Results 41 to 50 of about 2,605 (236)
BioEssays, 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
Cytochrome c signalosome in mitochondria [PDF]
, 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
Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries [PDF]
Antioxidants & Redox Signaling, 2011 Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are ...
Ruth, Pietri +2 more
openaire +2 more sources
Journal of Biological Chemistry, 1998 Chao Su, Margareta Sahlin, Ernst H. Oliw
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The 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
Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria [PDF]
, 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
Exploring protein phosphorylation by combining computational approaches and biochemical methods
Computational and Structural Biotechnology Journal, 2020 Post-translational modifications of proteins expand their functional diversity, regulating the response of cells to a variety of stimuli. Among these modifications, phosphorylation is the most ubiquitous and plays a prominent role in cell signaling.
Gonzalo Pérez-Mejías +7 more
doaj +1 more source
Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV [PDF]
, 2019 The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies.
Díaz Moreno, Irene +4 more
core +1 more source
Label-free photoacoustic microscopy of cytochromes [PDF]
, 2013 Photoacoustic microscopy (PAM) has achieved submicron lateral resolution in showing subcellular structures; however, relatively few endogenous subcellular contrasts have so far been imaged. Given that the hemeprotein, mostly cytochromes in general cells,
Wang, Lihong V. +4 more
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Design of Artificial Enzymes: Insights into Protein Scaffolds
ChemBioChem, 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