Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
2R01DK034083-15
Application #
2139226
Study Section
Hematology Subcommittee 2 (HEM)
Project Start
1983-07-01
Project End
2000-06-30
Budget Start
1996-08-01
Budget End
1997-06-30
Support Year
15
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Children's Hospital Boston
Department
Type
DUNS #
076593722
City
Boston
State
MA
Country
United States
Zip Code
02115
Peters, Luanne L; Swearingen, Rebecca A; Andersen, Sabra G et al. (2004) Identification of quantitative trait loci that modify the severity of hereditary spherocytosis in wan, a new mouse model of band-3 deficiency. Blood 103:3233-40
Eber, Stefan; Lux, Samuel E (2004) Hereditary spherocytosis--defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin Hematol 41:118-41
Tse, W T; Tang, J; Jin, O et al. (2001) A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix. J Biol Chem 276:23974-85
Peters, L L; Jindel, H K; Gwynn, B et al. (1999) Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice. J Clin Invest 103:1527-37
Cho, M R; Eber, S W; Liu, S C et al. (1998) Regulation of band 3 rotational mobility by ankyrin in intact human red cells. Biochemistry 37:17828-35
Hoock, T C; Peters, L L; Lux, S E (1997) Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes. J Cell Biol 136:1059-70
Lu, F M; Lux, S E (1996) Constitutively active human Notch1 binds to the transcription factor CBF1 and stimulates transcription through a promoter containing a CBF1-responsive element. Proc Natl Acad Sci U S A 93:5663-7
Eber, S W; Gonzalez, J M; Lux, M L et al. (1996) Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet 13:214-8
Peters, L L; Shivdasani, R A; Liu, S C et al. (1996) Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton. Cell 86:917-27
Shalev, O; Shinar, E; Lux, S E (1996) Isolated beta-globin chains reproduce, in normal red cell membranes, the defective binding of spectrin to alpha-thalassaemic membranes. Br J Haematol 94:273-8

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