title: Classification of the disorders of hemoglobin.
abstract: Over the years, study of the disorders of hemoglobin has served as a paradigm for gaining insights into the cellular and molecular biology, as well as the pathophysiology, of inherited genetic disorders. To date, more than 1000 disorders of hemoglobin synthesis and/or structure have been identified and characterized. Study of these disorders has established the principle of how a mutant genotype can alter the function of the encoded protein, which in turn can lead to a distinct clinical phenotype. Genotype/phenotype correlations have provided important understanding of pathophysiological mechanisms of disease. Before presenting a brief overview of these disorders, we provide a summary of the structure and function of hemoglobin, along with the mechanism of assembly of its subunits, as background for the rationale and basis of the different categories of disorders in the classification.
authors: Section of Hematology, Department of Medicine, Yale School of Medicine, New Haven, Connecticut 06520-8028, USA.
authors: Bernard G
authors: BG
authors: Forget
authors: H Franklin
authors: HF
authors: Bunn
mesh_terms: D000755:Anemia, Sickle Cell / Q000145:classification / Q000235:genetics; D005914:Globins / Q000378:metabolism; D006453:Hemoglobinopathies / Q000145:classification* / Q000235:genetics; D006454:Hemoglobins / Q000737:chemistry / Q000502:physiology; D006455:Hemoglobins, Abnormal / Q000235:genetics; D006801:Humans; D008607:Intellectual Disability / Q000235:genetics; D009154:Mutation; D009190:Myelodysplastic Syndromes / Q000235:genetics; D010100:Oxygen / Q000378:metabolism; D010641:Phenotype; D014176:Protein Biosynthesis; D013789:Thalassemia / Q000145:classification / Q000235:genetics
chemical_list: D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D005914:Globins; D010100:Oxygen
references: Blood. 1998 Feb 15;91(4):1438-45
references: 9454775
references: Cold Spring Harb Perspect Med. 2013 Jan 01;3(1):a011643
references: 23209159
references: Blood. 1998 Dec 1;92(11):4375-82
references: 9834244
references: Cold Spring Harb Perspect Med. 2013 Mar 01;3(3):a011858
references: 23388674
references: Nature. 1983 Dec 1-7;306(5942):498-500
references: 6646230
references: Cold Spring Harb Perspect Med. 2013 Oct 01;3(10):a011783
references: 23813607
references: Nature. 2002 Jun 13;417(6890):758-63
references: 12066189
references: Cold Spring Harb Perspect Med. 2013 Jan 01;3(1):a011718
references: 23284078
references: Cold Spring Harb Perspect Med. 2012 Dec 01;2(12):a011726
references: 23209183
references: Cell. 2004 Nov 24;119(5):629-40
references: 15550245
references: Cold Spring Harb Perspect Med. 2012 Oct 01;2(10):
references: 23028136
references: Cold Spring Harb Perspect Med. 2012 Aug 01;2(8):
references: 22908199
references: Antioxid Redox Signal. 2010 Feb;12(2):219-31
references: 19659437
references: Cold Spring Harb Perspect Med. 2013 Apr 01;3(4):a011676
references: 23471474
references: Blood. 1987 Jan;69(1):1-6
references: 3539223
references: Proc Natl Acad Sci U S A. 1982 Dec;79(23):7527-31
references: 6961429
references: N Engl J Med. 1990 Jul 19;323(3):179-82
references: 1694572
references: N Engl J Med. 1985 Nov 28;313(22):1402-5
references: 2414661
references: Cold Spring Harb Perspect Med. 2012 Jul;2(7):a013482
references: 22762026
references: J Biol Chem. 2012 Mar 30;287(14):11338-50
references: 22298770
references: Cold Spring Harb Perspect Med. 2013 May 01;3(5):a011700
references: 23637309
references: J Biol Chem. 1986 Apr 15;261(11):5222-8
references: 3957922