메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Functional analysis of Hsp70 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 PHENYLETHYNESULFONAMIDE; ANTINEOPLASTIC AGENT; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 INHIBITOR; UNCLASSIFIED DRUG; VER 155008;

EID: 84893203556     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0078443     Document Type: Article
Times cited : (174)

References (58)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • doi:10.1038/nature10317
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332. doi:10.1038/nature10317.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • Pearl LH, Prodromou C (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-294. doi:10.1146/annurev.biochem.75.103004.142738. (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 3
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: Implications in aging and disease
    • doi:10.1146/annurev-biochem-060809-095203
    • Anckar J, Sistonen L (2011) Regulation of HSF1 function in the heat stress response: implications in aging and disease. Annu Rev Biochem 80: 1089-1115. doi:10.1146/annurev-biochem-060809-095203.
    • (2011) Annu Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 4
    • 51949087754 scopus 로고    scopus 로고
    • Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response
    • doi:10.1128/MMBR.00007-08
    • Guisbert E, Yura T, Rhodius VA, Gross CA (2008) Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response. Microbiol Mol Biol Rev 72: 545-554. doi:10.1128/MMBR.00007- 08.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 545-554
    • Guisbert, E.1    Yura, T.2    Rhodius, V.A.3    Gross, C.A.4
  • 5
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • DOI 10.1016/S0962-8924(00)01874-2, PII S0962892400018742
    • Beere HM, Green DR (2001) Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol 11: 6-10. (Pubitemid 32056181)
    • (2001) Trends in Cell Biology , vol.11 , Issue.1 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 6
    • 68649113747 scopus 로고    scopus 로고
    • The role of molecular chaperones in human misfolding diseases
    • doi:10.1016/j.febslet. 2009.04.029
    • Broadley SA, Hartl FU (2009) The role of molecular chaperones in human misfolding diseases. FEBS LETTERS 583: 2647-2653. doi:10.1016/j.febslet. 2009.04.029.
    • (2009) FEBS LETTERS , vol.583 , pp. 2647-2653
    • Broadley, S.A.1    Hartl, F.U.2
  • 7
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • doi:10.1007/s00018-004-4464-6
    • Mayer MP, Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62: 670-684. doi:10.1007/s00018-004-4464- 6.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 8
    • 0032564386 scopus 로고    scopus 로고
    • Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ
    • DOI 10.1021/bi981762y
    • Pierpaoli EV, Gisler SM, Christen P (1998) Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 37: 16741-16748. doi:10.1021/bi981762y. (Pubitemid 28543936)
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16741-16748
    • Pierpaoli, E.V.1    Gisler, S.M.2    Christen, P.3
  • 9
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid D, Baici A, Gehring H, Christen P (1994) Kinetics of molecular chaperone action. Science 263: 971-973. (Pubitemid 24094562)
    • (1994) Science , vol.263 , Issue.5149 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 10
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • DOI 10.1038/76819
    • Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, et al. (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol 7: 586-593. doi:10.1038/76819. (Pubitemid 30445917)
    • (2000) Nature Structural Biology , vol.7 , Issue.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 11
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • DOI 10.1038/sj.onc.1207529
    • Mosser DD, Morimoto RI (2004) Molecular chaperones and the stress of oncogenesis. Oncogene 23: 2907-2918. doi:10.1038/sj.onc.1207529. (Pubitemid 38638852)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 12
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • doi:10.1038/sj.onc.1203753
    • Clarke PA, Hostein I, Banerji U, Stefano FD, Maloney A, et al. (2000) Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene 19: 4125-4133. doi:10.1038/sj.onc. 1203753.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3    Stefano, F.D.4    Maloney, A.5
  • 13
    • 77953576838 scopus 로고    scopus 로고
    • Targeting HSP70: The second potentially druggable heat shock protein and molecular chaperone?
    • Powers MV, Jones K, Barillari C, Westwood I, van Montfort RLM, et al. (2010) Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone? Cell Cycle 9: 1542-1550.
    • (2010) Cell Cycle , vol.9 , pp. 1542-1550
    • Powers, M.V.1    Jones, K.2    Barillari, C.3    Westwood, I.4    Van Montfort, R.L.M.5
  • 15
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • doi:10.1016/j.ccr.2008.08.002
    • Powers MV, Clarke PA, Workman P (2008) Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis. Cancer Cell 14: 250-262. doi:10.1016/j.ccr.2008.08.002.
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 16
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • doi:10.1021/ci800324m
    • Halgren TA (2009) Identifying and characterizing binding sites and assessing druggability. J Chem Inf Model 49: 377-389. doi:10.1021/ci800324m.
    • (2009) J Chem Inf Model , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 18
    • 31544442176 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones by a proline switch
    • doi:10.1016/j.molcel. 2005.12.017
    • Vogel M, Bukau B, Mayer MP (2006) Allosteric regulation of Hsp70 chaperones by a proline switch. Molecular Cell 21: 359-367. doi:10.1016/j. molcel. 2005.12.017.
    • (2006) Molecular Cell , vol.21 , pp. 359-367
    • Vogel, M.1    Bukau, B.2    Mayer, M.P.3
  • 19
    • 84880167772 scopus 로고    scopus 로고
    • Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
    • doi:10.1038/nsmb.2583
    • Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, et al. (2013) Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat Struct Mol Biol: 1-10. doi:10.1038/nsmb.2583.
    • (2013) Nat Struct Mol Biol , pp. 1-10
    • Qi, R.1    Sarbeng, E.B.2    Liu, Q.3    Le, K.Q.4    Xu, X.5
  • 20
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • doi:10.1016/j.cell.2012.11.002
    • Zhuravleva A, Clerico EM, Gierasch LM (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151: 1296-1307. doi:10.1016/j.cell.2012.11.002.
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 21
    • 84871689599 scopus 로고    scopus 로고
    • Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
    • doi:10.1016/j.molcel.2012.09.023
    • Kityk R, Kopp J, Sinning I, Mayer MP (2012) Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones. Molecular Cell 48: 821-823. doi:10.1016/j.molcel.2012.09.023.
    • (2012) Molecular Cell , vol.48 , pp. 821-823
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 22
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • doi:10.1038/nrm2941
    • 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.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 23
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • DOI 10.1016/j.ab.2007.08.020, PII S0003269707005416
    • Chang L, Bertelsen EB, Wisén S, Larsen EM, Zuiderweg ERP, et al. (2008) High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Analytical Biochemistry 372: 167-176. doi:10.1016/j.ab.2007.08.020. (Pubitemid 350116767)
    • (2008) Analytical Biochemistry , vol.372 , Issue.2 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.P.5    Gestwicki, J.E.6
  • 24
    • 64349121987 scopus 로고    scopus 로고
    • Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design
    • doi:10.1021/jm801627a
    • Williamson DS, Borgognoni J, Clay A, Daniels Z, Dokurno P, et al. (2009) Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design. J Med Chem 52: 1510-1513. doi:10.1021/jm801627a.
    • (2009) J Med Chem , vol.52 , pp. 1510-1513
    • Williamson, D.S.1    Borgognoni, J.2    Clay, A.3    Daniels, Z.4    Dokurno, P.5
  • 26
    • 70349768075 scopus 로고    scopus 로고
    • A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
    • doi:10.1016/j.molcel.2009.09.023
    • Leu JI-J, Pimkina J, Frank A, Murphy ME, George DL (2009) A Small Molecule Inhibitor of Inducible Heat Shock Protein 70. Molecular Cell 36: 15-27. doi:10.1016/j.molcel.2009.09.023.
    • (2009) Molecular Cell , vol.36 , pp. 15-27
    • Leu, J.I.-J.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 27
    • 79960694363 scopus 로고    scopus 로고
    • HSP70 Inhibition by the Small-Molecule 2-Phenylethynesulfonamide Impairs Protein Clearance Pathways in Tumor Cells
    • doi:10.1158/1541-7786.MCR-11-0019
    • Leu JIJ, Pimkina J, Pandey P, Murphy ME, George DL (2011) HSP70 Inhibition by the Small-Molecule 2-Phenylethynesulfonamide Impairs Protein Clearance Pathways in Tumor Cells. Molecular Cancer Research 9: 936-947. doi:10.1158/1541-7786.MCR-11-0019.
    • (2011) Molecular Cancer Research , vol.9 , pp. 936-947
    • Leu, J.I.J.1    Pimkina, J.2    Pandey, P.3    Murphy, M.E.4    George, D.L.5
  • 28
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • doi:10.1038/nsmb.2006
    • Schlecht R, Erbse AH, Bukau B, Mayer MP (2011) Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol 18: 345-351. doi:10.1038/nsmb.2006.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 29
    • 0030589149 scopus 로고    scopus 로고
    • The second step of ATP binding to DnaK induces peptide release
    • DOI 10.1006/jmbi.1996.0606
    • Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J (1996) The second step of ATP binding to DnaK induces peptide release. Journal of Molecular Biology 263: 657-670. doi:10.1006/jmbi.1996.0606. (Pubitemid 26395058)
    • (1996) Journal of Molecular Biology , vol.263 , Issue.5 , pp. 657-670
    • Theyssen, H.1    Schuster, H.-P.2    Packschies, L.3    Bukau, B.4    Reinstein, J.5
  • 31
    • 44049083594 scopus 로고    scopus 로고
    • Hsp110 is a nucleotide-activated exchange factor for Hsp70
    • doi:10.1074/jbc.M710063200
    • Andréasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B (2008) Hsp110 is a nucleotide-activated exchange factor for Hsp70. J Biol Chem 283: 8877-8884. doi:10.1074/jbc.M710063200.
    • (2008) J Biol Chem , vol.283 , pp. 8877-8884
    • Andréasson, C.1    Fiaux, J.2    Rampelt, H.3    Mayer, M.P.4    Bukau, B.5
  • 32
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • DOI 10.1038/nsmb.1425, PII NSMB1425
    • Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, et al. (2008) Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol 15: 641-650. doi:10.1038/nsmb.1425. (Pubitemid 351799133)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.6 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6    Bukau, B.7
  • 34
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • doi:10.1074/jbc.M105328200
    • Gässler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP (2001) Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J Biol Chem 276: 32538-32544. doi:10.1074/jbc.M105328200.
    • (2001) J Biol Chem , vol.276 , pp. 32538-32544
    • Gässler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 39
    • 79956219069 scopus 로고    scopus 로고
    • Differential expression of HSPA1 and HSPA2 proteins in human tissues; tissue microarray-based immunohistochemical study
    • doi:10.1007/s00418-011-0791-5
    • Scieglinska D, Piglowski W, Chekan M, Mazurek A, Krawczyk Z (2011) Differential expression of HSPA1 and HSPA2 proteins in human tissues; tissue microarray-based immunohistochemical study. Histochem Cell Biol 135: 337-350. doi:10.1007/s00418-011-0791-5.
    • (2011) Histochem Cell Biol , vol.135 , pp. 337-350
    • Scieglinska, D.1    Piglowski, W.2    Chekan, M.3    Mazurek, A.4    Krawczyk, Z.5
  • 40
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • DOI 10.1101/gad.305405
    • Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, et al. (2005) Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 19: 570-582. doi:10.1101/gad.305405. (Pubitemid 40314989)
    • (2005) Genes and Development , vol.19 , Issue.5 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jaattela, M.6
  • 41
    • 77954662908 scopus 로고    scopus 로고
    • A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
    • doi:10.1007/s00280-009-1194-3
    • Massey AJ, Williamson DS, Browne H, Murray JB, Dokurno P, et al. (2010) A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells. Cancer Chemother Pharmacol 66: 535-545. doi:10.1007/s00280-009-1194-3.
    • (2010) Cancer Chemother Pharmacol , vol.66 , pp. 535-545
    • Massey, A.J.1    Williamson, D.S.2    Browne, H.3    Murray, J.B.4    Dokurno, P.5
  • 42
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • DOI 10.1126/science.1057268
    • Sondermann H, Scheufler C, Schneider C, Höhfeld J, Hartl FU, et al. (2001) Structure of a Bag/Hsc70Complex: ConvergentFunctional Evolution of Hsp70Nucleotide Exchange Factors. Science 291: 1553-1557. (Pubitemid 32179223)
    • (2001) Science , vol.291 , Issue.5508 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.-U.5    Moarefi, I.6
  • 47
    • 0033561687 scopus 로고    scopus 로고
    • Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: Modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions
    • Brodsky JL (1999) Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions. Biochem Pharmacol 57: 877-880.
    • (1999) Biochem Pharmacol , vol.57 , pp. 877-880
    • Brodsky, J.L.1
  • 48
    • 0035847010 scopus 로고    scopus 로고
    • Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis
    • DOI 10.1074/jbc.M008535200
    • Fewell SW, Day BW, Brodsky JL (2001) Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J Biol Chem 276: 910-914. doi:10.1074/jbc.M008535200. (Pubitemid 32096508)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 910-914
    • Fewell, S.W.1    Day, B.W.2    Brodsky I, J.L.3
  • 49
    • 0028230782 scopus 로고
    • Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90
    • Nadeau K, Nadler SG, Saulnier M, Tepper MA, Walsh CT (1994) Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90. Biochemistry 33: 2561-2567. (Pubitemid 24099664)
    • (1994) Biochemistry , vol.33 , Issue.9 , pp. 2561-2567
    • Nadeau, K.1    Nadler, S.G.2    Saulnier, M.3    Tepper, M.A.4    Walsh, C.T.5
  • 52
    • 0023156658 scopus 로고
    • Preclinical antitumor activity and pharmacological properties of deoxyspergualin
    • Plowman J, Harrison SD, Trader MW, Griswold DP, Chadwick M, et al. (1987) Preclinical antitumor activity and pharmacological properties of deoxyspergualin. Cancer Research 47: 685-689. (Pubitemid 17027956)
    • (1987) Cancer Research , vol.47 , Issue.3 , pp. 685-689
    • Plowman, J.1    Harrison Jr., S.D.2    Trader, M.W.3
  • 54
    • 0034700271 scopus 로고    scopus 로고
    • Interaction between heat shock proteins and antimicrobial peptides
    • Otvos L, O I, Rogers ME, Consolvo PJ, Condie BA, et al. (2000) Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39: 14150-14159.
    • (2000) Biochemistry , vol.39 , pp. 14150-14159
    • Otvos, L.1    O, I.2    Rogers, M.E.3    Consolvo, P.J.4    Condie, B.A.5
  • 57
    • 62649101873 scopus 로고    scopus 로고
    • Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies
    • doi:10.1128/JB.01131-08
    • Liebscher M, Roujeinikova A (2009) Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies. Journal of Bacteriology 191: 1456-1462. doi:10.1128/JB.01131-08.
    • (2009) Journal of Bacteriology , vol.191 , pp. 1456-1462
    • Liebscher, M.1    Roujeinikova, A.2
  • 58
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • DOI 10.1074/jbc.271.27.15874
    • O'Brien MC, Flaherty KM, McKay DB (1996) Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis. J Biol Chem 271: 15874-15878. (Pubitemid 26236194)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.27 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.