메뉴 건너뛰기




Volumn 11, Issue 12, 2004, Pages 1677-1687

Using a small molecule inhibitor of peptide: N-glycanaseto probe its role in glycoprotein turnover

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLVALYL ALANYL ASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYL-ALANYL-ASPARTYL FLUOROMETHYL KETONE; CASPASE; GLYCOPEPTIDASE; GLYCOPROTEIN; HLA ANTIGEN CLASS 1; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE CHLOROMETHYL KETONE; Z VAL ALA ASP(OME) FLUOROMETHYLKETONE; Z-VAL-ALA-ASP(OME)-FLUOROMETHYLKETONE;

EID: 10644226176     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.11.010     Document Type: Article
Times cited : (104)

References (33)
  • 1
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • L. Ellgaard, M. Molinari, and A. Helenius Setting the standards: quality control in the secretory pathway Science 286 1999 1882 1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 2
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • L. Ellgaard, and A. Helenius ER quality control: towards an understanding at the molecular level Curr. Opin. Cell Biol. 13 2001 431 437
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 3
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • L. Ellgaard, and A. Helenius Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 4 2003 181 191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 4
    • 0036899975 scopus 로고    scopus 로고
    • Oligosaccharyl transferase: Gatekeeper to the secretory pathway
    • R.E. Dempski Jr., and B. Imperiali Oligosaccharyl transferase: gatekeeper to the secretory pathway Curr. Opin. Chem. Biol. 6 2002 844 850
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 844-850
    • Dempski Jr., R.E.1    Imperiali, B.2
  • 5
    • 2942620134 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
    • P.A. Wearsch, C.A. Jakob, A. Vallin, R.A. Dwek, P.M. Rudd, and P. Cresswell Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status J. Biol. Chem. 279 2004 25112 25121
    • (2004) J. Biol. Chem. , vol.279 , pp. 25112-25121
    • Wearsch, P.A.1    Jakob, C.A.2    Vallin, A.3    Dwek, R.A.4    Rudd, P.M.5    Cresswell, P.6
  • 6
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • D. Blom, C. Hirsch, P. Stern, D. Tortorella, and H.L. Ploegh A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised EMBO J. 23 2004 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
  • 7
    • 1442331636 scopus 로고    scopus 로고
    • Yeast N-glycanase distinguishes between native and non-native glycoproteins
    • C. Hirsch, S. Misaghi, D. Blom, M.E. Pacold, and H.L. Ploegh Yeast N-glycanase distinguishes between native and non-native glycoproteins EMBO Rep. 5 2004 201 206
    • (2004) EMBO Rep. , vol.5 , pp. 201-206
    • Hirsch, C.1    Misaghi, S.2    Blom, D.3    Pacold, M.E.4    Ploegh, H.L.5
  • 8
    • 0021189137 scopus 로고
    • Demonstration of peptide:N-glycosidase F activity in endo-beta-N- acetylglucosaminidase F preparations
    • T.H. Plummer Jr., J.H. Elder, S. Alexander, A.W. Phelan, and A.L. Tarentino Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations J. Biol. Chem. 259 1984 10700 10704
    • (1984) J. Biol. Chem. , vol.259 , pp. 10700-10704
    • Plummer Jr., T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 9
    • 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
    • H. Park, T. Suzuki, and W.J. Lennarz 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. USA 98 2001 11163 11168
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11163-11168
    • Park, H.1    Suzuki, T.2    Lennarz, W.J.3
  • 11
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • C. Hirsch, D. Blom, and H.L. Ploegh A role for N-glycanase in the cytosolic turnover of glycoproteins EMBO J. 22 2003 1036 1046
    • (2003) EMBO J. , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 12
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • M.T. Heemels, and H. Ploegh Generation, translocation, and presentation of MHC class I-restricted peptides Annu. Rev. Biochem. 64 1995 463 491
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463-491
    • Heemels, M.T.1    Ploegh, H.2
  • 13
    • 0036479140 scopus 로고    scopus 로고
    • Membrane-specific, host-derived factors are required for US2- and US11-mediated degradation of major histocompatibility complex class I molecules
    • M.H. Furman, H.L. Ploegh, and D. Tortorella Membrane-specific, host-derived factors are required for US2- and US11-mediated degradation of major histocompatibility complex class I molecules J. Biol. Chem. 277 2002 3258 3267
    • (2002) J. Biol. Chem. , vol.277 , pp. 3258-3267
    • Furman, M.H.1    Ploegh, H.L.2    Tortorella, D.3
  • 14
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • B.N. Lilley, and H.L. Ploegh A membrane protein required for dislocation of misfolded proteins from the ER Nature 429 2004 834 840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 15
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • E.J. Wiertz, D. Tortorella, M. Bogyo, J. Yu, W. Mothes, T.R. Jones, T.A. Rapoport, and H.L. Ploegh Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction Nature 384 1996 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
  • 16
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • E.J. Wiertz, T.R. Jones, L. Sun, M. Bogyo, H.J. Geuze, and H.L. Ploegh The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol Cell 84 1996 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
  • 18
    • 0037066733 scopus 로고    scopus 로고
    • Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation
    • S. Katiyar, T. Suzuki, B.J. Balgobin, and W.J. Lennarz Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation J. Biol. Chem. 277 2002 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
  • 20
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • H. Yu, G. Kaung, S. Kobayashi, and R.R. Kopito Cytosolic degradation of T-cell receptor alpha chains by the proteasome J. Biol. Chem. 272 1997 20800 20804
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 21
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • J.B. Huppa, and H.L. Ploegh The alpha chain of the T cell antigen receptor is degraded in the cytosol Immunity 7 1997 113 122
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 22
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • J.C. Powers, J.L. Asgian, O.D. Ekici, and K.E. James Irreversible inhibitors of serine, cysteine, and threonine proteases Chem. Rev. 102 2002 4639 4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 23
    • 0041666539 scopus 로고    scopus 로고
    • Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties
    • T.M. Caserta, A.N. Smith, A.D. Gultice, M.A. Reedy, and T.L. Brown Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties Apoptosis 8 2003 345 352
    • (2003) Apoptosis , vol.8 , pp. 345-352
    • Caserta, T.M.1    Smith, A.N.2    Gultice, A.D.3    Reedy, M.A.4    Brown, T.L.5
  • 24
    • 2442505584 scopus 로고    scopus 로고
    • Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation
    • R.G. Spiro Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation Cell. Mol. Life Sci. 61 2004 1025 1041
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1025-1041
    • Spiro, R.G.1
  • 25
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • T. Suzuki, H. Park, K. Kitajima, and W.J. Lennarz Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity J. Biol. Chem. 273 1998 21526 21530
    • (1998) J. Biol. Chem. , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 26
    • 0031042905 scopus 로고    scopus 로고
    • Demonstration of a peptide:N-glycosidase in the endoplasmic reticulum of rat liver
    • S. Weng, and R.G. Spiro Demonstration of a peptide:N-glycosidase in the endoplasmic reticulum of rat liver Biochem. J. 322 1997 655 661
    • (1997) Biochem. J. , vol.322 , pp. 655-661
    • Weng, S.1    Spiro, R.G.2
  • 27
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Y. Ye, Y. Shibata, C. Yun, D. Ron, and T.A. Rapoport A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol Nature 429 2004 841 847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 29
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • F. Hochstenbach, V. David, S. Watkins, and M.B. Brenner Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly Proc. Natl. Acad. Sci. USA 89 1992 4734 4738
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brenner, M.B.4
  • 31
    • 0035794608 scopus 로고    scopus 로고
    • Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor
    • A. Rehm, P. Stern, H.L. Ploegh, and D. Tortorella Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor EMBO J. 20 2001 1573 1582
    • (2001) EMBO J. , vol.20 , pp. 1573-1582
    • Rehm, A.1    Stern, P.2    Ploegh, H.L.3    Tortorella, D.4
  • 32
    • 84988088747 scopus 로고
    • A novel method for the rapid, nonaqueous tert-butoxycarbonylation of some O-17-labeled amino-acids and O-17-NMR parameters of the products
    • E. Ponnusamy, U. Fotadar, A. Spisni, and D. Fiat A novel method for the rapid, nonaqueous tert-butoxycarbonylation of some O-17-labeled amino-acids and O-17-NMR parameters of the products Synthesis (Stuttgart) 1 1986 48 49
    • (1986) Synthesis (Stuttgart) , vol.1 , pp. 48-49
    • Ponnusamy, E.1    Fotadar, U.2    Spisni, A.3    Fiat, D.4
  • 33
    • 10644238496 scopus 로고
    • May Process for forming a fluoromethyl ketone. U.S. patent 5,210,272.
    • Palmer, J.T. May 1993. Process for forming a fluoromethyl ketone. U.S. patent 5,210,272.
    • (1993)
    • Palmer, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.