메뉴 건너뛰기




Volumn 21, Issue 3, 2004, Pages 163-170

Polytopic membrane protein folding and assembly in vitro and in vivo

Author keywords

Endoplasmic reticulum; Folding; Membrane protein; Quality control; Translocon

Indexed keywords

MEMBRANE PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 2942623955     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/09687680410001697215     Document Type: Review
Times cited : (12)

References (74)
  • 2
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang, K.-S., Bayley, H., Liao, M.-J., London, E. and Khorana, H. G., 1981, Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem., 256, 3802-3809.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-3809
    • Huang, K.-S.1    Bayley, H.2    Liao, M.-J.3    London, E.4    Khorana, H.G.5
  • 3
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London, E. and Khorana, H. G., 1982, Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. J. Biol. Chem., 257, 7003-7011.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 4
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen, H., Finkenzeller, B. and Kühlein, N., 1993, Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem., 215, 809-817.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 809-817
    • Paulsen, H.1    Finkenzeller, B.2    Kühlein, N.3
  • 5
    • 0030000359 scopus 로고    scopus 로고
    • Assembly of the light harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements
    • Booth, P. J. and Paulsen, H., 1996, Assembly of the light harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements. Biochemistry, 35, 5103-5108.
    • (1996) Biochemistry , vol.35 , pp. 5103-5108
    • Booth, P.J.1    Paulsen, H.2
  • 6
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
    • Sanders, C. R., II and Landis, G. C., 1995, Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies. Biochemistry, 34, 4030-4040.
    • (1995) Biochemistry , vol.34 , pp. 4030-4040
    • Sanders II, C.R.1    Landis, G.C.2
  • 7
    • 0033534176 scopus 로고    scopus 로고
    • Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein
    • Gorzelle, B. M., Nagy, J. K., Oxenoid, K., Lonzer, W. L., Cafiso, D. S. and Sanders, C. R., 1999, Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein. Biochemistry, 38, 16373-16382.
    • (1999) Biochemistry , vol.38 , pp. 16373-16382
    • Gorzelle, B.M.1    Nagy, J.K.2    Oxenoid, K.3    Lonzer, W.L.4    Cafiso, D.S.5    Sanders, C.R.6
  • 9
    • 0037036754 scopus 로고    scopus 로고
    • Semisynthesis and folding of the potassium channel KcsA
    • Valiyaveetil, F. I., MacKinnon, R. and Muir, T. W., 2002, Semisynthesis and folding of the potassium channel KcsA. J. Am. Chem. Soc., 124, 9113-9120.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9113-9120
    • Valiyaveetil, F.I.1    MacKinnon, R.2    Muir, T.W.3
  • 10
    • 0037015161 scopus 로고    scopus 로고
    • Lipids in the structure, folding, and function of the KcsA K+ channel
    • Valiyaveetil, F. I., Zhou, Y. and MacKinnon, R., 2002, Lipids in the structure, folding, and function of the KcsA K+ channel. Biochemistry, 41, 10771-10777.
    • (2002) Biochemistry , vol.41 , pp. 10771-10777
    • Valiyaveetil, F.I.1    Zhou, Y.2    MacKinnon, R.3
  • 11
    • 0041743087 scopus 로고    scopus 로고
    • Folding of DsbB in mixed micelles: A kinetic analysis of the stability of a bacterial membrane protein
    • Otzen, D., 2003, Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein. J. Mol. Biol., 330, 641-649.
    • (2003) J. Mol. Biol. , vol.330 , pp. 641-649
    • Otzen, D.1
  • 14
    • 0029943869 scopus 로고    scopus 로고
    • Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin
    • Booth, P. J., Farooq, A. and Flitsch, S. L., 1996, Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin. Biochemistry, 35, 5902-5909.
    • (1996) Biochemistry , vol.35 , pp. 5902-5909
    • Booth, P.J.1    Farooq, A.2    Flitsch, S.L.3
  • 15
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • Lau, F. W. and Bowie, J. U., 1997, A method for assessing the stability of a membrane protein. Biochemistry, 36, 5884-5892.
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 16
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U., 2001, Stabilizing membrane proteins. Curr. Opin. Struct. Biol., 11, 397-402.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 17
    • 0035252652 scopus 로고    scopus 로고
    • Probing the interface between membrane proteins and membrane lipids by X-ray crystallography
    • Fyfe, P. K., McAuley, K. E., Roszak, A. W., Isaacs, N. W., Cogdell, R. J. and Jones, M. R., 2001, Probing the interface between membrane proteins and membrane lipids by X-ray crystallography. Trends Biochem. Sci., 26, 106-112.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 106-112
    • Fyfe, P.K.1    McAuley, K.E.2    Roszak, A.W.3    Isaacs, N.W.4    Cogdell, R.J.5    Jones, M.R.6
  • 18
    • 0036306814 scopus 로고    scopus 로고
    • The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition
    • Meijberg, W. and Booth, P. J., 2002, The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition. J. Mol. Biol., 319, 839-853.
    • (2002) J. Mol. Biol. , vol.319 , pp. 839-853
    • Meijberg, W.1    Booth, P.J.2
  • 19
    • 0242488929 scopus 로고    scopus 로고
    • Translocons, thermodynamics, and the folding of membrane proteins
    • White, S. H., 2003, Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett., 555, 116-121.
    • (2003) FEBS Lett. , vol.555 , pp. 116-121
    • White, S.H.1
  • 21
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two stage model
    • Popot, J.-L. and Engelman, D. M., 1990, Membrane protein folding and oligomerization: the two stage model. Biochemistry, 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 22
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge, K., Lee, S. and Yao, L., 1995, In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc. Natl Acad. Sci., 92, 3204-3208.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 3204-3208
    • Ridge, K.1    Lee, S.2    Yao, L.3
  • 23
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M. A. and 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
  • 24
    • 0035957523 scopus 로고    scopus 로고
    • Structure and function in bacteriorhodopsin: The role of the interhelical loops in folding and stability of bacteriorhodopsin
    • Allen, S. J., Kim, J.-M., Khorana, H. G., Lu, H. and Booth, P. J., 2001, Structure and function in bacteriorhodopsin: the role of the interhelical loops in folding and stability of bacteriorhodopsin. J. Mol. Biol., 308, 423-435.
    • (2001) J. Mol. Biol. , vol.308 , pp. 423-435
    • Allen, S.J.1    Kim, J.-M.2    Khorana, H.G.3    Lu, H.4    Booth, P.J.5
  • 25
    • 0035957510 scopus 로고    scopus 로고
    • Structure and function in bacteriorhodopsin: The role of the interhelical loops in the folding and stability of bacteriorhodopsin
    • Kim, J.-M., Booth, P. J., Allen, S. J. and Khorana, H. G., 2001, Structure and function in bacteriorhodopsin: the role of the interhelical loops in the folding and stability of bacteriorhodopsin. J. Mol. Biol., 308, 409-422.
    • (2001) J. Mol. Biol. , vol.308 , pp. 409-422
    • Kim, J.-M.1    Booth, P.J.2    Allen, S.J.3    Khorana, H.G.4
  • 26
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H. and 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
  • 27
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with β-branched residues at neighbouring positions
    • Senes, A., Gerstein, M. and Engelman, D. M., 2000, Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighbouring positions. J. Mol. Biol., 296, 921-936.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 28
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W. P. and Engelman, D. M., 2000, The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol., 296, 911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 29
    • 0025085912 scopus 로고
    • Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
    • Karnik, S. S. and Khorana, H. G., 1990, Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J. Biol. Chem., 265, 17520-17524.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17520-17524
    • Karnik, S.S.1    Khorana, H.G.2
  • 30
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushel, S. and Khorana, H. G., 1994, Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry, 33, 6121-6128.
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushel, S.1    Khorana, H.G.2
  • 31
    • 0024110575 scopus 로고    scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
    • Karnik, S. S., Sakmar, T. P., Chen, H. B. and Khorana, H. G., 1998, Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc. Natl Acad. Sci. USA, 85, 8459-8463.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8459-8463
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.B.3    Khorana, H.G.4
  • 32
    • 0033515036 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Further elucidation of the role of the intra-discal cysteines, Cys-110, -185 and -187 in rhodopsin folding and function
    • Hwa, J., Reeves, P., Klein-Seetharaman, J., Davidson, F. and Khorana, H., 1999, Structure and function in rhodopsin: further elucidation of the role of the intra-discal cysteines, Cys-110, -185 and -187 in rhodopsin folding and function. Proc. Natl Acad. Sci. USA, 96, 1932-1935.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1932-1935
    • Hwa, J.1    Reeves, P.2    Klein-Seetharaman, J.3    Davidson, F.4    Khorana, H.5
  • 33
    • 0030931599 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intra-discal domain are coupled
    • Hwa, J., Garriga, P., Liu, X. and Khorana, H. G., 1997, Structure and function in rhodopsin: packing of the helices in the transmembrane domain and folding to a tertiary structure in the intra-discal domain are coupled. Proc. Natl Acad. Sci. USA, 94, 10571-10576.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10571-10576
    • Hwa, J.1    Garriga, P.2    Liu, X.3    Khorana, H.G.4
  • 34
    • 0141755153 scopus 로고    scopus 로고
    • Retinitis pigmentosa rhodopsin mutations L125R and A164V perturb critical interhelical interactions: New insights through compensatory mutations and crystal structure analysis
    • Stojanovic, A., Hwang, I., Khorana, H. G. and Hwa, J., 2003, Retinitis pigmentosa rhodopsin mutations L125R and A164V perturb critical interhelical interactions: new insights through compensatory mutations and crystal structure analysis. J. Biol. Chem., 278, 39020-39028.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39020-39028
    • Stojanovic, A.1    Hwang, I.2    Khorana, H.G.3    Hwa, J.4
  • 35
    • 0036996692 scopus 로고    scopus 로고
    • Polar mutations in membrane proteins as a biophysical basis for disease
    • Partridge, A. W., Therien, A. G. and Deber, C. M., 2002, Polar mutations in membrane proteins as a biophysical basis for disease. Biopolymers, 66, 350-358.
    • (2002) Biopolymers , vol.66 , pp. 350-358
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 36
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran, A. R. and Engelman, D. M., 2003, Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol., 13, 412-417.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 37
    • 0034952420 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds in the CFTR membrane domain
    • Therien, A. G., Grant, F. E. and Deber, C. M., 2001, Interhelical hydrogen bonds in the CFTR membrane domain. Nat. Struct. Biol., 8, 597-601.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 597-601
    • Therien, A.G.1    Grant, F.E.2    Deber, C.M.3
  • 38
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V. and High, S., 1997, Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem., 272, 1983-1989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 39
    • 0346158365 scopus 로고    scopus 로고
    • Making membrane proteins at the mammalian endoplasmic reticulum
    • Lecomte, F. J., Ismail, N. and High, S., 2003, Making membrane proteins at the mammalian endoplasmic reticulum. Biochem. Soc. Trans., 31, 1248-1252.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1248-1252
    • Lecomte, F.J.1    Ismail, N.2    High, S.3
  • 41
    • 1342310756 scopus 로고    scopus 로고
    • Structural biology. Surprising news from the PCC
    • Dobberstein, B. and Sinning, I., 2004, Structural biology. Surprising news from the PCC. Science, 303, 320-322.
    • (2004) Science , vol.303 , pp. 320-322
    • Dobberstein, B.1    Sinning, I.2
  • 42
    • 0742305352 scopus 로고    scopus 로고
    • The endoplasmic reticulum membrane is permeable to small molecules
    • Le Gall, S., Neuhof, A. and Rapoport, T., 2004, The endoplasmic reticulum membrane is permeable to small molecules. Mol. Biol. Cell. 15, 447-455.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 447-455
    • Le Gall, S.1    Neuhof, A.2    Rapoport, T.3
  • 43
    • 0042815085 scopus 로고    scopus 로고
    • Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane
    • Heinrich, S. U. and Rapoport, T. A., 2003, Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane. EMBO J., 22, 3654-3663.
    • (2003) EMBO J. , vol.22 , pp. 3654-3663
    • Heinrich, S.U.1    Rapoport, T.A.2
  • 44
    • 0036906637 scopus 로고    scopus 로고
    • Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein
    • Meacock, S. L., Lecomte, F. J., Crawshaw, S. G. and High, S., 2002, Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein. Mol. Biol. Cell, 13, 4114-4129.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4114-4129
    • Meacock, S.L.1    Lecomte, F.J.2    Crawshaw, S.G.3    High, S.4
  • 45
  • 46
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich, S. U., Mothes, W., Brunner, J. and Rapoport, T. A., 2000, The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell, 102, 233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 47
    • 0030878575 scopus 로고    scopus 로고
    • Membrane protein biosynthesis - All sewn up?
    • High, S. and Laird, V., 1997, Membrane protein biosynthesis - all sewn up? Trends Cell Biol., 7, 206-210.
    • (1997) Trends Cell Biol. , vol.7 , pp. 206-210
    • High, S.1    Laird, V.2
  • 48
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • McCormick, P. J., Miao, Y., Shao, Y., Lin, J. and Johnson, A. E., 2003, Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Mol. Cell, 21, 329-341.
    • (2003) Mol. Cell , vol.21 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 49
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito, R. R., 1999, Biosynthesis and degradation of CFTR. Physiol. Rev, 79, S167-173.
    • (1999) Physiol. Rev. , vol.79
    • Kopito, R.R.1
  • 50
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo, M. A., Jensen, T. J., Cui, L., Hou, Y., Chang, X. B. and Riordan, J. R., 1998, Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J., 17, 6879-6887.
    • (1998) EMBO J. , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 51
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A. and Cyr, D. M., 1999, The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J., 18, 1492-1505.
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 52
    • 0038819926 scopus 로고    scopus 로고
    • The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation
    • Chapple, J. P. and Cheetham, M. E., 2003, The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. J. Biol. Chem., 278, 19087-19094.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19087-19094
    • Chapple, J.P.1    Cheetham, M.E.2
  • 53
    • 0038037820 scopus 로고    scopus 로고
    • Role of calnexin in the glycan-independent quality control of proteolipid protein
    • Swanton, E., High, S. and Woodman, P., 2003, Role of calnexin in the glycan-independent quality control of proteolipid protein. EMBO J., 22, 2948-2958.
    • (2003) EMBO J. , vol.22 , pp. 2948-2958
    • Swanton, E.1    High, S.2    Woodman, P.3
  • 54
    • 0037018773 scopus 로고    scopus 로고
    • Endoplasmic reticulum storage diseases
    • Rutishauser, J. and Spiess, M., 2002, Endoplasmic reticulum storage diseases. Swiss Med. Wkly, 132, 211-222.
    • (2002) Swiss Med. Wkly. , vol.132 , pp. 211-222
    • Rutishauser, J.1    Spiess, M.2
  • 55
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and Helenius, A., 2003, Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol., 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 56
    • 0033570916 scopus 로고    scopus 로고
    • An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator
    • Tector, M. and Hartl, F. U., 1999, An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator. EMBO J., 18, 6290-6298.
    • (1999) EMBO J. , vol.18 , pp. 6290-6298
    • Tector, M.1    Hartl, F.U.2
  • 57
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard, L., Molinari, M. and Helenius, A., 1999, Setting the standards: quality control in the secretory pathway. Science, 286, 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 58
    • 0034733916 scopus 로고    scopus 로고
    • Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?
    • High, S., Lecomte, F. J., Russell, S. J., Abell, B. M. and Oliver, J. D., 2000, Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones? FEBS Lett., 476, 38-41.
    • (2000) FEBS Lett. , vol.476 , pp. 38-41
    • High, S.1    Lecomte, F.J.2    Russell, S.J.3    Abell, B.M.4    Oliver, J.D.5
  • 60
    • 0037407666 scopus 로고    scopus 로고
    • EDEM an ER quality control receptor
    • Wang, T. and Hebert, D. N., 2003, EDEM an ER quality control receptor. Nat. Struct. Biol., 10, 319-321.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 319-321
    • Wang, T.1    Hebert, D.N.2
  • 61
    • 0028040839 scopus 로고
    • Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins
    • Landolt-Marticorena, C. and Reithmeier, R. A., 1994, Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins. Biochem. J., 302, 253-260.
    • (1994) Biochem. J. , vol.302 , pp. 253-260
    • Landolt-Marticorena, C.1    Reithmeier, R.A.2
  • 62
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels, R., Kurowski, B., Johnson, A. E. and Hebert, D. N., 2003, N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell, 11, 79-90.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 63
    • 0043026909 scopus 로고    scopus 로고
    • Substrate recognition in ER-associated degradation mediated by Epsl, a member of the protein disulfide isomerase family
    • Wang, Q. and Chang, A., 2003, Substrate recognition in ER-associated degradation mediated by Epsl, a member of the protein disulfide isomerase family. EMBO J., 22, 3792-3802.
    • (2003) EMBO J. , vol.22 , pp. 3792-3802
    • Wang, Q.1    Chang, A.2
  • 64
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y. and Rapoport, T. A., 2002, Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol., 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 65
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H. and Rapoport, T. A., 2001, The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature, 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 66
    • 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
  • 67
    • 0037193468 scopus 로고    scopus 로고
    • Dislocation and degradation from the ER are regulated by cytosolic stress
    • VanSlyke, J. K. and Musil, L. S., 2002, Dislocation and degradation from the ER are regulated by cytosolic stress. J. Cell. Biol., 157, 381-394.
    • (2002) J. Cell. Biol. , vol.157 , pp. 381-394
    • VanSlyke, J.K.1    Musil, L.S.2
  • 68
    • 0033490112 scopus 로고    scopus 로고
    • Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane
    • Romisch, K., 1999, Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J. Cell. Sci., 112, 4185-4191.
    • (1999) J. Cell. Sci. , vol.112 , pp. 4185-4191
    • Romisch, K.1
  • 69
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)
    • McCracken, A. A. and Brodsky, J. L., 2003, Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays, 25, 868-877.
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 70
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes, C. M., Caldwell, S. and Cooper, A. A., 2002, An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J. Cell Biol., 158, 91-101.
    • (2002) J. Cell Biol. , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 71
    • 0037343387 scopus 로고    scopus 로고
    • Recognition of a single transmembrane degron by sequential quality control check-points
    • Fayadat, L. and Kopito, R. R., 2003, Recognition of a single transmembrane degron by sequential quality control check-points. Mol. Biol. Cell, 14, 1268-1278.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1268-1278
    • Fayadat, L.1    Kopito, R.R.2
  • 72
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing, M. E., Rajan, R. S., Bence, N. F. and Kopito, R. R., 2002, A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J. Biol. Chem., 277, 34150-34160.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 73
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito, R. R. and Sitia, R., 2000, Aggresomes and Russell bodies. Symptoms of cellular indigestion? EMBO Rep., 1, 225-231.
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.