Signal peptidases in prokaryotes and eukaryotes--a new protease family.
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[1] G. Blobel,et al. POST‐TRANSLATIONAL PROCESSING OF FULL‐LENGTH PRESECRETORY PROTEINS WITH CANINE PANCREATIC SIGNAL PEPTIDASE , 1980, Annals of the New York Academy of Sciences.
[2] T. Date,et al. Leader peptidase is found in both the inner and outer membranes of Escherichia coli. , 1981, The Journal of biological chemistry.
[3] W. Wickner,et al. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. , 1983, The Journal of biological chemistry.
[4] W. DeGrado,et al. Purification and properties of thiol beta-lactamase. A mutant of pBR322 beta-lactamase in which the active site serine has been replaced with cysteine. , 1984, The Journal of biological chemistry.
[5] B. Guiard,et al. One nuclear gene controls the removal of transient pre‐sequences from two yeast proteins: one encoded by the nuclear the other by the mitochondrial genome. , 1986, The EMBO journal.
[6] S. Miura,et al. A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli. , 1987, The Journal of biological chemistry.
[7] M. Lively,et al. Purification and characterization of hen oviduct microsomal signal peptidase. , 1987, Biochemistry.
[8] R. Schekman,et al. SEC11 is required for signal peptide processing and yeast cell growth , 1988, The Journal of cell biology.
[9] J. Gordon,et al. Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position -1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II. , 1988, The Journal of biological chemistry.
[10] J. Gordon,et al. Eukaryotic signal peptide structure/function relationships. Identification of conformational features which influence the site and efficiency of co-translational proteolytic processing by site-directed mutagenesis of human pre(delta pro)apolipoprotein A-II. , 1989, The Journal of biological chemistry.
[11] R. Zimmermann,et al. The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. , 1989, The EMBO journal.
[12] G. von Heijne,et al. Domain structure of mitochondrial and chloroplast targeting peptides. , 1989, European journal of biochemistry.
[13] P. Novák,et al. Minimum substrate sequence for signal peptidase I of Escherichia coli. , 1990, The Journal of biological chemistry.
[14] G. Heijne,et al. Protein targeting signals. , 1990 .
[15] M. Chou,et al. Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides. , 1990, The Journal of biological chemistry.
[16] J. Gordon,et al. Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase. , 1990, The Journal of biological chemistry.
[17] G. Blobel,et al. Two subunits of the canine signal peptidase complex are homologous to yeast SEC11 protein. , 1990, The Journal of biological chemistry.
[18] G. Vonheijne. The signal peptide. , 1990 .
[19] G. Heijne,et al. Mapping of catalytically important domains in Escherichia coli leader peptidase. , 1990, The EMBO journal.
[20] C. Robinson,et al. Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. , 1991, The Journal of biological chemistry.
[21] A. Kuhn,et al. Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase. , 1991, Biochemistry.
[22] A. Schneider,et al. Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast. , 1991, The EMBO journal.
[23] Identification of potential active-site residues in the Escherichia coli leader peptidase. , 1992, The Journal of biological chemistry.
[24] S. Bron,et al. Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. , 1992, The EMBO journal.
[25] A. Allsop,et al. On the catalytic mechanism of prokaryotic leader peptidase 1. , 1992, The Biochemical journal.
[26] G. A. Barkocy-Gallagher,et al. Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo. , 1992, The Journal of biological chemistry.