메뉴 건너뛰기




Volumn 30, Issue 17, 2010, Pages 6132-6142

Identification of caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimer's disease: A novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CASPASE 3; CASPASE 6; CASPASE 7; EPITOPE; PROTEASOME; PROTEIN P97; RECOMBINANT PROTEIN; UBIQUITIN; VALOSIN CONTAINING PROTEIN;

EID: 77951653609     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.5874-09.2010     Document Type: Article
Times cited : (51)

References (54)
  • 2
    • 73349135640 scopus 로고    scopus 로고
    • Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or Presenilin I or Presenilin II mutations
    • Albrecht S, Bogdanovic N, Ghetti B, Winblad B, LeBlanc AC (2009) Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or Presenilin I or Presenilin II mutations. J Neuropathol Exp Neurol 68:1282-1293.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 1282-1293
    • Albrecht, S.1    Bogdanovic, N.2    Ghetti, B.3    Winblad, B.4    LeBlanc, A.C.5
  • 4
    • 14644416500 scopus 로고    scopus 로고
    • Mild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions
    • Bennett DA, Schneider JA, Bienias JL, Evans DA, Wilson RS (2005) Mild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions. Neurology 64:834-841.
    • (2005) Neurology , vol.64 , pp. 834-841
    • Bennett, D.A.1    Schneider, J.A.2    Bienias, J.L.3    Evans, D.A.4    Wilson, R.S.5
  • 5
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J, Levey AI, Weintraub ST, Rees HD, Gearing M, Chin LS, Li L (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J Biol Chem 279:13256-13264.
    • (2004) J Biol Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 6
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma NP, Lindsten K, Glas R, Jellne M, Masucci MG (2000) Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat Biotechnol 18:538-543.
    • (2000) Nat Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 7
    • 13844253945 scopus 로고    scopus 로고
    • Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering
    • Davies JM, Tsuruta H, May AP, Weis WI (2005) Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering. Structure 13:183-195.
    • (2005) Structure , vol.13 , pp. 183-195
    • Davies, J.M.1    Tsuruta, H.2    May, A.P.3    Weis, W.I.4
  • 9
    • 0025278909 scopus 로고
    • Ubiquitin immunoreactive structures in normal human brains: Distribution and developmental aspects
    • Dickson DW, Wertkin A, Kress Y, Ksiezak-Reding H, Yen SH (1990a) Ubiquitin immunoreactive structures in normal human brains: distribution and developmental aspects. Lab Invest 63:87-99.
    • (1990) Lab Invest , vol.63 , pp. 87-99
    • Dickson, D.W.1    Wertkin, A.2    Kress, Y.3    Ksiezak-Reding, H.4    Yen, S.H.5
  • 10
    • 0025210629 scopus 로고
    • Ubiquitin immunoelectron microscopy of dystrophic neurites in cerebellar senile plaques of Alzheimer's disease
    • Dickson DW, Wertkin A, Mattiace LA, Fier E, Kress Y, Davies P, Yen SH (1990b) Ubiquitin immunoelectron microscopy of dystrophic neurites in cerebellar senile plaques of Alzheimer's disease. Acta Neuropathol 79:486-493.
    • (1990) Acta Neuropathol , vol.79 , pp. 486-493
    • Dickson, D.W.1    Wertkin, A.2    Mattiace, L.A.3    Fier, E.4    Kress, Y.5    Davies, P.6    Yen, S.H.7
  • 11
    • 1842576796 scopus 로고    scopus 로고
    • Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47
    • Dreveny I, Kondo H, Uchiyama K, Shaw A, Zhang X, Freemont PS (2004) Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J 23:1030-1039.
    • (2004) EMBO J , vol.23 , pp. 1030-1039
    • Dreveny, I.1    Kondo, H.2    Uchiyama, K.3    Shaw, A.4    Zhang, X.5    Freemont, P.S.6
  • 12
    • 0041315902 scopus 로고    scopus 로고
    • Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane
    • Flierman D, Ye Y, Dai M, Chau V, Rapoport TA (2003) Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane. J Biol Chem 278:34774-34782.
    • (2003) J Biol Chem , vol.278 , pp. 34774-34782
    • Flierman, D.1    Ye, Y.2    Dai, M.3    Chau, V.4    Rapoport, T.A.5
  • 14
    • 0035889716 scopus 로고    scopus 로고
    • Ubiquitinated granular structures and initial neurofibrillary changes in the human brain
    • García Gil ML, Morán MA, Gómez-Ramos P (2001) Ubiquitinated granular structures and initial neurofibrillary changes in the human brain. J Neurol Sci 192:27-34.
    • (2001) J Neurol Sci , vol.192 , pp. 27-34
    • García Gil, M.L.1    Morán, M.A.2    Gómez-Ramos, P.3
  • 16
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC (2004) Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am J Pathol 165:523-531. (Pubitemid 38971382)
    • (2004) American Journal of Pathology , vol.165 , Issue.2 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Leblanc, A.C.6
  • 17
    • 33745224935 scopus 로고    scopus 로고
    • p97: The cell's molecular purgatory?
    • Halawani D, Latterich M (2006) p97: the cell's molecular purgatory? Mol Cell 22:713-717.
    • (2006) Mol Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 18
    • 68949098348 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation
    • Halawani D, LeBlanc AC, Rouiller I, Michnick SW, Servant MJ, Latterich M (2009) Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation. Mol Cell Biol 29:4484-4494.
    • (2009) Mol Cell Biol , vol.29 , pp. 4484-4494
    • Halawani, D.1    LeBlanc, A.C.2    Rouiller, I.3    Michnick, S.W.4    Servant, M.J.5    Latterich, M.6
  • 19
    • 0034746779 scopus 로고    scopus 로고
    • The conserved Np14 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock AL, Krebber H, Frietze S, Lin A, Latterich M, Silver PA (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12:3226-3241. (Pubitemid 33062975)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.10 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 21
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): A "molecular gearbox" in the ubiquitin pathway?
    • Jentsch S, Rumpf S (2007) Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem Sci 32:6-11.
    • (2007) Trends Biochem Sci , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 22
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S, Nitsch R, Grune T, Ullrich O (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 85:115-122. (Pubitemid 36389701)
    • (2003) Journal of Neurochemistry , vol.85 , Issue.1 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 23
    • 50249086898 scopus 로고    scopus 로고
    • Targets of caspase-6 activity in human neurons and Alzheimer disease
    • Klaiman G, Petzke TL, Hammond J, LeBlanc AC (2008) Targets of caspase-6 activity in human neurons and Alzheimer disease. Mol Cell Proteomics 7:1541-1555.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1541-1555
    • Klaiman, G.1    Petzke, T.L.2    Hammond, J.3    LeBlanc, A.C.4
  • 25
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96:635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 27
    • 0041816369 scopus 로고    scopus 로고
    • Kennedy's disease: Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death
    • LaFevre-Bernt MA, Ellerby LM (2003) Kennedy's disease: phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death. J Biol Chem 278: 34918-34924.
    • (2003) J Biol Chem , vol.278 , pp. 34918-34924
    • LaFevre-Bernt, M.A.1    Ellerby, L.M.2
  • 28
    • 0029609021 scopus 로고
    • Increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: Possible involvement of apoptosis
    • LeBlanc A (1995) Increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: possible involvement of apoptosis. J Neurosci 15:7837-7846.
    • (1995) J Neurosci , vol.15 , pp. 7837-7846
    • LeBlanc, A.1
  • 29
    • 24644453571 scopus 로고    scopus 로고
    • The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death
    • LeBlanc AC (2005) The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death. Curr Alzheimer Res 2:389-402.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 389-402
    • LeBlanc, A.C.1
  • 30
    • 0033551738 scopus 로고    scopus 로고
    • Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimer's disease
    • LeBlanc A, Liu H, Goodyer C, Bergeron C, Hammond J (1999) Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimer's disease. J Biol Chem 274:23426-23436.
    • (1999) J Biol Chem , vol.274 , pp. 23426-23436
    • LeBlanc, A.1    Liu, H.2    Goodyer, C.3    Bergeron, C.4    Hammond, J.5
  • 32
    • 22344439156 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: Implications for mutant huntingtin toxicity
    • Luo S, Vacher C, Davies JE, Rubinsztein DC (2005) Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J Cell Biol 169:647-656.
    • (2005) J Cell Biol , vol.169 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3    Rubinsztein, D.C.4
  • 33
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19:2181-2192.
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 34
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer HH, Wang Y, Warren G (2002) Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J 21:5645-5652.
    • (2002) EMBO J , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 35
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H, Kondo J, Ihara Y (1987) Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235:1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 36
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, Tessier-Lavigne M (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457:981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 38
    • 0024560685 scopus 로고
    • Immunochemical properties of ubiquitin conjugates in the paired helical filaments of Alzheimer disease
    • DOI 10.1111/j.1471-4159.1989.tb09203.x
    • Perry G, Mulvihill P, Fried VA, Smith HT, Grundke-Iqbal I, Iqbal K (1989) Immunochemical properties of ubiquitin conjugates in the paired helical filaments of Alzheimer disease. J Neurochem 52:1523-1528. (Pubitemid 19109505)
    • (1989) Journal of Neurochemistry , vol.52 , Issue.5 , pp. 1523-1528
    • Perry, G.1    Mulvihill, P.2    Fried, V.A.3    Smith, H.T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 39
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • DOI 10.1016/j.cell.2004.11.013, PII S0092867404010864
    • Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120:73-84. (Pubitemid 40094604)
    • (2005) Cell , vol.120 , Issue.1 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 40
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • DOI 10.1016/j.molcel.2005.12.014, PII S1097276505018976
    • Rumpf S, Jentsch S (2006) Functional division of substrate processing co-factors of the ubiquitin-selective Cdc48 chaperone. Mol Cell 21:261-269. (Pubitemid 43099941)
    • (2006) Molecular Cell , vol.21 , Issue.2 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 41
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz AL, Ciechanover A (1999) The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu Rev Med 50:57-74.
    • (1999) Annu Rev Med , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 42
    • 0023900638 scopus 로고
    • Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain
    • Shaw G, Chau V (1988) Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain. Proc Natl Acad Sci U S A 85:2854-2858.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2854-2858
    • Shaw, G.1    Chau, V.2
  • 43
    • 33846705026 scopus 로고    scopus 로고
    • Npl4p/Ufd1p Binds and Segregates Membrane-Anchored/ Tethered Complexes via a Polyubiquitin Signal Present on the Anchors
    • DOI 10.1016/j.molcel.2007.01.024, PII S1097276507000470
    • Shcherbik N, Haines DS (2007) Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol Cell 25:385-397. (Pubitemid 46199293)
    • (2007) Molecular Cell , vol.25 , Issue.3 , pp. 385-397
    • Shcherbik, N.1    Haines, D.S.2
  • 44
    • 0033927705 scopus 로고    scopus 로고
    • Determination of caspase specificities using a peptide combinatorial library
    • Thornberry NA, Chapman KT, Nicholson DW (2000) Determination of caspase specificities using a peptide combinatorial library. Methods Enzymol 322:100-110.
    • (2000) Methods Enzymol , vol.322 , pp. 100-110
    • Thornberry, N.A.1    Chapman, K.T.2    Nicholson, D.W.3
  • 46
    • 0041856469 scopus 로고    scopus 로고
    • D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP
    • Wang Q, Song C, Yang X, Li CC (2003) D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP. J Biol Chem 278:32784-32793.
    • (2003) J Biol Chem , vol.278 , pp. 32784-32793
    • Wang, Q.1    Song, C.2    Yang, X.3    Li, C.C.4
  • 47
    • 64349099993 scopus 로고    scopus 로고
    • The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Wang X, Su B, Zheng L, Perry G, Smith MA, Zhu X (2009a) The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J Neurochem 109 [Suppl 1]:153-159.
    • (2009) J Neurochem , vol.109 , Issue.SUPPL. 1 , pp. 153-159
    • Wang, X.1    Su, B.2    Zheng, L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 48
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X, Su B, Lee HG, Li X, Perry G, Smith MA, Zhu X (2009b) Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci 29:9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 49
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, Pestronk A, Whyte MP, Kimonis VE (2004) Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 36:377-381.
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 50
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • Wójcik C, Rowicka M, Kudlicki A, Nowis D, McConnell E, Kujawa M, DeMartino GN (2006) Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol Biol Cell 17:4606-4618.
    • (2006) Mol Biol Cell , vol.17 , pp. 4606-4618
    • Wójcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5    Kujawa, M.6    DeMartino, G.N.7
  • 51
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao J, Irwin RW, Zhao L, Nilsen J, Hamilton RT, Brinton RD (2009) Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 106:14670-14675.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 52
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 53
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162:71-84.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 54
    • 0034668842 scopus 로고    scopus 로고
    • Selective and protracted apoptosis in human primary neurons microinjected with active caspase-3, -6, -7, and -8
    • Zhang Y, Goodyer C, LeBlanc A (2000) Selective and protracted apoptosis in human primary neurons microinjected with active caspase-3, -6, -7, and -8. J Neurosci 20:8384-8389.
    • (2000) J Neurosci , vol.20 , pp. 8384-8389
    • Zhang, Y.1    Goodyer, C.2    LeBlanc, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.