메뉴 건너뛰기




Volumn 35, Issue 1-2, 2004, Pages 15-16

Tarantula hemocyanins imaged by atomic force microscopy

Author keywords

Atomic force microscopy; Hemocyanin

Indexed keywords

TARANTULA;

EID: 1242300263     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2003.10.005     Document Type: Conference Paper
Times cited : (1)

References (14)
  • 1
    • 0030590489 scopus 로고    scopus 로고
    • Small angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin
    • Decker H., Hartmann H., Sterner R., Schwarz E., Pilz I. Small angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin. FEBS Lett. 393:1996;226-230.
    • (1996) FEBS Lett. , vol.393 , pp. 226-230
    • Decker, H.1    Hartmann, H.2    Sterner, R.3    Schwarz, E.4    Pilz, I.5
  • 2
    • 0037121459 scopus 로고    scopus 로고
    • All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation
    • Hartmann H., Decker H. All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation. Biochim. Biophys. Acta. 1601:2002;132-137.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 132-137
    • Hartmann, H.1    Decker, H.2
  • 3
    • 1542299073 scopus 로고    scopus 로고
    • Small-angle scattering techniques for analysing conformational transitions in hemocyanins
    • J.M. Holt, M.L. Johnson, & G.K. Ackers. in press
    • Hartmann H., Decker H. Small-angle scattering techniques for analysing conformational transitions in hemocyanins. Holt J.M., Johnson M.L., Ackers G.K. Methods in Enzymology, Energetics of Biological Macromolecules. 2004;. in press.
    • (2004) Methods in Enzymology, Energetics of Biological Macromolecules
    • Hartmann, H.1    Decker, H.2
  • 4
    • 1242338977 scopus 로고    scopus 로고
    • Small-angle X-ray scattering based 3D reconstruction of the immunogen KLH1 reveals different oxygen dependent conformations
    • doi: 10.1074/jbc.M308959200
    • Hartmann, H., Bongers, A., Decker, H., 2004. Small-angle X-ray scattering based 3D reconstruction of the immunogen KLH1 reveals different oxygen dependent conformations. J. Biol. Chem. doi: 10.1074/jbc.M308959200.
    • (2004) J. Biol. Chem.
    • Hartmann, H.1    Bongers, A.2    Decker, H.3
  • 5
    • 0035827704 scopus 로고    scopus 로고
    • Lactate induced conformational changes of 12-meric lobster hemocyanin as revealed by SAXS
    • Hartmann H., Lohkamp B., Hellmann N., Decker H. Lactate induced conformational changes of 12-meric lobster hemocyanin as revealed by SAXS. J. Biol. Chem. 276:2001;19954-19958.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19954-19958
    • Hartmann, H.1    Lohkamp, B.2    Hellmann, N.3    Decker, H.4
  • 6
    • 0034778181 scopus 로고    scopus 로고
    • Small angle neutron scattering reveals an oxygen dependent conformational change of the immunogen keyhole limpet hemocyanin (KLH1)
    • Hartmann H., Bongers A., Decker H. Small angle neutron scattering reveals an oxygen dependent conformational change of the immunogen keyhole limpet hemocyanin (KLH1). Eur. Biophys. J. 30:2001;471-475.
    • (2001) Eur. Biophys. J. , vol.30 , pp. 471-475
    • Hartmann, H.1    Bongers, A.2    Decker, H.3
  • 7
    • 0027529265 scopus 로고
    • Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
    • Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., Hol W.G. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Protein Sci. 1993;597-597.
    • (1993) Protein Sci. , pp. 597-597
    • Hazes, B.1    Magnus, K.A.2    Bonaventura, C.3    Bonaventura, J.4    Dauter, Z.5    Kalk, K.H.6    Hol, W.G.7
  • 8
    • 0027981519 scopus 로고
    • Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
    • Magnus K.A., Hazes B., Ton-That H., Bonavenura C., Bonaventur J., Hol W.G. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins. 19:1994;302-309.
    • (1994) Proteins , vol.19 , pp. 302-309
    • Magnus, K.A.1    Hazes, B.2    Ton-That, H.3    Bonavenura, C.4    Bonaventur, J.5    Hol, W.G.6
  • 9
    • 0000222758 scopus 로고
    • Molecular structure of arthropodan hemocyanins
    • Markl J., Decker H. Molecular structure of arthropodan hemocyanins. Adv. Comp. Environ. Physiol. 13:1992;325-376.
    • (1992) Adv. Comp. Environ. Physiol. , vol.13 , pp. 325-376
    • Markl, J.1    Decker, H.2
  • 11
    • 0034915862 scopus 로고    scopus 로고
    • Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy
    • Valle F., Derose J.A., Dietler G., Kawe M., Plückthun A., Semenza G. Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy. J. Microsc. 203:2001;195-198.
    • (2001) J. Microsc. , vol.203 , pp. 195-198
    • Valle, F.1    Derose, J.A.2    Dietler, G.3    Kawe, M.4    Plückthun, A.5    Semenza, G.6
  • 14
    • 0024975122 scopus 로고
    • Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution
    • Volbeda A., Hol W.G. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J. Mol. Biol. 209:1989;249-279.
    • (1989) J. Mol. Biol. , vol.209 , pp. 249-279
    • Volbeda, A.1    Hol, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.