메뉴 건너뛰기




Volumn 280, Issue 5, 1998, Pages 799-810

Lambda repressor N-terminal DNA-binding domain as an assay for protein transmembrane segment interactions in vivo

Author keywords

Dimerization; Escherichia coli; Glycophorin A; Lambda repressor; Transmembrane

Indexed keywords

ALKALINE PHOSPHATASE; DNA BINDING PROTEIN; GLYCOPHORIN A; MEMBRANE PROTEIN; MUTANT PROTEIN; REPRESSOR PROTEIN; VIRUS PROTEIN;

EID: 0032584774     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1893     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 0026739805 scopus 로고
    • Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation
    • Amster-Choder, O. & Wright, A. (1992). Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation. Science 257, 1395-1397.
    • (1992) Science , vol.257 , pp. 1395-1397
    • Amster-Choder, O.1    Wright, A.2
  • 3
    • 0029022723 scopus 로고
    • In vivo characterization of the unorthodox BvgS two-component sensor protein of Bordetella pertussis
    • Beier, D., Schwarz, B., Fuchs, T. M. & Gross, R. (1995). In vivo characterization of the unorthodox BvgS two-component sensor protein of Bordetella pertussis. J. Mol. Biol. 248, 596-610.
    • (1995) J. Mol. Biol. , vol.248 , pp. 596-610
    • Beier, D.1    Schwarz, B.2    Fuchs, T.M.3    Gross, R.4
  • 4
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signaling
    • Bormann, B. J. & Engelman, D. M. (1992). Intramembrane helix-helix association in oligomerization and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struct. 21, 223-242.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 5
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann, B. J., Knowles, W. J. & Marchesi, V. T. (1989). Synthetic peptides mimic the assembly of transmembrane glycoproteins. J. Biol. Chem. 264, 4033-4037.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4033-4037
    • Bormann, B.J.1    Knowles, W.J.2    Marchesi, V.T.3
  • 6
    • 0024372724 scopus 로고
    • Positively charged amino acid residues can act as topogenic determinants in membrane proteins
    • Boyd, D. & Beckwith, J. (1989). Positively charged amino acid residues can act as topogenic determinants in membrane proteins. Proc. Natl Acad. Sci. USA, 86, 9446-9450.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9446-9450
    • Boyd, D.1    Beckwith, J.2
  • 7
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • Boyd, D. & Beckwith, J. (1990). The role of charged amino acids in the localization of secreted and membrane proteins. Cell, 62, 1031-1033.
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyd, D.1    Beckwith, J.2
  • 8
    • 0344562581 scopus 로고
    • Gene fusion approaches to membrane protein topology
    • Reuss, L., Russel, J. M., Jr & Jennings, M., eds., The Rockefeller University Press, New York
    • Boyd, D., Traxler, B., Jander, G., Prinz, W. & Beckwith, J. (1993). Gene fusion approaches to membrane protein topology. In Molecular Biology & Function of Carrier Proteins (Reuss, L., Russel, J. M., Jr & Jennings, M., eds.), pp. 24-37, The Rockefeller University Press, New York.
    • (1993) Molecular Biology & Function of Carrier Proteins , pp. 24-37
    • Boyd, D.1    Traxler, B.2    Jander, G.3    Prinz, W.4    Beckwith, J.5
  • 9
    • 0024307543 scopus 로고
    • Mutational analysis of the fine specificity of binding of monoclonal antibody 51F to λ repressor
    • Breyer, R. M. & Sauer, R. T. (1989a). Mutational analysis of the fine specificity of binding of monoclonal antibody 51F to λ repressor. J. Biol. Chem, 264, 13355-13360.
    • (1989) J. Biol. Chem , vol.264 , pp. 13355-13360
    • Breyer, R.M.1    Sauer, R.T.2
  • 10
    • 0024381520 scopus 로고
    • Production and characterization of monoclonal antibodies to the N-terminal domain of λ repressor
    • Breyer, R. M. & Sauer, R. T. (1989b). Production and characterization of monoclonal antibodies to the N-terminal domain of λ repressor. J. Biol. Chem. 264, 13348-13354.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13348-13354
    • Breyer, R.M.1    Sauer, R.T.2
  • 11
    • 0028909250 scopus 로고
    • Identification of a cDNa for SSRP1, an HMG-box protein, by interaction with the c-Myc oncoprotein in a novel bacterial expression screen
    • Bunker, C. A. & Kingston, R. E. (1995). Identification of a cDNA for SSRP1, an HMG-box protein, by interaction with the c-Myc oncoprotein in a novel bacterial expression screen. Nucl. Acids Res. 23, 269-276.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 269-276
    • Bunker, C.A.1    Kingston, R.E.2
  • 12
    • 0028284549 scopus 로고
    • Linking an easily detectable phenotype to the folding of a common structural motif
    • Castagnoli, L., Vetriani, C. & Cesareni, G. (1994). Linking an easily detectable phenotype to the folding of a common structural motif. J. Mol. Biol. 237, 378-387.
    • (1994) J. Mol. Biol. , vol.237 , pp. 378-387
    • Castagnoli, L.1    Vetriani, C.2    Cesareni, G.3
  • 13
    • 0017807890 scopus 로고
    • Construction and characterization of amplfiable multicopy DNA cloning vehicles derived from the p15A cryptic miniplasmid
    • Chang, A. C. Y. & Cohen, S. N. (1978). Construction and characterization of amplfiable multicopy DNA cloning vehicles derived from the p15A cryptic miniplasmid. J. Bacteriol. 134, 1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 14
    • 0029130732 scopus 로고
    • Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface
    • Chervitz, S. A., Lin, C. M. & Falke, J. J. (1995). Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface. Biochemistry, 34, 9722-9733.
    • (1995) Biochemistry , vol.34 , pp. 9722-9733
    • Chervitz, S.A.1    Lin, C.M.2    Falke, J.J.3
  • 15
    • 0017394458 scopus 로고
    • Immunochemical evidence for the transmembrane orientation of glycophorin A. Localization of ferritin-antibody conjugates in intact cells
    • Cotmore, S. F., Furthmayr, H. & Marchesi, V. T. (1977). Immunochemical evidence for the transmembrane orientation of glycophorin A. Localization of ferritin-antibody conjugates in intact cells. J. Mol. Biol. 113, 539-553.
    • (1977) J. Mol. Biol. , vol.113 , pp. 539-553
    • Cotmore, S.F.1    Furthmayr, H.2    Marchesi, V.T.3
  • 16
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson, A. L. & Nikaido, H. (1991). Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266, 8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 17
    • 0028001591 scopus 로고
    • Analysis of membrane protein interaction: ToxR can dimerize the amino terminus of phage lambda repressor
    • Dziejman, M. & Mekalanos, J. J. (1994). Analysis of membrane protein interaction: ToxR can dimerize the amino terminus of phage lambda repressor. Mol. Microbiol. 13, 485-494.
    • (1994) Mol. Microbiol. , vol.13 , pp. 485-494
    • Dziejman, M.1    Mekalanos, J.J.2
  • 18
    • 0025947624 scopus 로고
    • Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal
    • Ehrmann, M. & Beckwith, J. (1991). Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J. Biol. Chem. 266, 16530-16533.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16530-16533
    • Ehrmann, M.1    Beckwith, J.2
  • 19
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane α-helix dimerization
    • Fleming, K. G., Ackerman, A. L. & Engelman, D. M. (1997). The effect of point mutations on the free energy of transmembrane α-helix dimerization. J. Mol. Biol. 272, 266-275.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 20
    • 0021161867 scopus 로고
    • The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli
    • Froshauer, S. & Beckwith, J. (1984). The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. J. Biol. Chem. 259, 10896-10903.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10896-10903
    • Froshauer, S.1    Beckwith, J.2
  • 21
    • 0017251379 scopus 로고
    • Subunit structure of human erythrocyte glycophorin A
    • Furthmayr, H. & Marchesi, V. T. (1976). Subunit structure of human erythrocyte glycophorin A. Biochemistry, 15, 1137-1144.
    • (1976) Biochemistry , vol.15 , pp. 1137-1144
    • Furthmayr, H.1    Marchesi, V.T.2
  • 22
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L. M., Barondess, J. J. & Beckwith, J. (1992). FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J. Bacteriol. 174, 7716-7728.
    • (1992) J. Bacteriol. , vol.174 , pp. 7716-7728
    • Guzman, L.M.1    Barondess, J.J.2    Beckwith, J.3
  • 23
    • 0030756250 scopus 로고    scopus 로고
    • Domain-swapping analysis of FtsI, FtsL, & FtsQ, bitopic membrane proteins essential for cell division in Escherchia coli
    • Guzman, L. M., Weiss, D. S. & Beckwith, J. (1997). Domain-swapping analysis of FtsI, FtsL, & FtsQ, bitopic membrane proteins essential for cell division in Escherchia coli. J. Bacteriol. 179, 5094-5103.
    • (1997) J. Bacteriol. , vol.179 , pp. 5094-5103
    • Guzman, L.M.1    Weiss, D.S.2    Beckwith, J.3
  • 24
    • 0020626212 scopus 로고
    • Mutations in λ repressor's amino-terminal domain: Implications for protein stability and DNA binding
    • Hecht, M. H., Nelson, H. C. M. & Sauer, R. T. (1983). Mutations in λ repressor's amino-terminal domain: implications for protein stability and DNA binding. Proc. Natl Acad. Sci. USA, 80, 2676-2680.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2676-2680
    • Hecht, M.H.1    Nelson, H.C.M.2    Sauer, R.T.3
  • 25
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: Analysis with λ repressor-GCN4 leucine zipper fusions
    • Hu, J. C., O'Shea, E. K., Kim, P. S. & Sauer, R. T. (1990). Sequence requirements for coiled-coils: analysis with λ repressor-GCN4 leucine zipper fusions. Science, 250, 1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 26
    • 0027180729 scopus 로고
    • Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis
    • Hu, J. C., Newell, N E., Tidor, B. & Sauer, R. T. (1993). Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis. Protein Sci. 2, 1072-1084.
    • (1993) Protein Sci. , vol.2 , pp. 1072-1084
    • Hu, J.C.1    Newell, N.E.2    Tidor, B.3    Sauer, R.T.4
  • 27
    • 0030754288 scopus 로고    scopus 로고
    • Opening the door to more membrane protein structures
    • Kerr, R. A. (1997). Opening the door to more membrane protein structures. Science, 277, 1607-1608.
    • (1997) Science , vol.277 , pp. 1607-1608
    • Kerr, R.A.1
  • 28
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar, H., Hennecke, F., Gotze, K., Janzer, B., Vogt, B., Mayer, F. & Fritz, H. (1995). Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J. 14, 3895-3904.
    • (1995) EMBO J. , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Hennecke, F.2    Gotze, K.3    Janzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.7
  • 29
    • 0030575833 scopus 로고    scopus 로고
    • Dimerization of the glycophorin-A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D., Brosig, B., Kolmar, H. & Fritz, H. (1996). Dimerization of the glycophorin-A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263, 525-530.
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.4
  • 30
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking. the bacterial chemoreceptor Trg
    • Lee, G. F., Burrows, G. G., Lebert, M. R., Dutton, D. P. & Hazelbauer, G. L. (1994). Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg. J. Biol. Chem. 269, 29920-29927.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 31
    • 0000963997 scopus 로고
    • Helix-helix interactions inside lipid bilayers
    • Lemmon, M. A. & Engelman, D. M. (1992). Helix-helix interactions inside lipid bilayers. Curr. Opin. Struct. Biol. 2, 511-518.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 511-518
    • Lemmon, M.A.1    Engelman, D.M.2
  • 32
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M. A. & Engelman, D. M. (1994). Specificity and promiscuity in membrane helix interactions. Quart. Rev. Biophys. 27, 157-218.
    • (1994) Quart. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 34
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane α-helices
    • Lemmon, M. A., Flanagan, J. M., Treutlein, H. R., Zhang, J. & Engelman, D. M. (1992b). Sequence specificity in the dimerization of transmembrane α-helices. Biochemistry, 31, 12719-12725.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 35
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherchia coli
    • Lynch, B. A. & Koshland, J. D. E. (1991). Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherchia coli. Proc. Natl Acad. Sci. USA, 88, 10402-10406.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland, J.D.E.2
  • 36
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H. & Engelman, D. M. (1997). A transmembrane helix dimer: structure and implications. Science, 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 37
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C. & Beckwith, J. (1986). A genetic approach to analyzing membrane protein topology. Science, 233, 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 38
    • 0018942650 scopus 로고
    • Functional and structural properties of immobilized subunits of Escherichia coli alkaline phophatase
    • McCracken, S. & Meighen, E. (1979). Functional and structural properties of immobilized subunits of Escherichia coli alkaline phophatase. J. Biol. Chem. 255, 2396-2404.
    • (1979) J. Biol. Chem. , vol.255 , pp. 2396-2404
    • McCracken, S.1    Meighen, E.2
  • 39
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase of Escherichia coli
    • Michaelis, S., Inouye, H., Oliver, D. & Beckwith, J. (1983). Mutations that alter the signal sequence of alkaline phosphatase of Escherichia coli. J. Bacteriol. 154, 366-374.
    • (1983) J. Bacteriol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 40
    • 0027293043 scopus 로고
    • The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain
    • Millar, D. G. & Shore, G. C. (1993). The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain. J. Biol. Chem. 268, 18403-18406.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18403-18406
    • Millar, D.G.1    Shore, G.C.2
  • 41
    • 0031551579 scopus 로고    scopus 로고
    • Helix-helix packing in a membrane-like environment
    • Mingarro, I., Elofsson, A. & von Heijne, G. (1997). Helix-helix packing in a membrane-like environment. J. Mol. Biol. 272, 633-641.
    • (1997) J. Mol. Biol. , vol.272 , pp. 633-641
    • Mingarro, I.1    Elofsson, A.2    Von Heijne, G.3
  • 42
    • 0028334912 scopus 로고
    • Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region
    • Murphy, C. K. & Beckwith, J. (1994). Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region. Proc. Natl Acad. Sci. USA, 91, 2557-2561.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2557-2561
    • Murphy, C.K.1    Beckwith, J.2
  • 43
    • 0028951388 scopus 로고
    • Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins
    • Ottemann, K. M. & Mekalanos, J. J. (1995). Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins. Mol. Microbiol. 15, 719-731.
    • (1995) Mol. Microbiol. , vol.15 , pp. 719-731
    • Ottemann, K.M.1    Mekalanos, J.J.2
  • 45
    • 0026605299 scopus 로고
    • Determination of transmembrane protein structure by disulfide cross-liniking: The Escherchia coli Tar receptor
    • Pakula, A. A. & Simon, M. I. (1992). Determination of transmembrane protein structure by disulfide cross-liniking: the Escherchia coli Tar receptor. Proc. Natl Acad. Sci. USA, 89, 4144-4148.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4144-4148
    • Pakula, A.A.1    Simon, M.I.2
  • 46
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • Parsell, D. A. & Sauer, R. T. (1989). The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J. Biol. Chem. 264, 7590-7595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 47
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P. & Landau, E. M. (1997). X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science, 277, 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 48
    • 0004194541 scopus 로고
    • Blackwell Scientific Publications & Cell Press, Cambridge, MA
    • Ptashne, M. (1986). A Genetic Switch, Blackwell Scientific Publications & Cell Press, Cambridge, MA.
    • (1986) A Genetic Switch
    • Ptashne, M.1
  • 49
    • 0008567435 scopus 로고
    • Proteolytic cleavage of bacteriophage lambda repressor in induction
    • Roberts, J. W. & Roberts, C. W. (1975). Proteolytic cleavage of bacteriophage lambda repressor in induction. Proc. Natl Acad. Sci. USA, 72, 147-151.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 147-151
    • Roberts, J.W.1    Roberts, C.W.2
  • 50
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg, M. F., Callaghan, R., Ford, R. C. & Higgins, C. F. (1997). Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J. Biol. Chem. 272, 10685-10694.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 52
    • 0023006133 scopus 로고
    • An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of λ repressor
    • Sauer, R. T., Hehir, K., Stearman, R. S., Weiss, M. A., Jeitler-Nilsson, A., Suchanek, E. G. & Pabo, C. O. (1986). An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of λ repressor. Biochemistry, 25, 5992-5998.
    • (1986) Biochemistry , vol.25 , pp. 5992-5998
    • Sauer, R.T.1    Hehir, K.2    Stearman, R.S.3    Weiss, M.A.4    Jeitler-Nilsson, A.5    Suchanek, E.G.6    Pabo, C.O.7
  • 53
    • 0015914973 scopus 로고
    • Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE)
    • Sternberg, N. (1973). Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE). J. Mol. Biol. 76, 1-23.
    • (1973) J. Mol. Biol. , vol.76 , pp. 1-23
    • Sternberg, N.1
  • 54
    • 0030669210 scopus 로고    scopus 로고
    • The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus
    • Turner, L. R., Olsen, J. W. & Lory, S. (1997). The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus. Mol. Microbiol, 26, 877-887.
    • (1997) Mol. Microbiol , vol.26 , pp. 877-887
    • Turner, L.R.1    Olsen, J.W.2    Lory, S.3
  • 55
    • 0023128688 scopus 로고
    • Dimerization of the operator binding domain of phage λ repressor
    • Weiss, M. A., Pabo, C. O., Karplus, M. & Sauer, R. T. (1987). Dimerization of the operator binding domain of phage λ repressor. Biochemistry, 26, 897-904.
    • (1987) Biochemistry , vol.26 , pp. 897-904
    • Weiss, M.A.1    Pabo, C.O.2    Karplus, M.3    Sauer, R.T.4
  • 56
    • 0030025319 scopus 로고    scopus 로고
    • Exploring the allowed sequence space of a membrane protein
    • Wen, J. A., Chen, X. & Bowie, J. U. (1996). Exploring the allowed sequence space of a membrane protein. Nature Struct. Biol. 3, 141-148.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 141-148
    • Wen, J.A.1    Chen, X.2    Bowie, J.U.3
  • 57
    • 0027317361 scopus 로고
    • Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping
    • Whitley, P., Nilsson, L. & von Heijne, G. (1993). Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping. Biochemistry, 32, 8534-8539.
    • (1993) Biochemistry , vol.32 , pp. 8534-8539
    • Whitley, P.1    Nilsson, L.2    Von Heijne, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.