Ste24: An Integral Membrane Protein Zinc Metalloprotease with Provocative Structure and Emergent Biology

Author:

Goblirsch Brandon R.,Wiener Michael C.

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference83 articles.

1. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis;Boyartchuk;Science,1997

2. A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor;Fujimura-Kamada;J. Cell Biol.,1997

3. Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing;Tam;J. Cell Biol.,1998

4. A unique signature identifies a family of zinc-dependent metallopeptidases;Jongeneel;FEBS Lett.,1989

5. The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties;Hennekes;J. Cell Sci.,1994

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