Quantitative assessment of peptide sequence diversity in M13 combinatorial peptide phage display libraries.
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[1] T. Clackson,et al. A hot spot of binding energy in a hormone-receptor interface , 1995, Science.
[2] L. Castagnoli,et al. Construction, Exploitation and Evolution of a New Peptide Library Displayed at High Density by Fusion to the Major Coat Protein of Filamentous Phage , 1997, Biological chemistry.
[3] G. Heijne. A new method for predicting signal sequence cleavage sites. , 1986 .
[4] W. Wickner,et al. The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits , 1999, The EMBO journal.
[5] H R Hoogenboom,et al. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. , 1991, Journal of molecular biology.
[6] David Baker,et al. Detection of Protein Coding Sequences Using a Mixture Model for Local Protein Amino Acid Sequence , 2000, J. Comput. Biol..
[7] F. Fack,et al. Epitope mapping by phage display: random versus gene-fragment libraries. , 1997, Journal of immunological methods.
[8] D Perlman,et al. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. , 1983, Journal of molecular biology.
[9] A. Driessen,et al. Escherichia coli translocase: the unravelling of a molecular machine , 2000, Molecular microbiology.
[10] K. A. Noren,et al. Construction of high-complexity combinatorial phage display peptide libraries. , 2001, Methods.
[11] G von Heijne,et al. A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[12] P. Ray,et al. Signal peptidases and signal peptide hydrolases , 1990, Journal of bioenergetics and biomembranes.
[13] M. Inouye,et al. Signal peptide mutants ofEscherichia coli , 1990, Journal of bioenergetics and biomembranes.
[14] J. Scott,et al. Searching for peptide ligands with an epitope library. , 1990, Science.
[15] 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.
[16] J. Wells,et al. Comparison of a structural and a functional epitope. , 1993, Journal of molecular biology.
[17] S J Rodda,et al. A priori delineation of a peptide which mimics a discontinuous antigenic determinant. , 1986, Molecular immunology.
[18] H. Lowman,et al. Affinity maturation of human growth hormone by monovalent phage display. , 1993, Journal of molecular biology.
[19] S. Mizushima,et al. Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. Relation to the orientation of membrane proteins. , 1988, The Journal of biological chemistry.
[20] M. G. Bulmer,et al. Principles of Statistics. , 1969 .
[21] S. Brunak,et al. SHORT COMMUNICATION Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites , 1997 .
[22] E. Lane,et al. Epitope mapping of monoclonal antibodies to keratin 19 using keratin fragments, synthetic peptides and phage peptide libraries. , 1995, European journal of biochemistry.
[23] Lee Makowski,et al. One from column A and two from column B: the benefits of phage display in molecular-recognition studies. , 2002, Current opinion in chemical biology.
[24] R. Dalbey,et al. Direct Evidence That the Proton Motive Force Inhibits Membrane Translocation of Positively Charged Residues within Membrane Proteins* , 1999, The Journal of Biological Chemistry.
[25] F. Neidhardt,et al. Escherichia Coli and Salmonella: Typhimurium Cellular and Molecular Biology , 1987 .
[26] J. Larrick,et al. Identification of functional and structural amino-acid residues by parsimonious mutagenesis. , 1996, Gene.
[27] P. Y. Chou,et al. Prediction of the secondary structure of proteins from their amino acid sequence. , 2006 .
[28] G. von Heijne,et al. A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec‐independent protein , 1992, FEBS letters.
[29] Takashi Gojobori,et al. Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[30] R. Miceli,et al. Two-stage selection of sequences from a random phage display library delineates both core residues and permitted structural range within an epitope. , 1994, Journal of immunological methods.
[31] Jeffrey D. Jones,et al. Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[32] G Cesareni,et al. Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. , 2001, Journal of molecular biology.
[33] P Argos,et al. Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences , 1988, Proteins.
[34] J. Cannon,et al. Beta-turn formation in the processing region is important for efficient maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. , 1994, The Journal of biological chemistry.
[35] D. Marvin,et al. Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. , 1996, Journal of molecular biology.
[36] J. Knowles,et al. The consequences of stepwise deletions from the signal-processing site of beta-lactamase. , 1987, The Journal of biological chemistry.
[37] A Wlodawer,et al. Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. , 1999, Structure.
[38] A. Plückthun,et al. Beyond binding: using phage display to select for structure, folding and enzymatic activity in proteins. , 1999, Current opinion in structural biology.
[39] R. Doolittle,et al. A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.
[40] N. Adey,et al. An M13 phage library displaying random 38-amino-acid peptides as a source of novel sequences with affinity to selected targets. , 1993, Gene.
[41] R. Barrett,et al. Peptides on phage: a vast library of peptides for identifying ligands. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[42] R. Houghten,et al. Functional importance of amino acid residues making up peptide antigenic determinants. , 1993, Molecular immunology.
[43] R. E. Webster,et al. The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane. , 1998, Journal of molecular biology.
[44] D. Lane,et al. Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions. , 1995, Journal of molecular biology.
[45] J. Mott,et al. Biochemical diversity in a phage display library of random decapeptides. , 1993, Gene.
[46] W. Dower,et al. Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors , 1994, Journal of bacteriology.
[47] R. Zuckermann,et al. Simplified methods for construction, assessment and rapid screening of peptide libraries in bacteriophage. , 1992, Journal of molecular biology.