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Volumn 398, Issue 1-2 SPEC. ISS., 2007, Pages 35-41

Exploiting a list of protein sequences

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN;

EID: 34447527074     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.01.036     Document Type: Article
Times cited : (8)

References (11)
  • 1
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester T., Weich B., Reinhardt S., and Hankeln T. A vertebrate globin expressed in the brain. Nature 407 (2000) 520-523
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 2
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T., Ebner B., Weich B., and Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol. Biol. Evol. 19 (2002) 416-421
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 3
    • 0035914459 scopus 로고    scopus 로고
    • Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family
    • Dewilde S., et al. Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J. Biol. Chem. 276 (2001) 38949-38955
    • (2001) J. Biol. Chem. , vol.276 , pp. 38949-38955
    • Dewilde, S.1
  • 4
    • 8844285199 scopus 로고    scopus 로고
    • Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin
    • Feng L., et al. Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin. Cell 119 (2004) 629-640
    • (2004) Cell , vol.119 , pp. 629-640
    • Feng, L.1
  • 5
    • 9144247276 scopus 로고    scopus 로고
    • The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin
    • Hamdane D., et al. The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin. J. Biol. Chem. 278 (2003) 51713-51721
    • (2003) J. Biol. Chem. , vol.278 , pp. 51713-51721
    • Hamdane, D.1
  • 6
    • 0036190154 scopus 로고    scopus 로고
    • HbVar: A relational database of human hemoglobin variants and thalassemia mutations at the globin gene server
    • Hardison R.C., et al. HbVar: A relational database of human hemoglobin variants and thalassemia mutations at the globin gene server. Human Mutat. 19 (2002) 225-233
    • (2002) Human Mutat. , vol.19 , pp. 225-233
    • Hardison, R.C.1
  • 7
    • 0028843842 scopus 로고
    • Alignment of 700 globin sequences: extent of amino acid substitution and its correlation with variation in volume
    • Kapp O.H., Moens L., Vanfleteren J., Trotman C.N., Suzuki T., and Vinogradov S.N. Alignment of 700 globin sequences: extent of amino acid substitution and its correlation with variation in volume. Protein Sci. 4 (1995) 2179-2190
    • (1995) Protein Sci. , vol.4 , pp. 2179-2190
    • Kapp, O.H.1    Moens, L.2    Vanfleteren, J.3    Trotman, C.N.4    Suzuki, T.5    Vinogradov, S.N.6
  • 8
    • 0041833723 scopus 로고    scopus 로고
    • Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity
    • Pesce A., et al. Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure (Camb) 11 (2003) 1087-1095
    • (2003) Structure (Camb) , vol.11 , pp. 1087-1095
    • Pesce, A.1
  • 10
    • 33750908580 scopus 로고    scopus 로고
    • Impaired binding of AHSP to alpha chain variants: Hb Groene Hart illustrates a mechanism leading to unstable hemoglobins with alpha thalassemic like syndrome
    • Vasseur-Godbillon C., Marden M.C., Giordano P., Wajcman H., and Baudin-Creuza V. Impaired binding of AHSP to alpha chain variants: Hb Groene Hart illustrates a mechanism leading to unstable hemoglobins with alpha thalassemic like syndrome. Blood Cells Mol. Diseases 37 (2006) 173-179
    • (2006) Blood Cells Mol. Diseases , vol.37 , pp. 173-179
    • Vasseur-Godbillon, C.1    Marden, M.C.2    Giordano, P.3    Wajcman, H.4    Baudin-Creuza, V.5
  • 11
    • 34447565280 scopus 로고    scopus 로고
    • Weblinks: Protein families: http://pfam.wustl.edu/; Protein sequences: PIR: http://pir.georgetown.edu/home.shtml; ExPASy:http://au.expasy.org/; Swiss-Prot: http://us.expasy.org/cgi-bin/niceprot.pl?; Taxonomy information: NEWT: http://www.ebi.ac.uk/newt/index.html; general information: CalPhotos: http://elib.cs.berkeley.edu/photos/; FishBase: http://www.fishbase.org/home.htm; Google images: http://images.google.com; Wikipedia: http://en.wikipedia.org/wiki/Main_Page. A Database of Human Hemoglobin Variants and Thalassemias: http://globin.bx.psu.edu/hbvar/menu.html; Molecular graphics: accelrys.com or Jmol.org.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.