200-284-8

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Intracellular localization of processing events in human surfactant protein B biosynthesis.

A Korimilli et al.

The Journal of biological chemistry, 275(12), 8672-8679 (2000-03-18)

Surfactant protein B (SP-B) is essential to the function of pulmonary surfactant and to alveolar type 2 cell phenotype. Human SP-B is the 79-amino acid product of extensive post-translational processing of a 381-amino acid preproprotein. Processing involves modification of the

Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2).

Hewang Li et al.

Proceedings of the National Academy of Sciences of the United States of America, 100(4), 1627-1632 (2003-02-07)

Like other guanine nucleotide-exchange proteins (GEPs) that activate ADP-ribosylation factor (ARF) GTPases, brefeldin A-inhibited GEP2, BIG2, contains an approximately 200-aa Sec7 domain that is responsible for this catalytic activity and its inhibition by brefeldin A. The Sec7 domain is located

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