Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM033132-02S1
Application #
3282453
Study Section
Molecular Cytology Study Section (CTY)
Project Start
1983-06-01
Project End
1985-08-31
Budget Start
1985-06-01
Budget End
1985-08-31
Support Year
2
Fiscal Year
1985
Total Cost
Indirect Cost
Name
State University New York Stony Brook
Department
Type
Schools of Medicine
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794
Schneider, U; Mini, T; Jeno, P et al. (1999) Phosphorylation of the major Drosophila lamin in vivo: site identification during both M-phase (meiosis) and interphase by electrospray ionization tandem mass spectrometry. Biochemistry 38:4620-32
Goldberg, M; Lu, H; Stuurman, N et al. (1998) Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA. Mol Cell Biol 18:4315-23
Berrios, M; Fisher, P A; Matz, E C (1991) Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complexes. Proc Natl Acad Sci U S A 88:219-23
Lin, L; Fisher, P A (1990) Immunoaffinity purification and functional characterization of interphase and meiotic Drosophila nuclear lamin isoforms. J Biol Chem 265:12596-601
Smith, D E; Fisher, P A (1989) Interconversion of Drosophila nuclear lamin isoforms during oogenesis, early embryogenesis, and upon entry of cultured cells into mitosis. J Cell Biol 108:255-65
Fisher, P A; Smith, D E (1988) Affinity purification of antibodies using antigens immobilized on solid supports. Biochem Soc Trans 16:134-8
Gruenbaum, Y; Landesman, Y; Drees, B et al. (1988) Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene. J Cell Biol 106:585-96
Smith, D E; Gruenbaum, Y; Berrios, M et al. (1987) Biosynthesis and interconversion of Drosophila nuclear lamin isoforms during normal growth and in response to heat shock. J Cell Biol 105:771-90
Wu, L C; Fisher, P A; Broach, J R (1987) A yeast plasmid partitioning protein is a karyoskeletal component. J Biol Chem 262:883-91
McConnell, M; Whalen, A M; Smith, D E et al. (1987) Heat shock-induced changes in the structural stability of proteinaceous karyoskeletal elements in vitro and morphological effects in situ. J Cell Biol 105:1087-98

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