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Volumn 157, Issue 1, 2015, Pages 23-34

The cytoplasmic peptide:N-glycanase (Ngly1) - Basic science encounters a human genetic disorder

Author keywords

basic science; ERAD; genetic disorder; Ngly1; PNGase

Indexed keywords

CYTOPLASM PROTEIN; GLYCAN DERIVATIVE; GLYCOPEPTIDASE; GLYCOPEPTIDE; GLYCOPROTEIN; OLIGOSACCHARIDE;

EID: 84931583499     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvu068     Document Type: Review
Times cited : (58)

References (118)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger, R.S. and Lowe, J.B. (2004) Role of glycosylation in development. Annu. Rev. Biochem. 73, 491-537
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 3
    • 0017381301 scopus 로고
    • Demonstration of a new amidase acting on glycopeptides
    • Takahashi, N. (1977) Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76, 1194-1201
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 1194-1201
    • Takahashi, N.1
  • 4
    • 0021189137 scopus 로고
    • Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations
    • Plummer, T.H. Jr., Elder, J.H., Alexander, S., Phelan, A.W., and Tarentino, A.L. (1984) Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. J. Biol. Chem. 259, 10700-10704
    • (1984) J. Biol. Chem. , vol.259 , pp. 10700-10704
    • Plummer, T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 5
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley, F., Trimble, R.B., Tarentino, A.L., and Plummer, T.H. Jr. (1989) Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 180, 195-204
    • (1989) Anal. Biochem. , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer, T.H.4
  • 6
    • 84915791535 scopus 로고    scopus 로고
    • PNGases as valuable tools in glycoprotein analysis
    • Wang, T. and Voglmeir, J. (2014) PNGases as valuable tools in glycoprotein analysis. Protein Pept. Lett. 21, 976-985
    • (2014) Protein Pept. Lett. , vol.21 , pp. 976-985
    • Wang, T.1    Voglmeir, J.2
  • 7
    • 0025887531 scopus 로고
    • Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish),The first demonstration of the occurrence of peptide:N-glycosidase in animal cells and its implication for the presence of a de-N-glycosylation system in living organisms
    • Seko, A., Kitajima, K., Inoue, Y., and Inoue, S. (1991) Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish). The first demonstration of the occurrence of peptide:N-glycosidase in animal cells and its implication for the presence of a de-N-glycosylation system in living organisms. J. Biol. Chem. 266, 22110-22114
    • (1991) J. Biol. Chem. , vol.266 , pp. 22110-22114
    • Seko, A.1    Kitajima, K.2    Inoue, Y.3    Inoue, S.4
  • 8
    • 0027259262 scopus 로고
    • Identification of peptide:N-glycanase activity in mammalian-derived cultured cells
    • Suzuki, T., Seko, A., Kitajima, K., Inoue, Y., and Inoue, S. (1993) Identification of peptide:N-glycanase activity in mammalian-derived cultured cells. Biochem. Biophys. Res. Commun. 194, 1124-1130
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1124-1130
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 9
    • 0028362217 scopus 로고
    • Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells,Possible widespread occurrence of posttranslational remodification of proteins by N-deglycosylation
    • Suzuki, T., Seko, A., Kitajima, K., Inoue, Y., and Inoue, S. (1994) Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of posttranslational remodification of proteins by N-deglycosylation. J. Biol. Chem. 269, 17611-17618
    • (1994) J. Biol. Chem. , vol.269 , pp. 17611-17618
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 10
    • 0029033904 scopus 로고
    • Identification and distribution of peptide:N-glycanase (PNGase) in mouse organs
    • Kitajima, K., Suzuki, T., Kouchi, Z., Inoue, S., and Inoue, Y. (1995) Identification and distribution of peptide:N-glycanase (PNGase) in mouse organs. Arch. Biochem. Biophys. 319, 393-401
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 393-401
    • Kitajima, K.1    Suzuki, T.2    Kouchi, Z.3    Inoue, S.4    Inoue, Y.5
  • 11
    • 0028587113 scopus 로고
    • Occurrence and biological roles of proximal glycanases in animal cells
    • Suzuki, T., Kitajima, K., Inoue, S., and Inoue, Y. (1994) Occurrence and biological roles of proximal glycanases in animal cells. Glycobiology 4, 777-789
    • (1994) Glycobiology , vol.4 , pp. 777-789
    • Suzuki, T.1    Kitajima, K.2    Inoue, S.3    Inoue, Y.4
  • 12
    • 0029043240 scopus 로고
    • N-glycosylation/deglycosylation as a mechanism for the post-translational modification/remodification of proteins
    • Suzuki, T., Kitajima, K., Inoue, S., and Inoue, Y. (1995) N-glycosylation/deglycosylation as a mechanism for the post-translational modification/remodification of proteins. Glycoconj. J. 12, 183-193
    • (1995) Glycoconj. J. , vol.12 , pp. 183-193
    • Suzuki, T.1    Kitajima, K.2    Inoue, S.3    Inoue, Y.4
  • 13
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R.D. and Sitia, R. (1990) Protein degradation in the endoplasmic reticulum. Cell 62, 611-614
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 14
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S., and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 15
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitinproteasome pathway
    • Biederer, T., Volkwein, C., and Sommer, T. (1996) Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitinproteasome pathway. EMBO J. 15, 2069-2076
    • (1996) EMBO J. , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 16
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 17
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu, D., Teckman, J.H., Omura, S., and Perlmutter, D.H. (1996) Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271, 22791-22795
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 18
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulumassociated protein degradation: An unconventional route to a familiar fate
    • Werner, E.D., Brodsky, J.L., and McCracken, A.A. (1996) Proteasome-dependent endoplasmic reticulumassociated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. U S A. 93, 13797-13801
    • (1996) Proc. Natl. Acad. Sci. U S A , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 19
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class i heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E.J., Jones, T.R., Sun, L., Bogyo, M., Geuze, H.J., and Ploegh, H.L. (1996) The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 20
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R.R. (1997) ER quality control: the cytoplasmic connection. Cell 88, 427-430
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 21
    • 84880618745 scopus 로고    scopus 로고
    • How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: The early history of ERAD
    • Needham, P.G. and Brodsky, J.L. (2013) How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochim. Biophys. Acta 1833, 2447-2457
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2447-2457
    • Needham, P.G.1    Brodsky, J.L.2
  • 22
    • 84878986182 scopus 로고    scopus 로고
    • Specificity and regulation of the endoplasmic reticulum-associated degradation machinery
    • Merulla, J., Fasana, E., Solda, T., and Molinari, M. (2013) Specificity and regulation of the endoplasmic reticulum-associated degradation machinery. Traffic 14, 767-777
    • (2013) Traffic , vol.14 , pp. 767-777
    • Merulla, J.1    Fasana, E.2    Solda, T.3    Molinari, M.4
  • 23
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E.J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T.R., Rapoport, T.A., and Ploegh, H.L. (1996) Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 24
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class i heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes, E.A., Hammond, C., and Cresswell, P. (1997) Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. U S A. 94, 1896-1901
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 1896-1901
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 25
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • Huppa, J.B. and Ploegh, H.L. (1997) The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7, 113-122
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 26
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu, H., Kaung, G., Kobayashi, S., and Kopito, R.R. (1997) Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J. Biol. Chem. 272, 20800-20804
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 27
    • 0030912157 scopus 로고    scopus 로고
    • Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
    • Halaban, R., Cheng, E., Zhang, Y., Moellmann, G., Hanlon, D., Michalak, M., Setaluri, V., and Hebert, D.N. (1997) Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Natl. Acad. Sci. U S A. 94, 6210-6215
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 6210-6215
    • Halaban, R.1    Cheng, E.2    Zhang, Y.3    Moellmann, G.4    Hanlon, D.5    Michalak, M.6    Setaluri, V.7    Hebert, D.N.8
  • 28
    • 0030926458 scopus 로고    scopus 로고
    • Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide:N-glycanase as a quality control system for newly synthesized proteins
    • Suzuki, T., Kitajima, K., Emori, Y., Inoue, Y., and Inoue, S. (1997) Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide:N-glycanase as a quality control system for newly synthesized proteins. Proc. Natl. Acad. Sci. U S A. 94, 6244-6249
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 6244-6249
    • Suzuki, T.1    Kitajima, K.2    Emori, Y.3    Inoue, Y.4    Inoue, S.5
  • 29
    • 0031973735 scopus 로고    scopus 로고
    • The class i antigenprocessing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol
    • Mosse, C.A., Meadows, L., Luckey, C.J., Kittlesen, D.J., Huczko, E.L., Slingluff, C.L., Shabanowitz, J., Hunt, D.F., and Engelhard, V.H. (1998) The class I antigenprocessing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol. J. Exp. Med. 187, 37-48
    • (1998) J. Exp. Med. , vol.187 , pp. 37-48
    • Mosse, C.A.1    Meadows, L.2    Luckey, C.J.3    Kittlesen, D.J.4    Huczko, E.L.5    Slingluff, C.L.6    Shabanowitz, J.7    Hunt, D.F.8    Engelhard, V.H.9
  • 30
    • 0032491397 scopus 로고    scopus 로고
    • The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61beta and a cytosolic, deglycosylated intermediary
    • Bebok, Z., Mazzochi, C., King, S.A., Hong, J.S., and Sorscher, E.J. (1998) The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61beta and a cytosolic, deglycosylated intermediary. J. Biol. Chem. 273, 29873-29878
    • (1998) J. Biol. Chem. , vol.273 , pp. 29873-29878
    • Bebok, Z.1    Mazzochi, C.2    King, S.A.3    Hong, J.S.4    Sorscher, E.J.5
  • 31
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • de Virgilio, M., Weninger, H., and Ivessa, N.E. (1998) Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 273, 9734-9743
    • (1998) J. Biol. Chem. , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 32
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L., and Kopito, R.R. (1998) Aggresomes: a cellular response to misfolded proteins. J. Cell. Biol. 143, 1883-1898
    • (1998) J. Cell. Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 33
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide:N-glycanase activity
    • Suzuki, T., Park, H., Kitajima, K., and Lennarz, W.J. (1998) Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide:N-glycanase activity. J. Biol. Chem. 273, 21526-21530
    • (1998) J. Biol. Chem. , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 35
    • 0014086848 scopus 로고
    • Macromolecule synthesis in temperature-sensitive mutants of yeast
    • Hartwell, L.H. (1967) Macromolecule synthesis in temperature-sensitive mutants of yeast. J. Bacteriol. 93, 1662-1670
    • (1967) J. Bacteriol. , vol.93 , pp. 1662-1670
    • Hartwell, L.H.1
  • 36
    • 0037414456 scopus 로고    scopus 로고
    • Ngly1, a mouse gene encoding a deglycosylating enzyme implicated in proteasomal degradation: Expression, genomic organization, and chromosomal mapping
    • Suzuki, T., Kwofie, M.A., and Lennarz, W.J. (2003) Ngly1, a mouse gene encoding a deglycosylating enzyme implicated in proteasomal degradation: expression, genomic organization, and chromosomal mapping. Biochem. Biophys. Res. Commun. 304, 326-332
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 326-332
    • Suzuki, T.1    Kwofie, M.A.2    Lennarz, W.J.3
  • 37
    • 0036239939 scopus 로고    scopus 로고
    • Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: Occurrence, primary structure, and potential functions
    • Suzuki, T., Park, H., and Lennarz, W.J. (2002) Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions. FASEB J. 16, 635-641
    • (2002) FASEB J. , vol.16 , pp. 635-641
    • Suzuki, T.1    Park, H.2    Lennarz, W.J.3
  • 39
    • 35748935131 scopus 로고    scopus 로고
    • Unique peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulphide reductase as well as of deglycosylation
    • Kato, T., Kawahara, A., Ashida, H., and Yamamoto, K. (2007) Unique peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulphide reductase as well as of deglycosylation. J. Biochem. 142, 175-181
    • (2007) J. Biochem. , vol.142 , pp. 175-181
    • Kato, T.1    Kawahara, A.2    Ashida, H.3    Yamamoto, K.4
  • 40
    • 0030917149 scopus 로고    scopus 로고
    • Similar processes mediate glycopeptide export from the endoplasmic reticulum in mammalian cells and Saccharomyces cerevisiae
    • Romisch, K. and Ali, B.R. (1997) Similar processes mediate glycopeptide export from the endoplasmic reticulum in mammalian cells and Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U S A. 94, 6730-6734
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 6730-6734
    • Romisch, K.1    Ali, B.R.2
  • 41
    • 0032850389 scopus 로고    scopus 로고
    • Identification of two discrete peptide: N-glycanases in Oryzias latipes during embryogenesis
    • Seko, A., Kitajima, K., Iwamatsu, T., Inoue, Y., and Inoue, S. (1999) Identification of two discrete peptide: N-glycanases in Oryzias latipes during embryogenesis. Glycobiology 9, 887-895
    • (1999) Glycobiology , vol.9 , pp. 887-895
    • Seko, A.1    Kitajima, K.2    Iwamatsu, T.3    Inoue, Y.4    Inoue, S.5
  • 42
    • 84861945664 scopus 로고    scopus 로고
    • Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum
    • Gosain, A., Lohia, R., Shrivastava, A., and Saran, S. (2012) Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum. BMC Biochem. 13, 9
    • (2012) BMC Biochem. , vol.13 , pp. 9
    • Gosain, A.1    Lohia, R.2    Shrivastava, A.3    Saran, S.4
  • 43
    • 40049097698 scopus 로고    scopus 로고
    • Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe
    • Xin, F., Wang, S., Song, L., Liang, Q., and Qi, Q. (2008) Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe. Biochem. Biophys. Res. Commun. 368, 907-912
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 907-912
    • Xin, F.1    Wang, S.2    Song, L.3    Liang, Q.4    Qi, Q.5
  • 45
    • 34748833562 scopus 로고    scopus 로고
    • The Arabidopsis AtPNG1 gene encodes a peptide: N-glycanase
    • Diepold, A., Li, G., Lennarz, W.J., Nurnberger, T., and Brunner, F. (2007) The Arabidopsis AtPNG1 gene encodes a peptide: N-glycanase. Plant J. 52, 94-104
    • (2007) Plant J. , vol.52 , pp. 94-104
    • Diepold, A.1    Li, G.2    Lennarz, W.J.3    Nurnberger, T.4    Brunner, F.5
  • 46
    • 0035850770 scopus 로고    scopus 로고
    • The PUB domain: A putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway
    • Suzuki, T., Park, H., Till, E.A., and Lennarz, W.J. (2001) The PUB domain: a putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway. Biochem. Biophys. Res. Commun. 287, 1083-1087
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 1083-1087
    • Suzuki, T.1    Park, H.2    Till, E.A.3    Lennarz, W.J.4
  • 47
    • 0036143156 scopus 로고    scopus 로고
    • Systematic identification of novel protein domain families associated with nuclear functions
    • Doerks, T., Copley, R.R., Schultz, J., Ponting, C.P., and Bork, P. (2002) Systematic identification of novel protein domain families associated with nuclear functions. Genome Res. 12, 47-56
    • (2002) Genome Res. , vol.12 , pp. 47-56
    • Doerks, T.1    Copley, R.R.2    Schultz, J.3    Ponting, C.P.4    Bork, P.5
  • 48
    • 33748752425 scopus 로고    scopus 로고
    • The PUB domain functions as a p97 binding module in human peptide N-glycanase
    • Allen, M.D., Buchberger, A., and Bycroft, M. (2006) The PUB domain functions as a p97 binding module in human peptide N-glycanase. J. Biol. Chem. 281, 25502-25508
    • (2006) J. Biol. Chem. , vol.281 , pp. 25502-25508
    • Allen, M.D.1    Buchberger, A.2    Bycroft, M.3
  • 50
    • 84859894300 scopus 로고    scopus 로고
    • NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23
    • Kamiya, Y., Uekusa, Y., Sumiyoshi, A., Sasakawa, H., Hirao, T., Suzuki, T., and Kato, K. (2012) NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23. FEBS Lett. 586, 1141-1146
    • (2012) FEBS Lett. , vol.586 , pp. 1141-1146
    • Kamiya, Y.1    Uekusa, Y.2    Sumiyoshi, A.3    Sasakawa, H.4    Hirao, T.5    Suzuki, T.6    Kato, K.7
  • 51
    • 84899982792 scopus 로고    scopus 로고
    • Binding of OTULIN to the PUB domain of HOIP controls NFkappaB signaling
    • Schaeffer, V., Akutsu, M., Olma, M.H., Gomes, L.C., Kawasaki, M., and Dikic, I. (2014) Binding of OTULIN to the PUB domain of HOIP controls NFkappaB signaling. Mol. Cell. 54, 349-361
    • (2014) Mol. Cell , vol.54 , pp. 349-361
    • Schaeffer, V.1    Akutsu, M.2    Olma, M.H.3    Gomes, L.C.4    Kawasaki, M.5    Dikic, I.6
  • 52
    • 33751213902 scopus 로고    scopus 로고
    • Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannosebinding module
    • Zhou, X., Zhao, G., Truglio, J.J., Wang, L., Li, G., Lennarz, W.J., and Schindelin, H. (2006) Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannosebinding module. Proc. Natl. Acad. Sci. U S A. 103, 17214-17219
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 17214-17219
    • Zhou, X.1    Zhao, G.2    Truglio, J.J.3    Wang, L.4    Li, G.5    Lennarz, W.J.6    Schindelin, H.7
  • 53
    • 0028019396 scopus 로고
    • Does an animal peptide: N-glycanase have the dual role as an enzyme and a carbohydrate-binding protein
    • Suzuki, T., Kitajima, K., Inoue, S., and Inoue, Y. (1994) Does an animal peptide: N-glycanase have the dual role as an enzyme and a carbohydrate-binding protein? Glycoconj. J. 11, 469-476
    • (1994) Glycoconj.J , vol.11 , pp. 469-476
    • Suzuki, T.1    Kitajima, K.2    Inoue, S.3    Inoue, Y.4
  • 54
    • 0028998706 scopus 로고
    • Carbohydrate-binding property of peptide: N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides
    • Suzuki, T., Kitajima, K., Inoue, Y., and Inoue, S. (1995) Carbohydrate-binding property of peptide: N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides. J. Biol. Chem. 270, 15181-15186
    • (1995) J. Biol. Chem. , vol.270 , pp. 15181-15186
    • Suzuki, T.1    Kitajima, K.2    Inoue, Y.3    Inoue, S.4
  • 55
    • 77749326886 scopus 로고    scopus 로고
    • Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoproteins
    • Powell, G and McCabe, O., eds,Nova Science Publishers, Hauppauge, NY
    • Kamiya, Y., Kamiya, D., Urade, R., Suzuki, T., and Kato, K. (2009) Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoproteins in Glycobiology Research Trends (Powell, G. and McCabe, O., eds.) pp. 27-40, Nova Science Publishers, Hauppauge, NY
    • (2009) Glycobiology Research Trends , pp. 27-40
    • Kamiya, Y.1    Kamiya, D.2    Urade, R.3    Suzuki, T.4    Kato, K.5
  • 57
    • 58149327062 scopus 로고    scopus 로고
    • Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase
    • Zhao, G., Li, G., Zhou, X., Matsuo, I., Ito, Y., Suzuki, T., Lennarz, W.J., and Schindelin, H. (2009) Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase. Glycobiology 19, 118-125
    • (2009) Glycobiology , vol.19 , pp. 118-125
    • Zhao, G.1    Li, G.2    Zhou, X.3    Matsuo, I.4    Ito, Y.5    Suzuki, T.6    Lennarz, W.J.7    Schindelin, H.8
  • 58
    • 35148815642 scopus 로고    scopus 로고
    • Fluorescently labeled inhibitor for profiling cytoplasmic peptide:N-glycanase
    • Hagihara, S., Miyazaki, A., Matsuo, I., Tatami, A., Suzuki, T., and Ito, Y. (2007) Fluorescently labeled inhibitor for profiling cytoplasmic peptide:N-glycanase. Glycobiology 17, 1070-1076
    • (2007) Glycobiology , vol.17 , pp. 1070-1076
    • Hagihara, S.1    Miyazaki, A.2    Matsuo, I.3    Tatami, A.4    Suzuki, T.5    Ito, Y.6
  • 60
    • 77449127431 scopus 로고    scopus 로고
    • The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity
    • Maerz, S., Funakoshi, Y., Negishi, Y., Suzuki, T., and Seiler, S. (2010) The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity. J. Biol. Chem. 285, 2326-2332
    • (2010) J. Biol. Chem. , vol.285 , pp. 2326-2332
    • Maerz, S.1    Funakoshi, Y.2    Negishi, Y.3    Suzuki, T.4    Seiler, S.5
  • 61
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover
    • Misaghi, S., Pacold, M.E., Blom, D., Ploegh, H.L., and Korbel, G.A. (2004) Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem. Biol. 11, 1677-1687
    • (2004) Chem. Biol. , vol.11 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 63
    • 0035877846 scopus 로고    scopus 로고
    • Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast
    • Suzuki, T., Park, H., Kwofie, M.A., and Lennarz, W.J. (2001) Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast. J. Biol. Chem. 276, 21601-21607
    • (2001) J. Biol. Chem. , vol.276 , pp. 21601-21607
    • Suzuki, T.1    Park, H.2    Kwofie, M.A.3    Lennarz, W.J.4
  • 64
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • Watkins, J.F., Sung, P., Prakash, L., and Prakash, S. (1993) The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol. Cell. Biol. 13, 7757-7765
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 66
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • Heessen, S., Masucci, M.G., and Dantuma, N.P. (2005) The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol. Cell. 18, 225-235
    • (2005) Mol. Cell , vol.18 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 68
    • 21544450264 scopus 로고    scopus 로고
    • Structure of a peptide:N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins
    • Lee, J.H., Choi, J.M., Lee, C., Yi, K.J., and Cho, Y. (2005) Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins. Proc. Natl. Acad. Sci. U S A. 102, 9144-9149
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 9144-9149
    • Lee, J.H.1    Choi, J.M.2    Lee, C.3    Yi, K.J.4    Cho, Y.5
  • 69
    • 33744962966 scopus 로고    scopus 로고
    • Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways
    • Zhao, G., Zhou, X., Wang, L., Li, G., Kisker, C., Lennarz, W.J., and Schindelin, H. (2006) Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways. J. Biol. Chem. 281, 13751-13761
    • (2006) J. Biol. Chem. , vol.281 , pp. 13751-13761
    • Zhao, G.1    Zhou, X.2    Wang, L.3    Li, G.4    Kisker, C.5    Lennarz, W.J.6    Schindelin, H.7
  • 70
    • 0035421637 scopus 로고    scopus 로고
    • Peptide-N-glycanases and DNA repair proteins, Xp-C/Rad4, are, respectively, active and inactivated enzymes sharing a common transglutaminase fold
    • Anantharaman, V., Koonin, E.V., and Aravind, L. (2001) Peptide-N-glycanases and DNA repair proteins, Xp-C/Rad4, are, respectively, active and inactivated enzymes sharing a common transglutaminase fold. Hum. Mol. Genet. 10, 1627-1630
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1627-1630
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 71
    • 0035949651 scopus 로고    scopus 로고
    • Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation
    • Park, H., Suzuki, T., and Lennarz, W.J. (2001) Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation. Proc. Natl. Acad. Sci. U S A. 98, 11163-11168
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 11163-11168
    • Park, H.1    Suzuki, T.2    Lennarz, W.J.3
  • 72
    • 4644318292 scopus 로고    scopus 로고
    • A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins
    • Katiyar, S., Li, G., and Lennarz, W.J. (2004) A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. Proc. Natl. Acad. Sci. U S A. 101, 13774-13779
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 13774-13779
    • Katiyar, S.1    Li, G.2    Lennarz, W.J.3
  • 73
    • 26244466567 scopus 로고    scopus 로고
    • The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum
    • Katiyar, S., Joshi, S., and Lennarz, W.J. (2005) The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum. Mol. Biol. Cell 16, 4584-4594
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4584-4594
    • Katiyar, S.1    Joshi, S.2    Lennarz, W.J.3
  • 74
    • 27644581602 scopus 로고    scopus 로고
    • Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome
    • Li, G., Zhou, X., Zhao, G., Schindelin, H., and Lennarz, W.J. (2005) Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome. Proc. Natl. Acad. Sci. U S A. 102, 15809-15814
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 15809-15814
    • Li, G.1    Zhou, X.2    Zhao, G.3    Schindelin, H.4    Lennarz, W.J.5
  • 75
    • 33744817103 scopus 로고    scopus 로고
    • The AAA ATPase p97 links peptide Nglycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor
    • Li, G., Zhao, G., Zhou, X., Schindelin, H., and Lennarz, W.J. (2006) The AAA ATPase p97 links peptide Nglycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. Proc. Natl. Acad. Sci. U S A. 103, 8348-8353
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 8348-8353
    • Li, G.1    Zhao, G.2    Zhou, X.3    Schindelin, H.4    Lennarz, W.J.5
  • 77
    • 77949295782 scopus 로고    scopus 로고
    • Lectin-like ERAD players in ER and cytosol
    • Yoshida, Y. and Tanaka, K. (2010) Lectin-like ERAD players in ER and cytosol. Biochim. Biophys. Acta 1800, 172-180
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 172-180
    • Yoshida, Y.1    Tanaka, K.2
  • 79
    • 0037470364 scopus 로고    scopus 로고
    • Hypothesis: A glycoprotein-degradation complex formed by protein-protein interaction involves cytoplasmic peptide:N-glycanase
    • Suzuki, T. and Lennarz, W.J. (2003) Hypothesis: a glycoprotein-degradation complex formed by protein-protein interaction involves cytoplasmic peptide:N-glycanase. Biochem. Biophys. Res. Commun. 302, 1-5
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 1-5
    • Suzuki, T.1    Lennarz, W.J.2
  • 80
    • 36249024826 scopus 로고    scopus 로고
    • Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol
    • Suzuki, T. (2007) Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol. Semin. Cell Dev. Biol. 18, 762-769
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 762-769
    • Suzuki, T.1
  • 81
    • 0042068176 scopus 로고    scopus 로고
    • Freeoligosaccharide control in the yeast Saccharomyces cerevisiae: Roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p)
    • Chantret, I., Frenoy, J.P., and Moore, S.E. (2003) Freeoligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Biochem. J. 373, 901-908
    • (2003) Biochem. J. , vol.373 , pp. 901-908
    • Chantret, I.1    Frenoy, J.P.2    Moore, S.E.3
  • 82
    • 77951228197 scopus 로고    scopus 로고
    • Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae
    • Hirayama, H., Seino, J., Kitajima, T., Jigami, Y., and Suzuki, T. (2010) Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae. J. Biol. Chem. 285, 12390-12404
    • (2010) J. Biol. Chem. , vol.285 , pp. 12390-12404
    • Hirayama, H.1    Seino, J.2    Kitajima, T.3    Jigami, Y.4    Suzuki, T.5
  • 83
    • 82355181519 scopus 로고    scopus 로고
    • Endoplasmic reticulumassociated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae
    • Chantret, I., Kodali, V.P., Lahmouich, C., Harvey, D.J., and Moore, S.E. (2011) Endoplasmic reticulumassociated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae. J. Biol. Chem. 286, 41786-41800
    • (2011) J. Biol. Chem. , vol.286 , pp. 41786-41800
    • Chantret, I.1    Kodali, V.P.2    Lahmouich, C.3    Harvey, D.J.4    Moore, S.E.5
  • 84
    • 77955351291 scopus 로고    scopus 로고
    • Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells
    • Chantret, I., Fasseu, M., Zaoui, K., Le Bizec, C., Yaye, H.S., Dupre, T., and Moore, S.E. (2010) Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells. PLoS One 5, e11734
    • (2010) PLoS One , vol.5 , pp. e11734
    • Chantret, I.1    Fasseu, M.2    Zaoui, K.3    Le Bizec, C.4    Yaye, H.S.5    Dupre, T.6    Moore, S.E.7
  • 85
    • 84887453331 scopus 로고    scopus 로고
    • Eukaryotic oligosaccharyltransferase generates free oligosaccharides during Nglycosylation
    • Harada, Y., Buser, R., Ngwa, E.M., Hirayama, H., Aebi, M., and Suzuki, T. (2013) Eukaryotic oligosaccharyltransferase generates free oligosaccharides during Nglycosylation. J. Biol. Chem. 288, 32673-32684
    • (2013) J. Biol. Chem. , vol.288 , pp. 32673-32684
    • Harada, Y.1    Buser, R.2    Ngwa, E.M.3    Hirayama, H.4    Aebi, M.5    Suzuki, T.6
  • 86
    • 84908455205 scopus 로고    scopus 로고
    • Non-lysosomal degradation pathway for N-linked glycans and dolichollinked oligosaccharides
    • Suzuki, T. and Harada, Y. (2014) Non-lysosomal degradation pathway for N-linked glycans and dolichollinked oligosaccharides. Biochem. Biophys. Res. Commun. 453, 213-219
    • (2014) Biochem. Biophys. Res. Commun. , vol.453 , pp. 213-219
    • Suzuki, T.1    Harada, Y.2
  • 88
    • 0036798689 scopus 로고    scopus 로고
    • Identification of an endo-beta-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli
    • Kato, T., Fujita, K., Takeuchi, M., Kobayashi, K., Natsuka, S., Ikura, K., Kumagai, H., and Yamamoto, K. (2002) Identification of an endo-beta-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli. Glycobiology 12, 581-587
    • (2002) Glycobiology , vol.12 , pp. 581-587
    • Kato, T.1    Fujita, K.2    Takeuchi, M.3    Kobayashi, K.4    Natsuka, S.5    Ikura, K.6    Kumagai, H.7    Yamamoto, K.8
  • 91
    • 40549122304 scopus 로고    scopus 로고
    • Free oligosaccharide regulation during mammalian protein N-glycosylation
    • Chantret, I. and Moore, S.E. (2008) Free oligosaccharide regulation during mammalian protein N-glycosylation. Glycobiology 18, 210-224
    • (2008) Glycobiology , vol.18 , pp. 210-224
    • Chantret, I.1    Moore, S.E.2
  • 92
    • 74349120754 scopus 로고    scopus 로고
    • Introduction to ''glycometabolome''
    • Suzuki, T. (2009) Introduction to ''glycometabolome''. Trends Glycosci. Glycotechnol. 21, 219-227
    • (2009) Trends Glycosci. Glycotechnol. , vol.21 , pp. 219-227
    • Suzuki, T.1
  • 94
    • 77955301528 scopus 로고    scopus 로고
    • Identification of an Htm1 (EDEM)-dependent, Mns1-independent endoplasmic reticulum-associated degradation (ERAD) pathway in Saccharomyces cerevisiae: Application of a novel assay for glycoprotein ERAD
    • Hosomi, A., Tanabe, K., Hirayama, H., Kim, I., Rao, H., and Suzuki, T. (2010) Identification of an Htm1 (EDEM)-dependent, Mns1-independent endoplasmic reticulum-associated degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD. J. Biol. Chem. 285, 24324-24334
    • (2010) J. Biol. Chem. , vol.285 , pp. 24324-24334
    • Hosomi, A.1    Tanabe, K.2    Hirayama, H.3    Kim, I.4    Rao, H.5    Suzuki, T.6
  • 95
    • 79953182366 scopus 로고    scopus 로고
    • A new autophagy-related checkpoint in the degradation of an ERAD-M target
    • Kario, E., Amar, N., Elazar, Z., and Navon, A. (2011) A new autophagy-related checkpoint in the degradation of an ERAD-M target. J. Biol. Chem. 286, 11479-11491
    • (2011) J. Biol. Chem. , vol.286 , pp. 11479-11491
    • Kario, E.1    Amar, N.2    Elazar, Z.3    Navon, A.4
  • 97
    • 33749512798 scopus 로고    scopus 로고
    • Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic proteases
    • Altrich-VanLith, M.L., Ostankovitch, M., Polefrone, J.M., Mosse, C.A., Shabanowitz, J., Hunt, D.F., and Engelhard, V.H. (2006) Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic proteases. J. Immunol. 177, 5440-5450
    • (2006) J. Immunol. , vol.177 , pp. 5440-5450
    • Altrich-VanLith, M.L.1    Ostankovitch, M.2    Polefrone, J.M.3    Mosse, C.A.4    Shabanowitz, J.5    Hunt, D.F.6    Engelhard, V.H.7
  • 98
    • 38049186976 scopus 로고    scopus 로고
    • N-linked glycosylation does not impair proteasomal degradation but affects class i major histocompatibility complex presentation
    • Kario, E., Tirosh, B., Ploegh, H.L., and Navon, A. (2008) N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation. J. Biol. Chem. 283, 244-254
    • (2008) J. Biol. Chem. , vol.283 , pp. 244-254
    • Kario, E.1    Tirosh, B.2    Ploegh, H.L.3    Navon, A.4
  • 99
    • 65249117852 scopus 로고    scopus 로고
    • N-glycosylation enhances presentation of a MHC class I-restricted epitope from tyrosinase
    • Ostankovitch, M., Altrich-Vanlith, M., Robila, V., and Engelhard, V.H. (2009) N-glycosylation enhances presentation of a MHC class I-restricted epitope from tyrosinase. J. Immunol. 182, 4830-4835
    • (2009) J. Immunol. , vol.182 , pp. 4830-4835
    • Ostankovitch, M.1    Altrich-Vanlith, M.2    Robila, V.3    Engelhard, V.H.4
  • 101
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • Hirsch, C., Blom, D., and Ploegh, H.L. (2003) A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J. 22, 1036-1046
    • (2003) EMBO J. , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 102
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type i membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • Blom, D., Hirsch, C., Stern, P., Tortorella, D., and Ploegh, H.L. (2004) A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J. 23, 650-658
    • (2004) EMBO J. , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 103
    • 84874506918 scopus 로고    scopus 로고
    • Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation
    • Grotzke, J.E., Lu, Q., and Cresswell, P. (2013) Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation. Proc. Natl. Acad. Sci. U S A. 110, 3393-3398
    • (2013) Proc. Natl. Acad. Sci. U S A , vol.110 , pp. 3393-3398
    • Grotzke, J.E.1    Lu, Q.2    Cresswell, P.3
  • 104
    • 84905001446 scopus 로고    scopus 로고
    • ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase
    • Park, S., Jang, I., Zuber, C., Lee, Y., Cho, J.W., Matsuo, I., Ito, Y., and Roth, J. (2014) ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase. Histochem. Cell Biol. 142, 153-169
    • (2014) Histochem. Cell Biol. , vol.142 , pp. 153-169
    • Park, S.1    Jang, I.2    Zuber, C.3    Lee, Y.4    Cho, J.W.5    Matsuo, I.6    Ito, Y.7    Roth, J.8
  • 105
    • 0345687346 scopus 로고    scopus 로고
    • The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa
    • Seiler, S. and Plamann, M. (2003) The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa. Mol. Biol. Cell. 14, 4352-4364
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4352-4364
    • Seiler, S.1    Plamann, M.2
  • 106
    • 77956295730 scopus 로고    scopus 로고
    • Characterization of the temperature-sensitive mutations un-7 and png-1 in Neurospora crassa
    • Dieterle, M.G., Wiest, A.E., Plamann, M., and McCluskey, K. (2010) Characterization of the temperature-sensitive mutations un-7 and png-1 in Neurospora crassa. PLoS One 5, e10703
    • (2010) PLoS One , vol.5 , pp. e10703
    • Dieterle, M.G.1    Wiest, A.E.2    Plamann, M.3    McCluskey, K.4
  • 107
    • 84895882225 scopus 로고    scopus 로고
    • Peptide: N-glycanase is expressed in prestalk cells and plays a role in the differentiation of prespore cells during development of Dictyostelium discoideum
    • Gosain, A., Srivastava, A., and Saran, S. (2014) Peptide: N-glycanase is expressed in prestalk cells and plays a role in the differentiation of prespore cells during development of Dictyostelium discoideum. Indian J. Exp. Biol. 52, 197-206
    • (2014) Indian J. Exp. Biol. , vol.52 , pp. 197-206
    • Gosain, A.1    Srivastava, A.2    Saran, S.3
  • 108
    • 76149108805 scopus 로고    scopus 로고
    • The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans
    • Habibi-Babadi, N., Su, A., de Carvalho, C.E., and Colavita, A. (2010) The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans. J. Neurosci. 30, 1766-1776
    • (2010) J. Neurosci. , vol.30 , pp. 1766-1776
    • Habibi-Babadi, N.1    Su, A.2    De Carvalho, C.E.3    Colavita, A.4
  • 112
    • 0032800014 scopus 로고    scopus 로고
    • A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases
    • Makarova, K.S., Aravind, L., and Koonin, E.V. (1999) A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases. Protein Sci. 8, 1714-1719
    • (1999) Protein Sci. , vol.8 , pp. 1714-1719
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 113
    • 0037066733 scopus 로고    scopus 로고
    • Site-directed mutagenesis study of yeast peptide:n-glycanase,insight into the reaction mechanism of deglycosylation
    • Katiyar, S., Suzuki, T., Balgobin, B.J., and Lennarz, W.J. (2002) Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation. J. Biol. Chem. 277, 12953-12959
    • (2002) J. Biol. Chem. , vol.277 , pp. 12953-12959
    • Katiyar, S.1    Suzuki, T.2    Balgobin, B.J.3    Lennarz, W.J.4
  • 117
    • 84902078096 scopus 로고    scopus 로고
    • Endo-beta-N-acetylglucosamidases (engases) in the fungus trichoderma atroviride: Possible involvement of the filamentous fungi-specific cytosolic engase in the erad process
    • Tzelepis, G., Hosomi, A., Hossain, T.J., Hirayama, H., Dubey, M., Jensen, D.F., Suzuki, T., and Karlsson, M. (2014) Endo-beta-N-acetylglucosamidases (ENGases) in the fungus Trichoderma atroviride: possible involvement of the filamentous fungi-specific cytosolic ENGase in the ERAD process. Biochem. Biophys. Res. Commun. 449, 256-261
    • (2014) Biochem. Biophys. Res. Commun. , vol.449 , pp. 256-261
    • Tzelepis, G.1    Hosomi, A.2    Hossain, T.J.3    Hirayama, H.4    Dubey, M.5    Jensen, D.F.6    Suzuki, T.7    Karlsson, M.8
  • 118
    • 84923181324 scopus 로고    scopus 로고
    • The shifting model in clinical diagnostics: How next-generation sequencing and families are altering the way rare diseases are discovered, studied, and treated
    • Might, M. and Wilsey, M. (2014) The shifting model in clinical diagnostics: how next-generation sequencing and families are altering the way rare diseases are discovered, studied, and treated. Genet Med. 16, 736-737
    • (2014) Genet Med. , vol.16 , pp. 736-737
    • Might, M.1    Wilsey, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.