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0016612675
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Polycythemia produced by Hemoglobin Osler (β145(HC2) Tyr→Asp)
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[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.
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Charache, S.1
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2 145 Tyr→Asp, a new high-oxygen-affinity hemoglobin variant
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2 145 Tyr→Asp), a new high-oxygen-affinity hemoglobin variant, Biochim. Biophys. Acta 400 (1975) 343-347.
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Structural and functional study of Hb Nancy β145 (HC2) Tyr → Asp. A high oxygen affinity hemoglobin
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[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.
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Hemoglobin S/Hemoglobin Osler: A case with 3 β globin chains. DNA sequence (AAT) proves that Hb Osler is β 145 Tyr→Asn
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[4] Hutt P.J., Donaldson M.H., Khatri J., Fairbanks V.F., Hoyer J.D., Thibodeau S.N., Moxness M.S., McMorrow L.E., Green M.M., Jones R.T., Hemoglobin S/Hemoglobin Osler: A case with 3 β globin chains. DNA sequence (AAT) proves that Hb Osler is β 145 Tyr→Asn, Am. J. Hematol. 52 (1996) 305-309.
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Moxness, M.S.7
McMorrow, L.E.8
Green, M.M.9
Jones, R.T.10
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5
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0025788030
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Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
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[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.
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Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: The example of Hb La Rochesur-Yon [β81(EF5)Leu→His]
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[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.
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Cottenceau, D.6
Galacteros, F.7
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7
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0031003718
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Hb Osler [β145(HC2) Tyr→Asp] results from posttranslational modification
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[7] Kattamis A.C., Kelly K.M., Ohene-Frempong K., Reilly M.P., Keller M., Cubeddu R., Adachi K., Surrey S., Fortina P., Hb Osler [β145(HC2) Tyr→Asp] results from posttranslational modification, Hemoglobin 21 (1997) 109-120.
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Adachi, K.7
Surrey, S.8
Fortina, P.9
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8
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267(E11)Val→Met: A new unstable hemoglobin variant identified through sequencing of amplified DNA
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267(E11)Val→Met: a new unstable hemoglobin variant identified through sequencing of amplified DNA, Hemoglobin 17 (1993) 217-225.
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Molchanova, T.P.1
Postnikov, Yu.V.2
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Moschan, A.A.5
Kazanetz, E.G.6
Tokarev, Y.N.7
Huisman, T.H.J.8
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9
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A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (β67[E11] Val→Met→Asp)
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[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.
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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
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