메뉴 건너뛰기




Volumn 426, Issue 2, 2010, Pages 205-217

Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from saccharomyces cerevisiae, an α1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide

Author keywords

ALG11; Dolichol; Lipid linked oligosaccharide; Mannosyltransferase; Protein N glycosylation; Saccharomyces cerevisiae

Indexed keywords

ALG11; BIOCHEMICAL CHARACTERIZATION; CORE OLIGOSACCHARIDE; CYTOSOLIC; DOLICHOL; ENDOPLASMIC RETICULUM; GLYCANS; GLYCOSYL DONORS; GLYCOSYL TRANSFERASE; GLYCOSYLTRANSFERASES; HYDROPHOBIC DOMAINS; LYSINE RESIDUES; MEMBRANE ASSOCIATION; N-GLYCOSYLATION; N-TERMINAL DOMAINS; SACCHAROMYCES CEREVISIAE; SEQUENTIAL TRANSFER; SITE DIRECTED MUTAGENESIS; TRANSMEMBRANES;

EID: 76549121050     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091121     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A. and Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019-1049
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 2
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases
    • Lehle, L., Strahl, S. and Tanner, W. (2006) Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew. Chem. Int. Ed. Engl. 45, 6802-6818
    • (2006) Angew. Chem. Int. Ed. Engl , vol.45 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 3
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda, P. and Aebi, M. (1999) The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426, 239-257
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 4
    • 67749089456 scopus 로고    scopus 로고
    • Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-P-dolichol in sealed microsomes from yeast
    • Rush, J. S., Gao, N., Lehrman, M. A., Matveev, S. and Waechter, C. J. (2009) Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-P-dolichol in sealed microsomes from yeast. J. Biol. Chem. 284, 19835-19842
    • (2009) J. Biol. Chem , vol.284 , pp. 19835-19842
    • Rush, J.S.1    Gao, N.2    Lehrman, M.A.3    Matveev, S.4    Waechter, C.J.5
  • 5
    • 58849150433 scopus 로고    scopus 로고
    • Specific transbilayer translocation of dolichol-linked oligosaccharides by an endoplasmic reticulum flippase
    • Sanyal, S. and Menon, A. K. (2009) Specific transbilayer translocation of dolichol-linked oligosaccharides by an endoplasmic reticulum flippase. Proc. Natl. Acad. Sci. U.S.A. 106, 767-772
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 767-772
    • Sanyal, S.1    Menon, A.K.2
  • 6
    • 0033046227 scopus 로고    scopus 로고
    • Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases
    • Burda, P., Jakob, C. A., Beinhauer, J., Hegemann, J. H. and Aebi, M. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9, 617-625
    • (1999) Glycobiology , vol.9 , pp. 617-625
    • Burda, P.1    Jakob, C.A.2    Beinhauer, J.3    Hegemann, J.H.4    Aebi, M.5
  • 7
    • 0021067823 scopus 로고
    • Yeast mutants deficient in protein glycosylation
    • Huffaker, T. C. and Robbins, P. W. (1983) Yeast mutants deficient in protein glycosylation. Proc. Natl. Acad. Sci. U.S.A. 80, 7466-7470
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 7466-7470
    • Huffaker, T.C.1    Robbins, P.W.2
  • 8
    • 0025650995 scopus 로고
    • Complementing mutant alleles define three loci involved in mannosylation of Man5-GlcNAc2-P-P-dolichol in Chinese hamster ovary cells
    • Beck, P. J., Gething, M. J., Sambrook, J. and Lehrman, M. A. (1990) Complementing mutant alleles define three loci involved in mannosylation of Man5-GlcNAc2-P-P-dolichol in Chinese hamster ovary cells. Somat. Cell. Mol. Genet. 16, 539-548
    • (1990) Somat. Cell. Mol. Genet , vol.16 , pp. 539-548
    • Beck, P.J.1    Gething, M.J.2    Sambrook, J.3    Lehrman, M.A.4
  • 9
    • 0030610515 scopus 로고    scopus 로고
    • Reduced utilization of Man5GlcNAc2-P-P-lipid in a Lec9 mutant of Chinese hamster ovary cells: Analysis of the steps in oligosaccharide-lipid assembly
    • Hall, C. W., McLachlan, K. R., Krag, S. S. and Robbins, A. R. (1997) Reduced utilization of Man5GlcNAc2-P-P-lipid in a Lec9 mutant of Chinese hamster ovary cells: analysis of the steps in oligosaccharide-lipid assembly. J. Cell. Biochem. 67, 201-215
    • (1997) J. Cell. Biochem , vol.67 , pp. 201-215
    • Hall, C.W.1    McLachlan, K.R.2    Krag, S.S.3    Robbins, A.R.4
  • 10
    • 0026101693 scopus 로고
    • Isolation of Chinese hamster ovary cell lines producing Man3GlcNAc2 asparagine-linked glycans
    • Zeng, Y. and Lehrman, M. A. (1991) Isolation of Chinese hamster ovary cell lines producing Man3GlcNAc2 asparagine-linked glycans. Anal. Biochem. 193, 266-271
    • (1991) Anal. Biochem , vol.193 , pp. 266-271
    • Zeng, Y.1    Lehrman, M.A.2
  • 11
    • 27144514509 scopus 로고    scopus 로고
    • Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol
    • Bickel, T., Lehle, L., Schwarz, M., Aebi, M. and Jakob, C. A. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J. Biol. Chem. 280, 34500-34506
    • (2005) J. Biol. Chem , vol.280 , pp. 34500-34506
    • Bickel, T.1    Lehle, L.2    Schwarz, M.3    Aebi, M.4    Jakob, C.A.5
  • 12
    • 15744363474 scopus 로고    scopus 로고
    • Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae
    • Chantret, I., Dancourt, J., Barbat, A. and Moore, S. E. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 280, 9236-9242
    • (2005) J. Biol. Chem , vol.280 , pp. 9236-9242
    • Chantret, I.1    Dancourt, J.2    Barbat, A.3    Moore, S.E.4
  • 13
    • 27744580153 scopus 로고    scopus 로고
    • Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation
    • Gao, X. D., Tachikawa, H., Sato, T., Jigami, Y. and Dean, N. (2005) Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. J. Biol. Chem. 280, 36254-36262
    • (2005) J. Biol. Chem , vol.280 , pp. 36254-36262
    • Gao, X.D.1    Tachikawa, H.2    Sato, T.3    Jigami, Y.4    Dean, N.5
  • 14
    • 33747128154 scopus 로고    scopus 로고
    • In vitro evidence for the dual function of Alg2 and Alg11: Essential mannosyltransferases in N-linked glycoprotein biosynthesis
    • O'Reilly, M. K., Zhang, G. and Imperiali, B. (2006) In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45, 9593-9603
    • (2006) Biochemistry , vol.45 , pp. 9593-9603
    • O'Reilly, M.K.1    Zhang, G.2    Imperiali, B.3
  • 15
    • 66449125125 scopus 로고    scopus 로고
    • Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis
    • Kämpf, M., Absmanner, B., Schwarz, M. and Lehle, L. (2009) Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284, 11900-11912
    • (2009) J. Biol. Chem , vol.284 , pp. 11900-11912
    • Kämpf, M.1    Absmanner, B.2    Schwarz, M.3    Lehle, L.4
  • 16
    • 0035877608 scopus 로고    scopus 로고
    • The yeast ALG11 gene specifies addition of the terminal α1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum
    • Cipollo, J. F., Trimble, R. B., Chi, J. H., Yan, Q. and Dean, N. (2001) The yeast ALG11 gene specifies addition of the terminal α1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum. J. Biol. Chem. 276, 21828-21840
    • (2001) J. Biol. Chem , vol.276 , pp. 21828-21840
    • Cipollo, J.F.1    Trimble, R.B.2    Chi, J.H.3    Yan, Q.4    Dean, N.5
  • 18
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P. M., Deleury, E., Davies, G. J. and Henrissat, B. (2003) An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328, 307-317
    • (2003) J. Mol. Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 20
    • 0033546328 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex
    • Knauer, R. and Lehle, L. (1999) The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex. J. Biol. Chem. 274, 17249-17256
    • (1999) J. Biol. Chem , vol.274 , pp. 17249-17256
    • Knauer, R.1    Lehle, L.2
  • 21
    • 0028258760 scopus 로고
    • The N-oligosaccharyltransferase complex from yeast
    • Knauer, R. and Lehle, L. (1994) The N-oligosaccharyltransferase complex from yeast. FEBS Lett. 344, 83-86
    • (1994) FEBS Lett , vol.344 , pp. 83-86
    • Knauer, R.1    Lehle, L.2
  • 22
    • 0035080711 scopus 로고    scopus 로고
    • Biosynthesis of lipid-linked oligosaccharides in yeast: The ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase
    • Sharma, C. B., Knauer, R. and Lehle, L. (2001) Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. Biol. Chem. 382, 321-328
    • (2001) Biol. Chem , vol.382 , pp. 321-328
    • Sharma, C.B.1    Knauer, R.2    Lehle, L.3
  • 23
    • 0037590885 scopus 로고    scopus 로고
    • A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis
    • Thiel, C., Schwarz, M., Peng, J., Grzmil, M., Hasilik, M., Braulke, T., Kohlschutter, A., von Figura, K., Lehle, L. and Korner, C. (2003) A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis. J. Biol. Chem. 278, 22498-22505
    • (2003) J. Biol. Chem , vol.278 , pp. 22498-22505
    • Thiel, C.1    Schwarz, M.2    Peng, J.3    Grzmil, M.4    Hasilik, M.5    Braulke, T.6    Kohlschutter, A.7    von Figura, K.8    Lehle, L.9    Korner, C.10
  • 24
  • 25
    • 0028058793 scopus 로고
    • A new approach for isolating cell wall mutants in Saccharomyces cerevisiae by screening for hypersensitivity to calcofluor white
    • Ram, A. F., Wolters, A., Ten Hoopen, R. and Klis, F. M. (1994) A new approach for isolating cell wall mutants in Saccharomyces cerevisiae by screening for hypersensitivity to calcofluor white. Yeast 10 , 1019-1030
    • (1994) Yeast , vol.10 , pp. 1019-1030
    • Ram, A.F.1    Wolters, A.2    Ten Hoopen, R.3    Klis, F.M.4
  • 26
    • 0028920365 scopus 로고
    • The proliferation of MAP kinase signaling pathways in yeast
    • Levin, D. E. and Errede, B. (1995) The proliferation of MAP kinase signaling pathways in yeast. Curr. Opin. Cell Biol. 7, 197-202
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 197-202
    • Levin, D.E.1    Errede, B.2
  • 27
    • 0032573515 scopus 로고    scopus 로고
    • Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation
    • Stolz, J., Ludwig, A. and Sauer, N. (1998) Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation. FEBS Lett. 440, 213-217
    • (1998) FEBS Lett , vol.440 , pp. 213-217
    • Stolz, J.1    Ludwig, A.2    Sauer, N.3
  • 28
    • 0038236204 scopus 로고    scopus 로고
    • Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae
    • Kim, H., Yan, Q., Von Heijne, G., Caputo, G. A. and Lennarz, W. J. (2003) Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 100, 7460-7464
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 7460-7464
    • Kim, H.1    Yan, Q.2    Von Heijne, G.3    Caputo, G.A.4    Lennarz, W.J.5
  • 29
    • 0025099013 scopus 로고
    • Genetic and biochemical evaluation of eucaryotic membrane protein topology: Multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Sengstag, C., Stirling, C., Schekman, R. and Rine, J. (1990) Genetic and biochemical evaluation of eucaryotic membrane protein topology: multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol. Cell. Biol. 10, 672-680
    • (1990) Mol. Cell. Biol , vol.10 , pp. 672-680
    • Sengstag, C.1    Stirling, C.2    Schekman, R.3    Rine, J.4
  • 30
    • 0035443118 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases: Families and functional modules
    • Bourne, Y. and Henrissat, B. (2001) Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11, 593-600
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 593-600
    • Bourne, Y.1    Henrissat, B.2
  • 31
    • 0034704103 scopus 로고    scopus 로고
    • Identification of essential amino acids in the bacterial α-mannosyltransferase aceA
    • Abdian, P. L., Lellouch, A. C., Gautier, C., Ielpi, L. and Geremia, R. A. (2000) Identification of essential amino acids in the bacterial α-mannosyltransferase aceA. J. Biol. Chem. 275, 40568-40575
    • (2000) J. Biol. Chem , vol.275 , pp. 40568-40575
    • Abdian, P.L.1    Lellouch, A.C.2    Gautier, C.3    Ielpi, L.4    Geremia, R.A.5
  • 32
    • 0034721854 scopus 로고    scopus 로고
    • Identification of two essential glutamic acid residues in glycogen synthase
    • Cid, E., Gomis, R. R., Geremia, R. A., Guinovart, J. J. and Ferrer, J. C. (2000) Identification of two essential glutamic acid residues in glycogen synthase. J. Biol. Chem. 275, 33614-33621
    • (2000) J. Biol. Chem , vol.275 , pp. 33614-33621
    • Cid, E.1    Gomis, R.R.2    Geremia, R.A.3    Guinovart, J.J.4    Ferrer, J.C.5
  • 33
    • 0344011651 scopus 로고    scopus 로고
    • Comparative importance in vivo of conserved glutamate residues in the EX7E motif retaining glycosyltransferase Gpi3p, the UDP-GlcNAc-binding subunit of the first enzyme in glycosylphosphatidylinositol assembly
    • Kostova, Z., Yan, B. C., Vainauskas, S., Schwartz, R., Menon, A. K. and Orlean, P. (2003) Comparative importance in vivo of conserved glutamate residues in the EX7E motif retaining glycosyltransferase Gpi3p, the UDP-GlcNAc-binding subunit of the first enzyme in glycosylphosphatidylinositol assembly. Eur. J. Biochem. 270, 4507-4514
    • (2003) Eur. J. Biochem , vol.270 , pp. 4507-4514
    • Kostova, Z.1    Yan, B.C.2    Vainauskas, S.3    Schwartz, R.4    Menon, A.K.5    Orlean, P.6
  • 34
    • 11844280851 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in glycosyltransferases
    • Qasba, P. K., Ramakrishnan, B. and Boeggeman, E. (2005) Substrate-induced conformational changes in glycosyltransferases. Trends Biochem. Sci. 30, 53-62
    • (2005) Trends Biochem. Sci , vol.30 , pp. 53-62
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 35
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu, Y., Chen, L., Ha, S., Gross, B., Falcone, B., Walker, D., Mokhtarzadeh, M. and Walker, S. (2003) Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc. Natl. Acad. Sci. U.S.A. 100, 845-849
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6    Mokhtarzadeh, M.7    Walker, S.8
  • 36
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl, J. O. and Grishin, N. V. (2001) Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J. Mol. Biol. 314, 365-374
    • (2001) J. Mol. Biol , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 37
    • 27944444124 scopus 로고    scopus 로고
    • ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis
    • Frank, C. G. and Aebi, M. (2005) ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15, 1156-1163
    • (2005) Glycobiology , vol.15 , pp. 1156-1163
    • Frank, C.G.1    Aebi, M.2
  • 38
    • 65249118772 scopus 로고    scopus 로고
    • Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions
    • Troutman, J. M. and Imperiali, B. (2009) Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. Biochemistry 48, 2807-2816
    • (2009) Biochemistry , vol.48 , pp. 2807-2816
    • Troutman, J.M.1    Imperiali, B.2
  • 39
    • 0028236034 scopus 로고
    • New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: Cloning of the ALG8 locus
    • Stagljar, I., te Heesen, S. and Aebi, M. (1994) New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. U.S.A. 91, 5977-5981
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 5977-5981
    • Stagljar, I.1    te Heesen, S.2    Aebi, M.3
  • 44
    • 0028787440 scopus 로고
    • The essential OST2 gene encodes the 16-kD subunit of the yeast oligosaccharyltransferase, a highly conserved protein expressed in diverse eukaryotic organisms
    • Silberstein, S., Collins, P. G., Kelleher, D. J. and Gilmore, R. (1995) The essential OST2 gene encodes the 16-kD subunit of the yeast oligosaccharyltransferase, a highly conserved protein expressed in diverse eukaryotic organisms. J. Cell Biol. 131, 371-383
    • (1995) J. Cell Biol , vol.131 , pp. 371-383
    • Silberstein, S.1    Collins, P.G.2    Kelleher, D.J.3    Gilmore, R.4
  • 45
    • 0034683236 scopus 로고    scopus 로고
    • Protein targeting (Nobel lecture)
    • Blobel, G. (2000) Protein targeting (Nobel lecture). Chembiochem 1, 86-102
    • (2000) Chembiochem , vol.1 , pp. 86-102
    • Blobel, G.1
  • 46
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson, B. M., Critchley, A. J. and Stirling, C. J. (1996) Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271, 25590-25597
    • (1996) J. Biol. Chem , vol.271 , pp. 25590-25597
    • Wilkinson, B.M.1    Critchley, A.J.2    Stirling, C.J.3
  • 47
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • Bracey, M. H., Hanson, M. A., Masuda, K. R., Stevens, R. C. and Cravatt, B. F. (2002) Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. Science 298, 1793-1796
    • (2002) Science , vol.298 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 48
    • 0037820642 scopus 로고    scopus 로고
    • A transmembrane segment mimic derived from Escherichia coli diacylglycerol kinase inhibits protein activity
    • Partridge, A. W., Melnyk, R. A., Yang, D., Bowie, J. U. and Deber, C. M. (2003) A transmembrane segment mimic derived from Escherichia coli diacylglycerol kinase inhibits protein activity. J. Biol. Chem. 278, 22056-22060
    • (2003) J. Biol. Chem , vol.278 , pp. 22056-22060
    • Partridge, A.W.1    Melnyk, R.A.2    Yang, D.3    Bowie, J.U.4    Deber, C.M.5
  • 49
    • 0036589171 scopus 로고    scopus 로고
    • Insertion intermediates of pore-forming colicins in membrane two-dimensional space
    • Zakharov, S. D. and Cramer, W. A. (2002) Insertion intermediates of pore-forming colicins in membrane two-dimensional space. Biochimie 84, 465-475
    • (2002) Biochimie , vol.84 , pp. 465-475
    • Zakharov, S.D.1    Cramer, W.A.2
  • 50
    • 3042723501 scopus 로고    scopus 로고
    • Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum
    • Gao, X. D., Nishikawa, A. and Dean, N. (2004) Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum. Glycobiology 14, 559-570
    • (2004) Glycobiology , vol.14 , pp. 559-570
    • Gao, X.D.1    Nishikawa, A.2    Dean, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.