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Volumn 10, Issue 1, 2015, Pages

Human mitochondrial Hsp70 (mortalin): Shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 1A; MAGNESIUM ION; MITOCHONDRIAL PROTEIN; MORTALIN; UNCLASSIFIED DRUG; HSPA9 PROTEIN, HUMAN; MAGNESIUM; RECOMBINANT PROTEIN;

EID: 84921713006     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0117170     Document Type: Article
Times cited : (45)

References (71)
  • 1
    • 0027414085 scopus 로고
    • Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype
    • PMID: 8454632
    • Wadhwa R, Kaul SC, Ikawa Y, Sugimoto Y (1993) Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype. J Biol Chem 268: 6615-6621. PMID: 8454632
    • (1993) J Biol Chem , vol.268 , pp. 6615-6621
    • Wadhwa, R.1    Kaul, S.C.2    Ikawa, Y.3    Sugimoto, Y.4
  • 2
    • 0028926541 scopus 로고
    • Cloning and subcellular localization of human mitochondrial hsp70
    • PMID: 7829505
    • Bhattacharyya T, Karnezis AN, Murphy SP, Hoang T, Freeman BC, et al. (1995) Cloning and Subcellular Localization of Human Mitochondrial hsp70. J Biol Chem 270: 1705-1710. doi: 10.1074/jbc.270.4. 1705 PMID: 7829505
    • (1995) J Biol Chem , vol.270 , pp. 1705-1710
    • Bhattacharyya, T.1    Karnezis, A.N.2    Murphy, S.P.3    Hoang, T.4    Freeman, B.C.5
  • 3
    • 0027263325 scopus 로고
    • Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family
    • PMID: 7684501
    • Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK (1993) Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol Cell Biol 13: 3598-3610. PMID: 7684501
    • (1993) Mol Cell Biol , vol.13 , pp. 3598-3610
    • Domanico, S.Z.1    DeNagel, D.C.2    Dahlseid, J.N.3    Green, J.M.4    Pierce, S.K.5
  • 4
    • 84994618255 scopus 로고    scopus 로고
    • Mortalin, Apoptosis, and Neurodegeneration
    • PMID: 24970131
    • Londono C, Osorio C, Gama V, Alzate O (2012) Mortalin, Apoptosis, and Neurodegeneration. Biomolecules 2: 143-164. doi: 10.3390/biom2010143 PMID: 24970131
    • (2012) Biomolecules , vol.2 , pp. 143-164
    • Londono, C.1    Osorio, C.2    Gama, V.3    Alzate, O.4
  • 5
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • PMID: 11156371
    • Wadhwa R, Sugihara T, Yoshida A, Nomura H, Reddel RR, et al. (2000) Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res 60: 6818-6821. PMID: 11156371
    • (2000) Cancer Res , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5
  • 6
    • 0036346345 scopus 로고    scopus 로고
    • Hsp70 family member, mot-2/ mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein
    • PMID: 11900485
    • Wadhwa R, Yaguchi T, Hasan K, Mitsui Y, Reddel RR, et al. (2002) Hsp70 family member, mot-2/ mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein. Exp Cell Res 274: 246-253. doi: 10.1006/excr.2002.5468 PMID: 11900485
    • (2002) Exp Cell Res , vol.274 , pp. 246-253
    • Wadhwa, R.1    Yaguchi, T.2    Hasan, K.3    Mitsui, Y.4    Reddel, R.R.5
  • 7
    • 33847651284 scopus 로고    scopus 로고
    • Three faces of mortalin: A housekeeper, guardian and killer
    • PMID: 17188442
    • Kaul SC, Deocaris CC, Wadhwa R (2007) Three faces of mortalin: A housekeeper, guardian and killer. Exp Gerontol 42: 263-274. doi: 10.1016/j.exger.2006.10.020 PMID: 17188442
    • (2007) Exp Gerontol , vol.42 , pp. 263-274
    • Kaul, S.C.1    Deocaris, C.C.2    Wadhwa, R.3
  • 8
    • 79952133235 scopus 로고    scopus 로고
    • Function of cytosolic chaperones in Tom70-mediated mitochondrial import
    • Fan ACY, Young JC (2011) Function of Cytosolic Chaperones in Tom70-Mediated Mitochondrial Import. Prot Pept Lett 18: 122-131. doi: 10.2174/092986611794475020
    • (2011) Prot Pept Lett , vol.18 , pp. 122-131
    • Fan, A.C.Y.1    Young, J.C.2
  • 9
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • PMID: 16857931
    • Dolezal P, Likic V, Tachezy J, Lithgow T (2006) Evolution of the molecular machines for protein import into mitochondria. Science 313: 314-318. doi: 10.1126/science.1127895 PMID: 16857931
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 10
    • 56349144637 scopus 로고    scopus 로고
    • Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling
    • Mokranjac D, NeupertW(2009) Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling. BBA-Mol Cell Res 1793: 33-41.
    • (2009) BBA-Mol Cell Res , vol.1793 , pp. 33-41
    • Mokranjac, D.1    Neupert, W.2
  • 11
    • 34249897492 scopus 로고    scopus 로고
    • A dynamic machinery for import of mitochondrial precursor proteins
    • PMID: 17376437
    • Bohnert M, Pfanner N, van der Laan M (2007) A dynamic machinery for import of mitochondrial precursor proteins. Febs Lett 581: 2802-2810. doi: 10.1016/j.febslet.2007.03.004 PMID: 17376437
    • (2007) Febs Lett , vol.581 , pp. 2802-2810
    • Bohnert, M.1    Pfanner, N.2    Van Der Laan, M.3
  • 12
    • 0034595925 scopus 로고    scopus 로고
    • Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2
    • Kaul SC, Reddel RR, Sugihara T, Mitsui Y, Wadhwa R (2000) Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2. Febs Lett 474: 159-164. doi: 10.1016/S0014-5793(00) 01594-5
    • (2000) Febs Lett , vol.474 , pp. 159-164
    • Kaul, S.C.1    Reddel, R.R.2    Sugihara, T.3    Mitsui, Y.4    Wadhwa, R.5
  • 13
    • 33646409045 scopus 로고    scopus 로고
    • Upregulation of mortalin/ mthsp70/Grp75 contributes to human carcinogenesis
    • Wadhwa R, Takano S, Kaur K, Deocaris CC, Pereira-Smith OM, et al. (2006) Upregulation of mortalin/ mthsp70/Grp75 contributes to human carcinogenesis. Inter J Cancer 118: 2973-2980. doi: 10.1002/ ijc.21773
    • (2006) Inter J Cancer , vol.118 , pp. 2973-2980
    • Wadhwa, R.1    Takano, S.2    Kaur, K.3    Deocaris, C.C.4    Pereira-Smith, O.M.5
  • 14
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells
    • PMID: 20974113
    • Qu M, Zhou Z, Xu S, Chen C, Yu Z, et al. (2011) Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells. Brain Res 1368: 336-345. doi: 10.1016/j.brainres.2010.10.068 PMID: 20974113
    • (2011) Brain Res , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5
  • 15
    • 14244268253 scopus 로고    scopus 로고
    • Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells
    • PMID: 15724436
    • Liu Y, Liu W, Song XD, Zuo J (2005) Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Mol Cell Biochem 268: 45-51. doi: 10.1007/s11010-005-2996-1 PMID: 15724436
    • (2005) Mol Cell Biochem , vol.268 , pp. 45-51
    • Liu, Y.1    Liu, W.2    Song, X.D.3    Zuo, J.4
  • 16
    • 33746296891 scopus 로고    scopus 로고
    • Proteomic identification of a stress protein, mortalin/mthsp70/GRP75-Relevance to Parkinson disease
    • PMID: 16565515
    • Jin JH, Hulette C, Wang Y, Zhang T, Pan C, et al. (2006) Proteomic identification of a stress protein, mortalin/mthsp70/GRP75-Relevance to Parkinson disease. Mol Cell Proteomics 5: 1193-1204. doi: 10.1074/mcp.M500382-MCP200 PMID: 16565515
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1193-1204
    • Jin, J.H.1    Hulette, C.2    Wang, Y.3    Zhang, T.4    Pan, C.5
  • 17
    • 59149091608 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia
    • PMID: 18985056
    • Xu L, Voloboueva LA, Ouyang Y, Emery JF, Giffard RG (2008) Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J Cereb Blood Flow Metab 29: 365-374. doi: 10.1038/jcbfm.2008.125 PMID: 18985056
    • (2008) J Cereb Blood Flow Metab , vol.29 , pp. 365-374
    • Xu, L.1    Voloboueva, L.A.2    Ouyang, Y.3    Emery, J.F.4    Giffard, R.G.5
  • 18
    • 27444442414 scopus 로고    scopus 로고
    • Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60
    • PMID: 15957980
    • Wadhwa R, Takano S, Kaur K, Aida S, Yaguchi T, et al. (2005) Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60. Biochem J 391: 185- 190. doi: 10.1042/ BJ20050861 PMID: 15957980
    • (2005) Biochem J , vol.391 , pp. 185-190
    • Wadhwa, R.1    Takano, S.2    Kaur, K.3    Aida, S.4    Yaguchi, T.5
  • 19
    • 3042778732 scopus 로고    scopus 로고
    • Mitochondrial import and the twin-pore translocase
    • PMID: 15232570
    • Rehling P, Brandner K, Pfanner N (2004) Mitochondrial import and the twin-pore translocase. Nat Rev Mol Cell Biol 5: 519-530. doi: 10.1038/nrm1426 PMID: 15232570
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 519-530
    • Rehling, P.1    Brandner, K.2    Pfanner, N.3
  • 20
    • 4644278673 scopus 로고    scopus 로고
    • Hsp70 and Hsp90-a relay team for protein folding
    • PMID: 14740253
    • Wegele H, Muller L, Buchner J (2004) Hsp70 and Hsp90-a relay team for protein folding. Rev Physiol Biochem Pharmacol 151: 1-44. doi: 10.1007/s10254-003-0021-1 PMID: 14740253
    • (2004) Rev Physiol Biochem Pharmacol , vol.151 , pp. 1-44
    • Wegele, H.1    Muller, L.2    Buchner, J.3
  • 21
    • 27744517366 scopus 로고    scopus 로고
    • Heat shock proteins as emerging therapeutic targets
    • PMID: 16170327
    • Soti C, Nagy E, Giricz Z, Vigh L, Csermely P, et al. (2005) Heat shock proteins as emerging therapeutic targets. Br J Pharmacol 146: 769-780. doi: 10.1038/sj.bjp.0706396 PMID: 16170327
    • (2005) Br J Pharmacol , vol.146 , pp. 769-780
    • Soti, C.1    Nagy, E.2    Giricz, Z.3    Vigh, L.4    Csermely, P.5
  • 22
    • 79952158492 scopus 로고    scopus 로고
    • The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism
    • PMID: 21121894
    • da Silva KP, Borges JC (2011) The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism. Protein Pept Lett 18: 132-142. doi: 10.2174/ 092986611794475057 PMID: 21121894
    • (2011) Protein Pept Lett , vol.18 , pp. 132-142
    • Da Silva, K.P.1    Borges, J.C.2
  • 23
    • 68649113747 scopus 로고    scopus 로고
    • The role of molecular chaperones in human misfolding diseases
    • PMID: 19393652
    • Broadley SA, Hartl FU (2009) The role of molecular chaperones in human misfolding diseases. FEBS Lett 583: 2647-2653. doi: 10.1016/j.febslet.2009.04.029 PMID: 19393652
    • (2009) FEBS Lett , vol.583 , pp. 2647-2653
    • Broadley, S.A.1    Hartl, F.U.2
  • 25
    • 0027425062 scopus 로고
    • Induction of cellular senescence by transfection of cytosolic mortalin Cdna in Nih-3T3-Cells
    • PMID: 7693662
    • Wadhwa R, Kaul SC, Sugimoto Y, Mitsui Y (1993) Induction of Cellular Senescence by Transfection of Cytosolic Mortalin Cdna in Nih-3T3-Cells. J Biol Chem 268: 22239-22242. PMID: 7693662
    • (1993) J Biol Chem , vol.268 , pp. 22239-22242
    • Wadhwa, R.1    Kaul, S.C.2    Sugimoto, Y.3    Mitsui, Y.4
  • 27
    • 0027227379 scopus 로고
    • Differential subcellular-distribution of mortalin in mortal and immortal mouse and human fibroblasts
    • PMID: 8344392
    • Wadhwa R, Kaul SC, Mitsui Y, Sugimoto Y (1993) Differential Subcellular-Distribution of Mortalin in Mortal and Immortal Mouse and Human Fibroblasts. Exp Cell Res 207: 442-448. doi: 10.1006/excr. 1993.1213 PMID: 8344392
    • (1993) Exp Cell Res , vol.207 , pp. 442-448
    • Wadhwa, R.1    Kaul, S.C.2    Mitsui, Y.3    Sugimoto, Y.4
  • 28
    • 0034682972 scopus 로고    scopus 로고
    • Extramitochondrial localization of mortalin/ mthsp70/PBP74/GRP75
    • PMID: 10944461
    • Ran QT, Wadhwa R, Kawai R, Kaul SC, Sifers RN, et al. (2000) Extramitochondrial localization of mortalin/ mthsp70/PBP74/GRP75. Biochem Biophys Res Comm 275: 174-179. doi: 10.1006/bbrc.2000. 3237 PMID: 10944461
    • (2000) Biochem Biophys Res Comm , vol.275 , pp. 174-179
    • Ran, Q.T.1    Wadhwa, R.2    Kawai, R.3    Kaul, S.C.4    Sifers, R.N.5
  • 29
    • 34249291074 scopus 로고    scopus 로고
    • Mortalin sensitizes human cancer cells to MKT-077-induced senescence
    • PMID: 17306926
    • Deocaris CC, Widodo N, Shrestha BG, Kaur K, Ohtaka M, et al. (2007) Mortalin sensitizes human cancer cells to MKT-077-induced senescence. Cancer Lett 252: 259-269. doi: 10.1016/j.canlet.2006.12. 038 PMID: 17306926
    • (2007) Cancer Lett , vol.252 , pp. 259-269
    • Deocaris, C.C.1    Widodo, N.2    Shrestha, B.G.3    Kaur, K.4    Ohtaka, M.5
  • 30
    • 22044447800 scopus 로고    scopus 로고
    • Inactivation of the mitochondrial heat shock protein Zim17 leads to aggregation of matrix Hsp70s followed by plelotropic effects on morphology and protein biogenesis
    • Szklarz LKS, Guiard B, Rissler M, Wiedemann N, Kozjak V, et al. (2005) Inactivation of the mitochondrial heat shock protein Zim17 leads to aggregation of matrix Hsp70s followed by plelotropic effects on morphology and protein biogenesis. J Mol Biol 351: 206-218. doi: 10.1016/j.jmb.2005.05.068
    • (2005) J Mol Biol , vol.351 , pp. 206-218
    • Szklarz, L.K.S.1    Guiard, B.2    Rissler, M.3    Wiedemann, N.4    Kozjak, V.5
  • 31
    • 16344363965 scopus 로고    scopus 로고
    • Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1
    • PMID: 15719019
    • Sichting M, Mokranjac D, Azem A, Neupert W, Hell K (2005) Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J 24: 1046-1056. doi: 10. 1038/sj.emboj.7600580 PMID: 15719019
    • (2005) EMBO J , vol.24 , pp. 1046-1056
    • Sichting, M.1    Mokranjac, D.2    Azem, A.3    Neupert, W.4    Hell, K.5
  • 32
    • 54449089692 scopus 로고    scopus 로고
    • The human escort protein hep binds to the ATPase domain of mitochondrial Hsp70 and regulates ATP hydrolysis
    • PMID: 18632665
    • Zhai P, Stanworth C, Liu S, Silberg JJ (2008) The human escort protein hep binds to the ATPase domain of mitochondrial Hsp70 and regulates ATP hydrolysis. J Biol Chem 283: 26098-26106. doi: 10. 1074/jbc.M803475200 PMID: 18632665
    • (2008) J Biol Chem , vol.283 , pp. 26098-26106
    • Zhai, P.1    Stanworth, C.2    Liu, S.3    Silberg, J.J.4
  • 33
    • 77951106537 scopus 로고    scopus 로고
    • Kinetic and structural characterization of human mortalin
    • PMID: 20152901
    • Luo WI, Dizin E, Yoon T, Cowan JA (2010) Kinetic and structural characterization of human mortalin. Protein Expr Purif 72: 75-81. doi: 10.1016/j.pep.2010.02.003 PMID: 20152901
    • (2010) Protein Expr Purif , vol.72 , pp. 75-81
    • Luo, W.I.1    Dizin, E.2    Yoon, T.3    Cowan, J.A.4
  • 34
    • 84875093357 scopus 로고    scopus 로고
    • Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone
    • PMID: 23462535
    • Dores-Silva PR, Minari K, Ramos CHI, Barbosa LRS, Borges JC (2013) Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone. Int J Biol Macromol 56: 140-148. doi: 10.1016/j.ijbiomac.2013.02.009 PMID: 23462535
    • (2013) Int J Biol Macromol , vol.56 , pp. 140-148
    • Dores-Silva, P.R.1    Minari, K.2    Ramos, C.H.I.3    Barbosa, L.R.S.4    Borges, J.C.5
  • 35
    • 84862913771 scopus 로고    scopus 로고
    • The DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9
    • 10.1002/pro.2012 PMID: 22162012
    • Vu MT, Zhai P, Lee J, Guerra C, Liu S, et al. (2012) The DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9. Protein Sci 21: 258-267. 10.1002/pro.2012. doi: 10.1002/pro.2012 PMID: 22162012
    • (2012) Protein Sci , vol.21 , pp. 258-267
    • Vu, M.T.1    Zhai, P.2    Lee, J.3    Guerra, C.4    Liu, S.5
  • 36
    • 79956221173 scopus 로고    scopus 로고
    • A conserved histidine in human DNLZ/HEP is required for stimulation of HSPA9 ATPase activity
    • Zhai P, Vu MT, Hoff KG, Silberg JJ (2011) A conserved histidine in human DNLZ/HEP is required for stimulation of HSPA9 ATPase activity. Biochem Bioph Res Co 408: 589-594. doi: 10.1016/j.bbrc. 2011.04.066
    • (2011) Biochem Bioph Res Co , vol.408 , pp. 589-594
    • Zhai, P.1    Vu, M.T.2    Hoff, K.G.3    Silberg, J.J.4
  • 37
    • 33746286154 scopus 로고    scopus 로고
    • Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein
    • PMID: 16806043
    • Borges JC, Ramos CHI (2006) Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein. Arch Biochem Biophys 452: 46-54. doi: 10.1016/j.abb.2006.05.006 PMID: 16806043
    • (2006) Arch Biochem Biophys , vol.452 , pp. 46-54
    • Borges, J.C.1    Ramos, C.H.I.2
  • 38
    • 0026530383 scopus 로고
    • Quantitative-Analysis of protein far Uv circular-dichroism spectra by neural networks
    • PMID: 1409538
    • Bohm G, Muhr R, Jaenicke R (1992) Quantitative-Analysis of Protein Far Uv Circular-Dichroism Spectra by Neural Networks. Protein Eng 5: 191-195. doi: 10.1093/protein/5.3.191 PMID: 1409538
    • (1992) Protein Eng , vol.5 , pp. 191-195
    • Bohm, G.1    Muhr, R.2    Jaenicke, R.3
  • 39
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • PMID: 12192063
    • Lebowitz J, Lewis MS, Schuck P (2002) Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci 11: 2067-2079. doi: 10.1110/ps.0207702 PMID: 12192063
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 40
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • PMID: 11806949
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys J 82: 1096-1111. doi: 10.1016/S0006-3495(02)75469-6 PMID: 11806949
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 41
    • 79952787283 scopus 로고    scopus 로고
    • Analysis of molecular targets of mycobacterium tuberculosis by analytical ultracentrifugation
    • PMID: 21366535
    • Borges JC, Ramos CHI (2011) Analysis of molecular targets of mycobacterium tuberculosis by analytical ultracentrifugation. Curr Med Chem 18: 1276-1285. doi: 10.2174/092986711795029537 PMID: 21366535
    • (2011) Curr Med Chem , vol.18 , pp. 1276-1285
    • Borges, J.C.1    Ramos, C.H.I.2
  • 42
    • 0034484513 scopus 로고    scopus 로고
    • SAXS experiments on absolute scale with Kratky systems using water as a secondary standard
    • Orthaber D, Bergmann A, Glatter O (2000) SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J Appl Cryst 33: 218-225. doi: 10.1107/S0021889899015216
    • (2000) J Appl Cryst , vol.33 , pp. 218-225
    • Orthaber, D.1    Bergmann, A.2    Glatter, O.3
  • 43
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • PMID: 10354416
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76: 2879-2886. doi: 10.1016/S0006-3495(99)77443-6 PMID: 10354416
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 44
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 36: 860-864. doi: 10.1107/S0021889803000268
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 45
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • de la Torre JG, Huertas ML, Carrasco B (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78: 719-730. doi: 10.1016/S0006-3495(00)76630-6
    • (2000) Biophys J , vol.78 , pp. 719-730
    • De La Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 46
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-Bound open conformation of Hsp70 chaperones
    • PMID: 23123194
    • Kityk R, Kopp J, Sinning I, Mayer MP (2012) Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones. Mol Cell 48: 863-874. doi: 10.1016/j.molcel.2012.09.023 PMID: 23123194
    • (2012) Mol Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 47
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. Coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • PMID: 19439666
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ERP (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 106: 8471-8476. doi: 10.1073/pnas.0903503106 PMID: 19439666
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.P.4
  • 48
    • 84901840260 scopus 로고    scopus 로고
    • GENFIT: Software for the analysis of small-angle X-ray and neutron scattering data of macromolecules in solution
    • Spinozzi F, Ferrero C, Ortore MG, De Maria Antolinos A, Mariani P (2014) GENFIT: software for the analysis of small-angle X-ray and neutron scattering data of macromolecules in solution. J Appl Cryst 47: 1132-1139. doi: 10.1107/S1600576714005147
    • (2014) J Appl Cryst , vol.47 , pp. 1132-1139
    • Spinozzi, F.1    Ferrero, C.2    Ortore, M.G.3    De Maria Antolinos, A.4    Mariani, P.5
  • 49
    • 69949130768 scopus 로고    scopus 로고
    • Combining structure and dynamics: Non-denaturing high-pressure effect on lysozyme in solution
    • PMID: 19570795
    • Ortore MG, Spinozzi F, Mariani P, Paciaroni A, Barbosa LRS, et al. (2009) Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution. J R Soc Interface 6: S619-S634. doi: 10.1098/rsif.2009.0163.focus PMID: 19570795
    • (2009) J R Soc Interface , vol.6 , pp. S619-S634
    • Ortore, M.G.1    Spinozzi, F.2    Mariani, P.3    Paciaroni, A.4    Barbosa, L.R.S.5
  • 50
    • 84871721498 scopus 로고    scopus 로고
    • Structural and functional studies of Leishmania braziliensis Hsp90
    • Silva KP, Seraphim TV, Borges JC (2013) Structural and functional studies of Leishmania braziliensis Hsp90. BBA-Proteins Proteom 1834: 351-361. doi: 10.1016/j.bbapap.2012.08.004
    • (2013) BBA-Proteins Proteom , vol.1834 , pp. 351-361
    • Silva, K.P.1    Seraphim, T.V.2    Borges, J.C.3
  • 51
    • 67449094633 scopus 로고    scopus 로고
    • Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70.1 by analytical ultracentrifugation
    • PMID: 19336004
    • Borges JC, Ramos CHI (2009) Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70.1 by analytical ultracentrifugation. BMB Rep 42: 166-171. doi: 10.5483/BMBRep.2009.42.3.166 PMID: 19336004
    • (2009) BMB Rep , vol.42 , pp. 166-171
    • Borges, J.C.1    Ramos, C.H.I.2
  • 52
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • PMID: 1829527
    • Palleros DR, Welch WJ, Fink AL (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc Natl Acad Sci U S A 88: 5719-5723. doi: 10.1073/ pnas.88.13.5719 PMID: 1829527
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 53
    • 0033605086 scopus 로고    scopus 로고
    • Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling
    • PMID: 10024459
    • Montgomery DL, Morimoto RI, Gierasch LM (1999) Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. J Mol Biol 286: 915-932. doi: 10.1006/jmbi.1998.2514 PMID: 10024459
    • (1999) J Mol Biol , vol.286 , pp. 915-932
    • Montgomery, D.L.1    Morimoto, R.I.2    Gierasch, L.M.3
  • 54
    • 0027485771 scopus 로고
    • DnaK ATPase activity revisited
    • PMID: 8262193
    • Palleros DR, Reid KL, Shi L, Fink AL (1993) DnaK ATPase activity revisited. Febs Letters 336: 124-128. doi: 10.1016/0014-5793(93)81624-9 PMID: 8262193
    • (1993) Febs Letters , vol.336 , pp. 124-128
    • Palleros, D.R.1    Reid, K.L.2    Shi, L.3    Fink, A.L.4
  • 55
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin MB, Svergun DI (2001) Automated matching of high- and low-resolution structural models. J Appl Cryst 34: 33-41. doi: 10.1107/S0021889800014126
    • (2001) J Appl Cryst , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 57
    • 84904261221 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone
    • PMID: 24687350
    • Amick J, Schlanger SE, Wachnowsky C, Moseng MA, Emerson CC, et al. (2014) Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone. Protein Sci 23: 833-842. doi: 10.1002/pro.2466 PMID: 24687350
    • (2014) Protein Sci , vol.23 , pp. 833-842
    • Amick, J.1    Schlanger, S.E.2    Wachnowsky, C.3    Moseng, M.A.4    Emerson, C.C.5
  • 58
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • PMID: 8658133
    • Zhu XT, Zhao X, Burkholder WF, Gragerov A, Ogata CM, et al. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272: 1606-1614. doi: 10.1126/science.272.5268. 1606 PMID: 8658133
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.T.1    Zhao, X.2    Burkholder, W.F.3    Gragerov, A.4    Ogata, C.M.5
  • 59
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • PMID: 17052976
    • Vogel M, Mayer MP, Bukau B (2006) Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem 281: 38705-38711. doi: 10.1074/jbc.M609020200 PMID: 17052976
    • (2006) J Biol Chem , vol.281 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 60
    • 0026768015 scopus 로고
    • DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat
    • Palleros DR, Reid KL, McCarty JS, Walker GC, Fink AL (1992) DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat. J Biol Chem 267: 5279-5285.
    • (1992) J Biol Chem , vol.267 , pp. 5279-5285
    • Palleros, D.R.1    Reid, K.L.2    McCarty, J.S.3    Walker, G.C.4    Fink, A.L.5
  • 61
    • 58649109565 scopus 로고    scopus 로고
    • Functional characterization of the DnaK chaperone system from the archaeon Methanothermobacter thermautotrophicus +öH
    • PMID: 19162025
    • Popp SL, Reinstein J (2009) Functional characterization of the DnaK chaperone system from the archaeon Methanothermobacter thermautotrophicus +öH. FEBS Lett 583: 573-578. doi: 10.1016/j. febslet.2008.12.062 PMID: 19162025
    • (2009) FEBS Lett , vol.583 , pp. 573-578
    • Popp, S.L.1    Reinstein, J.2
  • 62
    • 0034127485 scopus 로고    scopus 로고
    • Structural insights into substrate binding by the molecular chaperone DnaK
    • PMID: 10742174
    • Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, et al. (2000) Structural insights into substrate binding by the molecular chaperone DnaK. Nat Struct Biol 7: 298-303. doi: 10.1038/ 74062 PMID: 10742174
    • (2000) Nat Struct Biol , vol.7 , pp. 298-303
    • Pellecchia, M.1    Montgomery, D.L.2    Stevens, S.Y.3    Vander Kooi, C.W.4    Feng, H.P.5
  • 63
    • 84890860170 scopus 로고    scopus 로고
    • Identification of an allosteric pocket on human Hsp70 reveals a mode of inhibition of this therapeutically important protein
    • Rodina A, Patel P, Kang Y, Patel Y, Baaklini I, et al. (2013) Identification of an Allosteric Pocket on Human Hsp70 Reveals a Mode of Inhibition of This Therapeutically Important Protein. Chem Biol 20: 1-12. doi: 10.1016/j.chembiol.2013.10.008
    • (2013) Chem Biol , vol.20 , pp. 1-12
    • Rodina, A.1    Patel, P.2    Kang, Y.3    Patel, Y.4    Baaklini, I.5
  • 64
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric Drugs: The interaction of antitumor compound MKT-077 with human Hsp70 chaperones
    • PMID: 21708173
    • Rousaki A, Miyata Y, Jinwal UK, Dickey CA, Gestwicki JE, et al. (2011) Allosteric Drugs: The Interaction of Antitumor Compound MKT-077 with Human Hsp70 Chaperones. J Mol Biol 411: 614-632. doi: 10. 1016/j.jmb.2011.06.003 PMID: 21708173
    • (2011) J Mol Biol , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3    Dickey, C.A.4    Gestwicki, J.E.5
  • 65
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • PMID: 1835085
    • McCarty JS, Walker GC (1991) DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc Natl Acad Sci U S A 88: 9513-9517. doi: 10.1073/pnas.88.21. 9513 PMID: 1835085
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 66
    • 0034678084 scopus 로고    scopus 로고
    • Kinetic Characterization of the ATPase cycle of the molecular chaperone Hsc66 from escherichia coli
    • PMID: 10713091
    • Silberg JJ, Vickery LE (2000) Kinetic Characterization of the ATPase Cycle of the Molecular Chaperone Hsc66 from Escherichia coli. J Biol Chem 275: 7779-7786. doi: 10.1074/jbc.275.11.7779 PMID: 10713091
    • (2000) J Biol Chem , vol.275 , pp. 7779-7786
    • Silberg, J.J.1    Vickery, L.E.2
  • 67
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
    • PMID: 1356434
    • Sadis S, Hightower LE (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31: 9406-9412. doi: 10.1021/bi00154a012 PMID: 1356434
    • (1992) Biochemistry , vol.31 , pp. 9406-9412
    • Sadis, S.1    Hightower, L.E.2
  • 68
    • 0027519155 scopus 로고
    • Aspartyl residue 10 is essential for ATPase activity of rat hsc70
    • PMID: 8420978
    • Huang SP, Tsai MY, Tzou YM, Wu WG, Wang C (1993) Aspartyl residue 10 is essential for ATPase activity of rat hsc70. J Biol Chem 268: 2063-2068. PMID: 8420978
    • (1993) J Biol Chem , vol.268 , pp. 2063-2068
    • Huang, S.P.1    Tsai, M.Y.2    Tzou, Y.M.3    Wu, W.G.4    Wang, C.5
  • 69
    • 84899455497 scopus 로고    scopus 로고
    • In-vitro characterization of bacterial and chloroplast Hsp70 systems reveals an evolutionary optimization of the co-chaperones for their Hsp70 partner
    • PMID: 24564700
    • Veyel D, Sommer F, Muranaka LS, Rtgers M, Lemaire SD, et al. (2014) In-vitro characterization of bacterial and chloroplast Hsp70 systems reveals an evolutionary optimization of the co-chaperones for their Hsp70 partner. Biochem J 460: 13-24. doi: 10.1042/BJ20140001 PMID: 24564700
    • (2014) Biochem J , vol.460 , pp. 13-24
    • Veyel, D.1    Sommer, F.2    Muranaka, L.S.3    Rtgers, M.4    Lemaire, S.D.5
  • 70
    • 0032417527 scopus 로고    scopus 로고
    • The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains
    • PMID: 9860955
    • Lopez-Buesa P, Pfund C, Craig EA (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95: 15253-15258. doi: 10.1073/pnas.95.26.15253 PMID: 9860955
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15253-15258
    • Lopez-Buesa, P.1    Pfund, C.2    Craig, E.A.3
  • 71
    • 84900531605 scopus 로고    scopus 로고
    • Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
    • PMID: 24739062
    • Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Junior RS, et al. (2014) Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry 53: 2884-2889. doi: 10.1021/bi500004q PMID: 24739062
    • (2014) Biochemistry , vol.53 , pp. 2884-2889
    • Araujo, T.L.S.1    Borges, J.C.2    Ramos, C.H.I.3    Meyer-Fernandes, J.R.4    Oliveira Junior, R.S.5


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