Protein targeting signals.

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[2]  A. Baker,et al.  The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. , 1989, The Journal of biological chemistry.

[3]  I. Shimada,et al.  N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: a proton nuclear magnetic resonance study. , 1989, Journal of biochemistry.

[4]  K. Ohno,et al.  Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus , 1989, Molecular and cellular biology.

[5]  W. Neupert,et al.  Early steps in mitochondrial protein import: Receptor functions can be substituted by the membrane insertion activity of apocytochrome c , 1990, Cell.

[6]  S. Subramani,et al.  Antibodies directed against the peroxisomal targeting signal of firefly luciferase recognize multiple mammalian peroxisomal proteins , 1990, The Journal of cell biology.

[7]  L. Gierasch,et al.  Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties. , 1989, The Journal of biological chemistry.

[8]  K. Keegstra.  Transport and routing of proteins into chloroplasts , 1989, Cell.

[9]  Y. Yamamoto,et al.  Important role of the proline residue in the signal sequence that directs the secretion of human lysozyme in Saccharomyces cerevisiae. , 1989, Biochemistry.

[10]  P. Silver,et al.  Yeast proteins that recognize nuclear localization sequences , 1989, The Journal of cell biology.

[11]  J. Hendrick,et al.  Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[12]  R. Zimmermann,et al.  The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. , 1989, The EMBO journal.

[13]  S. Adam,et al.  Identification of specific binding proteins for a nuclear location sequence , 1989, Nature.

[14]  G. von Heijne,et al.  Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii share features with both mitochondrial and higher plant chloroplast presequences , 1990, FEBS letters.

[15]  L. Gierasch,et al.  Helix formation and stability in a signal sequence. , 1989, Biochemistry.

[16]  D. Chelsky,et al.  Sequence requirements for synthetic peptide-mediated translocation to the nucleus , 1989, Molecular and cellular biology.

[17]  L. Gierasch,et al.  Conformations and orientations of a signal peptide interacting with phospholipid monolayers. , 1989, Biochemistry.

[18]  S Subramani,et al.  A conserved tripeptide sorts proteins to peroxisomes , 1989, The Journal of cell biology.

[19]  N. Pfanner,et al.  Mitochondrial protein import. , 1989, Biochimica et biophysica acta.

[20]  P. Weisbeek,et al.  Protein transport into and within chloroplasts. , 1990, Trends in biochemical sciences.

[21]  G. von Heijne,et al.  A conserved cleavage‐site motif in chloroplast transit peptides , 1990, FEBS letters.

[22]  J. Fikes,et al.  Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. , 1990, The Journal of biological chemistry.