Results 41 to 50 of about 2,618 (230)

The Effect of 5-Aminolevulinic Acid on Cytochrome P450-Mediated Prodrug Activation. [PDF]

open access: yesPLoS ONE, 2015
Of late, numerous prodrugs are widely used for therapy. The hemeprotein cytochrome P450 (CYP) catalyzes the activation of prodrugs to form active metabolites.
Mai Miura   +5 more
doaj   +1 more source

Tracking Heme-Protein Interactions in Healthy and Pathological Human Serum in Native Conditions by Miniaturized FFF-Multidetection

open access: yesApplied Sciences, 2022
The interaction of heme with blood serum proteins plays an important role in many physiological and pathological processes involving enzyme activity, gene expression and cell proliferation.
Valentina Marassi   +4 more
doaj   +1 more source

Theoretical Study on the Effective Magnetic Moments of Some Hemeproteins [PDF]

open access: bronzeProgress of Theoretical Physics Supplement, 1961
It is pointed out that the measurement of the static magnetic susceptibilities over a wide temperature range will be able to the detailed information about the electronic structure of the paramagnetic heme derivatives. On the basis of the data given by the electron paramagnetic resonance experiment, formulas for the temperature dependence of the ...
Masao Kotani
openalex   +3 more sources

Hemeprotein Tpx1 interacts with cell‐surface heme transporter Str3 in Schizosaccharomyces pombe

open access: yesMolecular Microbiology, 2020
Str3 is a transmembrane protein that mediates low‐affinity heme uptake in Schizosaccharomyces pombe. Under iron‐limiting conditions, Str3 remains at the cell surface in the presence of increasing hemin concentrations.
Vincent Normant   +6 more
semanticscholar   +1 more source

A natural heme deficiency exists in biology that allows nitric oxide to control heme protein functions by regulating cellular heme distribution

open access: yesBioEssays, Volume 45, Issue 8, August 2023., 2023
We hypothesize that tissues exist naturally in a heme‐deficient condition that limits the heme content and functions of heme proteins. The nitric oxide (NO) that is made in our tissues can control cell heme availability in a bimodal way, and so regulate heme protein functions in health and disease.
Dennis J. Stuehr   +5 more
wiley   +1 more source

Critical role for uricase and xanthine dehydrogenase in soybean nitrogen fixation and nodule development

open access: yesThe Plant Genome, Volume 16, Issue 2, June 2023., 2023
Abstract De novo purine biosynthesis is required for the incorporation of fixed nitrogen in ureide exporting nodules, as formed on soybean [Glycine max (L.) Merr.] roots. However, in many cases, the enzymes involved in this pathway have been deduced strictly from genome annotations with little direct genetic evidence, such as mutant studies, to confirm
Cuong X. Nguyen   +5 more
wiley   +1 more source

Cytochrome c signalosome in mitochondria [PDF]

open access: yes, 2011
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the cytoplasmic adducts of cytochrome
Díaz Moreno, Irene   +3 more
core   +1 more source

Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria [PDF]

open access: yes, 2018
Respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 in the postischemic brain upon neuroprotective insulin treatment, but how such posttranslational modification affects mitochondrial metabolism is unclear.
Díaz Moreno, Irene   +7 more
core   +1 more source

Design of Artificial Enzymes: Insights into Protein Scaffolds

open access: yesChemBioChem, Volume 24, Issue 6, March 14, 2023., 2023
The design of artificial enzymes has emerged as a promising tool for the generation of potent biocatalysts able to promote new‐to‐nature reactions. This review aims to give a general overview of suitable protein scaffolds, that could be functionalized with an artificial moiety to develop versatile artificial catalysts. Abstract The design of artificial
Stefanie Hanreich   +2 more
wiley   +1 more source

Selective chemical modification of Cys264 with diiodofluorescein iodacetamide as a tool to study the membrane topology of cytochrome P450scc (CYP11A1) [PDF]

open access: yes, 1994
Cys264 of cytochrome P450scc (CYPIIAI) was selectively labelled with diiodofluorescein iodacetamide in solution and in proteoliposomes. The labelling affected the interaction of P450scc with adrenodoxin and significantly inhibited the side-chain cleavage
Chernogolov, Alexey   +3 more
core   +1 more source

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