Results 51 to 60 of about 1,725 (195)
Hemoglobin I from Lucina pectinata on Collagen Scaffold: A Prospective Hydrogen Sulfide Scavenger
Hydrogen sulfide (H2S), independently of being a toxic gas with a characteristic smell of rotten eggs, is a crucial signaling molecule with significant physiological functions.
Jennifer Vargas Santiago+2 more
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Myoglobin is a hemeprotein that reversibly binds oxygen and gives muscle its red color. Here, the authors report a genetic variant in the MB gene that associates with myoglobinopathy, an autosomal dominant progressive myopathy, and altered oxygen binding
Montse Olivé+43 more
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Background Systemic inflammatory response syndrome (SIRS) is a clinical syndrome following inflammation. Clinically, it is difficult to distinguish SIRS following an infection, i.e., sepsis, from non-infectious SIRS.
Irene T. Schrijver+4 more
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Background: Thalassemia is the name of a group of genetically (acquired) blood diseases, which include defects on the production of hemeprotein, and fractional or complete damage to the combination of a particular sort of simple protein chain. The defect
Ismail Khalil Abd, Israa Ghassan Zainal
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Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein from Bacillus cereus
The nitric oxide synthase-like protein from Bacillus cereus (bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer.
Heather J. Montgomery+3 more
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Hydrogen sulfide activation in hemeproteins: The sulfheme scenario [PDF]
Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins.
Juan López-Garriga+3 more
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Evaluation of hemolysis effect on hemoglobin measurement by capillary electrophoresis
Background Hemoglobin (Hb) is a hemeprotein with two linked pairs of globin chains. Each chain is connected to a heme residue in its center. Hemoglobinopathies are divided into quantitative and qualitative defects in globin synthesis.
Armin Mokhtariye+4 more
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PP2A is activated by cytochrome c upon formation of a diffuse encounter complex with SET/TAF-Iβ
Intrinsic protein flexibility is of overwhelming relevance for intermolecular recognition and adaptability of highly dynamic ensemble of complexes, and the phenomenon is essential for the understanding of numerous biological processes.
Miguel Á. Casado-Combreras+12 more
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A number of surface residues of cytochrome c(6) from the cyanobacterium Anabaena sp. PCC 7119 have been modified by site-directed mutagenesis. Changes were made in six amino acids, two near the heme group (Val-25 and Lys-29) and four in the positively ...
F. P. Molina-Heredia+4 more
semanticscholar +1 more source
Glycation of heme-protein, “myoglobin” by 3-deoxyglucosone: Implications in immunogenicity
The Reactive carbonyl species (RCS) like, 3-deoxyglucosone (3-DG) is a highly reactive intermediate of the glycation reaction which may result into the formation of protein advanced glycation end-products (AGEs), like myoglobin-AGEs (Mb-AGEs) which ...
Rongfang Tang+5 more
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