Shin C, Hong M, Kim M, Lee J
BMC Pediatr. 2019; 19(1):221.
PMID: 31269924
PMC: 6607536.
DOI: 10.1186/s12887-019-1601-9.
Hooven T, Hooper E, Wontakal S, Francis R, Sahni R, Lee M
BMJ Case Rep. 2016; 2016:10.1136/bcr-2016-215193.
PMID: 27095814
PMC: 4840678.
DOI: 10.1136/bcr-2016-215193.
Elboraee M, Clarke G, Belletrutti M, Escoredo S
BMJ Case Rep. 2015; 2015.
PMID: 26494721
PMC: 4620215.
DOI: 10.1136/bcr-2015-212336.
Huehns E
Proc R Soc Med. 2009; 58(7):514-6.
PMID: 19994423
PMC: 1898643.
Aki Y, Nagai M, Nagai Y, Imai K, Aki M, Sato A
J Biol Inorg Chem. 2009; 15(2):147-58.
PMID: 19701784
DOI: 10.1007/s00775-009-0579-4.
Structure-function relations of human hemoglobins.
Marengo-Rowe A
Proc (Bayl Univ Med Cent). 2007; 19(3):239-45.
PMID: 17252042
PMC: 1484532.
DOI: 10.1080/08998280.2006.11928171.
HUMAN HAEMOGLOBINS.
Huehns E, SHOOTER E
J Med Genet. 1965; 2(1):48-90.
PMID: 14296925
PMC: 1012805.
DOI: 10.1136/jmg.2.1.48.
HEREDITARY METHEMOGLOBINEMIC CYANOSIS IN A MAN WITH ATRIAL SEPTAL DEFECT.
SPEARS J, NAIMAN J, Evans J, CROOKSTON J
Can Med Assoc J. 1965; 92:468-70.
PMID: 14259339
PMC: 1927825.
[The globins].
Hilschmann N
Blut. 1961; 7:433-43.
PMID: 14036228
DOI: 10.1007/BF01636097.
Relations between mutations and base sequences in the amino acid code.
Jukes T
Proc Natl Acad Sci U S A. 1962; 48:1809-15.
PMID: 14029847
PMC: 221044.
DOI: 10.1073/pnas.48.10.1809.
[Contribution of studies on human hemoglobin to the solution of some basic problems of genetics].
Vogel F
Blut. 1962; 8:449-63.
PMID: 13997622
DOI: 10.1007/BF01631299.
A comparison of the tryptic peptides obtained from immobilization antigens of Paramecium aurelia.
Steers Jr E
Proc Natl Acad Sci U S A. 1962; 48:867-74.
PMID: 13916508
PMC: 220868.
DOI: 10.1073/pnas.48.5.867.
Nucleotide base coding and amino acid replacements in proteins.
Smith E
Proc Natl Acad Sci U S A. 1962; 48:677-84.
PMID: 13914208
PMC: 220832.
DOI: 10.1073/pnas.48.4.677.
[Hemoglobin anomalies].
Betke K
Blut. 1961; 7:443-51.
PMID: 13868621
DOI: 10.1007/BF01636098.
An exceptional amino acid replacement on the distal side of the iron atom in proboscidean myoglobin.
Goodman M, Dene H, Bartnicki D, Mizukami H
J Mol Evol. 1981; 17(3):140-7.
PMID: 7265266
DOI: 10.1007/BF01733907.
Hemoglobins, XLVIIII. The primary structure of a monomeric hemoglobin from the hagfish, Myxine glutinosa L.: evolutionary aspects and comparative studies of the function with special reference to the heme linkage.
Liljeqvist G, PALEUS S, Braunitzer G
J Mol Evol. 1982; 18(2):102-8.
PMID: 7097771
DOI: 10.1007/BF01810828.
Hb M Milwaukee: direct detection of the beta-globin gene mutation in three generations of an afflicted family.
Oehme R, Kohne E, Kleihauer E, Horst J
Hum Genet. 1983; 64(4):376-9.
PMID: 6311728
DOI: 10.1007/BF00292370.
[HbM Hamburg, a beta chain anomaly: alpha-2-beta-2-63Tyr (equals HbM Saskatoon)].
Betke K, Kleihauer E, Braunitzer G, Jacobi J, Schmidt I
Klin Wochenschr. 1966; 44(16):961-6.
PMID: 5996551
DOI: 10.1007/BF01711469.
[Hb Tübingen. A new beta-chain variant (beta Tp 10-21) with increased spontaneous oxidation].
Kleihauer E, Waller H, Benohr H, Kohne E, GELINSKY P
Klin Wochenschr. 1971; 49(11):651-8.
PMID: 5579703
DOI: 10.1007/BF01492044.
Comparative study of the primary structures of cytochrome b5 from four species.
Tsugita A, Kobayashi M, Tani S, Kyo S, Rashid M
Proc Natl Acad Sci U S A. 1970; 67(1):442-7.
PMID: 5272324
PMC: 283224.
DOI: 10.1073/pnas.67.1.442.
