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Volumn 126, Issue 18, 2013, Pages 4160-4172

The cytosolic chaperone α-crystallin B rescues folding and compartmentalization of misfolded multispan transmembrane proteins

Author keywords

ATP7B; Frizzled4; sHsp

Indexed keywords

ALPHA CRYSTALLIN; COPPER; DISULFIDE; MEMBRANE PROTEIN; OLIGOMER; WILSON DISEASE PROTEIN;

EID: 84884256858     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.125443     Document Type: Article
Times cited : (32)

References (69)
  • 1
    • 43049183420 scopus 로고    scopus 로고
    • Oxidative stress and calpain inhibition induce alpha B-crystallin phosphorylation via p38-MAPK and calcium signalling pathways in H9c2 cells
    • Aggeli, I. K., Beis, I. and Gaitanaki, C. (2008). Oxidative stress and calpain inhibition induce alpha B-crystallin phosphorylation via p38-MAPK and calcium signalling pathways in H9c2 cells. Cell. Signal. 20, 1292-1302.
    • (2008) Cell. Signal. , vol.20 , pp. 1292-1302
    • Aggeli, I.K.1    Beis, I.2    Gaitanaki, C.3
  • 2
    • 37349032463 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant
    • Ahmad, M. F., Raman, B., Ramakrishna, T. and Rao, C. M. (2008). Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant. J. Mol. Biol. 375, 1040-1051.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1040-1051
    • Ahmad, M.F.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 4
    • 0027513233 scopus 로고
    • Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection
    • Aoyama, A., Fröhli, E., Schäfer, R. and Klemenz, R. (1993). Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection. Mol. Cell. Biol. 13, 1824-1835.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1824-1835
    • Aoyama, A.1    Fröhli, E.2    Schäfer, R.3    Klemenz, R.4
  • 6
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A. and Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 7
    • 47249102165 scopus 로고    scopus 로고
    • Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1
    • Banci, L., Bertini, I., Cantini, F., Rosenzweig, A. C. and Yatsunyk, L. A. (2008). Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Biochemistry 47, 7423-7429.
    • (2008) Biochemistry , vol.47 , pp. 7423-7429
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Rosenzweig, A.C.4    Yatsunyk, L.A.5
  • 8
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly
    • Beckmann, R. P., Mizzen, L. E. and Welch, W. J. (1990). Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 9
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperonelike function
    • Bova, M. P., Yaron, O., Huang, Q., Ding, L., Haley, D. A., Stewart, P. L. and Horwitz, J. (1999). Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperonelike function. Proc. Natl. Acad. Sci. USA 96, 6137-6142.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 10
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I. and Bulleid, N. J. (2011). Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71-99.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 12
    • 32044432823 scopus 로고    scopus 로고
    • ATP7B mediates vesicular sequestration of copper: insight into biliary copper excretion
    • Cater, M. A., La Fontaine, S., Shield, K., Deal, Y. and Mercer, J. F. (2006). ATP7B mediates vesicular sequestration of copper: insight into biliary copper excretion. Gastroenterology 130, 493-506.
    • (2006) Gastroenterology , vol.130 , pp. 493-506
    • Cater, M.A.1    La Fontaine, S.2    Shield, K.3    Deal, Y.4    Mercer, J.F.5
  • 13
    • 0027455337 scopus 로고
    • Tubulation of Golgi membranes in vivo and in vitro in the absence of brefeldin A
    • Cluett, E. B., Wood, S. A., Banta, M. and Brown, W. J. (1993). Tubulation of Golgi membranes in vivo and in vitro in the absence of brefeldin A. J. Cell Biol. 120, 15-24.
    • (1993) J. Cell Biol. , vol.120 , pp. 15-24
    • Cluett, E.B.1    Wood, S.A.2    Banta, M.3    Brown, W.J.4
  • 15
    • 81355161233 scopus 로고    scopus 로고
    • Ligand of Numb proteins LNX1p80 and LNX2 interact with the human glycoprotein CD8a and promote its ubiquitylation and endocytosis
    • D'Agostino, M., Tornillo, G., Caporaso, M. G., Barone, M. V., Ghigo, E., Bonatti, S. and Mottola, G. (2011). Ligand of Numb proteins LNX1p80 and LNX2 interact with the human glycoprotein CD8a and promote its ubiquitylation and endocytosis. J. Cell Sci. 124, 3545-3556.
    • (2011) J. Cell Sci. , vol.124 , pp. 3545-3556
    • D'Agostino, M.1    Tornillo, G.2    Caporaso, M.G.3    Barone, M.V.4    Ghigo, E.5    Bonatti, S.6    Mottola, G.7
  • 17
    • 36448983237 scopus 로고    scopus 로고
    • Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes
    • de Bie, P., Muller, P., Wijmenga, C. and Klomp, L. W. (2007). Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes. J. Med. Genet. 44, 673-688.
    • (2007) J. Med. Genet. , vol.44 , pp. 673-688
    • de Bie, P.1    Muller, P.2    Wijmenga, C.3    Klomp, L.W.4
  • 18
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes
    • de Silva, A., Braakman, I. and Helenius, A. (1993). Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. 120, 647-655.
    • (1993) J. Cell Biol. , vol.120 , pp. 647-655
    • de Silva, A.1    Braakman, I.2    Helenius, A.3
  • 19
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham, B. K. and Harding, J. J. (1999). Alpha-crystallin as a molecular chaperone. Prog. Retin. Eye Res. 18, 463-509.
    • (1999) Prog. Retin. Eye Res. , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 20
    • 79955541723 scopus 로고    scopus 로고
    • Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B
    • Dmitriev, O. Y., Bhattacharjee, A., Nokhrin, S., Uhlemann, E. M. and Lutsenko, S. (2011). Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B. J. Biol. Chem. 286, 16355-16362.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16355-16362
    • Dmitriev, O.Y.1    Bhattacharjee, A.2    Nokhrin, S.3    Uhlemann, E.M.4    Lutsenko, S.5
  • 21
    • 0021795178 scopus 로고
    • A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
    • Gallione, C. J. and Rose, J. K. (1985). A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J. Virol. 54, 374-382.
    • (1985) J. Virol. , vol.54 , pp. 374-382
    • Gallione, C.J.1    Rose, J.K.2
  • 22
    • 30744476478 scopus 로고    scopus 로고
    • Retinal angiogenesis in development and disease
    • Gariano, R. F. and Gardner, T. W. (2005). Retinal angiogenesis in development and disease. Nature 438, 960-966.
    • (2005) Nature , vol.438 , pp. 960-966
    • Gariano, R.F.1    Gardner, T.W.2
  • 23
    • 80052277733 scopus 로고    scopus 로고
    • Rescue of DF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway
    • Gee, H. Y., Noh, S. H., Tang, B. L., Kim, K. H. and Lee, M. G. (2011). Rescue of DF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway. Cell 146, 746-760.
    • (2011) Cell , vol.146 , pp. 746-760
    • Gee, H.Y.1    Noh, S.H.2    Tang, B.L.3    Kim, K.H.4    Lee, M.G.5
  • 24
    • 0345059398 scopus 로고    scopus 로고
    • Wilson disease
    • Gitlin, J. D. (2003). Wilson disease. Gastroenterology 125, 1868-1877.
    • (2003) Gastroenterology , vol.125 , pp. 1868-1877
    • Gitlin, J.D.1
  • 25
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 27
    • 84857219453 scopus 로고    scopus 로고
    • Protein localization in disease and therapy
    • Hung, M. C. and Link, W. (2011). Protein localization in disease and therapy. J. Cell Sci. 124, 3381-3392.
    • (2011) J. Cell Sci. , vol.124 , pp. 3381-3392
    • Hung, M.C.1    Link, W.2
  • 28
    • 0037309679 scopus 로고    scopus 로고
    • Defective cellular localization of mutant ATP7B in Wilson's disease patients and hepatoma cell lines
    • Huster, D., Hoppert, M., Lutsenko, S., Zinke, J., Lehmann, C., Mössner, J., Berr, F. and Caca, K. (2003). Defective cellular localization of mutant ATP7B in Wilson's disease patients and hepatoma cell lines. Gastroenterology 124, 335-345.
    • (2003) Gastroenterology , vol.124 , pp. 335-345
    • Huster, D.1    Hoppert, M.2    Lutsenko, S.3    Zinke, J.4    Lehmann, C.5    Mössner, J.6    Berr, F.7    Caca, K.8
  • 32
    • 84867401896 scopus 로고    scopus 로고
    • Novel roles for a-crystallins in retinal function and disease
    • Kannan, R., Sreekumar, P. G. and Hinton, D. R. (2012). Novel roles for a-crystallins in retinal function and disease. Prog. Retin. Eye Res. 31, 576-604.
    • (2012) Prog. Retin. Eye Res. , vol.31 , pp. 576-604
    • Kannan, R.1    Sreekumar, P.G.2    Hinton, D.R.3
  • 33
    • 1342332090 scopus 로고    scopus 로고
    • Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization
    • Kaykas, A., Yang-Snyder, J., Héroux, M., Shah, K. V., Bouvier, M. and Moon, R. T. (2004). Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization. Nat. Cell Biol. 6, 52-58.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 52-58
    • Kaykas, A.1    Yang-Snyder, J.2    Héroux, M.3    Shah, K.V.4    Bouvier, M.5    Moon, R.T.6
  • 35
    • 0029417002 scopus 로고
    • Dishevelled is a component of the frizzled signaling pathway in Drosophila
    • Krasnow, R. E., Wong, L. L. and Adler, P. N. (1995). Dishevelled is a component of the frizzled signaling pathway in Drosophila. Development 121, 4095-4102.
    • (1995) Development , vol.121 , pp. 4095-4102
    • Krasnow, R.E.1    Wong, L.L.2    Adler, P.N.3
  • 36
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface
    • Kreis, T. E. and Lodish, H. F. (1986). Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46, 929-937.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodish, H.F.2
  • 37
    • 34447103789 scopus 로고    scopus 로고
    • Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis
    • La Fontaine, S. and Mercer, J. F. (2007). Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. Arch. Biochem. Biophys. 463, 149-167.
    • (2007) Arch. Biochem. Biophys. , vol.463 , pp. 149-167
    • La Fontaine, S.1    Mercer, J.F.2
  • 38
    • 0030475229 scopus 로고    scopus 로고
    • Transgenic mice carrying the dominant rhodopsin mutation P347S: evidence for defective vectorial transport of rhodopsin to the outer segments
    • Li, T., Snyder, W. K., Olsson, J. E. and Dryja, T. P. (1996). Transgenic mice carrying the dominant rhodopsin mutation P347S: evidence for defective vectorial transport of rhodopsin to the outer segments. Proc. Natl. Acad. Sci. USA 93, 14176-14181.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14176-14181
    • Li, T.1    Snyder, W.K.2    Olsson, J.E.3    Dryja, T.P.4
  • 39
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis
    • Lindquist, S. L. and Kelly, J. W. (2011). Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol. 3, a004507.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 40
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S. and Klausner, R. D. (1989). Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 41
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C. and Klausner, R. D. (1990). Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 42
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • Lutsenko, S., Barnes, N. L., Bartee, M. Y. and Dmitriev, O. Y. (2007). Function and regulation of human copper-transporting ATPases. Physiol. Rev. 87, 1011-1046.
    • (2007) Physiol. Rev. , vol.87 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 44
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T. and Helenius, A. (1992). Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117, 505-513.
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 45
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer, M. P. and Bukau, B. (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 46
    • 0034604579 scopus 로고    scopus 로고
    • A new determinant of endoplasmic reticulum localization is contained in the juxtamembrane region of the ectodomain of hepatitis C virus glycoprotein E1
    • Mottola, G., Jourdan, N., Castaldo, G., Malagolini, N., Lahm, A., Serafini-Cessi, F., Migliaccio, G. and Bonatti, S. (2000). A new determinant of endoplasmic reticulum localization is contained in the juxtamembrane region of the ectodomain of hepatitis C virus glycoprotein E1. J. Biol. Chem. 275, 24070-24079.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24070-24079
    • Mottola, G.1    Jourdan, N.2    Castaldo, G.3    Malagolini, N.4    Lahm, A.5    Serafini-Cessi, F.6    Migliaccio, G.7    Bonatti, S.8
  • 47
    • 0036258862 scopus 로고    scopus 로고
    • Glucocorticoid treatment induces expression of small heat shock proteins in human satellite cell populations: consequences for a desmin-related myopathy involving the R120G alpha B-crystallin mutation
    • Nédellec, P., Edling, Y., Perret, E., Fardeau, M. and Vicart, P. (2002). Glucocorticoid treatment induces expression of small heat shock proteins in human satellite cell populations: consequences for a desmin-related myopathy involving the R120G alpha B-crystallin mutation. Neuromuscul. Disord. 12, 457-465.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 457-465
    • Nédellec, P.1    Edling, Y.2    Perret, E.3    Fardeau, M.4    Vicart, P.5
  • 48
    • 79954416821 scopus 로고    scopus 로고
    • Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases
    • Ong, D. S. and Kelly, J. W. (2011). Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases. Curr. Opin. Cell Biol. 23, 231-238.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 231-238
    • Ong, D.S.1    Kelly, J.W.2
  • 49
    • 0032167856 scopus 로고    scopus 로고
    • Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation
    • Payne, A. S., Kelly, E. J. and Gitlin, J. D. (1998). Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation. Proc. Natl. Acad. Sci. USA 95, 10854-10859.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10854-10859
    • Payne, A.S.1    Kelly, E.J.2    Gitlin, J.D.3
  • 51
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W. and Balch, W. E. (2009). Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78, 959-991.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4    Balch, W.E.5
  • 53
    • 0033862878 scopus 로고    scopus 로고
    • Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion
    • Roelofsen, H., Wolters, H., Van Luyn, M. J., Miura, N., Kuipers, F. and Vonk, R. J. (2000). Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion. Gastroenterology 119, 782-793.
    • (2000) Gastroenterology , vol.119 , pp. 782-793
    • Roelofsen, H.1    Wolters, H.2    Van Luyn, M.J.3    Miura, N.4    Kuipers, F.5    Vonk, R.J.6
  • 54
    • 79954414554 scopus 로고    scopus 로고
    • Modeling general proteostasis: proteome balance in health and disease
    • Roth, D. M. and Balch, W. E. (2011). Modeling general proteostasis: proteome balance in health and disease. Curr. Opin. Cell Biol. 23, 126-134.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 126-134
    • Roth, D.M.1    Balch, W.E.2
  • 55
    • 0018404107 scopus 로고
    • Morphological and biochemical characterization of viral particles produced by the tsO45 mutant of vesicular stomatitis virus at restrictive temperature
    • Schnitzer, T. J., Dickson, C. and Weiss, R. A. (1979). Morphological and biochemical characterization of viral particles produced by the tsO45 mutant of vesicular stomatitis virus at restrictive temperature. J. Virol. 29, 185-195.
    • (1979) J. Virol. , vol.29 , pp. 185-195
    • Schnitzer, T.J.1    Dickson, C.2    Weiss, R.A.3
  • 56
    • 48049110299 scopus 로고    scopus 로고
    • Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay
    • Söderberg, O., Leuchowius, K. J., Gullberg, M., Jarvius, M., Weibrecht, I., Larsson, L. G. and Landegren, U. (2008). Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay. Methods 45, 227-232.
    • (2008) Methods , vol.45 , pp. 227-232
    • Söderberg, O.1    Leuchowius, K.J.2    Gullberg, M.3    Jarvius, M.4    Weibrecht, I.5    Larsson, L.G.6    Landegren, U.7
  • 57
    • 0037339919 scopus 로고    scopus 로고
    • KDEL and KKXX retrieval signals appended to the same reporter protein determine different trafficking between endoplasmic reticulum, intermediate compartment, and Golgi complex
    • Stornaiuolo, M., Lotti, L. V., Borgese, N., Torrisi, M. R., Mottola, G., Martire, G. and Bonatti, S. (2003). KDEL and KKXX retrieval signals appended to the same reporter protein determine different trafficking between endoplasmic reticulum, intermediate compartment, and Golgi complex. Mol. Biol. Cell 14, 889-902.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 889-902
    • Stornaiuolo, M.1    Lotti, L.V.2    Borgese, N.3    Torrisi, M.R.4    Mottola, G.5    Martire, G.6    Bonatti, S.7
  • 64
    • 56949106691 scopus 로고    scopus 로고
    • Stably overexpressed human Frizzled-2 signals through the beta-catenin pathway and does not activate Ca2+-mobilization in Human Embryonic Kidney 293 cells
    • Verkaar, F., van Rosmalen, J. W., Smits, J. F., Blankesteijn, W. M. and Zaman, G. J. (2009). Stably overexpressed human Frizzled-2 signals through the beta-catenin pathway and does not activate Ca2+-mobilization in Human Embryonic Kidney 293 cells. Cell. Signal. 21, 22-33.
    • (2009) Cell. Signal. , vol.21 , pp. 22-33
    • Verkaar, F.1    van Rosmalen, J.W.2    Smits, J.F.3    Blankesteijn, W.M.4    Zaman, G.J.5
  • 65
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice
    • Wang, X., Osinska, H., Klevitsky, R., Gerdes, A. M., Nieman, M., Lorenz, J., Hewett, T. and Robbins, J. (2001). Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice. Circ. Res. 89, 84-91.
    • (2001) Circ. Res. , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8
  • 68
    • 77956267435 scopus 로고    scopus 로고
    • The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
    • Ye, X., Wang, Y. and Nathans, J. (2010). The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease. Trends Mol. Med. 16, 417-425.
    • (2010) Trends Mol. Med. , vol.16 , pp. 417-425
    • Ye, X.1    Wang, Y.2    Nathans, J.3
  • 69
    • 78149416783 scopus 로고    scopus 로고
    • Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways
    • Zhang, H., Rajasekaran, N. S., Orosz, A., Xiao, X., Rechsteiner, M. and Benjamin, I. J. (2010). Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways. J. Mol. Cell. Cardiol. 49, 918-930.
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 918-930
    • Zhang, H.1    Rajasekaran, N.S.2    Orosz, A.3    Xiao, X.4    Rechsteiner, M.5    Benjamin, I.J.6


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