stiffness.
Jin-Guang Liu   +5 more
doaj   +1 more source

Biogenesis of mitochondrial c-type cytochromes [PDF]

open access: yes, 1990
Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
core   +2 more sources

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