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Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

140 related items for PubMed ID: 3317833

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  • 3. Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence.
    Soekarjo M, Eisenhawer M, Kuhn A, Vogel H.
    Biochemistry; 1996 Jan 30; 35(4):1232-41. PubMed ID: 8573578
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  • 4. Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion.
    Kuhn A, Zhu HY, Dalbey RE.
    EMBO J; 1990 Aug 30; 9(8):2385-9. PubMed ID: 2196172
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  • 5. Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacteriophage M13 procoat.
    Wickner W, Moore K, Dibb N, Geissert D, Rice M.
    J Bacteriol; 1987 Aug 30; 169(8):3821-2. PubMed ID: 3301818
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  • 6. The function of a leader peptide in translocating charged amino acyl residues across a membrane.
    Rohrer J, Kuhn A.
    Science; 1990 Dec 07; 250(4986):1418-21. PubMed ID: 2124001
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  • 7. Translational and post-translational cleavage of M13 procoat protein: extracts of both the cytoplasmic and outer membranes of Escherichia coli contain leader peptidase activity.
    Mandel G, Wickner W.
    Proc Natl Acad Sci U S A; 1979 Jan 07; 76(1):236-40. PubMed ID: 370824
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  • 10. M13 procoat inserts into liposomes in the absence of other membrane proteins.
    Geller BL, Wickner W.
    J Biol Chem; 1985 Oct 25; 260(24):13281-5. PubMed ID: 3902814
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  • 13. Soluble precursor of an integral membrane protein: synthesis of procoat protein in Escherichia coli infected with bacteriophage M13.
    Ito K, Mandel G, Wickner W.
    Proc Natl Acad Sci U S A; 1979 Mar 25; 76(3):1199-203. PubMed ID: 375229
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  • 15. Membrane assembly from purified components. I. Isolated M13 procoat does not require ribosomes or soluble proteins for processing by membranes.
    Silver P, Watts C, Wickner W.
    Cell; 1981 Aug 25; 25(2):341-5. PubMed ID: 7026042
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  • 16. 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.
    Shen LM, Lee JI, Cheng SY, Jutte H, Kuhn A, Dalbey RE.
    Biochemistry; 1991 Dec 24; 30(51):11775-81. PubMed ID: 1751494
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  • 17. Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YIDC structural requirements for membrane protein insertion.
    Chen M, Xie K, Nouwen N, Driessen AJ, Dalbey RE.
    J Biol Chem; 2003 Jun 27; 278(26):23295-300. PubMed ID: 12707259
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  • 18. Conserved residues of the leader peptide are essential for cleavage by leader peptidase.
    Kuhn A, Wickner W.
    J Biol Chem; 1985 Dec 15; 260(29):15914-8. PubMed ID: 3905798
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  • 19. Identification of potential active-site residues in the Escherichia coli leader peptidase.
    Sung M, Dalbey RE.
    J Biol Chem; 1992 Jul 05; 267(19):13154-9. PubMed ID: 1618816
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  • 20. Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy-terminal extension retain their independence of secY function.
    Kuhn A, Kreil G, Wickner W.
    EMBO J; 1987 Feb 05; 6(2):501-5. PubMed ID: 3034592
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