Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
暂无分享,去创建一个
Zhexin Xiang | Z. Xiang | L. Neckers | M. Marcu | E. Mimnaugh | Len Neckers | Wanping Xu | Wanping Xu | Xitong Yuan | Edward Mimnaugh | Monica Marcu | Xitong Yuan | Zhexin Xiang
[1] K. Arndt,et al. Identification of a Conserved Sequence Motif That Promotes Cdc37 and Cyclin D1 Binding to Cdk4* , 2004, Journal of Biological Chemistry.
[2] Z. Xiang,et al. Extending the accuracy limits of prediction for side-chain conformations. , 2001, Journal of molecular biology.
[3] Neal Rosen,et al. Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent , 1997, Cell.
[4] L. Neckers,et al. Polyubiquitination and Proteasomal Degradation of the p185c-erbB-2 Receptor Protein-tyrosine Kinase Induced by Geldanamycin* , 1996, The Journal of Biological Chemistry.
[5] A. Citri,et al. Drug‐induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy , 2002, The EMBO journal.
[6] S. Uma,et al. High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients. , 2003, Biochemistry.
[7] J. Brugge,et al. Controlled Dimerization of ErbB Receptors Provides Evidence for Differential Signaling by Homo- and Heterodimers , 1999, Molecular and Cellular Biology.
[8] G. Carpenter,et al. Geldanamycin Induces ErbB-2 Degradation by Proteolytic Fragmentation* , 2000, The Journal of Biological Chemistry.
[9] L. Neckers,et al. p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. , 1996, The Journal of biological chemistry.
[10] D. Toft,et al. The Assembly and Intermolecular Properties of the hsp70-Hop-hsp90 Molecular Chaperone Complex* , 2002, The Journal of Biological Chemistry.
[11] T. Yagi,et al. Induction of a variety of tumors by c‐erbB2 and clonal nature of lymphomas even with the mutated gene (Val659‐‐‐‐Glu659). , 1990, The EMBO journal.
[12] M. Dowsett,et al. Overexpression of HER-2 as a resistance mechanism to hormonal therapy for breast cancer. , 2001, Endocrine-related cancer.
[13] L. Neckers,et al. Hsp90, not Grp94, regulates the intracellular trafficking and stability of nascent ErbB2 , 2002, Cell stress & chaperones.
[14] Cinque S. Soto,et al. Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[15] Paul Workman,et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. , 2002, Molecular cell.
[16] Y. Yarden,et al. Sensitivity of Mature ErbB2 to Geldanamycin Is Conferred by Its Kinase Domain and Is Mediated by the Chaperone Protein Hsp90* , 2001, The Journal of Biological Chemistry.
[17] L. Pearl,et al. Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50 cdc37 * , 2002, The Journal of Biological Chemistry.
[18] Y. Miyata,et al. CK2 Controls Multiple Protein Kinases by Phosphorylating a Kinase-Targeting Molecular Chaperone, Cdc37 , 2004, Molecular and Cellular Biology.
[19] M. Sliwkowski,et al. Structure of the Epidermal Growth Factor Receptor Kinase Domain Alone and in Complex with a 4-Anilinoquinazoline Inhibitor* , 2002, The Journal of Biological Chemistry.
[20] T. Tsuruo,et al. Modulation of Akt kinase activity by binding to Hsp90. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[21] R. Matts,et al. Phosphorylation of Serine 13 Is Required for the Proper Function of the Hsp90 Co-chaperone, Cdc37* , 2003, Journal of Biological Chemistry.
[22] A. Marrogi,et al. p53, c-erbB2, and PCNA status in benign, proliferative and malignant ovarian surface epithelial neoplasms: a study of 75 cases. , 1999, Archives of pathology & laboratory medicine.
[23] L. Neckers,et al. Heat shock protein 90 as a molecular target for cancer therapeutics. , 2003, Cancer cell.
[24] R. Matts,et al. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. , 2003, Biochemistry.
[25] B. Honig,et al. An integrated approach to the analysis and modeling of protein sequences and structures. III. A comparative study of sequence conservation in protein structural families using multiple structural alignments. , 2000, Journal of molecular biology.
[26] B. Honig,et al. On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles. , 2003, Journal of molecular biology.
[27] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[28] M. Galigniana,et al. Visualization and Mechanism of Assembly of a Glucocorticoid Receptor·Hsp70 Complex That Is Primed for Subsequent Hsp90-dependent Opening of the Steroid Binding Cleft* , 2003, Journal of Biological Chemistry.
[29] M. Hung,et al. Expression of activated rat neu oncogene is sufficient to induce experimental metastasis in 3T3 cells. , 1991, Oncogene.
[30] Chrisostomos Prodromou,et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. , 2003, Molecular cell.
[31] G. Merlino,et al. Genetic instability favoring transversions associated with ErbB2-induced mammary tumorigenesis , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[32] P. Miller,et al. Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins. , 1994, Cancer research.
[33] Noah Craft,et al. A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase , 1999, Nature Medicine.
[34] S. Jackson,et al. Stimulation of the weak ATPase activity of human hsp90 by a client protein. , 2002, Journal of molecular biology.
[35] G. Carpenter,et al. Identification of ErbB-2 kinase domain motifs required for geldanamycin-induced degradation. , 2003, Cancer research.
[36] L. Neckers,et al. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. , 2000, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.
[37] R. Kumar,et al. The role of HER2 in angiogenesis. , 2001, Seminars in oncology.
[38] W. Pratt,et al. Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1 , 2003, Experimental biology and medicine.
[39] R. Hartmann-Petersen,et al. Transferring substrates to the 26S proteasome. , 2003, Trends in biochemical sciences.
[40] Wei Zhang,et al. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. , 2004, Journal of molecular biology.
[41] S. Aaronson,et al. Implications for Cancer Therapy , 2003 .
[42] W. McGuire,et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. , 1987, Science.
[43] Timothy A. J. Haystead,et al. The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation* , 1997, The Journal of Biological Chemistry.