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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Decapodiformes

 
 
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Disease relevance of Decapodiformes

  • The acidosis provoked by octopine formation in Illex was demonstrated to promote the use of the phosphagen and to protect the free energy change of ATP such that the anaerobic scope of metabolism during swimming is extended and expressed more in Illex than in Loligo [1].
 

High impact information on Decapodiformes

 

Biological context of Decapodiformes

 

Anatomical context of Decapodiformes

 

Associations of Decapodiformes with chemical compounds

  • An empirical equation relating O2 consumption (power input) to pressure production during jet-propelled swimming in the squid (Illex illecebrosus) is compared with hydrodynamic estimates of the pressure-flow power output also calculated from pressure data [10].
  • Three fucose-rich glycosaminoglycans (GAGs), illexin A, illexin B and illexin C, were isolated from squid ink of Illex argentinus [11].
  • Tyrosinase (monophenol, L-DOPA:oxygen oxidoreductase) was isolated from the ink of the squid, Illex argentinus [12].
  • A cysteine-activated protease isolated from todarodes pacificus squid degrades collagen below its denaturation temperature [13].
  • Squid (Todarodes pacificus) was sliced, washed, and then salted with 5, 10, and 20% (wt/wt) sodium chloride [14].
 

Gene context of Decapodiformes

  • A cDNA for rhodopsin was isolated from a library constructed from poly(A)+RNA of the squid (Todarodes pacificus) retina [3].
  • Anti-IRBP also reacted with pure RALBP prepared from Todarodes pacificus [15].
  • Squid (Todarodes pacificus) liver RNase (RNase Tp) was purified [16].
  • Comparison of two offshore squid species (Loligo pealei and Illex illecebrosus) with the estuarine squid L.brevis indicates that the latter uses a strategy to delay the exploitation of high-energy phosphates and protect energy levels at higher than the minimum levels (-42 kJ/mol) characterizing fatigue in the other species [17].
 

Analytical, diagnostic and therapeutic context of Decapodiformes

References

  1. Metabolism and energetics in squid (Illex illecebrosus, Loligo pealei) during muscular fatigue and recovery. Pörtner, H.O., Webber, D.M., O'Dor, R.K., Boutilier, R.G. Am. J. Physiol. (1993) [Pubmed]
  2. Identification of the first major allergen of a squid (Todarodes pacificus). Miyazawa, H., Fukamachi, H., Inagaki, Y., Reese, G., Daul, C.B., Lehrer, S.B., Inouye, S., Sakaguchi, M. J. Allergy Clin. Immunol. (1996) [Pubmed]
  3. Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus. Hara-Nishimura, I., Kondo, M., Nishimura, M., Hara, R., Hara, T. FEBS Lett. (1993) [Pubmed]
  4. Amino acid sequence surrounding the retinal-binding site in retinochrome of the squid, Todarodes pacificus. Hara-Nishimura, I., Kondo, M., Nishimura, M., Hara, R., Hara, T. FEBS Lett. (1993) [Pubmed]
  5. Cadmium-binding proteins of three marine molluscs and characterization of two cadmium-binding glycoproteins from the hepatopancreas of a whelk, Buccinum tenuissimum. Dohi, Y., Kosaka, K., Ohba, K., Yoneyama, Y. Environ. Health Perspect. (1986) [Pubmed]
  6. A source of large axons for neurophysiology: the North Atlantic squid Illex illecebrosus. Geduldig, D., Hoekman, T. Can. J. Physiol. Pharmacol. (1979) [Pubmed]
  7. Amino acid sequence of the regulatory light chain of squid mantle muscle myosin. Maita, T., Tanaka, H., Konno, K., Matsuda, G. J. Biochem. (1987) [Pubmed]
  8. Histochemical localization of retinochrome and rhodopsin studied by fluorescence microscopy. Ozaki, K., Hara, R., Hara, T. Cell Tissue Res. (1983) [Pubmed]
  9. Identification of high molecular weight proteins in squid muscle by Western blotting analysis and postmortem rheological changes. Kasamatsu, C., Kimura, S., Kagawa, M., Hatae, K. Biosci. Biotechnol. Biochem. (2004) [Pubmed]
  10. Limitations on locomotor performance in squid. O'Dor, R.K. J. Appl. Physiol. (1988) [Pubmed]
  11. Novel fucose-rich glycosaminoglycans from squid ink bearing repeating unit of trisaccharide structure (-6GalNAc alpha 1-3GlcA beta 1-3Fuc alpha 1-)n. Takaya, Y., Uchisawa, H., Hanamatsu, K., Narumi, F., Okuzaki, B., Matsue, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  12. Purification, characterization and molecular cloning of tyrosinase from the cephalopod mollusk, Illex argentinus. Naraoka, T., Uchisawa, H., Mori, H., Matsue, H., Chiba, S., Kimura, A. Eur. J. Biochem. (2003) [Pubmed]
  13. A cysteine-activated protease isolated from todarodes pacificus squid degrades collagen below its denaturation temperature. Miura-Yokota, Y., Matsubara, Y., Ebihara, T., Hattori, S., Irie, S. Connect. Tissue Res. (2004) [Pubmed]
  14. Effects of gamma radiation on sensory qualities, microbiological and chemical properties of salted and fermented squid. Byun, M.W., Lee, K.H., Kim, D.H., Kim, J.H., Yook, H.S., Ahn, H.J. J. Food Prot. (2000) [Pubmed]
  15. IRBP-like proteins in the eyes of six cephalopod species--immunochemical relationship to vertebrate interstitial retinol-binding protein (IRBP) and cephalopod retinal-binding protein. Fong, S.L., Lee, P.G., Ozaki, K., Hara, R., Hara, T., Bridges, C.D. Vision Res. (1988) [Pubmed]
  16. Primary structure of a squid acid and base non-specific ribonuclease. Kusano, A., Iwama, M., Ohgi, K., Irie, M. Biosci. Biotechnol. Biochem. (1998) [Pubmed]
  17. Metabolic and energy correlates of intracellular pH in progressive fatigue of squid (L. brevis) mantle muscle. Pörtner, H.O., Finke, E., Lee, P.G. Am. J. Physiol. (1996) [Pubmed]
  18. Purification of a 63 kDa beta-D-galactoside binding lectin from cuttlefish, Todarodes pacificus. Ozeki, Y. Biochem. Mol. Biol. Int. (1997) [Pubmed]
  19. Circular dichroism of squid rhodopsin and its intermediates. Shichida, Y., Tokunaga, F., Yoshizawa, T. Biochim. Biophys. Acta (1978) [Pubmed]
 
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