Results 31 to 40 of about 232,755 (310)
The Multifaceted Role of Heme in Cancer
Frontiers in Oncology, 2020 Heme, an iron-containing porphyrin, is of vital importance for cells due to its involvement in several biological processes, including oxygen transport, energy production and drug metabolism.
V. Fiorito +4 more
semanticscholar +1 more source
Discovering How Heme Controls Genome Function Through Heme-omics
Cell Reports, 2020 Summary: Protein ensembles control genome function by establishing, maintaining, and deconstructing cell-type-specific chromosomal landscapes. A plethora of small molecules orchestrate cellular functions and therefore may link physiological processes ...
Ruiqi Liao +12 more
doaj +1 more source
Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
Chemical Reviews, 2017 As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection against reactive oxygen species. Despite the diverse structures and functions of these proteins, they
Xiong Huang, J. Groves
semanticscholar +1 more source
mBio, 2018 Staphylococcus aureus is responsible for a significant amount of devastating disease. Its ability to colonize the host and cause infection is supported by a variety of proteins that are dependent on the cofactor heme.
Jacob E. Choby +5 more
doaj +1 more source
A Dual Role of Heme Oxygenase-1 in Cancer Cells
International Journal of Molecular Sciences, 2018 Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.
Shih-Kai Chiang +2 more
semanticscholar +1 more source
Biochimica et biophysica acta. Molecular cell research, 2020 Heme, as a hydrophobic iron-containing organic ring, is lipid soluble and can interact with biological membranes. The very same properties of heme that nature exploits to support life also renders heme potentially cytotoxic.
I. Chambers +3 more
semanticscholar +1 more source
Heme Oxygenase-2 Is a Hemoprotein and Binds Heme through Heme Regulatory Motifs That Are Not Involved in Heme Catalysis [PDF]
Journal of Biological Chemistry, 1997 The heme oxygenase (HO) system degrades heme to biliverdin and CO and releases chelated iron. In the primary sequence of the constitutive form, HO-2, there are three potential heme binding sites: two heme regulatory motifs (HRMs) with the absolutely conserved Cys-Pro pair, and a conserved 24-residue heme catalytic pocket with a histidine residue ...
W K, McCoubrey, T J, Huang, M D, Maines
openaire +2 more sources
Heme Catabolism and Heme Oxygenase in Neurodegenerative Disease
Antioxidants & 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
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The heme-responsive PrrH sRNA regulates Pseudomonas aeruginosa pyochelin gene expression
mSphere, 2023 Pseudomonas aeruginosa is an opportunistic pathogen that requires iron for growth and virulence, yet this nutrient is sequestered by the innate immune system during infection. When iron is limiting, P. aeruginosa expresses the PrrF1 and PrrF2 small RNAs (
Tra-My Hoang +8 more
doaj +1 more source
Frontiers in Microbiology, 2020 Ferric uptake regulator (Fur) is a transcriptional regulator playing a central role in iron homeostasis of many bacteria, and Fur inactivation commonly results in pleiotropic phenotypes.
Lulu Liu +5 more
doaj +1 more source