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Volumn 356, Issue 3, 2006, Pages 746-758

The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins

Author keywords

Heat shock; Hsp90; Molecular chaperone; p23; Protein folding

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 90; NUCLEOTIDE; PROTEIN P23;

EID: 31344474558     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.085     Document Type: Article
Times cited : (165)

References (57)
  • 1
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • M.P. Mayer, and B. Bukau Molecular chaperones: the busy life of Hsp90 Curr. Biol. 9 1999 R322 R325
    • (1999) Curr. Biol. , vol.9
    • Mayer, M.P.1    Bukau, B.2
  • 3
    • 0031895351 scopus 로고    scopus 로고
    • The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • W.B. Pratt The Hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors Proc. Soc. Expt. Biol. Med. 217 1998 420 434
    • (1998) Proc. Soc. Expt. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 4
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • D. Picard Heat-shock protein 90, a chaperone for folding and regulation Cell Mol. Life Sci. 59 2002 1640 1648
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 5
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • J.C. Young, I. Moarefi, and F.U. Hartl Hsp90: a specialized but essential protein-folding tool J. Cell Biol. 154 2001 267 273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 6
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the Hsp90 chaperone
    • R. Zhao, M. Davey, Y.C. Hsu, P. Kaplanek, A. Tong, and A.B. Parsons Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone Cell 120 2005 715 727
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3    Kaplanek, P.4    Tong, A.5    Parsons, A.B.6
  • 7
    • 18944365231 scopus 로고    scopus 로고
    • A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)
    • S.H. Millson, A.W. Truman, V. King, C. Prodromou, L.H. Pearl, and P.W. Piper A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p) Eukaryot. Cell. 4 2005 849 860
    • (2005) Eukaryot. Cell. , vol.4 , pp. 849-860
    • Millson, S.H.1    Truman, A.W.2    King, V.3    Prodromou, C.4    Pearl, L.H.5    Piper, P.W.6
  • 8
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • C. Prodromou, S.M. Roe, D.N. O'Brien, J.E. Ladbury, P.W. Piper, and L.H. Pearl Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone Cell 90 1997 65 75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, D.N.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 10
    • 0034663806 scopus 로고    scopus 로고
    • The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
    • C. Prodromou, B. Panaretou, S. Chohan, G. Siligardi, R. O'Brien, and J.E. Ladbury The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains EMBO J. 19 2000 4383 4392
    • (2000) EMBO J. , vol.19 , pp. 4383-4392
    • Prodromou, C.1    Panaretou, B.2    Chohan, S.3    Siligardi, G.4    O'Brien, R.5    Ladbury, J.E.6
  • 12
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • J.C. Young, and F.U. Hartl Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23 EMBO J. 19 2000 5930 5940
    • (2000) EMBO J. , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2
  • 13
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human Hsp90 by a client protein
    • S.H. McLaughlin, H.W. Smith, and S.E. Jackson Stimulation of the weak ATPase activity of human Hsp90 by a client protein J. Mol. Biol. 315 2002 787 798
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 14
    • 7944225978 scopus 로고    scopus 로고
    • Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform
    • S.H. McLaughlin, L.-A. Ventouras, B. Lobbezoo, and S.E. Jackson Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform J. Mol. Biol. 344 2004 813 826
    • (2004) J. Mol. Biol. , vol.344 , pp. 813-826
    • McLaughlin, S.H.1    Ventouras, L.-A.2    Lobbezoo, B.3    Jackson, S.E.4
  • 15
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle
    • K. Richter, P. Muschler, O. Hainzl, J. Reinstein, and J. Buchner Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle J. Biol. Chem. 278 2003 10328 10333
    • (2003) J. Biol. Chem. , vol.278 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 18
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • J.L. Johnson, T.G. Beito, C.J. Krco, and D.O. Toft Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes Mol. Cell. Biol. 14 1994 1956 1963
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Krco, C.J.3    Toft, D.O.4
  • 19
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23
    • J.L. Johnson, and D.O. Toft A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23 J. Biol. Chem. 269 1994 24989 24993
    • (1994) J. Biol. Chem. , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 20
    • 0029161506 scopus 로고
    • The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with Hsp90
    • K.A. Hutchison, L.F. Stancato, J.K. Owens-Grillo, J.L. Johnson, P. Krishna, D.O. Toft, and W.B. Pratt The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with Hsp90 J. Biol. Chem. 270 1995 18841 18847
    • (1995) J. Biol. Chem. , vol.270 , pp. 18841-18847
    • Hutchison, K.A.1    Stancato, L.F.2    Owens-Grillo, J.K.3    Johnson, J.L.4    Krishna, P.5    Toft, D.O.6    Pratt, W.B.7
  • 21
    • 0031848850 scopus 로고    scopus 로고
    • Recent advances in the study of Hsp90 structure and mechanism of action
    • D.O. Toft Recent advances in the study of Hsp90 structure and mechanism of action Trends Endocrinol. Metab. 9 1998 238 243
    • (1998) Trends Endocrinol. Metab. , vol.9 , pp. 238-243
    • Toft, D.O.1
  • 22
    • 0034487854 scopus 로고    scopus 로고
    • Chaperones in progesterone receptor complexes
    • D.F. Smith Chaperones in progesterone receptor complexes Semin. Cell Dev. Biol. 11 2000 45 52
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 45-52
    • Smith, D.F.1
  • 23
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. the role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70
    • K.D. Dittmar, D.R. Demady, L.F. Stancato, P. Krishna, and W.B. Pratt Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70 J. Biol. Chem. 272 1997 21213 21220
    • (1997) J. Biol. Chem. , vol.272 , pp. 21213-21220
    • Dittmar, K.D.1    Demady, D.R.2    Stancato, L.F.3    Krishna, P.4    Pratt, W.B.5
  • 24
    • 0032484127 scopus 로고    scopus 로고
    • The assembly of progesterone receptor-Hsp90 complexes using purified proteins
    • H. Kosano, B. Stensgard, M.C. Charlesworth, N. McMahon, and D. Toft The assembly of progesterone receptor-Hsp90 complexes using purified proteins J. Biol. Chem. 273 1998 32973 32979
    • (1998) J. Biol. Chem. , vol.273 , pp. 32973-32979
    • Kosano, H.1    Stensgard, B.2    Charlesworth, M.C.3    McMahon, N.4    Toft, D.5
  • 25
    • 0032915424 scopus 로고    scopus 로고
    • Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
    • R. Knoblauch, and M.J. Garabedian Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction Mol. Cell. Biol. 19 1999 3748 3759
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3748-3759
    • Knoblauch, R.1    Garabedian, M.J.2
  • 26
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • S. Bose, T. Weikl, H. Bugl, and J. Buchner Chaperone function of Hsp90-associated proteins Science 274 1996 1715 1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 27
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • B.C. Freeman, D.O. Toft, and R.I. Morimoto Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23 Science 274 1996 1718 1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 28
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • B.C. Freeman, S.J. Felts, D.O. Toft, and K.R. Yamamoto The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies Genes Dev. 14 2000 422 434
    • (2000) Genes Dev. , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 29
    • 0031868061 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins
    • S.P. Bohen Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins Mol. Cell. Biol. 18 1998 3330 3339
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3330-3339
    • Bohen, S.P.1
  • 30
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
    • Y. Fang, A.E. Fliss, J. Rao, and A.J. Caplan SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins Mol. Cell. Biol. 18 1998 3727 3734
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3727-3734
    • Fang, Y.1    Fliss, A.E.2    Rao, J.3    Caplan, A.J.4
  • 31
    • 0029075280 scopus 로고
    • Binding of p23 and Hsp90 during assembly with the progesterone receptor
    • J.L. Johnson, and D.O. Toft Binding of p23 and Hsp90 during assembly with the progesterone receptor Mol. Endocrinol. 9 1995 670 678
    • (1995) Mol. Endocrinol. , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 32
    • 0037195951 scopus 로고    scopus 로고
    • The influence of ATP and p23 on the conformation of Hsp90
    • W.P. Sullivan, B.A. Owen, and D.O. Toft The influence of ATP and p23 on the conformation of Hsp90 J. Biol. Chem. 277 2002 45942 45948
    • (2002) J. Biol. Chem. , vol.277 , pp. 45942-45948
    • Sullivan, W.P.1    Owen, B.A.2    Toft, D.O.3
  • 33
    • 4444291743 scopus 로고    scopus 로고
    • The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • K. Richter, S. Walter, and J. Buchner The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle J. Mol. Biol. 342 2004 1403 1413
    • (2004) J. Mol. Biol. , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 35
    • 2942741244 scopus 로고    scopus 로고
    • Evolutionary epitopes of Hsp90 and p23: Implications for their interaction
    • S. Zhu, and J. Tytgat Evolutionary epitopes of Hsp90 and p23: implications for their interaction FASEB J. 18 2004 940 947
    • (2004) FASEB J. , vol.18 , pp. 940-947
    • Zhu, S.1    Tytgat, J.2
  • 36
    • 0141592432 scopus 로고    scopus 로고
    • Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling
    • E. Oxelmark, R. Knoblauch, S. Arnal, L.F. Su, M. Schapira, and M.J. Garabedian Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling J. Biol. Chem. 278 2003 36547 36555
    • (2003) J. Biol. Chem. , vol.278 , pp. 36547-36555
    • Oxelmark, E.1    Knoblauch, R.2    Arnal, S.3    Su, L.F.4    Schapira, M.5    Garabedian, M.J.6
  • 39
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of hptG, the Escherichia coli Hsp90, reveals apotential substrate binding site
    • S.F. Harris, A.K. Shiau, and D.A. Agard The crystal structure of the carboxy-terminal dimerization domain of hptG, the Escherichia coli Hsp90, reveals apotential substrate binding site Structure 12 2004 1087 1097
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 40
    • 0034725641 scopus 로고    scopus 로고
    • Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone
    • A.J. Weaver, W.P. Sullivan, S.J. Felts, B.A. Owen, and D.O. Toft Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone J. Biol. Chem. 275 2000 23045 23052
    • (2000) J. Biol. Chem. , vol.275 , pp. 23045-23052
    • Weaver, A.J.1    Sullivan, W.P.2    Felts, S.J.3    Owen, B.A.4    Toft, D.O.5
  • 41
    • 0032760261 scopus 로고    scopus 로고
    • An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function
    • T. Weikl, K. Abelmann, and J. Buchner An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function J. Mol. Biol. 293 1999 685 691
    • (1999) J. Mol. Biol. , vol.293 , pp. 685-691
    • Weikl, T.1    Abelmann, K.2    Buchner, J.3
  • 42
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes
    • J.P. Grenert, B.D. Johnson, and D.O. Toft The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes J. Biol. Chem. 274 1999 17525 17533
    • (1999) J. Biol. Chem. , vol.274 , pp. 17525-17533
    • Grenert, J.P.1    Johnson, B.D.2    Toft, D.O.3
  • 43
    • 0026428621 scopus 로고
    • Crystal structure of an N-terminal fragment of the DNA gyrase B protein
    • D.B. Wigley, G.J. Davies, E.J. Dodson, A. Maxwell, and G. Dodson Crystal structure of an N-terminal fragment of the DNA gyrase B protein Nature 351 1991 624 629
    • (1991) Nature , vol.351 , pp. 624-629
    • Wigley, D.B.1    Davies, G.J.2    Dodson, E.J.3    Maxwell, A.4    Dodson, G.5
  • 45
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of Hsp90. Implications for ATP hydrolysis and client protein and cochaperone interactions
    • P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, and B. Panaretou Structural and functional analysis of the middle segment of Hsp90. Implications for ATP hydrolysis and client protein and cochaperone interactions Mol. Cell. 11 2003 647 658
    • (2003) Mol. Cell. , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6
  • 46
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Q. Huai, H. Wang, Y. Liu, H.Y. Kim, D. Toft, and H. Ke Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding Structure 13 2005 579 590
    • (2005) Structure , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.Y.4    Toft, D.5    Ke, H.6
  • 47
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(Cdc37)
    • S.M. Roe, M.M. Ali, P. Meyer, C.K. Vaughan, B. Panaretou, and P.W. Piper The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(Cdc37) Cell 116 2004 87 98
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3    Vaughan, C.K.4    Panaretou, B.5    Piper, P.W.6
  • 48
    • 18844406200 scopus 로고    scopus 로고
    • Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation
    • A. Harst, H. Lin, and W.M. Obermann Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation Biochem. J. 387 2005 789 796
    • (2005) Biochem. J. , vol.387 , pp. 789-796
    • Harst, A.1    Lin, H.2    Obermann, W.M.3
  • 50
    • 11144357391 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • P. Meyer, C. Prodromou, C. Liao, B. Hu, S. Mark Roe, and C.K. Vaughan Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery EMBO J. 23 2004 1402 1410
    • (2004) EMBO J. , vol.23 , pp. 1402-1410
    • Meyer, P.1    Prodromou, C.2    Liao, C.3    Hu, B.4    Mark Roe, S.5    Vaughan, C.K.6
  • 51
    • 0036754939 scopus 로고    scopus 로고
    • The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically
    • T. Abbas-Terki, P.A. Briand, O. Donze, and D. Picard The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically Biol. Chem. 383 2002 1335 1342
    • (2002) Biol. Chem. , vol.383 , pp. 1335-1342
    • Abbas-Terki, T.1    Briand, P.A.2    Donze, O.3    Picard, D.4
  • 52
    • 0033081968 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
    • C. Prodromou, G. Siligardi, R. O'Brien, D.N. Woolfson, L. Regan, and B. Panaretou Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones EMBO J. 18 1999 754 762
    • (1999) EMBO J. , vol.18 , pp. 754-762
    • Prodromou, C.1    Siligardi, G.2    O'Brien, R.3    Woolfson, D.N.4    Regan, L.5    Panaretou, B.6
  • 53
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • F. Sobott, H. Hernandez, M.G. McCammon, M.A. Tito, and C.V. Robinson A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies Anal. Chem. 74 2002 1402 1407
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 55
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • A.J. Heck, and R.H. Van Den Heuvel Investigation of intact protein complexes by mass spectrometry Mass Spectrom. Rev. 23 2004 368 389
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 56
    • 0033926938 scopus 로고    scopus 로고
    • A brief overview of the present status of the mechanisms involved in electrospray mass spectrometry
    • P. Kebarle A brief overview of the present status of the mechanisms involved in electrospray mass spectrometry J. Mass Spectrom. 35 2000 804 817
    • (2000) J. Mass Spectrom. , vol.35 , pp. 804-817
    • Kebarle, P.1
  • 57


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