메뉴 건너뛰기




Volumn 11, Issue 7, 2004, Pages 991-998

Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BENZOQUINONE DERIVATIVE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MACROCYCLIC LACTAM; QUINONE DERIVATIVE; SERINE;

EID: 3242893125     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.05.010     Document Type: Article
Times cited : (38)

References (29)
  • 2
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of HSP90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Akinaga S., Soga S., Sullivan W., Stensgard B., Toft D., Neckers L.M. Antibiotic radicicol binds to the N-terminal domain of HSP90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones. 3:1998;100-108
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 3
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma S.V., Agatsuma T., Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene. 16:1998;2639-2645
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 4
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., Neckers L.M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins. essential role for stress proteins in oncogenic transformation Proc. Natl. Acad. Sci. USA. 91:1994;8324-8328
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 5
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs J.S., Xu W., Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell. 3:2003;213-217
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 6
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the HSP90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Structural basis for inhibition of the HSP90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42:1999;260-266
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 7
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an HSP90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an HSP90-geldanamycin complex. targeting of a protein chaperone by an antitumor agent Cell. 89:1997;239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 8
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the HSP90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. 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, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 9
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of HSP90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis G., Timaul M.N., Lucas B., Munster P.N., Zheng F.F., Sepp-Lorenzino L., Rosen N. A small molecule designed to bind to the adenine nucleotide pocket of HSP90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem. Biol. 8:2001;289-299
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6    Rosen, N.7
  • 10
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Neckers L.M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42:1998;273-279
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 13
    • 0001402694 scopus 로고
    • Tandem [3,3]-sigmatropic rearrangements in an ansamycin: Stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative
    • Schnur R., Corman M. Tandem [3,3]-sigmatropic rearrangements in an ansamycin. Stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative J. Org. Chem. 59:1994;2581-2584
    • (1994) J. Org. Chem. , vol.59 , pp. 2581-2584
    • Schnur, R.1    Corman, M.2
  • 15
    • 0019428141 scopus 로고
    • The structures of macbecin I and II: New tumor antibiotics
    • Muroi M., Haibara K., Asai M., Kamiya K., Kishi T. The structures of macbecin I and II. new tumor antibiotics Tetrahedron. 37:1981;1123-1130
    • (1981) Tetrahedron , vol.37 , pp. 1123-1130
    • Muroi, M.1    Haibara, K.2    Asai, M.3    Kamiya, K.4    Kishi, T.5
  • 16
    • 0344511727 scopus 로고    scopus 로고
    • Crystal Structure and Molecular Modeling of 17-DMAG in Complex with Human HSP90
    • Jez J.M., Chen J.C., Rastelli G., Stroud R.M., Santi D.V. Crystal Structure and Molecular Modeling of 17-DMAG in Complex with Human HSP90. Chem. Biol. 10:2003;361-368
    • (2003) Chem. Biol. , vol.10 , pp. 361-368
    • Jez, J.M.1    Chen, J.C.2    Rastelli, G.3    Stroud, R.M.4    Santi, D.V.5
  • 17
    • 0037162748 scopus 로고    scopus 로고
    • Theory supplemented by experiment. Electronic effects on the rotational stability of the amide group in p-substituted acetalinides
    • Ilieva S., Hadjieva B., Galabov B. Theory supplemented by experiment. Electronic effects on the rotational stability of the amide group in p-substituted acetalinides. J. Org. Chem. 67:2002;6210-6215
    • (2002) J. Org. Chem. , vol.67 , pp. 6210-6215
    • Ilieva, S.1    Hadjieva, B.2    Galabov, B.3
  • 18
    • 0034419296 scopus 로고    scopus 로고
    • Chemical aspects of peptide bond isomerization
    • Fischer G. Chemical aspects of peptide bond isomerization. Chem. Soc. Rev. 29:2000;119-127
    • (2000) Chem. Soc. Rev. , vol.29 , pp. 119-127
    • Fischer, G.1
  • 19
    • 0037015443 scopus 로고    scopus 로고
    • Total synthesis of (+)-geldanamycin and (-)-o-quinogeldanamycin with use of asymmetric anti- and syn-glycolate aldol reactions
    • Andrus M.B., Meredith E.L., Simmons B.L., Soma-Sekhar B.B., Hicken E.J. Total synthesis of (+)-geldanamycin and (-)-o-quinogeldanamycin with use of asymmetric anti- and syn-glycolate aldol reactions. Org. Lett. 4:2002;3549-3552
    • (2002) Org. Lett. , vol.4 , pp. 3549-3552
    • Andrus, M.B.1    Meredith, E.L.2    Simmons, B.L.3    Soma-Sekhar, B.B.4    Hicken, E.J.5
  • 21
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones-cellular machines for protein folding
    • Walter S., Buchner J. Molecular chaperones-cellular machines for protein folding. Angew. Chem. Int. Ed. Engl. 41:2002;1098-1113
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 22
    • 0036263966 scopus 로고    scopus 로고
    • The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
    • Scheine-Fischer C., Habazettl J., Schmid F., Fischer G. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nat. Struct. Biol. 9:2002;419-424
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 419-424
    • Scheine-Fischer, C.1    Habazettl, J.2    Schmid, F.3    Fischer, G.4
  • 23
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in HSP90 differing in substrate specificity and ATP dependence
    • Scheibel T., Weikl T., Buchner J. Two chaperone sites in HSP90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. USA. 95:1998;1495-1499
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 24
    • 0030862486 scopus 로고    scopus 로고
    • In vitro evidence that HSP90 contains two independent chaperone sites
    • Young J.C., Schneider C., Hartl F.U. In vitro evidence that HSP90 contains two independent chaperone sites. FEBS Lett. 418:1997;139-143
    • (1997) FEBS Lett. , vol.418 , pp. 139-143
    • Young, J.C.1    Schneider, C.2    Hartl, F.U.3
  • 29
    • 0343791148 scopus 로고
    • Electric moments of molecules in liquids
    • Onsager L. Electric moments of molecules in liquids. J. Am. Chem. Soc. 58:1938;1486-1493
    • (1938) J. Am. Chem. Soc. , vol.58 , pp. 1486-1493
    • Onsager, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.