Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase.
暂无分享,去创建一个
Oliver Hantschel | Giulio Superti-Furga | John Kuriyan | J. M. Davies | G. Superti-Furga | O. Hantschel | J. Kuriyan | W. Weis | M. Seeliger | B. Nagar | Bhushan Nagar | William I Weis | Markus Seeliger | Jason M Davies | J. Davies
[1] J. Kuriyan,et al. High yield bacterial expression of active c‐Abl and c‐Src tyrosine kinases , 2005, Protein science : a publication of the Protein Society.
[2] D. Fabbro,et al. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation. , 2005, Structure.
[3] P. Cole,et al. Protein tyrosine kinases Src and Csk: a tail's tale. , 2003, Current opinion in chemical biology.
[4] Dmitri I. Svergun,et al. PRIMUS: a Windows PC-based system for small-angle scattering data analysis , 2003 .
[5] Anna Westlund,et al. Conformation of full‐length Bruton tyrosine kinase (Btk) from synchrotron X‐ray solution scattering , 2003, The EMBO journal.
[6] A. Strife,et al. Chronic myelogenous leukemia as a paradigm of early cancer and possible curative strategies , 2003, Leukemia.
[7] G. Daley,et al. Mechanisms of Autoinhibition and STI-571/Imatinib Resistance Revealed by Mutagenesis of BCR-ABL , 2003, Cell.
[8] G. Superti-Furga,et al. A Myristoyl/Phosphotyrosine Switch Regulates c-Abl , 2003, Cell.
[9] G. Superti-Furga,et al. Structural Basis for the Autoinhibition of c-Abl Tyrosine Kinase , 2003, Cell.
[10] Satoru Takeuchi,et al. Structure of the Carboxyl-terminal Src Kinase, Csk* , 2002, The Journal of Biological Chemistry.
[11] C. Sawyers. Disabling Abl-perspectives on Abl kinase regulation and cancer therapeutics. , 2002, Cancer cell.
[12] G. Superti-Furga,et al. Autoinhibition of c-Abl , 2002, Cell.
[13] Yun Wu,et al. Inhibition of the Bcr-Abl oncoprotein by Bcr requires phosphoserine 354. , 2002, Cancer research.
[14] R. A. Etten,et al. Mutational analysis of the regulatory function of the c-Abl Src homology 3 domain , 2001, Oncogene.
[15] T. Hunter,et al. Inhibition of c-Abl Tyrosine Kinase Activity by Filamentous Actin* , 2001, The Journal of Biological Chemistry.
[16] D I Svergun,et al. Determination of domain structure of proteins from X-ray solution scattering. , 2001, Biophysical journal.
[17] John Kuriyan,et al. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). , 2001, Cancer research.
[18] Giulio Superti-Furga,et al. Dynamic Coupling between the SH2 and SH3 Domains of c-Src and Hck Underlies Their Inactivation by C-Terminal Tyrosine Phosphorylation , 2001, Cell.
[19] M. Yaffe,et al. Phosphoserine/threonine-binding domains. , 2001, Current opinion in cell biology.
[20] Dmitri I. Svergun,et al. Automated matching of high- and low-resolution structural models , 2001 .
[21] R. V. van Etten,et al. c-Abl Has High Intrinsic Tyrosine Kinase Activity That Is Stimulated by Mutation of the Src Homology 3 Domain and by Autophosphorylation at Two Distinct Regulatory Tyrosines* , 2000, The Journal of Biological Chemistry.
[22] H. D. Showalter,et al. Biochemical and cellular effects of c-Src kinase-selective pyrido[2, 3-d]pyrimidine tyrosine kinase inhibitors. , 2000, Biochemical pharmacology.
[23] R. A. Etten. Cycling, stressed-out and nervous: cellular functions of c-Abl , 1999 .
[24] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[25] John Kuriyan,et al. Crystal structure of the Src family tyrosine kinase Hck , 1997, Nature.
[26] Michael J. Eck,et al. Three-dimensional structure of the tyrosine kinase c-Src , 1997, Nature.
[27] D. Svergun,et al. CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates , 1995 .
[28] D. Kassel,et al. Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process. , 1995, Biochemistry.
[29] R. Sakai,et al. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases , 1995, Current Biology.
[30] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[31] E. Medico,et al. Phosphorylation of serine 985 negatively regulates the hepatocyte growth factor receptor kinase. , 1994, The Journal of biological chemistry.
[32] Dmitri I. Svergun,et al. Determination of the regularization parameter in indirect-transform methods using perceptual criteria , 1992 .
[33] O. Witte,et al. BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner , 1991, Cell.
[34] Florante A. Quiocho,et al. Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units , 1987, Nature.
[35] Jonathan A. Cooper,et al. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane , 1984, Nature.
[36] W. T. Heller. Influence of multiple well defined conformations on small-angle scattering of proteins in solution. , 2005, Acta crystallographica. Section D, Biological crystallography.
[37] Oliver Hantschel,et al. Regulation of the c-Abl and Bcr–Abl tyrosine kinases , 2004, Nature Reviews Molecular Cell Biology.
[38] W. Delano. The PyMOL Molecular Graphics System , 2002 .
[39] A. Pendergast. The Abl family kinases: mechanisms of regulation and signaling. , 2002, Advances in cancer research.
[40] M. Wall,et al. Large-scale shape changes in proteins and macromolecular complexes. , 2000, Annual review of physical chemistry.
[41] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.