메뉴 건너뛰기




Volumn 290, Issue 39, 2015, Pages 23631-23645

The protein-disulfide isomerase ERp57 regulates the steady-state levels of the prion protein

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; CELL MEMBRANES; MAMMALS; PROTEINS; QUALITY CONTROL; SULFUR COMPOUNDS;

EID: 84942287897     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.635565     Document Type: Article
Times cited : (49)

References (70)
  • 2
    • 79952449094 scopus 로고    scopus 로고
    • Prion hypothesis: The end of the controversy?
    • Soto, C. (2011) Prion hypothesis: the end of the controversy? Trends Biochem. Sci. 36, 151-158
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 151-158
    • Soto, C.1
  • 3
    • 33646175291 scopus 로고    scopus 로고
    • Stressing out the ER: A role of the unfolded protein response in prion-related disorders
    • Hetz, C. A., and Soto, C. (2006) Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr. Mol. Med. 6, 37-43
    • (2006) Curr. Mol. Med. , vol.6 , pp. 37-43
    • Hetz, C.A.1    Soto, C.2
  • 4
    • 84896928901 scopus 로고    scopus 로고
    • The GPI-anchoring of PrP: Implications in sorting and pathogenesis
    • Puig, B., Altmeppen, H., and Glatzel, M. (2014) The GPI-anchoring of PrP: implications in sorting and pathogenesis. Prion 8, 1-8
    • (2014) Prion , vol.8 , pp. 1-8
    • Puig, B.1    Altmeppen, H.2    Glatzel, M.3
  • 5
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia, Y., Horonchik, L., Tzaban, S., Yanai, A., and Taraboulos, A. (2001) Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20, 5383-5391
    • (2001) EMBO J. , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 6
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma, J., and Lindquist, S. (2001) Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. U.S.A. 98, 14955-14960
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 9
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz, C., Russelakis-Carneiro, M., Maundrell, K., Castilla, J., and Soto, C. (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 22, 5435-5445
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 13
    • 51449098355 scopus 로고    scopus 로고
    • Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration
    • Rane, N. S., Kang, S. W., Chakrabarti, O., Feigenbaum, L., and Hegde, R. S. (2008) Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Dev. Cell. 15, 359-370
    • (2008) Dev. Cell. , vol.15 , pp. 359-370
    • Rane, N.S.1    Kang, S.W.2    Chakrabarti, O.3    Feigenbaum, L.4    Hegde, R.S.5
  • 15
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres, M., Castillo, K., Armisén, R., Stutzin, A., Soto, C., and Hetz, C. (2010) Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS ONE 5, e15658
    • (2010) PLoS ONE , vol.5
    • Torres, M.1    Castillo, K.2    Armisén, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 16
    • 84860513477 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and prion diseases
    • Xu, K., and Zhu, X.-P. (2012) Endoplasmic reticulum stress and prion diseases. Rev. Neurosci. 23, 79-84
    • (2012) Rev. Neurosci. , vol.23 , pp. 79-84
    • Xu, K.1    Zhu, X.-P.2
  • 18
    • 84862001706 scopus 로고    scopus 로고
    • Protein-disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity
    • Wang, S. B, Shi, Q., Xu, Y., Xie, W. L., Zhang, J., Tian, C., Guo, Y., Wang, K., Zhang, B. Y., Chen, C., Gao, C., and Dong, X. P. (2012) Protein-disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity. PLoS ONE 7, e38221
    • (2012) PLoS ONE , vol.7
    • Wang, S.B.1    Shi, Q.2    Xu, Y.3    Xie, W.L.4    Zhang, J.5    Tian, C.6    Guo, Y.7    Wang, K.8    Zhang, B.Y.9    Chen, C.10    Gao, C.11    Dong, X.P.12
  • 19
    • 79551507564 scopus 로고    scopus 로고
    • Familial CJD associated PrP mutants within transmembrane region induced CTM-PrP retention in ER and triggered apoptosis by ER stress in SH-SY5Y cells
    • Wang, X., Shi, Q., Xu, K., Gao, C., Chen, C., Li, X. L., Wang, G. R., Tian, C., Han, J., and Dong, X. P. (2011) Familial CJD associated PrP mutants within transmembrane region induced CTM-PrP retention in ER and triggered apoptosis by ER stress in SH-SY5Y cells. PLoS ONE 6, e14602
    • (2011) PLoS ONE , vol.6
    • Wang, X.1    Shi, Q.2    Xu, K.3    Gao, C.4    Chen, C.5    Li, X.L.6    Wang, G.R.7    Tian, C.8    Han, J.9    Dong, X.P.10
  • 20
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz, C. (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 21
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P., and Ron, D. (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 22
    • 84934275896 scopus 로고    scopus 로고
    • Proteostasis control by the unfolded protein response
    • Hetz, C., Chevet, E., and Oakes, S. A. (2015) Proteostasis control by the unfolded protein response. Nat. Cell Biol. 17, 1-10
    • (2015) Nat. Cell Biol. , vol.17 , pp. 1-10
    • Hetz, C.1    Chevet, E.2    Oakes, S.A.3
  • 23
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang, S. W., Rane, N. S., Kim, S. J., Garrison, J. L., Taunton, J., and Hegde, R. S. (2006) Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 24
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • Orsi, A., Fioriti, L., Chiesa, R., and Sitia, R. (2006) Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J. Biol. Chem. 281, 30431-30438
    • (2006) J. Biol. Chem. , vol.281 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 25
    • 80053212141 scopus 로고    scopus 로고
    • Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein
    • Nunziante, M., Ackermann, K., Dietrich, K., Wolf, H., Gädtke, L., Gilch, S., Vorberg, I., Groschup, M., and Schätzl, H. M. (2011) Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein. J. Biol. Chem. 286, 33942-33953
    • (2011) J. Biol. Chem. , vol.286 , pp. 33942-33953
    • Nunziante, M.1    Ackermann, K.2    Dietrich, K.3    Wolf, H.4    Gädtke, L.5    Gilch, S.6    Vorberg, I.7    Groschup, M.8    Schätzl, H.M.9
  • 26
    • 34250351315 scopus 로고    scopus 로고
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication
    • Hetz, C., Castilla, J., and Soto, C. (2007) Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J. Biol. Chem. 282, 12725-12733
    • (2007) J. Biol. Chem. , vol.282 , pp. 12725-12733
    • Hetz, C.1    Castilla, J.2    Soto, C.3
  • 27
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C., and Mollereau, B. (2014) Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15, 233-249
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 28
    • 0037121618 scopus 로고    scopus 로고
    • Overexpressed protein-disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease
    • Yoo, B. C., Krapfenbauer, K., Cairns, N., Belay, G., Bajo, M., and Lubec, G. (2002) Overexpressed protein-disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease. Neurosci. Lett. 334, 196-200
    • (2002) Neurosci. Lett. , vol.334 , pp. 196-200
    • Yoo, B.C.1    Krapfenbauer, K.2    Cairns, N.3    Belay, G.4    Bajo, M.5    Lubec, G.6
  • 29
    • 79954417748 scopus 로고    scopus 로고
    • Disulfide bonds in ER protein folding and homeostasis
    • Feige, M. J., and Hendershot, L. M. (2011) Disulfide bonds in ER protein folding and homeostasis. Curr. Opin. Cell Biol. 23, 167-175
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 167-175
    • Feige, M.J.1    Hendershot, L.M.2
  • 30
    • 84864956245 scopus 로고    scopus 로고
    • Protein-disulfide isomerases in neurodegeneration: From disease mechanisms to biomedical applications
    • Andreu, C. I., Woehlbier, U., Torres, M., and Hetz, C. (2012) Protein-disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications. FEBS Lett. 586, 2826-2834
    • (2012) FEBS Lett. , vol.586 , pp. 2826-2834
    • Andreu, C.I.1    Woehlbier, U.2    Torres, M.3    Hetz, C.4
  • 31
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop, C. E., Tavender, T. J., Watkins, R. H., Chambers, J. E., and Bulleid, N. J. (2009) Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J. Biol. Chem. 284, 2194-2202
    • (2009) J. Biol. Chem. , vol.284 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 32
    • 77953809347 scopus 로고    scopus 로고
    • ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe, H., and Michalak, M. (2010) ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase. Int. J. Biochem. Cell Biol. 42, 796-799
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 33
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptideloading complex in mice deficient in the oxidoreductase ERp57
    • Garbi, N., Tanaka, S., Momburg, F., and Hämmerling, G. J. (2006) Impaired assembly of the major histocompatibility complex class I peptideloading complex in mice deficient in the oxidoreductase ERp57. Nat. Immunol. 7, 93-102
    • (2006) Nat. Immunol. , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hämmerling, G.J.4
  • 34
    • 77949879489 scopus 로고    scopus 로고
    • ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum
    • Coe, H., Jung, J., Groenendyk, J., Prins, D., and Michalak, M. (2010) ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J. Biol. Chem. 285, 6725-6738
    • (2010) J. Biol. Chem. , vol.285 , pp. 6725-6738
    • Coe, H.1    Jung, J.2    Groenendyk, J.3    Prins, D.4    Michalak, M.5
  • 35
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop, C. E., Chakravarthi, S., Garbi, N., Hämmerling, G. J., Lovell, S., and Bulleid, N. J. (2007) ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 26, 28-40
    • (2007) EMBO J. , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hämmerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 36
    • 33646594461 scopus 로고    scopus 로고
    • Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
    • Soldà, T., Garbi, N., Hämmerling, G. J., and Molinari, M. (2006) Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J. Biol. Chem. 281, 6219-6226
    • (2006) J. Biol. Chem. , vol.281 , pp. 6219-6226
    • Soldà, T.1    Garbi, N.2    Hämmerling, G.J.3    Molinari, M.4
  • 37
    • 33846044754 scopus 로고    scopus 로고
    • Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes
    • Garbi, N., Hämmerling, G., and Tanaka, S. (2007) Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. Curr. Opin. Immunol. 19, 99-105
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 99-105
    • Garbi, N.1    Hämmerling, G.2    Tanaka, S.3
  • 38
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch, P. A., and Cresswell, P. (2007) Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat. Immunol. 8, 873-881
    • (2007) Nat. Immunol. , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 39
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper, D. R., and Cresswell, P. (2008) The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc. Natl. Acad. Sci. U.S.A. 105, 10477-10482
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 41
    • 0347753252 scopus 로고    scopus 로고
    • 2+ -dependent redox modulation of SERCA 2b by ERp57
    • 2+ -dependent redox modulation of SERCA 2b by ERp57. J. Cell Biol. 164, 35-46
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 45
    • 0037446508 scopus 로고    scopus 로고
    • In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups
    • Lucassen, R., Nishina, K., and Supattapone, S. (2003) In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry 42, 4127-4135
    • (2003) Biochemistry , vol.42 , pp. 4127-4135
    • Lucassen, R.1    Nishina, K.2    Supattapone, S.3
  • 46
    • 0036215455 scopus 로고    scopus 로고
    • The role of dimerization in prion replication
    • Tompa, P., Tusnády, G. E., Friedrich, P., and Simon, I. (2002) The role of dimerization in prion replication. Biophys. J. 82, 1711-1718
    • (2002) Biophys. J. , vol.82 , pp. 1711-1718
    • Tompa, P.1    Tusnády, G.E.2    Friedrich, P.3    Simon, I.4
  • 48
    • 0032885260 scopus 로고    scopus 로고
    • Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop
    • Yanai, A., Meiner, Z., Gahali, I., Gabizon, R., and Taraboulos, A. (1999) Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop. FEBS Lett. 460, 11-16
    • (1999) FEBS Lett. , vol.460 , pp. 11-16
    • Yanai, A.1    Meiner, Z.2    Gahali, I.3    Gabizon, R.4    Taraboulos, A.5
  • 49
    • 84860428854 scopus 로고    scopus 로고
    • Altered prion protein expression pattern in CSF as a biomarker for Creutzfeldt-Jakob Disease
    • Torres, M., Cartier, L., Matamala, J., Hernandez, N., Woehvier, U., and Hetz, C. (2012) Altered prion protein expression pattern in CSF as a biomarker for Creutzfeldt-Jakob Disease. PLoS One 7, e36159
    • (2012) PLoS One , vol.7
    • Torres, M.1    Cartier, L.2    Matamala, J.3    Hernandez, N.4    Woehvier, U.5    Hetz, C.6
  • 50
    • 0035834680 scopus 로고    scopus 로고
    • Mutant prion proteins are partially retained in the endoplasmic reticulum
    • Ivanova, L., Barmada, S., Kummer, T., and Harris, D. A. (2001) Mutant prion proteins are partially retained in the endoplasmic reticulum. J. Biol. Chem. 276, 42409-42421
    • (2001) J. Biol. Chem. , vol.276 , pp. 42409-42421
    • Ivanova, L.1    Barmada, S.2    Kummer, T.3    Harris, D.A.4
  • 52
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop, C. E., Watkins, R. H., Simmons, J. J., Tasab, M., and Bulleid, N. J. (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J. Cell Sci. 122, 4287-4295
    • (2009) J. Cell Sci. , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 61
    • 16344384722 scopus 로고    scopus 로고
    • Neurode-generative illness in transgenic mice expressing a transmembrane form of the prion protein
    • Stewart, R. S., Piccardo, P., Ghetti, B., and Harris, D. A. (2005) Neurode-generative illness in transgenic mice expressing a transmembrane form of the prion protein. J. Neurosci. 25, 3469-3477
    • (2005) J. Neurosci. , vol.25 , pp. 3469-3477
    • Stewart, R.S.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 62
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa, R., Piccardo, P., Ghetti, B., and Harris, D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 64
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi, B., Stewart, R. S., Adles, C., Stewart, L. R., Quaglio, E., Biasini, E., Fioriti, L., Chiesa, R., and Harris, D. A. (2003) Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J. Biol. Chem. 278, 21732-21743
    • (2003) J. Biol. Chem. , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 65
    • 0035158658 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum
    • Stewart, R. S., Drisaldi, B., and Harris, D. A. (2001) A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum. Mol. Biol. Cell 12, 881-889
    • (2001) Mol. Biol. Cell , vol.12 , pp. 881-889
    • Stewart, R.S.1    Drisaldi, B.2    Harris, D.A.3
  • 66
    • 54249087710 scopus 로고    scopus 로고
    • Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation
    • Ashok, A., and Hegde, R. S. (2008) Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation. Mol. Biol. Cell 19, 3463-3476
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3463-3476
    • Ashok, A.1    Hegde, R.S.2
  • 67
    • 84905398989 scopus 로고    scopus 로고
    • ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway
    • Satpute-Krishnan, P., Ajinkya, M., Bhat, S., Itakura, E., Hegde, R. S., and Lippincott-Schwartz, J. (2014) ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway. Cell 158, 522-533
    • (2014) Cell , vol.158 , pp. 522-533
    • Satpute-Krishnan, P.1    Ajinkya, M.2    Bhat, S.3    Itakura, E.4    Hegde, R.S.5    Lippincott-Schwartz, J.6
  • 68
    • 14844300843 scopus 로고    scopus 로고
    • Axonal transport of the cellular prion protein is increased during axon regeneration
    • Moya, K. L., Hässig, R., Breen, K. C., Volland, H., and Di Giamberardino, L. (2005) Axonal transport of the cellular prion protein is increased during axon regeneration. J. Neurochem. 92, 1044-1053
    • (2005) J. Neurochem. , vol.92 , pp. 1044-1053
    • Moya, K.L.1    Hässig, R.2    Breen, K.C.3    Volland, H.4    Di Giamberardino, L.5
  • 70
    • 33745315287 scopus 로고    scopus 로고
    • S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z.-Q., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., and Lipton, S. A. (2006) S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441, 513-517
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.-Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.