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Volumn 47, Issue 4, 2007, Pages 628-630

The integrative and evolutionary biology of gas-binding copper proteins: An introduction

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EID: 38749131276     PISSN: 15407063     EISSN: 15577023     Source Type: Journal    
DOI: 10.1093/icb/icm038     Document Type: Article
Times cited : (1)

References (14)
  • 2
    • 34447498407 scopus 로고    scopus 로고
    • Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F. 2007a. Similar enzyme activation process and catalysis in hemocyanins and tyrosinases. Gene, 2007 May 13; [Epub ahead of print] PMID: 17566671 doi: 10.1016/j.gene.2007.02.051.
    • Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F. 2007a. Similar enzyme activation process and catalysis in hemocyanins and tyrosinases. Gene, 2007 May 13; [Epub ahead of print] PMID: 17566671 doi: 10.1016/j.gene.2007.02.051.
  • 3
    • 33746291588 scopus 로고    scopus 로고
    • The first crystal structure of tyrosinase: All questions answered? Highlight in Angewandte
    • Decker H, Schweikardt T, Tuczek F. 2006. The first crystal structure of tyrosinase: all questions answered? Highlight in Angewandte Chemie Engl Ed 45:4546-50.
    • (2006) Chemie Engl Ed , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 4
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M. 2006. Crystallographic evidence that dinuclear copper center of tyrosinase is flexible during catalysis. J Biol Chem 281:8981-90.
    • (2006) J Biol Chem , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 5
    • 33846638741 scopus 로고    scopus 로고
    • Limulus polyphemus hemocyanin: 10 Å structure, sequence analysis, molecular modelling and rigid-body fitting reveal the interfaces between the eight hexamers
    • Martin A, et al. 2007. Limulus polyphemus hemocyanin: 10 Å structure, sequence analysis, molecular modelling and rigid-body fitting reveal the interfaces between the eight hexamers. J Mol Biol 366:1332-50.
    • (2007) J Mol Biol , vol.366 , pp. 1332-1350
    • Martin, A.1
  • 6
    • 34547699086 scopus 로고    scopus 로고
    • Meissner U, Gatsogiannis C, Moeller A, Depoix F, Harris JR, Markl J. 2007. Comparative HA structure of two molluscan hemocyanins from 3D cryo-electron microscopy. Micron [epub 2006 Dec 8; ahead of print]. PMID: 17204427.
    • Meissner U, Gatsogiannis C, Moeller A, Depoix F, Harris JR, Markl J. 2007. Comparative HA structure of two molluscan hemocyanins from 3D cryo-electron microscopy. Micron [epub 2006 Dec 8; ahead of print]. PMID: 17204427.
  • 8
    • 23044512589 scopus 로고    scopus 로고
    • Allosteric models for multimeric proteins: Oxygen-linked effector binding in hemocyanin
    • Menze MA, Hellmann N, Decker H, Grieshaber MK. 2005. Allosteric models for multimeric proteins: oxygen-linked effector binding in hemocyanin. Biochemistry 44:10328-38.
    • (2005) Biochemistry , vol.44 , pp. 10328-10338
    • Menze, M.A.1    Hellmann, N.2    Decker, H.3    Grieshaber, M.K.4
  • 9
    • 34447509224 scopus 로고    scopus 로고
    • Paoli M, Giomi F, Hellmann N, Jaenicke E, Decker H, Di Muro P, Beltramini M. 2007. The molecular heterogeneity of hemocyanin: structural and functional properties of the 4 × 6-meric protein of Crustacea. Gene, 2007 Apr 25; [Epub ahead of print] doi:10.1016/j.gene.2007.02.035.
    • Paoli M, Giomi F, Hellmann N, Jaenicke E, Decker H, Di Muro P, Beltramini M. 2007. The molecular heterogeneity of hemocyanin: structural and functional properties of the 4 × 6-meric protein of Crustacea. Gene, 2007 Apr 25; [Epub ahead of print] doi:10.1016/j.gene.2007.02.035.
  • 10
    • 0034978152 scopus 로고    scopus 로고
    • Climate change and temperature dependent biogeography: Oxygen limitation of thermal tolerance in animals
    • Pörtner HO. 2001. Climate change and temperature dependent biogeography: oxygen limitation of thermal tolerance in animals. Naturwissenschaften 88:137-16.
    • (2001) Naturwissenschaften , vol.88 , pp. 137-216
    • Pörtner, H.O.1
  • 11
    • 33846695363 scopus 로고    scopus 로고
    • Climate change affects marine fishes through the oxygen limitation of thermal tolerance
    • Pörtner HO, Knust R. 2007. Climate change affects marine fishes through the oxygen limitation of thermal tolerance. Science 315:95-97.
    • (2007) Science , vol.315 , pp. 95-97
    • Pörtner, H.O.1    Knust, R.2
  • 13
    • 33644927531 scopus 로고    scopus 로고
    • Functional and phylogenetic analyses of phenoloxidases from brachyuran (Cancer magister) and branchiopod (Artemia franciscana, Triops longicaudatus) crustaceans
    • Terwilliger N, Ryan M. 2006. Functional and phylogenetic analyses of phenoloxidases from brachyuran (Cancer magister) and branchiopod (Artemia franciscana, Triops longicaudatus) crustaceans. Biol Bull 210:38-50.
    • (2006) Biol Bull , vol.210 , pp. 38-50
    • Terwilliger, N.1    Ryan, M.2
  • 14
    • 0035844294 scopus 로고    scopus 로고
    • Hemocyanins and invertebrate evolution
    • van Holde K, Miller K, Decker H. 2001. Hemocyanins and invertebrate evolution. J Biol Chem 276:15563-66.
    • (2001) J Biol Chem , vol.276 , pp. 15563-15566
    • van Holde, K.1    Miller, K.2    Decker, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.