A putative molecular-activation switch in the transmembrane domain of erbB2
暂无分享,去创建一个
Sarel J. Fleishman | Nir Ben-Tal | Joseph Schlessinger | N. Ben-Tal | S. Fleishman | J. Schlessinger
[1] D. Engelman,et al. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation , 1997, Oncogene.
[2] A. Ullrich,et al. The epidermal growth factor receptor family as a central element for cellular signal transduction and diversification. , 2001, Endocrine-related cancer.
[3] Cori Bargmann,et al. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185 , 1986, Cell.
[4] D. Engelman,et al. Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices. , 1992, The Journal of biological chemistry.
[5] B. Bormann,et al. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor , 1996, Nature Structural Biology.
[6] B. Bormann,et al. A subdomain in the transmembrane domain is necessary for p185neu* activation. , 1992, The EMBO journal.
[7] C. Chothia,et al. Helix to helix packing in proteins. , 1981, Journal of molecular biology.
[8] D. Weiner,et al. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation , 1989, Nature.
[9] N. Hynes,et al. Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling , 1995, Molecular and cellular biology.
[10] Sarel J Fleishman,et al. A novel scoring function for predicting the conformations of tightly packed pairs of transmembrane alpha-helices. , 2002, Journal of molecular biology.
[11] D. Engelman,et al. The GxxxG motif: a framework for transmembrane helix-helix association. , 2000, Journal of molecular biology.
[12] Tony Hunter,et al. Receptor signaling: When dimerization is not enough , 1999, Current Biology.
[13] Y. Yarden,et al. ErbB‐2 is a common auxiliary subunit of NDF and EGF receptors: implications for breast cancer. , 1996, The EMBO journal.
[14] S. Aaronson,et al. Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene , 1988, Molecular and cellular biology.
[15] I. Maruyama,et al. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. , 2001, Journal of molecular biology.
[16] A. N. Meyer,et al. Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase. , 2000, Molecular biology of the cell.
[17] N. Hynes,et al. ErbB‐2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling , 1997, The EMBO journal.
[18] M. Gerstein,et al. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. , 2000, Journal of molecular biology.
[19] M. Lemmon,et al. The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes* , 2002, The Journal of Biological Chemistry.
[20] L. Cantley,et al. A neu acquaintance for ErbB3 and ErbB4: A role for receptor heterodimerization in growth signaling , 1994, Cell.
[21] Joseph Schlessinger,et al. Signal transduction by receptors with tyrosine kinase activity , 1990, Cell.
[22] M. Sternberg,et al. A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization. , 1990, Protein engineering.
[23] W. Gullick,et al. Neu receptor dimerization , 1989, Nature.
[24] X. Shu,et al. Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk. , 2000, Journal of the National Cancer Institute.
[25] James H. Prestegard,et al. A Transmembrane Helix Dimer: Structure and Implications , 1997, Science.