Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA036434-13
Application #
2089109
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1984-01-01
Project End
1996-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
13
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Anatomy/Cell Biology
Type
Schools of Medicine
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461
Dong, Zhizhong; Zuber, Christian; Pierce, Michael et al. (2014) Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V. Histochem Cell Biol 141:153-64
Miwa, Hazuki E; Koba, Wade R; Fine, Eugene J et al. (2013) Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human breast cancer. Glycobiology 23:1477-90
Müller, Reto; Jenny, Andreas; Stanley, Pamela (2013) The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila. PLoS One 8:e62835
Miwa, Hazuki E; Song, Yinghui; Alvarez, Richard et al. (2012) The bisecting GlcNAc in cell growth control and tumor progression. Glycoconj J 29:609-18
Zheng, Tianqing; Jiang, Hao; Gros, Marilyn et al. (2011) Tracking N-acetyllactosamine on cell-surface glycans in vivo. Angew Chem Int Ed Engl 50:4113-8
Varki, Ajit; Cummings, Richard D; Esko, Jeffrey D et al. (2009) Symbol nomenclature for glycan representation. Proteomics 9:5398-9
Chen, Wei; Stanley, Pamela (2003) Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I. Glycobiology 13:43-50
Haltiwanger, Robert S; Stanley, Pamela (2002) Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase. Biochim Biophys Acta 1573:328-35
Lee, J; Sundaram, S; Shaper, N L et al. (2001) Chinese hamster ovary (CHO) cells may express six beta 4-galactosyltransferases (beta 4GalTs). Consequences of the loss of functional beta 4GalT-1, beta 4GalT-6, or both in CHO glycosylation mutants. J Biol Chem 276:13924-34
Chen, W; Unligil, U M; Rini, J M et al. (2001) Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI. Biochemistry 40:8765-72

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