-
1
-
-
78649357985
-
Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
-
Buchberger A, Bukau B, Sommer T, (2010) Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 40: 238–252. doi: 10.1016/j.molcel.2010.10.001 20965419
-
(2010)
Mol Cell
, vol.40
, pp. 238-252
-
-
Buchberger, A.1
Bukau, B.2
Sommer, T.3
-
2
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
Hartl FU, Bracher A, Hayer-Hartl M, (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324–332. doi: 10.1038/nature10317 21776078
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
3
-
-
84886412961
-
Chaperone machines for protein folding, unfolding and disaggregation
-
Saibil H, (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol 14: 630–642. doi: 10.1038/nrm3658 24026055
-
(2013)
Nat Rev Mol Cell Biol
, vol.14
, pp. 630-642
-
-
Saibil, H.1
-
4
-
-
84883387793
-
Targeting the unfolded protein response in disease
-
Hetz C, Chevet E, Harding HP, (2013) Targeting the unfolded protein response in disease. Nat Rev Drug Discov 12: 703–719. doi: 10.1038/nrd3976 23989796
-
(2013)
Nat Rev Drug Discov
, vol.12
, pp. 703-719
-
-
Hetz, C.1
Chevet, E.2
Harding, H.P.3
-
5
-
-
84892865694
-
Sorting out the trash: the spatial nature of eukaryotic protein quality control
-
Sontag EM, Vonk WI, Frydman J, (2014) Sorting out the trash: the spatial nature of eukaryotic protein quality control. Curr Opin Cell Biol 26: 139–146. doi: 10.1016/j.ceb.2013.12.006 24463332
-
(2014)
Curr Opin Cell Biol
, vol.26
, pp. 139-146
-
-
Sontag, E.M.1
Vonk, W.I.2
Frydman, J.3
-
6
-
-
0033625965
-
The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s
-
Easton DP, Kaneko Y, Subjeck JR, (2000) The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5: 276–290. 11048651
-
(2000)
Cell Stress Chaperones
, vol.5
, pp. 276-290
-
-
Easton, D.P.1
Kaneko, Y.2
Subjeck, J.R.3
-
7
-
-
33745762927
-
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
-
Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU, (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25: 2519–2528. 16688212
-
(2006)
EMBO J
, vol.25
, pp. 2519-2528
-
-
Dragovic, Z.1
Broadley, S.A.2
Shomura, Y.3
Bracher, A.4
Hartl, F.U.5
-
8
-
-
29344449706
-
Human and yeast Hsp110 chaperones exhibit functional differences
-
Raviol H, Bukau B, Mayer MP, (2006) Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett 580: 168–174. 16364315
-
(2006)
FEBS Lett
, vol.580
, pp. 168-174
-
-
Raviol, H.1
Bukau, B.2
Mayer, M.P.3
-
9
-
-
44649110104
-
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
-
Polier S, Dragovic Z, Hartl FU, Bracher A, (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133: 1068–1079. doi: 10.1016/j.cell.2008.05.022 18555782
-
(2008)
Cell
, vol.133
, pp. 1068-1079
-
-
Polier, S.1
Dragovic, Z.2
Hartl, F.U.3
Bracher, A.4
-
10
-
-
84924187480
-
GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones
-
Bracher A, Verghese J, (2015) GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones. Subcell Biochem 78: 1–33. doi: 10.1007/978-3-319-11731-7_1 25487014
-
(2015)
Subcell Biochem
, vol.78
, pp. 1-33
-
-
Bracher, A.1
Verghese, J.2
-
11
-
-
84934286870
-
Heat Shock Protein A4 Controls Cell Migration and Gastric Ulcer Healing
-
Sakurai T, Kashida H, Hagiwara S, Nishida N, Watanabe T, et al. (2015) Heat Shock Protein A4 Controls Cell Migration and Gastric Ulcer Healing. Dig Dis Sci.
-
(2015)
Dig Dis Sci
-
-
Sakurai, T.1
Kashida, H.2
Hagiwara, S.3
Nishida, N.4
Watanabe, T.5
-
12
-
-
84866395411
-
Hsp110 is required for spindle length control
-
Makhnevych T, Wong P, Pogoutse O, Vizeacoumar FJ, Greenblatt JF, et al. (2012) Hsp110 is required for spindle length control. J Cell Biol 198: 623–636. doi: 10.1083/jcb.201111105 22908312
-
(2012)
J Cell Biol
, vol.198
, pp. 623-636
-
-
Makhnevych, T.1
Wong, P.2
Pogoutse, O.3
Vizeacoumar, F.J.4
Greenblatt, J.F.5
-
13
-
-
84940767899
-
HSP105 Recruits PP2A to Dephosphorylate beta-Catenin
-
Yu N, Kakunda M, Pham V, Lill JR, Du P, et al. (2015) HSP105 Recruits PP2A to Dephosphorylate beta-Catenin. Mol Cell Biol.
-
(2015)
Mol Cell Biol
-
-
Yu, N.1
Kakunda, M.2
Pham, V.3
Lill, J.R.4
Du, P.5
-
14
-
-
34547893834
-
Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS
-
Yamashita H, Kawamata J, Okawa K, Kanki R, Nakamizo T, et al. (2007) Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS. J Neurochem 102: 1497–1505. 17403032
-
(2007)
J Neurochem
, vol.102
, pp. 1497-1505
-
-
Yamashita, H.1
Kawamata, J.2
Okawa, K.3
Kanki, R.4
Nakamizo, T.5
-
15
-
-
84875845592
-
Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm
-
Song Y, Nagy M, Ni W, Tyagi NK, Fenton WA, et al. (2013) Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm. Proc Natl Acad Sci U S A 110: 5428–5433. doi: 10.1073/pnas.1303279110 23509252
-
(2013)
Proc Natl Acad Sci U S A
, vol.110
, pp. 5428-5433
-
-
Song, Y.1
Nagy, M.2
Ni, W.3
Tyagi, N.K.4
Fenton, W.A.5
-
16
-
-
46149116088
-
Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
-
Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andreasson C, et al. (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 3: e1763. doi: 10.1371/journal.pone.0001763 18335038
-
(2008)
PLoS One
, vol.3
, pp. 1763
-
-
Sadlish, H.1
Rampelt, H.2
Shorter, J.3
Wegrzyn, R.D.4
Andreasson, C.5
-
17
-
-
77956672926
-
Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta
-
Eroglu B, Moskophidis D, Mivechi NF, (2010) Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta. Mol Cell Biol 30: 4626–4643. doi: 10.1128/MCB.01493-09 20679486
-
(2010)
Mol Cell Biol
, vol.30
, pp. 4626-4643
-
-
Eroglu, B.1
Moskophidis, D.2
Mivechi, N.F.3
-
18
-
-
84861749562
-
Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels
-
Saxena A, Banasavadi-Siddegowda YK, Fan Y, Bhattacharya S, Roy G, et al. (2012) Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels. J Biol Chem 287: 19158–19170. doi: 10.1074/jbc.M111.297580 22505710
-
(2012)
J Biol Chem
, vol.287
, pp. 19158-19170
-
-
Saxena, A.1
Banasavadi-Siddegowda, Y.K.2
Fan, Y.3
Bhattacharya, S.4
Roy, G.5
-
19
-
-
84871752624
-
Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers
-
Muralidharan V, Oksman A, Pal P, Lindquist S, Goldberg DE, (2012) Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nat Commun 3: 1310. doi: 10.1038/ncomms2306 23250440
-
(2012)
Nat Commun
, vol.3
, pp. 1310
-
-
Muralidharan, V.1
Oksman, A.2
Pal, P.3
Lindquist, S.4
Goldberg, D.E.5
-
20
-
-
84887473021
-
Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110
-
Kuo Y, Ren S, Lao U, Edgar BA, Wang T, (2013) Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110. Cell Death Dis 4: e833. doi: 10.1038/cddis.2013.351 24091676
-
(2013)
Cell Death Dis
, vol.4
, pp. 833
-
-
Kuo, Y.1
Ren, S.2
Lao, U.3
Edgar, B.A.4
Wang, T.5
-
21
-
-
77954947810
-
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
-
Kampinga HH, Craig EA, (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11: 579–592. doi: 10.1038/nrm2941 20651708
-
(2010)
Nat Rev Mol Cell Biol
, vol.11
, pp. 579-592
-
-
Kampinga, H.H.1
Craig, E.A.2
-
22
-
-
0001133526
-
Hsp110 protects heat-denatured proteins and confers cellular thermoresistance
-
Oh HJ, Chen X, Subjeck JR, (1997) Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J Biol Chem 272: 31636–31640. 9395504
-
(1997)
J Biol Chem
, vol.272
, pp. 31636-31640
-
-
Oh, H.J.1
Chen, X.2
Subjeck, J.R.3
-
23
-
-
80054699747
-
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
-
Shorter J, (2011) The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6: e26319. doi: 10.1371/journal.pone.0026319 22022600
-
(2011)
PLoS One
, vol.6
, pp. 26319
-
-
Shorter, J.1
-
24
-
-
84868525116
-
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
-
Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, et al. (2012) Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J 31: 4221–4235. doi: 10.1038/emboj.2012.264 22990239
-
(2012)
EMBO J
, vol.31
, pp. 4221-4235
-
-
Rampelt, H.1
Kirstein-Miles, J.2
Nillegoda, N.B.3
Chi, K.4
Scholz, S.R.5
-
25
-
-
84880515581
-
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
-
Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P, (2013) Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem 288: 21399–21411. doi: 10.1074/jbc.M113.479253 23737532
-
(2013)
J Biol Chem
, vol.288
, pp. 21399-21411
-
-
Mattoo, R.U.1
Sharma, S.K.2
Priya, S.3
Finka, A.4
Goloubinoff, P.5
-
26
-
-
0035017308
-
Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
-
Pelkmans L, Kartenbeck J, Helenius A, (2001) Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 3: 473–483. 11331875
-
(2001)
Nat Cell Biol
, vol.3
, pp. 473-483
-
-
Pelkmans, L.1
Kartenbeck, J.2
Helenius, A.3
-
27
-
-
8744221758
-
Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy
-
Bernacchi S, Mueller G, Langowski J, Waldeck W, (2004) Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy. Biochem Soc Trans 32: 746–749. 15494004
-
(2004)
Biochem Soc Trans
, vol.32
, pp. 746-749
-
-
Bernacchi, S.1
Mueller, G.2
Langowski, J.3
Waldeck, W.4
-
28
-
-
33746758880
-
Retrograde transport pathways utilised by viruses and protein toxins
-
Spooner RA, Smith DC, Easton AJ, Roberts LM, Lord JM, (2006) Retrograde transport pathways utilised by viruses and protein toxins. Virol J 3: 26. 16603059
-
(2006)
Virol J
, vol.3
, pp. 26
-
-
Spooner, R.A.1
Smith, D.C.2
Easton, A.J.3
Roberts, L.M.4
Lord, J.M.5
-
29
-
-
78650668745
-
Cellular entry of polyomaviruses
-
Tsai B, Qian M, (2010) Cellular entry of polyomaviruses. Curr Top Microbiol Immunol 343: 177–194. doi: 10.1007/82_2010_38 20373089
-
(2010)
Curr Top Microbiol Immunol
, vol.343
, pp. 177-194
-
-
Tsai, B.1
Qian, M.2
-
30
-
-
0026064632
-
Structure of simian virus 40 at 3.8-A resolution
-
Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, et al. (1991) Structure of simian virus 40 at 3.8-A resolution. Nature 354: 278–284. 1659663
-
(1991)
Nature
, vol.354
, pp. 278-284
-
-
Liddington, R.C.1
Yan, Y.2
Moulai, J.3
Sahli, R.4
Benjamin, T.L.5
-
31
-
-
0030584124
-
The structure of simian virus 40 refined at 3.1 A resolution
-
Stehle T, Gamblin SJ, Yan Y, Harrison SC, (1996) The structure of simian virus 40 refined at 3.1 A resolution. Structure 4: 165–182. 8805523
-
(1996)
Structure
, vol.4
, pp. 165-182
-
-
Stehle, T.1
Gamblin, S.J.2
Yan, Y.3
Harrison, S.C.4
-
32
-
-
0024844490
-
Endocytosis of simian virus 40 into the endoplasmic reticulum
-
Kartenbeck J, Stukenbrok H, Helenius A, (1989) Endocytosis of simian virus 40 into the endoplasmic reticulum. J Cell Biol 109: 2721–2729. 2556405
-
(1989)
J Cell Biol
, vol.109
, pp. 2721-2729
-
-
Kartenbeck, J.1
Stukenbrok, H.2
Helenius, A.3
-
33
-
-
67650912077
-
A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection
-
Qian M, Cai D, Verhey KJ, Tsai B, (2009) A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog 5: e1000465. doi: 10.1371/journal.ppat.1000465 19503604
-
(2009)
PLoS Pathog
, vol.5
, pp. 1000465
-
-
Qian, M.1
Cai, D.2
Verhey, K.J.3
Tsai, B.4
-
34
-
-
79955436301
-
Role of endosomes in simian virus 40 entry and infection
-
Engel S, Heger T, Mancini R, Herzog F, Kartenbeck J, et al. (2011) Role of endosomes in simian virus 40 entry and infection. J Virol 85: 4198–4211. doi: 10.1128/JVI.02179-10 21345959
-
(2011)
J Virol
, vol.85
, pp. 4198-4211
-
-
Engel, S.1
Heger, T.2
Mancini, R.3
Herzog, F.4
Kartenbeck, J.5
-
35
-
-
36348964305
-
A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane
-
Rainey-Barger EK, Magnuson B, Tsai B, (2007) A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J Virol 81: 12996–13004. 17881435
-
(2007)
J Virol
, vol.81
, pp. 12996-13004
-
-
Rainey-Barger, E.K.1
Magnuson, B.2
Tsai, B.3
-
36
-
-
35548992416
-
Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells
-
Schelhaas M, Malmstrom J, Pelkmans L, Haugstetter J, Ellgaard L, et al. (2007) Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 131: 516–529. 17981119
-
(2007)
Cell
, vol.131
, pp. 516-529
-
-
Schelhaas, M.1
Malmstrom, J.2
Pelkmans, L.3
Haugstetter, J.4
Ellgaard, L.5
-
37
-
-
80455143829
-
BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
-
Geiger R, Andritschke D, Friebe S, Herzog F, Luisoni S, et al. (2011) BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. Nat Cell Biol 13: 1305–1314. doi: 10.1038/ncb2339 21947079
-
(2011)
Nat Cell Biol
, vol.13
, pp. 1305-1314
-
-
Geiger, R.1
Andritschke, D.2
Friebe, S.3
Herzog, F.4
Luisoni, S.5
-
38
-
-
84855195138
-
BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection
-
Goodwin EC, Lipovsky A, Inoue T, Magaldi TG, Edwards AP, et al. (2011) BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection. MBio 2: e00101–00111. doi: 10.1128/mBio.00101-11 21673190
-
(2011)
MBio
, vol.2
, pp. 00101-00111
-
-
Goodwin, E.C.1
Lipovsky, A.2
Inoue, T.3
Magaldi, T.G.4
Edwards, A.P.5
-
39
-
-
79958051219
-
A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol
-
Inoue T, Tsai B, (2011) A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol. PLoS Pathog 7: e1002037. doi: 10.1371/journal.ppat.1002037 21589906
-
(2011)
PLoS Pathog
, vol.7
, pp. 1002037
-
-
Inoue, T.1
Tsai, B.2
-
40
-
-
26944450514
-
ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
-
Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, et al. (2005) ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 20: 289–300. 16246730
-
(2005)
Mol Cell
, vol.20
, pp. 289-300
-
-
Magnuson, B.1
Rainey, E.K.2
Benjamin, T.3
Baryshev, M.4
Mkrtchian, S.5
-
41
-
-
0036233218
-
Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles
-
Norkin LC, Anderson HA, Wolfrom SA, Oppenheim A, (2002) Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles. J Virol 76: 5156–5166. 11967331
-
(2002)
J Virol
, vol.76
, pp. 5156-5166
-
-
Norkin, L.C.1
Anderson, H.A.2
Wolfrom, S.A.3
Oppenheim, A.4
-
42
-
-
33845655873
-
SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER
-
Daniels R, Rusan NM, Wadsworth P, Hebert DN, (2006) SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER. Mol Cell 24: 955–966. 17189196
-
(2006)
Mol Cell
, vol.24
, pp. 955-966
-
-
Daniels, R.1
Rusan, N.M.2
Wadsworth, P.3
Hebert, D.N.4
-
43
-
-
84897416878
-
A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum
-
Walczak CP, Ravindran MS, Inoue T, Tsai B, (2014) A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum. PLoS Pathog 10: e1004007. doi: 10.1371/journal.ppat.1004007 24675744
-
(2014)
PLoS Pathog
, vol.10
, pp. 1004007
-
-
Walczak, C.P.1
Ravindran, M.S.2
Inoue, T.3
Tsai, B.4
-
44
-
-
84885942427
-
A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins
-
Sopha P, Kadokura H, Yamamoto YH, Takeuchi M, Saito M, et al. (2012) A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins. Cell Struct Funct 37: 177–187. 23018488
-
(2012)
Cell Struct Funct
, vol.37
, pp. 177-187
-
-
Sopha, P.1
Kadokura, H.2
Yamamoto, Y.H.3
Takeuchi, M.4
Saito, M.5
-
45
-
-
84900426647
-
Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast
-
Abrams JL, Verghese J, Gibney PA, Morano KA, (2014) Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast. J Biol Chem 289: 13155–13167. doi: 10.1074/jbc.M113.530014 24671421
-
(2014)
J Biol Chem
, vol.289
, pp. 13155-13167
-
-
Abrams, J.L.1
Verghese, J.2
Gibney, P.A.3
Morano, K.A.4
-
46
-
-
45849091944
-
Structure of the Hsp110:Hsc70 nucleotide exchange machine
-
Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, et al. (2008) Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 31: 232–243. doi: 10.1016/j.molcel.2008.05.006 18550409
-
(2008)
Mol Cell
, vol.31
, pp. 232-243
-
-
Schuermann, J.P.1
Jiang, J.2
Cuellar, J.3
Llorca, O.4
Wang, L.5
-
47
-
-
34748918368
-
The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum—a quantitative approach
-
Weitzmann A, Baldes C, Dudek J, Zimmermann R, (2007) The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum—a quantitative approach. FEBS J 274: 5175–5187. 17850331
-
(2007)
FEBS J
, vol.274
, pp. 5175-5187
-
-
Weitzmann, A.1
Baldes, C.2
Dudek, J.3
Zimmermann, R.4
-
48
-
-
77951229568
-
The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110
-
Andreasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B, (2010) The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J Biol Chem 285: 12445–12453. doi: 10.1074/jbc.M109.096735 20177057
-
(2010)
J Biol Chem
, vol.285
, pp. 12445-12453
-
-
Andreasson, C.1
Rampelt, H.2
Fiaux, J.3
Druffel-Augustin, S.4
Bukau, B.5
-
49
-
-
77954366161
-
Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct
-
Hale SJ, Lovell SC, de Keyzer J, Stirling CJ, (2010) Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct. J Biol Chem 285: 21600–21606. doi: 10.1074/jbc.M110.111211 20430899
-
(2010)
J Biol Chem
, vol.285
, pp. 21600-21606
-
-
Hale, S.J.1
Lovell, S.C.2
de Keyzer, J.3
Stirling, C.J.4
-
50
-
-
70450245119
-
Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo
-
de Keyzer J, Steel GJ, Hale SJ, Humphries D, Stirling CJ, (2009) Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo. J Biol Chem 284: 31564–31571. doi: 10.1074/jbc.M109.055160 19759005
-
(2009)
J Biol Chem
, vol.284
, pp. 31564-31571
-
-
de Keyzer, J.1
Steel, G.J.2
Hale, S.J.3
Humphries, D.4
Stirling, C.J.5
-
51
-
-
84924215619
-
A Nucleotide Exchange Factor Promotes ER-to-cytosol Membrane Penetration of the Non-enveloped Virus SV40
-
Inoue T, Tsai B, (2015) A Nucleotide Exchange Factor Promotes ER-to-cytosol Membrane Penetration of the Non-enveloped Virus SV40. J Virol.
-
(2015)
J Virol
-
-
Inoue, T.1
Tsai, B.2
-
52
-
-
77949894225
-
N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol
-
Wernick NL, De Luca H, Kam WR, Lencer WI, (2010) N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol. J Biol Chem 285: 6145–6152. doi: 10.1074/jbc.M109.062067 20056601
-
(2010)
J Biol Chem
, vol.285
, pp. 6145-6152
-
-
Wernick, N.L.1
De Luca, H.2
Kam, W.R.3
Lencer, W.I.4
-
53
-
-
79551714334
-
A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection
-
Walczak CP, Tsai B, (2011) A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. J Virol 85: 2386–2396. doi: 10.1128/JVI.01855-10 21159867
-
(2011)
J Virol
, vol.85
, pp. 2386-2396
-
-
Walczak, C.P.1
Tsai, B.2
-
54
-
-
84940776888
-
The ER membrane J protein C18 executes a distinct role in promoting SV40 membrane penetration
-
Bagchi P, Walczak CP, Tsai B, (2015) The ER membrane J protein C18 executes a distinct role in promoting SV40 membrane penetration. J Virol.
-
(2015)
J Virol
-
-
Bagchi, P.1
Walczak, C.P.2
Tsai, B.3
-
55
-
-
33646444561
-
Chaperone-mediated in vitro disassembly of polyoma- and papillomaviruses
-
Chromy LR, Oltman A, Estes PA, Garcea RL, (2006) Chaperone-mediated in vitro disassembly of polyoma- and papillomaviruses. J Virol 80: 5086–5091. 16641302
-
(2006)
J Virol
, vol.80
, pp. 5086-5091
-
-
Chromy, L.R.1
Oltman, A.2
Estes, P.A.3
Garcea, R.L.4
-
56
-
-
84906096557
-
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
-
Mattoo RU, Goloubinoff P, (2014) Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins. Cell Mol Life Sci 71: 3311–3325. doi: 10.1007/s00018-014-1627-y 24760129
-
(2014)
Cell Mol Life Sci
, vol.71
, pp. 3311-3325
-
-
Mattoo, R.U.1
Goloubinoff, P.2
-
57
-
-
29244432181
-
Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
-
Yam AY, Albanese V, Lin HT, Frydman J, (2005) Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J Biol Chem 280: 41252–41261. 16219770
-
(2005)
J Biol Chem
, vol.280
, pp. 41252-41261
-
-
Yam, A.Y.1
Albanese, V.2
Lin, H.T.3
Frydman, J.4
-
59
-
-
84870907436
-
Cleaning up: ER-associated degradation to the rescue
-
Brodsky JL, (2012) Cleaning up: ER-associated degradation to the rescue. Cell 151: 1163–1167. doi: 10.1016/j.cell.2012.11.012 23217703
-
(2012)
Cell
, vol.151
, pp. 1163-1167
-
-
Brodsky, J.L.1
-
60
-
-
84897986050
-
Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR
-
Houck SA, Ren HY, Madden VJ, Bonner JN, Conlin MP, et al. (2014) Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR. Mol Cell 54: 166–179. doi: 10.1016/j.molcel.2014.02.025 24685158
-
(2014)
Mol Cell
, vol.54
, pp. 166-179
-
-
Houck, S.A.1
Ren, H.Y.2
Madden, V.J.3
Bonner, J.N.4
Conlin, M.P.5
-
61
-
-
79551678082
-
The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508
-
Grove DE, Fan CY, Ren HY, Cyr DM, (2011) The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Mol Biol Cell 22: 301–314. doi: 10.1091/mbc.E10-09-0760 21148293
-
(2011)
Mol Biol Cell
, vol.22
, pp. 301-314
-
-
Grove, D.E.1
Fan, C.Y.2
Ren, H.Y.3
Cyr, D.M.4
-
62
-
-
79952524195
-
A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR
-
Yamamoto YH, Kimura T, Momohara S, Takeuchi M, Tani T, et al. (2010) A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR. Cell Struct Funct 35: 107–116. 21150129
-
(2010)
Cell Struct Funct
, vol.35
, pp. 107-116
-
-
Yamamoto, Y.H.1
Kimura, T.2
Momohara, S.3
Takeuchi, M.4
Tani, T.5
-
63
-
-
36349015924
-
The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
-
Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, et al. (2007) The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). J Biol Chem 282: 32665–32675. 17823116
-
(2007)
J Biol Chem
, vol.282
, pp. 32665-32675
-
-
Hrizo, S.L.1
Gusarova, V.2
Habiel, D.M.3
Goeckeler, J.L.4
Fisher, E.A.5
-
64
-
-
0030886889
-
Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
-
Hazes B, Read RJ, (1997) Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 36: 11051–11054. 9333321
-
(1997)
Biochemistry
, vol.36
, pp. 11051-11054
-
-
Hazes, B.1
Read, R.J.2
-
65
-
-
12244305596
-
Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation
-
Rodighiero C, Tsai B, Rapoport TA, Lencer WI, (2002) Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation. EMBO Rep 3: 1222–1227. 12446567
-
(2002)
EMBO Rep
, vol.3
, pp. 1222-1227
-
-
Rodighiero, C.1
Tsai, B.2
Rapoport, T.A.3
Lencer, W.I.4
-
66
-
-
0035818999
-
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. 11740563
-
(2001)
Nature
, vol.414
, pp. 652-656
-
-
Ye, Y.1
Meyer, H.H.2
Rapoport, T.A.3
-
67
-
-
23044460010
-
Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate
-
Kothe M, Ye Y, Wagner JS, De Luca HE, Kern E, et al. (2005) Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate. J Biol Chem 280: 28127–28132. 15932873
-
(2005)
J Biol Chem
, vol.280
, pp. 28127-28132
-
-
Kothe, M.1
Ye, Y.2
Wagner, J.S.3
De Luca, H.E.4
Kern, E.5
-
68
-
-
84885395221
-
Establishment of an in vitro transport assay that reveals mechanistic differences in cytosolic events controlling cholera toxin and T-cell receptor alpha retro-translocation
-
Moore P, He K, Tsai B, (2013) Establishment of an in vitro transport assay that reveals mechanistic differences in cytosolic events controlling cholera toxin and T-cell receptor alpha retro-translocation. Plos One 8: e75801. doi: 10.1371/journal.pone.0075801 24146777
-
(2013)
Plos One
, vol.8
, pp. 75801
-
-
Moore, P.1
He, K.2
Tsai, B.3
-
69
-
-
84857067637
-
Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm
-
Kuksin D, Norkin LC, (2012) Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm. J Virol 86: 1555–1562. doi: 10.1128/JVI.05753-11 22090139
-
(2012)
J Virol
, vol.86
, pp. 1555-1562
-
-
Kuksin, D.1
Norkin, L.C.2
-
70
-
-
0028808230
-
Role of auxilin in uncoating clathrin-coated vesicles
-
Ungewickell E, Ungewickell H, Holstein SE, Lindner R, Prasad K, et al. (1995) Role of auxilin in uncoating clathrin-coated vesicles. Nature 378: 632–635. 8524399
-
(1995)
Nature
, vol.378
, pp. 632-635
-
-
Ungewickell, E.1
Ungewickell, H.2
Holstein, S.E.3
Lindner, R.4
Prasad, K.5
-
71
-
-
0027358782
-
A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase
-
Prasad K, Barouch W, Greene L, Eisenberg E, (1993) A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase. J Biol Chem 268: 23758–23761. 8226905
-
(1993)
J Biol Chem
, vol.268
, pp. 23758-23761
-
-
Prasad, K.1
Barouch, W.2
Greene, L.3
Eisenberg, E.4
-
72
-
-
0024595608
-
Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation
-
Heuser JE, Anderson RG, (1989) Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation. J Cell Biol 108: 389–400. 2563728
-
(1989)
J Cell Biol
, vol.108
, pp. 389-400
-
-
Heuser, J.E.1
Anderson, R.G.2
-
73
-
-
28544442609
-
Protein translocation across biological membranes
-
Wickner W, Schekman R, (2005) Protein translocation across biological membranes. Science 310: 1452–1456. 16322447
-
(2005)
Science
, vol.310
, pp. 1452-1456
-
-
Wickner, W.1
Schekman, R.2
-
74
-
-
0033612302
-
BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
-
Matlack KE, Misselwitz B, Plath K, Rapoport TA, (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97: 553–564. 10367885
-
(1999)
Cell
, vol.97
, pp. 553-564
-
-
Matlack, K.E.1
Misselwitz, B.2
Plath, K.3
Rapoport, T.A.4
-
75
-
-
37249017924
-
Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells
-
Tanimura S, Hirano AI, Hashizume J, Yasunaga M, Kawabata T, et al. (2007) Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells. J Biol Chem 282: 35430–35439. 17855353
-
(2007)
J Biol Chem
, vol.282
, pp. 35430-35439
-
-
Tanimura, S.1
Hirano, A.I.2
Hashizume, J.3
Yasunaga, M.4
Kawabata, T.5
-
76
-
-
70350005336
-
Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response
-
Uemura A, Oku M, Mori K, Yoshida H, (2009) Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response. J Cell Sci 122: 2877–2886. doi: 10.1242/jcs.040584 19622636
-
(2009)
J Cell Sci
, vol.122
, pp. 2877-2886
-
-
Uemura, A.1
Oku, M.2
Mori, K.3
Yoshida, H.4
-
77
-
-
0347033285
-
BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
-
Chung KT, Shen Y, Hendershot LM, (2002) BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 277: 47557–47563. 12356756
-
(2002)
J Biol Chem
, vol.277
, pp. 47557-47563
-
-
Chung, K.T.1
Shen, Y.2
Hendershot, L.M.3
-
78
-
-
0346727523
-
Coordinated activation of Hsp70 chaperones
-
Steel GJ, Fullerton DM, Tyson JR, Stirling CJ, (2004) Coordinated activation of Hsp70 chaperones. Science 303: 98–101. 14704430
-
(2004)
Science
, vol.303
, pp. 98-101
-
-
Steel, G.J.1
Fullerton, D.M.2
Tyson, J.R.3
Stirling, C.J.4
|