메뉴 건너뛰기




Volumn 6, Issue , 2014, Pages

Protein quality control in the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; PROTEIN;

EID: 84904971870     PISSN: None     EISSN: 20517599     Source Type: Journal    
DOI: 10.12703/P6-49     Document Type: Review
Times cited : (18)

References (120)
  • 1
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith MH, Ploegh HL, Weissman JS: Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 2011, 334:1086-90.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 4
    • 84890204277 scopus 로고    scopus 로고
    • Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system
    • Amm I, Sommer T, Wolf DH: Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta 2014, 1843:182-96.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 6
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • DOI 10.1038/35008096
    • Schubert U, Antón LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR: Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000, 404:770-4. (Pubitemid 30212405)
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 8
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • Salvador N, Aguado C, Horst M, Knecht E: Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 2000, 275:27447-56.
    • (2000) J Biol Chem , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 10
    • 0023749075 scopus 로고
    • Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins
    • Lippincott-Schwartz J, Bonifacino JS, Yuan LC, Klausner RD: Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell 1988, 54:209-20.
    • (1988) Cell , vol.54 , pp. 209-220
    • Lippincott-Schwartz, J.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 11
    • 84866623060 scopus 로고    scopus 로고
    • Flagging and docking: Dual roles for N-glycans in protein quality control and cellular proteostasis
    • Hebert DN, Molinari M: Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis. Trends Biochem Sci 2012, 37:404-10.
    • (2012) Trends Biochem Sci , vol.37 , pp. 404-410
    • Hebert, D.N.1    Molinari, M.2
  • 12
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D: The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334:1081-6.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 14
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • DOI 10.1016/S1074-7613(03)00024-4
    • van Anken E, Romijn EP, Maggioni C, Mezghrani A, Sitia R, Braakman I, Heck Albert J R: Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 2003, 18:243-53. (Pubitemid 36262999)
    • (2003) Immunity , vol.18 , Issue.2 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.R.7
  • 15
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop M, Finger A, Braun T, Hellmuth K, Wolf DH: Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 1996, 15:753-63. (Pubitemid 26064282)
    • (1996) EMBO Journal , vol.15 , Issue.4 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 16
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • DOI 10.1038/365176a0
    • Sommer T, Jentsch S: A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 1993, 365:176-9. (Pubitemid 23282065)
    • (1993) Nature , vol.365 , Issue.6442 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 17
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton RY, Rine J: Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J Cell Biol 1994, 125:299-312. (Pubitemid 24135944)
    • (1994) Journal of Cell Biology , vol.125 , Issue.2 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 18
    • 84859365389 scopus 로고    scopus 로고
    • The ERMES complex and ER-mitochondria connections
    • Michel AH, Kornmann B: The ERMES complex and ER-mitochondria connections. Biochem Soc Trans 2012, 40:445-50.
    • (2012) Biochem Soc Trans , vol.40 , pp. 445-450
    • Michel, A.H.1    Kornmann, B.2
  • 21
    • 84891165725 scopus 로고    scopus 로고
    • Autoadaptive ER-associated degradation defines a preemptive unfolded protein response pathway
    • Bernasconi R, Galli C, Kokame K, Molinari M: Autoadaptive ER-associated degradation defines a preemptive unfolded protein response pathway. Mol Cell 2013, 52:783-93.
    • (2013) Mol Cell , vol.52 , pp. 783-793
    • Bernasconi, R.1    Galli, C.2    Kokame, K.3    Molinari, M.4
  • 22
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • DOI 10.1038/384432a0
    • Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL: Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996, 384:432-8. (Pubitemid 26414653)
    • (1996) Nature , vol.384 , Issue.6608 , pp. 432-438
    • Wiertz, E.J.H.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
  • 23
    • 80455164551 scopus 로고    scopus 로고
    • Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum
    • Greenblatt EJ, Olzmann JA, Kopito RR: Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum. Nat Struct Mol Biol 2011, 18:1147-52.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1147-1152
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 24
    • 84867198276 scopus 로고    scopus 로고
    • Making the cut: Intramembrane cleavage by a rhomboid protease promotes ERAD
    • Greenblatt EJ, Olzmann JA, Kopito RR: Making the cut: intramembrane cleavage by a rhomboid protease promotes ERAD. Nat Struct Mol Biol 2012, 19:979-81.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 979-981
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 25
  • 26
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • Ploegh HL: A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 2007, 448:435-8.
    • (2007) Nature , vol.448 , pp. 435-438
    • Ploegh, H.L.1
  • 27
    • 84872840929 scopus 로고    scopus 로고
    • Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover
    • Olzmann JA, Richter CM, Kopito RR: Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc Natl Acad Sci USA 2013, 110:1345-50.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 1345-1350
    • Olzmann, J.A.1    Richter, C.M.2    Kopito, R.R.3
  • 28
    • 84873355211 scopus 로고    scopus 로고
    • Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methyl-glutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes
    • Jo Y, Hartman IZ, DeBose-Boyd RA: Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methyl-glutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes. Mol Biol Cell 2013, 24:169-83.
    • (2013) Mol Biol Cell , vol.24 , pp. 169-183
    • Jo, Y.1    Hartman, I.Z.2    DeBose-Boyd, R.A.3
  • 29
    • 80054801259 scopus 로고    scopus 로고
    • Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control
    • Klemm EJ, Spooner E, Ploegh HL: Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control. J Biol Chem 2011, 286:37602-14.
    • (2011) J Biol Chem , vol.286 , pp. 37602-37614
    • Klemm, E.J.1    Spooner, E.2    Ploegh, H.L.3
  • 31
    • 78650060743 scopus 로고    scopus 로고
    • BiP, an endoplasmic reticulum chaperone, modulates the development of morphine antinociceptive tolerance
    • Dobashi T, Tanabe S, Jin H, Mimura N, Yamamoto T, Nishino T, Aoe T: BiP, an endoplasmic reticulum chaperone, modulates the development of morphine antinociceptive tolerance. J Cell Mol Med 2010, 14:2816-26.
    • (2010) J Cell Mol Med , vol.14 , pp. 2816-2826
    • Dobashi, T.1    Tanabe, S.2    Jin, H.3    Mimura, N.4    Yamamoto, T.5    Nishino, T.6    Aoe, T.7
  • 32
    • 37549033821 scopus 로고    scopus 로고
    • Dysfunction of the ER chaperone BiP accelerates the renal tubular injury
    • Kimura K, Jin H, Ogawa M, Aoe T: Dysfunction of the ER chaperone BiP accelerates the renal tubular injury. Biochem Biophys Res Commun 2008, 366:1048-53.
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 1048-1053
    • Kimura, K.1    Jin, H.2    Ogawa, M.3    Aoe, T.4
  • 33
    • 37549015265 scopus 로고    scopus 로고
    • Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP
    • Mimura N, Yuasa S, Soma M, Jin H, Kimura K, Goto S, Koseki H, Aoe T: Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP. Mol Cell Biol 2008, 28:293-301.
    • (2008) Mol Cell Biol , vol.28 , pp. 293-301
    • Mimura, N.1    Yuasa, S.2    Soma, M.3    Jin, H.4    Kimura, K.5    Goto, S.6    Koseki, H.7    Aoe, T.8
  • 35
    • 84871457375 scopus 로고    scopus 로고
    • Mutation of the BiP/GRP78 gene causes axon outgrowth and fasciculation defects in the thalamocortical connections of the mammalian forebrain
    • Favero CB, Henshaw RN, Grimsley-Myers CM, Shrestha A, Beier DR, Dwyer ND: Mutation of the BiP/GRP78 gene causes axon outgrowth and fasciculation defects in the thalamocortical connections of the mammalian forebrain. J Comp Neurol 2013, 521:677-96.
    • (2013) J Comp Neurol , vol.521 , pp. 677-696
    • Favero, C.B.1    Henshaw, R.N.2    Grimsley-Myers, C.M.3    Shrestha, A.4    Beier, D.R.5    Dwyer, N.D.6
  • 36
    • 33746500168 scopus 로고    scopus 로고
    • GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
    • DOI 10.1128/MCB.00779-06
    • Luo S, Mao C, Lee B, Lee AS: GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 2006, 26:5688-97. (Pubitemid 44134326)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5688-5697
    • Luo, S.1    Mao, C.2    Lee, B.3    Lee, A.S.4
  • 38
    • 58049209726 scopus 로고    scopus 로고
    • Pten null prostate tumorigenesis and AKT activation are blocked by targeted knockout of ER chaperone GRP78/BiP in prostate epithelium
    • Fu Y, Wey S, Wang M, Ye R, Liao C, Roy-Burman P, Lee AS: Pten null prostate tumorigenesis and AKT activation are blocked by targeted knockout of ER chaperone GRP78/BiP in prostate epithelium. Proc Natl Acad Sci USA 2008, 105:19444-9.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19444-19449
    • Fu, Y.1    Wey, S.2    Wang, M.3    Ye, R.4    Liao, C.5    Roy-Burman, P.6    Lee, A.S.7
  • 39
    • 77449096697 scopus 로고    scopus 로고
    • Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance
    • Ye R, Jung DY, Jun JY, Li J, Luo S, Ko HJ, Kim JK, Lee AS: Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance. Diabetes 2010, 59:6-16.
    • (2010) Diabetes , vol.59 , pp. 6-16
    • Ye, R.1    Jung, D.Y.2    Jun, J.Y.3    Li, J.4    Luo, S.5    Ko, H.J.6    Kim, J.K.7    Lee, A.S.8
  • 41
    • 78650209729 scopus 로고    scopus 로고
    • Grp78 heterozygosity regulates chaperone balance in exocrine pancreas with differential response to cerulein-induced acute pancreatitis
    • Ye R, Mareninova OA, Barron E, Wang M, Hinton DR, Pandol SJ, Lee AS: Grp78 heterozygosity regulates chaperone balance in exocrine pancreas with differential response to cerulein-induced acute pancreatitis. Am J Pathol 2010, 177:2827-36.
    • (2010) Am J Pathol , vol.177 , pp. 2827-2836
    • Ye, R.1    Mareninova, O.A.2    Barron, E.3    Wang, M.4    Hinton, D.R.5    Pandol, S.J.6    Lee, A.S.7
  • 42
    • 84862908844 scopus 로고    scopus 로고
    • Inducible knockout of GRP78/BiP in the hematopoietic system suppresses Pten-null leukemogenesis and AKT oncogenic signaling
    • Wey S, Luo B, Tseng C, Ni M, Zhou H, Fu Y, Bhojwani D, Carroll WL, Lee AS: Inducible knockout of GRP78/BiP in the hematopoietic system suppresses Pten-null leukemogenesis and AKT oncogenic signaling. Blood 2012, 119:817-25.
    • (2012) Blood , vol.119 , pp. 817-825
    • Wey, S.1    Luo, B.2    Tseng, C.3    Ni, M.4    Zhou, H.5    Fu, Y.6    Bhojwani, D.7    Carroll, W.L.8    Lee, A.S.9
  • 45
    • 79959544189 scopus 로고    scopus 로고
    • Liver-specific loss of glucose-regulated protein 78 perturbs the unfolded protein response and exacerbates a spectrum of liver diseases in mice
    • Ji C, Kaplowitz N, Lau MY, Kao E, Petrovic LM, Lee AS: Liver-specific loss of glucose-regulated protein 78 perturbs the unfolded protein response and exacerbates a spectrum of liver diseases in mice. Hepatology 2011, 54:229-39.
    • (2011) Hepatology , vol.54 , pp. 229-239
    • Ji, C.1    Kaplowitz, N.2    Lau, M.Y.3    Kao, E.4    Petrovic, L.M.5    Lee, A.S.6
  • 46
    • 84862488769 scopus 로고    scopus 로고
    • Acute inducible ablation of GRP78 reveals its role in hematopoietic stem cell survival, lymphogenesis and regulation of stress signaling
    • Wey S, Luo B, Lee AS: Acute inducible ablation of GRP78 reveals its role in hematopoietic stem cell survival, lymphogenesis and regulation of stress signaling. PLoS ONE 2012, 7:e39047.
    • (2012) PLoS ONE , vol.7
    • Wey, S.1    Luo, B.2    Lee, A.S.3
  • 47
    • 33847260278 scopus 로고    scopus 로고
    • Heat Shock Protein gp96 Is a Master Chaperone for Toll-like Receptors and Is Important in the Innate Function of Macrophages
    • DOI 10.1016/j.immuni.2006.12.005, PII S1074761307001161
    • Yang Y, Liu B, Dai J, Srivastava PK, Zammit DJ, Lefrançois L, Li Z: Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Immunity 2007, 26:215-26. (Pubitemid 46329432)
    • (2007) Immunity , vol.26 , Issue.2 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrancois, L.6    Li, Z.7
  • 48
    • 51649117657 scopus 로고    scopus 로고
    • Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin
    • Liu B, Li Z: Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Blood 2008, 112:1223-30.
    • (2008) Blood , vol.112 , pp. 1223-1230
    • Liu, B.1    Li, Z.2
  • 49
    • 77950601859 scopus 로고    scopus 로고
    • gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis
    • Staron M, Yang Y, Liu B, Li J, Shen Y, Zúñiga-Pflücker JC, Aguila HL, Goldschneider I, Li Z: gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis. Blood 2010, 115:2380-90.
    • (2010) Blood , vol.115 , pp. 2380-2390
    • Staron, M.1    Yang, Y.2    Liu, B.3    Li, J.4    Shen, Y.5    Zúñiga-Pflücker, J.C.6    Aguila, H.L.7    Goldschneider, I.8    Li, Z.9
  • 50
    • 79959825676 scopus 로고    scopus 로고
    • Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex
    • Staron M, Wu S, Hong F, Stojanovic A, Du X, Bona R, Liu B, Li Z: Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex. Blood 2011, 117:7136-44.
    • (2011) Blood , vol.117 , pp. 7136-7144
    • Staron, M.1    Wu, S.2    Hong, F.3    Stojanovic, A.4    Du, X.5    Bona, R.6    Liu, B.7    Li, Z.8
  • 51
    • 79951894303 scopus 로고    scopus 로고
    • Oocyte-targeted deletion reveals that hsp90b1 is needed for the completion of first mitosis in mouse zygotes
    • Audouard C, Le Masson F, Charry C, Li Z, Christians ES: Oocyte-targeted deletion reveals that hsp90b1 is needed for the completion of first mitosis in mouse zygotes. PLoS ONE 2011, 6:e17109.
    • (2011) PLoS ONE , vol.6
    • Audouard, C.1    Le Masson, F.2    Charry, C.3    Li, Z.4    Christians, E.S.5
  • 52
    • 79952444652 scopus 로고    scopus 로고
    • Hsp90b1 knockout targeted to male germline: A mouse model for globozoospermia
    • Audouard C, Christians E: Hsp90b1 knockout targeted to male germline: a mouse model for globozoospermia. Fertil Steril 2011, 95:1475-7.e1-4.
    • (2011) Fertil Steril , vol.95
    • Audouard, C.1    Christians, E.2
  • 54
    • 84862505087 scopus 로고    scopus 로고
    • Murine but not human basophil undergoes cell-specific proteolysis of a major endoplasmic reticulum chaperone
    • Liu B, Staron M, Li Z: Murine but not human basophil undergoes cell-specific proteolysis of a major endoplasmic reticulum chaperone. PLoS ONE 2012, 7:e39442.
    • (2012) PLoS ONE , vol.7
    • Liu, B.1    Staron, M.2    Li, Z.3
  • 59
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion
    • DOI 10.1091/mbc.E07-03-0275
    • Wanderling S, Simen BB, Ostrovsky O, Ahmed NT, Vogen SM, Gidalevitz T, Argon Y: GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion. Mol Biol Cell 2007, 18:3764-75. (Pubitemid 47519471)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.10 , pp. 3764-3775
    • Wanderling, S.1    Simen, B.B.2    Ostrovsky, O.3    Ahmed, N.T.4    Vogen, S.M.5    Gidalevitz, T.6    Argon, Y.7
  • 60
    • 65249092612 scopus 로고    scopus 로고
    • The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation
    • Ostrovsky O, Ahmed NT, Argon Y: The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation. Mol Biol Cell 2009, 20:1855-64.
    • (2009) Mol Biol Cell , vol.20 , pp. 1855-1864
    • Ostrovsky, O.1    Ahmed, N.T.2    Argon, Y.3
  • 61
    • 77956296890 scopus 로고    scopus 로고
    • Targeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signaling
    • Mao C, Wang M, Luo B, Wey S, Dong D, Wesselschmidt R, Rawlings S, Lee AS: Targeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signaling. PLoS ONE 2010, 5:e10852.
    • (2010) PLoS ONE , vol.5
    • Mao, C.1    Wang, M.2    Luo, B.3    Wey, S.4    Dong, D.5    Wesselschmidt, R.6    Rawlings, S.7    Lee, A.S.8
  • 62
    • 79956352798 scopus 로고    scopus 로고
    • The endoplasmic reticulum chaperone protein GRP94 is required for maintaining hematopoietic stem cell interactions with the adult bone marrow niche
    • Luo B, Lam BS, Lee SH, Wey S, Zhou H, Wang M, Chen S, Adams GB, Lee AS: The endoplasmic reticulum chaperone protein GRP94 is required for maintaining hematopoietic stem cell interactions with the adult bone marrow niche. PLoS ONE 2011, 6:e20364.
    • (2011) PLoS ONE , vol.6
    • Luo, B.1    Lam, B.S.2    Lee, S.H.3    Wey, S.4    Zhou, H.5    Wang, M.6    Chen, S.7    Adams, G.B.8    Lee, A.S.9
  • 63
    • 84896699712 scopus 로고    scopus 로고
    • Liver-specific knockout of GRP94 in mice disrupts cell adhesion, activates liver progenitor cells, and accelerates liver tumorigenesis
    • Chen W, Tseng C, Pfaffenbach K, Kanel G, Luo B, Stiles BL, Lee AS: Liver-specific knockout of GRP94 in mice disrupts cell adhesion, activates liver progenitor cells, and accelerates liver tumorigenesis. Hepatology 2014, 59:947-57.
    • (2014) Hepatology , vol.59 , pp. 947-957
    • Chen, W.1    Tseng, C.2    Pfaffenbach, K.3    Kanel, G.4    Luo, B.5    Stiles, B.L.6    Lee, A.S.7
  • 64
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • DOI 10.1038/ni1288, PII N1288
    • Garbi N, Tanaka S, Momburg F, Hämmerling GJ: Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 2006, 7:93-102. (Pubitemid 41823873)
    • (2006) Nature Immunology , vol.7 , Issue.1 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 65
    • 77949879489 scopus 로고    scopus 로고
    • ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum
    • Coe H, Jung J, Groenendyk J, Prins D, Michalak M: ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J Biol Chem 2010, 285:6725-38.
    • (2010) J Biol Chem , vol.285 , pp. 6725-6738
    • Coe, H.1    Jung, J.2    Groenendyk, J.3    Prins, D.4    Michalak, M.5
  • 66
    • 80255123366 scopus 로고    scopus 로고
    • Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57
    • Prins D, Groenendyk J, Touret N, Michalak M: Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57. EMBO Rep 2011, 12:1182-8.
    • (2011) EMBO Rep , vol.12 , pp. 1182-1188
    • Prins, D.1    Groenendyk, J.2    Touret, N.3    Michalak, M.4
  • 67
    • 84888229791 scopus 로고    scopus 로고
    • Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbß3 integrin
    • Wang L, Wu Y, Zhou J, Ahmad SS, Mutus B, Garbi N, Hämmerling G, Liu J, Essex DW: Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbß3 integrin. Blood 2013, 122:3642-50.
    • (2013) Blood , vol.122 , pp. 3642-3650
    • Wang, L.1    Wu, Y.2    Zhou, J.3    Ahmad, S.S.4    Mutus, B.5    Garbi, N.6    Hämmerling, G.7    Liu, J.8    Essex, D.W.9
  • 68
    • 77957785488 scopus 로고    scopus 로고
    • Intestinal cell calcium uptake and the targeted knockout of the 1,25D3-MARRS (membrane-associated, rapid response steroid-binding) receptor/PDIA3/Erp57
    • Nemere I, Garbi N, Hämmerling GJ, Khanal RC: Intestinal cell calcium uptake and the targeted knockout of the 1,25D3-MARRS (membrane-associated, rapid response steroid-binding) receptor/PDIA3/Erp57. J Biol Chem 2010, 285:31859-66.
    • (2010) J Biol Chem , vol.285 , pp. 31859-31866
    • Nemere, I.1    Garbi, N.2    Hämmerling, G.J.3    Khanal, R.C.4
  • 69
    • 72449129195 scopus 로고    scopus 로고
    • Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland
    • Hosoda A, Tokuda M, Akai R, Kohno K, Iwawaki T: Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland. Biochem J 2010, 425:117-25.
    • (2010) Biochem J , vol.425 , pp. 117-125
    • Hosoda, A.1    Tokuda, M.2    Akai, R.3    Kohno, K.4    Iwawaki, T.5
  • 70
    • 84894270152 scopus 로고    scopus 로고
    • Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic reticulum stress and metabolic defects
    • Fritz JM, Dong M, Apsley KS, Martin EP, Na C, Sitaraman S, Weaver TE: Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic reticulum stress and metabolic defects. Mol Biol Cell 2014, 25:431-40.
    • (2014) Mol Biol Cell , vol.25 , pp. 431-440
    • Fritz, J.M.1    Dong, M.2    Apsley, K.S.3    Martin, E.P.4    Na, C.5    Sitaraman, S.6    Weaver, T.E.7
  • 72
    • 77649283223 scopus 로고    scopus 로고
    • SEL1L deficiency impairs growth and differentiation of pancreatic epithelial cells
    • Li S, Francisco AB, Munroe RJ, Schimenti JC, Long Q: SEL1L deficiency impairs growth and differentiation of pancreatic epithelial cells. BMC Dev Biol 2010, 10:19.
    • (2010) BMC Dev Biol , vol.10 , pp. 19
    • Li, S.1    Francisco, A.B.2    Munroe, R.J.3    Schimenti, J.C.4    Long, Q.5
  • 73
  • 75
    • 84859031557 scopus 로고    scopus 로고
    • Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice
    • Eura Y, Yanamoto H, Arai Y, Okuda T, Miyata T, Kokame K: Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice. PLoS ONE 2012, 7:e34298.
    • (2012) PLoS ONE , vol.7
    • Eura, Y.1    Yanamoto, H.2    Arai, Y.3    Okuda, T.4    Miyata, T.5    Kokame, K.6
  • 83
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • Liu T, Tang J, Li P, Shen Y, Li J, Miao H, Li B, Song B: Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis. Cell Metab 2012, 16:213-25.
    • (2012) Cell Metab , vol.16 , pp. 213-225
    • Liu, T.1    Tang, J.2    Li, P.3    Shen, Y.4    Li, J.5    Miao, H.6    Li, B.7    Song, B.8
  • 88
    • 19344370546 scopus 로고    scopus 로고
    • CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice
    • DOI 10.1152/ajpheart.01122.2004
    • Zhang C, Xu Z, He X, Michael LH, Patterson C: CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice. Am J Physiol Heart Circ Physiol 2005, 288:H2836-42. (Pubitemid 40720665)
    • (2005) American Journal of Physiology - Heart and Circulatory Physiology , vol.288 , Issue.6
    • Zhang, C.1    Xu, Z.2    He, X.-R.3    Michael, L.H.4    Patterson, C.5
  • 89
    • 84860999545 scopus 로고    scopus 로고
    • Haploinsufficiency of the E3 ubiquitin ligase C-terminus of heat shock cognate 70 interacting protein (CHIP) produces specific behavioral impairments
    • McLaughlin B, Buendia MA, Saborido TP, Palubinsky AM, Stankowski JN, Stanwood GD: Haploinsufficiency of the E3 ubiquitin ligase C-terminus of heat shock cognate 70 interacting protein (CHIP) produces specific behavioral impairments. PLoS ONE 2012, 7:e36340.
    • (2012) PLoS ONE , vol.7
    • McLaughlin, B.1    Buendia, M.A.2    Saborido, T.P.3    Palubinsky, A.M.4    Stankowski, J.N.5    Stanwood, G.D.6
  • 96
    • 34249946941 scopus 로고    scopus 로고
    • Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage
    • DOI 10.1093/hmg/ddm083
    • Stichel CC, Zhu X, Bader V, Linnartz B, Schmidt S, Lübbert H: Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage. Hum Mol Genet 2007, 16:2377-93. (Pubitemid 47514484)
    • (2007) Human Molecular Genetics , vol.16 , Issue.20 , pp. 2377-2393
    • Stichel, C.C.1    Zhu, X.-R.2    Bader, V.3    Linnartz, B.4    Schmidt, S.5    Lubbert, H.6
  • 98
    • 77949729459 scopus 로고    scopus 로고
    • Parkin regulates metal transport via proteasomal degradation of the 1B isoforms of divalent metal transporter 1
    • Roth JA, Singleton S, Feng J, Garrick M, Paradkar PN: Parkin regulates metal transport via proteasomal degradation of the 1B isoforms of divalent metal transporter 1. J Neurochem 2010, 113:454-64.
    • (2010) J Neurochem , vol.113 , pp. 454-464
    • Roth, J.A.1    Singleton, S.2    Feng, J.3    Garrick, M.4    Paradkar, P.N.5
  • 100
    • 70349336998 scopus 로고    scopus 로고
    • Abnormal retinal development in the Btrc null mouse
    • Baguma-Nibasheka M, Kablar B: Abnormal retinal development in the Btrc null mouse. Dev Dyn 2009, 238:2680-7.
    • (2009) Dev Dyn , vol.238 , pp. 2680-2687
    • Baguma-Nibasheka, M.1    Kablar, B.2
  • 101
    • 55349127867 scopus 로고    scopus 로고
    • The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation by mediating degradation of clock protein PER2
    • Ohsaki K, Oishi K, Kozono Y, Nakayama K, Nakayama KI, Ishida N: The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation by mediating degradation of clock protein PER2. J Biochem 2008, 144:609-18.
    • (2008) J Biochem , vol.144 , pp. 609-618
    • Ohsaki, K.1    Oishi, K.2    Kozono, Y.3    Nakayama, K.4    Nakayama, K.I.5    Ishida, N.6
  • 108
    • 67649229630 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
    • Wang C, Chen T, Zhang J, Yang M, Li N, Xu X, Cao X: The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon. Nat Immunol 2009, 10:744-52.
    • (2009) Nat Immunol , vol.10 , pp. 744-752
    • Wang, C.1    Chen, T.2    Zhang, J.3    Yang, M.4    Li, N.5    Xu, X.6    Cao, X.7
  • 109
    • 79955541868 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of E3 ligase Nrdp1 increases ischemia and reperfusion-induced cardiac injury
    • Zhang Y, Zeng Y, Wang M, Tian C, Ma X, Chen H, Fang Q, Jia L, Du J, Li H: Cardiac-specific overexpression of E3 ligase Nrdp1 increases ischemia and reperfusion-induced cardiac injury. Basic Res Cardiol 2011, 106:371-83.
    • (2011) Basic Res Cardiol , vol.106 , pp. 371-383
    • Zhang, Y.1    Zeng, Y.2    Wang, M.3    Tian, C.4    Ma, X.5    Chen, H.6    Fang, Q.7    Jia, L.8    Du, J.9    Li, H.10
  • 110
    • 79959612558 scopus 로고    scopus 로고
    • Overexpression of Nrdp1 in the heart exacerbates doxorubicin-induced cardiac dysfunction inmice
    • Zhang Y, Kang Y, Tian C, Zeng Y, Jia L, Ma X, Du J, Li H: Overexpression of Nrdp1 in the heart exacerbates doxorubicin-induced cardiac dysfunction inmice. PLoS ONE 2011, 6:e21104.
    • (2011) PLoS ONE , vol.6
    • Zhang, Y.1    Kang, Y.2    Tian, C.3    Zeng, Y.4    Jia, L.5    Ma, X.6    Du, J.7    Li, H.8
  • 111
    • 17044414102 scopus 로고    scopus 로고
    • Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation
    • Yamashita M, Ying S, Zhang G, Li C, Cheng SY, Deng C, Zhang YE: Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 2005, 121:101-13.
    • (2005) Cell , vol.121 , pp. 101-113
    • Yamashita, M.1    Ying, S.2    Zhang, G.3    Li, C.4    Cheng, S.Y.5    Deng, C.6    Zhang, Y.E.7
  • 114
    • 77952084417 scopus 로고    scopus 로고
    • Increased E4 activity in mice leads to ubiquitin-containing aggregates and degeneration of hypothalamic neurons resulting in obesity
    • Susaki E, Kaneko-Oshikawa C, Miyata K, Tabata M, Yamada T, Oike Y, Katagiri H, Nakayama KI: Increased E4 activity in mice leads to ubiquitin-containing aggregates and degeneration of hypothalamic neurons resulting in obesity. J Biol Chem 2010, 285:15538-47.
    • (2010) J Biol Chem , vol.285 , pp. 15538-15547
    • Susaki, E.1    Kaneko-Oshikawa, C.2    Miyata, K.3    Tabata, M.4    Yamada, T.5    Oike, Y.6    Katagiri, H.7    Nakayama, K.I.8
  • 117
    • 84874090275 scopus 로고    scopus 로고
    • A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation
    • Sehrawat S, Koenig P, Kirak O, Schlieker C, Fankhauser M, Ploegh HL: A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation. Blood 2013, 121:1145-56.
    • (2013) Blood , vol.121 , pp. 1145-1156
    • Sehrawat, S.1    Koenig, P.2    Kirak, O.3    Schlieker, C.4    Fankhauser, M.5    Ploegh, H.L.6
  • 120
    • 27944464985 scopus 로고    scopus 로고
    • Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence
    • DOI 10.1016/j.molcel.2005.09.027, PII S1097276505017338
    • Molinari M, Galli C, Vanoni O, Arnold SM, Kaufman RJ: Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol Cell 2005, 20:503-12. (Pubitemid 41668636)
    • (2005) Molecular Cell , vol.20 , Issue.4 , pp. 503-512
    • Molinari, M.1    Galli, C.2    Vanoni, O.3    Arnold, S.M.4    Kaufman, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.