Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Research Project (R01)
Project #
2R01AR039848-06A1
Application #
2079731
Study Section
General Medicine A Subcommittee 2 (GMA)
Project Start
1990-04-01
Project End
1999-11-30
Budget Start
1996-02-20
Budget End
1996-11-30
Support Year
6
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Yale University
Department
Dermatology
Type
Schools of Medicine
DUNS #
082359691
City
New Haven
State
CT
Country
United States
Zip Code
06520
Halaban, Ruth; Patton, Robin S; Cheng, Elaine et al. (2002) Abnormal acidification of melanoma cells induces tyrosinase retention in the early secretory pathway. J Biol Chem 277:14821-8
Halaban, R; Cheng, E; Svedine, S et al. (2001) Proper folding and endoplasmic reticulum to golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J Biol Chem 276:11933-8
Ujvari, A; Aron, R; Eisenhaure, T et al. (2001) Translation rate of human tyrosinase determines its N-linked glycosylation level. J Biol Chem 276:5924-31
Halaban, R (2000) The regulation of normal melanocyte proliferation. Pigment Cell Res 13:14-Apr
Halaban, R; Svedine, S; Cheng, E et al. (2000) Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. Proc Natl Acad Sci U S A 97:5889-94
Watson, M L; Zinn, A R; Inoue, N et al. (1998) Identification of morc (microrchidia), a mutation that results in arrest of spermatogenesis at an early meiotic stage in the mouse. Proc Natl Acad Sci U S A 95:14361-6
Yayon, A; Ma, Y S; Safran, M et al. (1997) Suppression of autocrine cell proliferation and tumorigenesis of human melanoma cells and fibroblast growth factor transformed fibroblasts by a kinase-deficient FGF receptor 1: evidence for the involvement of Src-family kinases. Oncogene 14:2999-3009
Halaban, R; Cheng, E; Zhang, Y et al. (1997) Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci U S A 94:6210-5
Lee, Z H; Hou, L; Moellmann, G et al. (1996) Characterization and subcellular localization of human Pmel 17/silver, a 110-kDa (pre)melanosomal membrane protein associated with 5,6,-dihydroxyindole-2-carboxylic acid (DHICA) converting activity. J Invest Dermatol 106:605-10
Halaban, R; Bohm, M; Dotto, P et al. (1996) Growth regulatory proteins that repress differentiation markers in melanocytes also downregulate the transcription factor microphthalmia. J Invest Dermatol 106:1266-72

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