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CYGB encodes a globin protein found in vertebrate cells. Additionally we are shipping Cytoglobin Antibodies (74) and Cytoglobin Kits (19) and many more products for this protein.
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The results uncover unexpected properties of zebrafish cytoglobin 1 and reveal the pivotal role of cytoglobin 1 in the transition of heme cytoglobin 1 from six-coordinate to five-coordinate oxygen carriers and nitrite reductases.
This study demonstrated the role of CYGB in fibroblast cell motility and proliferation. CYGB could be a promising candidate for further studies as a potential target for diseases related to cell migration such as cancer and chronic wound treatment.
Thus, the absence of Cygb in pericytes provokes organ abnormalities, possibly via derangement of the nitric oxide and antioxidant defence system and through accelerated cellular senescence.
Findings provide evidence for the loss of globin-linked neuroprotection to be linked to Alzheimer's disease angiopathogenesis, while raising the possibility of REST/ NRSF being an upstream regulator.
Cygb, expressed in hepatic stellate cells during liver fibrosis, plays role in cancer development with nonalcoholic steatohepatitis.
Studied hepatic stellate cell cytoglobin involvement in acetaminophen induced hepatotoxicity through the regulation of CYP2E1 (show CYP2E1 Proteins).
cytoglobin serves an important role in muscle repair and regeneration
Cygb deficiency induces susceptibility to cancer development in the liver and lungs of mice exposed to N,N-diethylnitrosamine
The anatomical data indicate a role in NO signalling for cytoglobin and involvement in sleep-wake cycling for cytoglobin and neuroglobin (show NGB Proteins)
The nuclear localization of cytoglobin opens new perspectives for possible function(s) of globin-folded proteins as transcriptional regulators.
differential expression of cytoglobin argues against a general respiratory function of this molecule, but rather indicates a connective tissue-specific function
the study reveals a novel mechanism for the regulated expression of Cygb and also assigns a new role to Cygb in cell cycle control.
Data suggest that cytochrome b5 (CYB5 (show CYB5A Proteins)) and cytochrome b5 reductase 3 (CYB5R3 (show CYB5R3 Proteins)) can reduce human cytoglobin (CYGB) and zebrafish cytoglobins at rates up to 250-fold higher than those reported for the known physiological substrates, hemoglobin (show HBB Proteins) and myoglobin (show MB Proteins); the three proteins (CYB5 (show CYB5A Proteins)+CYB5R3 (show CYB5R3 Proteins)+CYGB) appear to constitute a metabolon involved in generation of nitric oxide.
DeltaNp63-CYGB axis is also present in lung and breast cancer cell lines, indicating that CYGB-mediated ROS (show ROS1 Proteins)-scavenging activity may also have a role in epithelial tumours
Propose a bipartite lipid binding model that rationalizes the modes of interactions of cytoglobin with phospholipids, the effects on structural re-arrangements and the peroxidase activity of the hemoprotein.
This review provides an overview of the proposed role of cytoglobin and explores its potential functional role as a biomarker for cancer and other diseases
Cygb stabilizes p53 (show TP53 Proteins) by inhibiting its ubiquitination and elicit cell cycle arrest in DNA damaged cells.
The cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding in human cytoglobin.
The monomeric cytoglobin protein with an internal disulfide bond between the two cysteine residues Cys38 and Cys83, interacts with lipids to induce a change in haem co-ordination.
Protein multimerization may be a mechanism that triggers physiological functions of human cytoglobin.
This gene encodes a globin protein found in vertebrate cells. The encoded protein is described as a hexacoordinate hemoglobin which binds ligand differently from the pentacoordinate hemoglobins involved in oxygen transport, and may be involved in protection during oxidative stress. This gene is located on chromosome 17 in the same region as a retinal gene which is mutated in progressive rod-cone degeneration, but in the opposite orientation.
, stellate cell activation associated protein
, stellate cell activation-associated protein