메뉴 건너뛰기




Volumn 29, Issue 12, 2004, Pages 648-655

Quality control of integral membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 8544263812     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.10.009     Document Type: Review
Times cited : (32)

References (72)
  • 1
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • B. Tsai Retro-translocation of proteins from the endoplasmic reticulum into the cytosol Nat. Rev. Mol. Cell Biol. 3 2002 246 255
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1
  • 2
    • 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
  • 3
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • A.A. McCracken, and J.L. Brodsky Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD) BioEssays 25 2003 868 877
    • (2003) BioEssays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 4
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Z. Kostova, and D.H. Wolf For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection EMBO J. 22 2003 2309 2317
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 5
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems
    • P. Arvan Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems Traffic 3 2002 771 780
    • (2002) Traffic , vol.3 , pp. 771-780
    • Arvan, P.1
  • 6
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • G. Blobel Intracellular protein topogenesis Proc. Natl. Acad. Sci. U. S. A. 77 1980 1496 1500
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 7
    • 0242488929 scopus 로고    scopus 로고
    • Translocons, thermodynamics, and the folding of membrane proteins
    • S.H. White Translocons, thermodynamics, and the folding of membrane proteins FEBS Lett. 555 2003 116 121
    • (2003) FEBS Lett. , vol.555 , pp. 116-121
    • White, S.H.1
  • 8
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • S.H. White, and W.C. Wimley Membrane protein folding and stability: physical principles Annu. Rev. Biophys. Biomol. Struct. 28 1999 319 365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 9
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • T. Haltia, and E. Freire Forces and factors that contribute to the structural stability of membrane proteins Biochim. Biophys. Acta 1241 1995 295 322
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 10
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • J.L. Popot, and D.M. Engelman Helical membrane protein folding, stability, and evolution Annu. Rev. Biochem. 69 2000 881 922
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 11
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • M.A. Lemmon, and D.M. Engelman Specificity and promiscuity in membrane helix interactions Q. Rev. Biophys. 27 1994 157 218
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 12
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • C. Choma Asparagine-mediated self-association of a model transmembrane helix Nat. Struct. Biol. 7 2000 161 166
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 161-166
    • Choma, C.1
  • 13
    • 0034952420 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds in the CFTR membrane domain
    • A.G. Therien Interhelical hydrogen bonds in the CFTR membrane domain Nat. Struct. Biol. 8 2001 597 601
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 597-601
    • Therien, A.G.1
  • 14
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • F.X. Zhou Interhelical hydrogen bonding drives strong interactions in membrane proteins Nat. Struct. Biol. 7 2000 154 160
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 154-160
    • Zhou, F.X.1
  • 15
    • 0035956884 scopus 로고    scopus 로고
    • Polar residues drive association of polyleucine transmembrane helices
    • F.X. Zhou Polar residues drive association of polyleucine transmembrane helices Proc. Natl. Acad. Sci. U. S. A. 98 2001 2250 2255
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2250-2255
    • Zhou, F.X.1
  • 16
    • 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
  • 17
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Y. Ye 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
  • 18
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 19
    • 0037343387 scopus 로고    scopus 로고
    • Recognition of a single transmembrane degron by sequential quality control checkpoints
    • L. Fayadat, and R.R. Kopito Recognition of a single transmembrane degron by sequential quality control checkpoints Mol. Biol. Cell 14 2003 1268 1278
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1268-1278
    • Fayadat, L.1    Kopito, R.R.2
  • 20
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • T.J. Jensen Multiple proteolytic systems, including the proteasome, contribute to CFTR processing Cell 83 1995 129 135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1
  • 21
    • 12144287602 scopus 로고    scopus 로고
    • Misfolding diverts CFTR from recycling to degradation: Quality control at early endosomes
    • M. Sharma Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes J. Cell Biol. 164 2004 923 933
    • (2004) J. Cell Biol. , vol.164 , pp. 923-933
    • Sharma, M.1
  • 22
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • S. Vashist, and D.T. Ng Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control J. Cell Biol. 165 2004 41 52
    • (2004) J. Cell Biol. , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 23
    • 0035875665 scopus 로고    scopus 로고
    • The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
    • K. Yamamoto The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum EMBO J. 20 2001 3082 3091
    • (2001) EMBO J. , vol.20 , pp. 3082-3091
    • Yamamoto, K.1
  • 24
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • J.M. Kowalski Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control J. Biol. Chem. 273 1998 19453 19458
    • (1998) J. Biol. Chem. , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1
  • 25
    • 0032477891 scopus 로고    scopus 로고
    • Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability
    • J.M. Kowalski Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability Biochemistry 37 1998 1264 1273
    • (1998) Biochemistry , vol.37 , pp. 1264-1273
    • Kowalski, J.M.1
  • 26
    • 0037166252 scopus 로고    scopus 로고
    • Engineering-enhanced protein secretory expression in yeast with application to insulin
    • T. Kjeldsen Engineering-enhanced protein secretory expression in yeast with application to insulin J. Biol. Chem. 277 2002 18245 18248
    • (2002) J. Biol. Chem. , vol.277 , pp. 18245-18248
    • Kjeldsen, T.1
  • 27
    • 0035937847 scopus 로고    scopus 로고
    • Conformational and temperature-sensitive stability defects of the Δf508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments
    • M. Sharma Conformational and temperature-sensitive stability defects of the ΔF508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments J. Biol. Chem. 276 2001 8942 8950
    • (2001) J. Biol. Chem. , vol.276 , pp. 8942-8950
    • Sharma, M.1
  • 28
    • 0035947777 scopus 로고    scopus 로고
    • COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments
    • M. Benharouga COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments J. Cell Biol. 153 2001 957 970
    • (2001) J. Cell Biol. , vol.153 , pp. 957-970
    • Benharouga, M.1
  • 29
    • 0035056623 scopus 로고    scopus 로고
    • 2a-adrenergic receptor conformational stability and cell-surface turnover
    • 2a-adrenergic receptor conformational stability and cell-surface turnover Mol. Pharmacol. 59 2001 929 938
    • (2001) Mol. Pharmacol. , vol.59 , pp. 929-938
    • Wilson, M.H.1
  • 30
    • 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
    • M.E. Illing A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system J. Biol. Chem. 277 2002 34150 34160
    • (2002) J. Biol. Chem. , vol.277 , pp. 34150-34160
    • Illing, M.E.1
  • 31
    • 0029943263 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa
    • X. Liu Structure and function in rhodopsin: correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa Proc. Natl. Acad. Sci. U. S. A. 93 1996 4554 4559
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4554-4559
    • Liu, X.1
  • 32
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • S.M. Noorwez Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa J. Biol. Chem. 278 2003 14442 14450
    • (2003) J. Biol. Chem. , vol.278 , pp. 14442-14450
    • Noorwez, S.M.1
  • 33
    • 1942469395 scopus 로고    scopus 로고
    • Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H
    • S.M. Noorwez Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H J. Biol. Chem. 279 2004 16278 16284
    • (2004) J. Biol. Chem. , vol.279 , pp. 16278-16284
    • Noorwez, S.M.1
  • 34
    • 0025076114 scopus 로고
    • Empty MHC class I molecules come out in the cold
    • H.G. Ljunggren Empty MHC class I molecules come out in the cold Nature 346 1990 476 480
    • (1990) Nature , vol.346 , pp. 476-480
    • Ljunggren, H.G.1
  • 35
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • B.H. Qu Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding J. Biol. Chem. 272 1997 15739 15744
    • (1997) J. Biol. Chem. , vol.272 , pp. 15739-15744
    • Qu, B.H.1
  • 37
    • 10744230777 scopus 로고    scopus 로고
    • Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator
    • H.A. Lewis Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator EMBO J. 23 2004 282 293
    • (2004) EMBO J. , vol.23 , pp. 282-293
    • Lewis, H.A.1
  • 38
    • 0037008685 scopus 로고    scopus 로고
    • Introduction of the most common cystic fibrosis mutation (ΔF508) into human P-glycoprotein disrupts packing of the transmembrane segments
    • T.W. Loo Introduction of the most common cystic fibrosis mutation (ΔF508) into human P-glycoprotein disrupts packing of the transmembrane segments J. Biol. Chem. 277 2002 27585 27588
    • (2002) J. Biol. Chem. , vol.277 , pp. 27585-27588
    • Loo, T.W.1
  • 39
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • D.M. Cyr Protein quality control: U-box-containing E3 ubiquitin ligases join the fold Trends Biochem. Sci. 27 2002 368 375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1
  • 40
    • 0038779355 scopus 로고    scopus 로고
    • Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase
    • S.C. Taylor Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase EMBO Rep. 4 2003 405 411
    • (2003) EMBO Rep. , vol.4 , pp. 405-411
    • Taylor, S.C.1
  • 41
    • 0742322956 scopus 로고    scopus 로고
    • The ER protein folding sensor UDP-glucose glycoprotein- glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
    • S.C. Taylor The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation Nat. Struct. Mol. Biol. 11 2004 128 134
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 128-134
    • Taylor, S.C.1
  • 42
    • 0038037820 scopus 로고    scopus 로고
    • Role of calnexin in the glycan-independent quality control of proteolipid protein
    • E. Swanton Role of calnexin in the glycan-independent quality control of proteolipid protein EMBO J. 22 2003 2948 2958
    • (2003) EMBO J. , vol.22 , pp. 2948-2958
    • Swanton, E.1
  • 43
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • R.Y. Hampton ER-associated degradation in protein quality control and cellular regulation Curr. Opin. Cell Biol. 14 2002 476 482
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 44
    • 4644243461 scopus 로고    scopus 로고
    • Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including N-terminus, in transmembrane region of mammalian 3-hydroxy-3- methylglutaryl coenzyme a reductase: Implications for sterol-regulated enzyme degradation
    • R. Doolman Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including N-terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme a reductase: implications for sterol-regulated enzyme degradation J. Biol. Chem. 279 2004 38184 38193
    • (2004) J. Biol. Chem. , vol.279 , pp. 38184-38193
    • Doolman, R.1
  • 45
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • F. Reggiori, and H.R. Pelham A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies Nat. Cell Biol. 4 2002 117 123
    • (2002) Nat. Cell Biol. , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 46
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • E.H. Hettema Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins EMBO J. 23 2004 1279 1288
    • (2004) EMBO J. , vol.23 , pp. 1279-1288
    • Hettema, E.H.1
  • 47
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • R.S. Saliba The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation J. Cell Sci. 115 2002 2907 2918
    • (2002) J. Cell Sci. , vol.115 , pp. 2907-2918
    • Saliba, R.S.1
  • 48
    • 3042800569 scopus 로고    scopus 로고
    • Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: Molecular basis of the dominant-negative effect
    • S.P. Brothers Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: molecular basis of the dominant-negative effect Mol. Endocrinol. 18 2004 1787 1797
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1787-1797
    • Brothers, S.P.1
  • 49
    • 0038637206 scopus 로고    scopus 로고
    • Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: A trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans
    • A. Leanos-Miranda Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: a trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans J. Clin. Endocrinol. Metab. 88 2003 3360 3367
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 3360-3367
    • Leanos-Miranda, A.1
  • 50
    • 3042540232 scopus 로고    scopus 로고
    • Pharmacological chaperones: Potential treatment for conformational diseases
    • V. Bernier Pharmacological chaperones: potential treatment for conformational diseases Trends Endocrinol. Metab. 15 2004 222 228
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 222-228
    • Bernier, V.1
  • 51
    • 0034421921 scopus 로고    scopus 로고
    • Pharmacological chaperones: A new twist on receptor folding
    • J.P. Morello Pharmacological chaperones: a new twist on receptor folding Trends Pharmacol. Sci. 21 2000 466 469
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 466-469
    • Morello, J.P.1
  • 52
    • 0037113890 scopus 로고    scopus 로고
    • A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation
    • B.E. Kim A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation J. Biol. Chem. 277 2002 44079 44084
    • (2002) J. Biol. Chem. , vol.277 , pp. 44079-44084
    • Kim, B.E.1
  • 53
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • U.E. Petaja-Repo Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation EMBO J. 21 2002 1628 1637
    • (2002) EMBO J. , vol.21 , pp. 1628-1637
    • Petaja-Repo, U.E.1
  • 54
    • 0035830863 scopus 로고    scopus 로고
    • Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome
    • U.E. Petaja-Repo Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome J. Biol. Chem. 276 2001 4416 4423
    • (2001) J. Biol. Chem. , vol.276 , pp. 4416-4423
    • Petaja-Repo, U.E.1
  • 55
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor
    • U.E. Petaja-Repo Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor J. Biol. Chem. 275 2000 13727 13736
    • (2000) J. Biol. Chem. , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1
  • 56
    • 3042788953 scopus 로고    scopus 로고
    • Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors
    • D. Mizrachi, and D.L. Segaloff Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors Mol. Endocrinol. 18 2004 1768 1777
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1768-1777
    • Mizrachi, D.1    Segaloff, D.L.2
  • 57
    • 0012999148 scopus 로고    scopus 로고
    • Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII
    • S.J. Lavictoire Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII J. Biol. Chem. 278 2003 5292 5299
    • (2003) J. Biol. Chem. , vol.278 , pp. 5292-5299
    • Lavictoire, S.J.1
  • 58
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • G.C. Meacham The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis EMBO J. 18 1999 1492 1505
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1
  • 59
    • 0032491397 scopus 로고    scopus 로고
    • The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary
    • Z. Bebok The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary J. Biol. Chem. 273 1998 29873 29878
    • (1998) J. Biol. Chem. , vol.273 , pp. 29873-29878
    • Bebok, Z.1
  • 60
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Y. Ye The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol Nature 414 2001 652 656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1
  • 61
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • G.C. Meacham The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Nat. Cell Biol. 3 2001 100 105
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1
  • 62
    • 18444413218 scopus 로고    scopus 로고
    • E3 ubiquitin ligase that recognizes sugar chains
    • Y. Yoshida E3 ubiquitin ligase that recognizes sugar chains Nature 418 2002 438 442
    • (2002) Nature , vol.418 , pp. 438-442
    • Yoshida, Y.1
  • 63
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Y. Yoshida Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains J. Biol. Chem. 278 2003 43877 43884
    • (2003) J. Biol. Chem. , vol.278 , pp. 43877-43884
    • Yoshida, Y.1
  • 64
    • 0035203949 scopus 로고    scopus 로고
    • Correction of delF508-CFTR activity with benzo(c)quinolizinium compounds through facilitation of its processing in cystic fibrosis airway cells
    • R.L. Dormer Correction of delF508-CFTR activity with benzo(c) quinolizinium compounds through facilitation of its processing in cystic fibrosis airway cells J. Cell Sci. 114 2001 4073 4081
    • (2001) J. Cell Sci. , vol.114 , pp. 4073-4081
    • Dormer, R.L.1
  • 65
    • 0035827680 scopus 로고    scopus 로고
    • Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds
    • L.J. Galietta Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds J. Biol. Chem. 276 2001 19723 19728
    • (2001) J. Biol. Chem. , vol.276 , pp. 19723-19728
    • Galietta, L.J.1
  • 66
    • 0029099301 scopus 로고
    • P-glycoprotein. Associations between domains and between domains and molecular chaperones
    • T.W. Loo, and D.M. Clarke P-glycoprotein. Associations between domains and between domains and molecular chaperones J. Biol. Chem. 270 1995 21839 21844
    • (1995) J. Biol. Chem. , vol.270 , pp. 21839-21844
    • Loo, T.W.1    Clarke, D.M.2
  • 67
    • 1542376209 scopus 로고    scopus 로고
    • Missense mutations in transmembrane domains of proteins: Phenotypic propensity of polar residues for human disease
    • A.W. Partridge Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease Proteins 54 2004 648 656
    • (2004) Proteins , vol.54 , pp. 648-656
    • Partridge, A.W.1
  • 68
    • 0033615646 scopus 로고    scopus 로고
    • Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects
    • Z. Zhou Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects J. Biol. Chem. 274 1999 31123 31126
    • (1999) J. Biol. Chem. , vol.274 , pp. 31123-31126
    • Zhou, Z.1
  • 69
    • 0034118221 scopus 로고    scopus 로고
    • Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants
    • J.P. Morello Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants J. Clin. Invest. 105 2000 887 895
    • (2000) J. Clin. Invest. , vol.105 , pp. 887-895
    • Morello, J.P.1
  • 70
    • 0036322898 scopus 로고    scopus 로고
    • Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: Misrouted proteins as a novel disease etiology and therapeutic target
    • J.A. Janovick Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: misrouted proteins as a novel disease etiology and therapeutic target J. Clin. Endocrinol. Metab. 87 2002 3255 3262
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 3255-3262
    • Janovick, J.A.1
  • 71
    • 0344059035 scopus 로고    scopus 로고
    • Structure-activity relations of successful pharmacologic chaperones for rescue of naturally occurring and manufactured mutants of the gonadotropin-releasing hormone receptor
    • J.A. Janovick Structure-activity relations of successful pharmacologic chaperones for rescue of naturally occurring and manufactured mutants of the gonadotropin-releasing hormone receptor J. Pharmacol. Exp. Ther. 305 2003 608 614
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 608-614
    • Janovick, J.A.1
  • 72
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 Å resolution: Transverse tunnels in the channel wall
    • A. Miyazawa Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel wall J. Mol. Biol. 288 1999 765 786
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.