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Volumn 321, Issue 5, 1998, Pages 373-376

Hb Nancy and Hb Osler: Two distinct genetic variants with identical clinical and hemoglobin phenotype;HB NANCY ET HB OSLER: DEUX VARIANTS DISTINCTS PARTAGEANT UN MEME PHENOTYPE CLINIQUE ET HEMOGLOBINIQUE

Author keywords

Abnormal hemoglobins; Deamidation; Erythrocytosis

Indexed keywords

ASPARTIC ACID; DNA; HEMOGLOBIN VARIANT; TYROSINE;

EID: 0032077611     PISSN: 07644469     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0764-4469(98)80300-4     Document Type: Article
Times cited : (5)

References (9)
  • 1
    • 0016612675 scopus 로고
    • Polycythemia produced by Hemoglobin Osler (β145(HC2) Tyr→Asp)
    • [1] Charache S., Brimhall B., Jones R.T., Polycythemia produced by Hemoglobin Osler (β145(HC2) Tyr→Asp), Johns Hopkins Med. J. 136 (1975) 132-136.
    • (1975) Johns Hopkins Med. J. , Issue.136 , pp. 132-136
    • Charache, S.1    Brimhall, B.2    Jones, R.T.3
  • 3
    • 0016795880 scopus 로고
    • Structural and functional study of Hb Nancy β145 (HC2) Tyr → Asp. A high oxygen affinity hemoglobin
    • [3] Gacon G., Wajcman H., Labie D., Vigneron C., Structural and functional study of Hb Nancy β145 (HC2) Tyr → Asp. A high oxygen affinity hemoglobin, FEBS Lett. 56 (1975) 39-42.
    • (1975) FEBS Lett. , vol.56 , pp. 39-42
    • Gacon, G.1    Wajcman, H.2    Labie, D.3    Vigneron, C.4
  • 5
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • [5] Tyler-Cross R., Schirch V., Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides, J. Biol. Chem. 266 (1991) 22549-22556.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 6
    • 0026500336 scopus 로고
    • Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: The example of Hb La Rochesur-Yon [β81(EF5)Leu→His]
    • [6] Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C., Cottenceau D., Galacteros F., Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Rochesur-Yon [β81(EF5)Leu→His], Biochim. Biophys. Acta 1138 (1992) 127-132.
    • (1992) Biochim. Biophys. Acta , vol.1138 , pp. 127-132
    • Wajcman, H.1    Kister, J.2    Vasseur, C.3    Blouquit, Y.4    Trastour, J.C.5    Cottenceau, D.6    Galacteros, F.7
  • 9
    • 8944258107 scopus 로고    scopus 로고
    • A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (β67[E11] Val→Met→Asp)
    • [9] Rees D.C., Rochette J., Schofield C., Green B., Morris M., Parker N.E., Sasaki H., Tanaka A., Ohba Y., Clegg J.B., A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (β67[E11] Val→Met→Asp), Blood 88 (1996) 341-348.
    • (1996) Blood , vol.88 , pp. 341-348
    • Rees, D.C.1    Rochette, J.2    Schofield, C.3    Green, B.4    Morris, M.5    Parker, N.E.6    Sasaki, H.7    Tanaka, A.8    Ohba, Y.9    Clegg, J.B.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.