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THBD  -  thrombomodulin

Canis lupus familiaris

 
 
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High impact information on THBD

  • Obviously, the polyglycine spacer facilitates the accessibility of the O-glycans in GH-SI(Gly/SR/TM) to a putative sorting receptor, whereas these glycans are inadequately recognized in GH-SI(SR/TM) [1].
  • Only when a polyglycine spacer is inserted between the stalk region of SI and the luminal part of rGH in the GH-SI(Gly/SR/TM) fusion protein does efficient apical sorting of an O-glycosylated protein as well as a time-dependent association with detergent-insoluble lipid microdomains occur [1].
  • Scanning N-glycosylation mutagenesis and Mlo-Lep fusion proteins demonstrated that Mlo is membrane-anchored by 7 transmembrane (TM) helices such that the N terminus is located extracellularly and the C terminus intracellularly [2].
  • Point mutations were characterized that alter the conformation of the SU/TM heterodimers on the viral particles [3].
  • Mutation of either G541R in the amphotropic 4070A TM, V421M in the 4070A SU, or deletion of S39 and P40 at the N-terminus of the M-MuLV SU results in an irreversible cold-sensitive phenotype at 4 degrees C. This loss of viral titer can be restored by incorporating V421M plus G541R or del S39 P40 plus G541R in cis within the SU/TM [3].
 

Biological context of THBD

  • The entire open reading frame of canine TM cDNA comprises 1737 bp, encoding 578 amino acid residues [4].
  • Comparison of the deduced amino acid sequence from canine TM with those of human, mouse, rat, rabbit and bovine (partial) TM sequences revealed 73.1%, 69.1%, 65.8%, 74.3% and 69.5% identity, respectively [4].
 

Anatomical context of THBD

 

Other interactions of THBD

  • Immunohistochemical labeling for von Willebrand factor, tissue factor, factor XII, tissue factor pathway inhibitor, thrombomodulin, protein C, protein S and prothrombin activation fragment F1 + 2 was performed [5].
 

Analytical, diagnostic and therapeutic context of THBD

  • Molecular cloning of canine thrombomodulin cDNA and expression in normal tissues [4].
  • Mutation of position E311 within the Moloney MuLV SU protein alters the conformation of the TM protein and its recognition by antibody 42-114 in immunoprecipitation reactions [3].
  • The systemic and hepatic hemodynamics were measured, before and 180 min after the hepatectomy, and the remaining liver tissue was then examined immunohistochemically by light microscopy using the thrombomodulin (TM) staining method [6].

References

  1. Characteristics and structural requirements of apical sorting of the rat growth hormone through the O-glycosylated stalk region of intestinal sucrase-isomaltase. Spodsberg, N., Alfalah, M., Naim, H.Y. J. Biol. Chem. (2001) [Pubmed]
  2. Topology, subcellular localization, and sequence diversity of the Mlo family in plants. Devoto, A., Piffanelli, P., Nilsson, I., Wallin, E., Panstruga, R., von Heijne, G., Schulze-Lefert, P. J. Biol. Chem. (1999) [Pubmed]
  3. Identification of conformational and cold-sensitive mutations in the MuLV envelope protein. O'Reilly, L., Roth, M.J. Virology (2003) [Pubmed]
  4. Molecular cloning of canine thrombomodulin cDNA and expression in normal tissues. Maruyama, H., Oguma, K., Maeda, S., Kano, R., Tsujimoto, H., Watari, T., Tokuriki, M., Hasegawa, A. J. Vet. Med. Sci. (2004) [Pubmed]
  5. Coagulation activators and inhibitors in the neointima of polyester vascular grafts. Kowalewski, R., Zimnoch, L., Wojtukiewicz, M.Z., Glowinski, S., Glowinski, J. Blood Coagul. Fibrinolysis (2003) [Pubmed]
  6. Effect of prior portosystemic shunt on early hepatic hemodynamics and sinusoids following 84% hepatectomy in dogs. Ueno, S., Kobayashi, Y., Kurita, K., Tanabe, G., Aikou, T. Research in experimental medicine. Zeitschrift für die gesamte experimentelle Medizin einschliesslich experimenteller Chirurgie. (1995) [Pubmed]
 
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