Cytoglobin

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Cytoglobin
PDB rendering based on 1umo.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols CYGB ; HGB; STAP
External IDs Template:OMIM5 Template:MGI HomoloGene12706
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Cytoglobin, also known as CYGB, is a human gene.[1]

Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or other reactive oxygen species, or serve a protective function during oxidative stress (Trent and Hargrove, 2002).[supplied by OMIM][1]

References

  1. 1.0 1.1 "Entrez Gene: CYGB cytoglobin".

Further reading

  • Kawada N, Kristensen DB, Asahina K; et al. (2001). "Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells". J. Biol. Chem. 276 (27): 25318–23. doi:10.1074/jbc.M102630200. PMID 11320098.
  • Trent JT, Hargrove MS (2002). "A ubiquitously expressed human hexacoordinate hemoglobin". J. Biol. Chem. 277 (22): 19538–45. doi:10.1074/jbc.M201934200. PMID 11893755.
  • Burmester T, Ebner B, Weich B, Hankeln T (2002). "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues". Mol. Biol. Evol. 19 (4): 416–21. PMID 11919282.
  • Asahina K, Kawada N, Kristensen DB; et al. (2002). "Characterization of human stellate cell activation-associated protein and its expression in human liver". Biochim. Biophys. Acta. 1577 (3): 471–5. PMID 12359339.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Sawai H, Kawada N, Yoshizato K; et al. (2003). "Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans". Biochemistry. 42 (17): 5133–42. doi:10.1021/bi027067e. PMID 12718557.
  • Geuens E, Brouns I, Flamez D; et al. (2003). "A globin in the nucleus!". J. Biol. Chem. 278 (33): 30417–20. doi:10.1074/jbc.C300203200. PMID 12796507.
  • Hamdane D, Kiger L, Dewilde S; et al. (2004). "The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin". J. Biol. Chem. 278 (51): 51713–21. doi:10.1074/jbc.M309396200. PMID 14530264.
  • Schmidt M, Gerlach F, Avivi A; et al. (2004). "Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia". J. Biol. Chem. 279 (9): 8063–9. doi:10.1074/jbc.M310540200. PMID 14660570.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Hünermund G, Schirmacher A, Ringelstein B; et al. (2004). "Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy". Muscle Nerve. 29 (4): 601–4. doi:10.1002/mus.20009. PMID 15052627.
  • de Sanctis D, Dewilde S, Pesce A; et al. (2004). "Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination". J. Mol. Biol. 336 (4): 917–27. PMID 15095869.
  • Sugimoto H, Makino M, Sawai H; et al. (2004). "Structural basis of human cytoglobin for ligand binding". J. Mol. Biol. 339 (4): 873–85. doi:10.1016/j.jmb.2004.04.024. PMID 15165856.
  • Fago A, Hundahl C, Dewilde S; et al. (2004). "Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance". J. Biol. Chem. 279 (43): 44417–26. doi:10.1074/jbc.M407126200. PMID 15299006.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Hamdane D, Kiger L, Dewilde S; et al. (2005). "Hyperthermal stability of neuroglobin and cytoglobin". FEBS J. 272 (8): 2076–84. doi:10.1111/j.1742-4658.2005.04635.x. PMID 15819897.
  • Sawai H, Makino M, Mizutani Y; et al. (2006). "Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin". Biochemistry. 44 (40): 13257–65. doi:10.1021/bi050997o. PMID 16201751.
  • Shaw RJ, Liloglou T, Rogers SN; et al. (2006). "Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing". Br. J. Cancer. 94 (4): 561–8. doi:10.1038/sj.bjc.6602972. PMID 16449996.
  • McRonald FE, Liloglou T, Xinarianos G; et al. (2006). "Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression". Hum. Mol. Genet. 15 (8): 1271–7. doi:10.1093/hmg/ddl042. PMID 16510494.
  • Xinarianos G, McRonald FE, Risk JM; et al. (2006). "Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer". Hum. Mol. Genet. 15 (13): 2038–44. doi:10.1093/hmg/ddl128. PMID 16698880.


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