Processing and Routing of Secretory Granule Enzymes

Milgram, Sharon L.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Postdoctoral Individual National Research Service Award (F32)
• Project #: 1F32GM015293-01
• Application #: 3046748
• Study Section: Biological Sciences 2 (BIOL)
• Project Start: 1993-01-19
• Budget Start: 1992-09-01
• Budget End: 1993-08-31
• Support Year: 1
• Fiscal Year: 1992

Institution

• Name: Johns Hopkins University
• Type: Schools of Medicine
• DUNS #: 045911138
• City: Baltimore
• State: MD
• Country: United States
• Zip Code: 21218

Publications

Milgram, S L; Kho, S T; Martin, G V et al. (1997) Localization of integral membrane peptidylglycine alpha-amidating monooxygenase in neuroendocrine cells. J Cell Sci 110 ( Pt 6):695-706

Milgram, S L; Chang, E Y; Mains, R E (1996) Processing and routing of a membrane-anchored form of proneuropeptide Y. Mol Endocrinol 10:837-46

Milgram, S L; Mains, R E; Eipper, B A (1996) Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein. J Biol Chem 271:17526-35

Mains, R E; Milgram, S L; Keutmann, H T et al. (1995) The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins. Mol Endocrinol 9:3-13

Milgram, S L; Mains, R E (1994) Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins. J Cell Sci 107 ( Pt 3):737-45