Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation
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Elizabeth J. Goldsmith | E. Goldsmith | B. Canagarajah | M. Cobb | A. Khokhlatchev | Bertram J. Canagarajah | Andrei Khokhlatchev | Melanie H. Cobb
[1] M. Cobb,et al. Reconstitution of Mitogen-activated Protein Kinase Phosphorylation Cascades in Bacteria , 1997, The Journal of Biological Chemistry.
[2] John Kuriyan,et al. Crystal structure of the Src family tyrosine kinase Hck , 1997, Nature.
[3] Michael J. Eck,et al. Three-dimensional structure of the tyrosine kinase c-Src , 1997, Nature.
[4] E. Goldsmith,et al. Contributions of the Mitogen-activated Protein (MAP) Kinase Backbone and Phosphorylation Loop to MEK Specificity* , 1996, The Journal of Biological Chemistry.
[5] T. Soderling,et al. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1 , 1996, Molecular and cellular biology.
[6] Paul R. Caron,et al. Crystal Structure of p38 Mitogen-activated Protein Kinase* , 1996, The Journal of Biological Chemistry.
[7] J. Avruch,et al. Sounding the Alarm: Protein Kinase Cascades Activated by Stress and Inflammation* , 1996, The Journal of Biological Chemistry.
[8] P. Jeffrey,et al. Structural basis of cyclin-dependent kinase activation by phosphorylation , 1996, Nature Structural Biology.
[9] A. Brunet,et al. Identification of MAP Kinase Domains by Redirecting Stress Signals into Growth Factor Responses , 1996, Science.
[10] E. Goldsmith,et al. Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5'-triphosphate. , 1996, Biochemistry.
[11] E. Goldsmith. Allosteric enzymes as models for chemomechanical energy transducing assemblies , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[12] L. Johnson,et al. Active and Inactive Protein Kinases: Structural Basis for Regulation , 1996, Cell.
[13] K. Longenecker,et al. Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition. , 1996, Journal of molecular biology.
[14] John A Tainer,et al. Crystal Structure and Mutational Analysis of the Human CDK2 Kinase Complex with Cell Cycle–Regulatory Protein CksHs1 , 1996, Cell.
[15] Jiahuai Han,et al. Primary structure of BMK1: a new mammalian map kinase. , 1995, Biochemical and biophysical research communications.
[16] N. Xuong,et al. Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains , 1995, Science.
[17] Kornelia Polyak,et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex , 1995, Nature.
[18] E. Goldsmith,et al. How MAP Kinases Are Regulated (*) , 1995, The Journal of Biological Chemistry.
[19] E. Krebs,et al. The MAPK signaling cascade , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[20] Gaochao Zhou,et al. Components of a New Human Protein Kinase Signal Transduction Pathway (*) , 1995, The Journal of Biological Chemistry.
[21] T. Hunter,et al. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1 , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[22] L. Johnson,et al. Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. , 1995, Structure.
[23] N. Jones,et al. ATF‐2 contains a phosphorylation‐dependent transcriptional activation domain. , 1995, The EMBO journal.
[24] A. Levitzki,et al. Tyrosine kinase inhibition: an approach to drug development. , 1995, Science.
[25] E. Goldsmith,et al. Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. , 1995, Structure.
[26] R M Sweet,et al. Crystal structure of casein kinase‐1, a phosphate‐directed protein kinase. , 1995, The EMBO journal.
[27] I. Tsigelny,et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. , 1994, Genes & development.
[28] Zhou Songyang,et al. Use of an oriented peptide library to determine the optimal substrates of protein kinases , 1994, Current Biology.
[29] R. Davis,et al. MAP kinase binds to the NH2‐terminal activation domain of c‐Myc , 1994, FEBS letters.
[30] K. Xia,et al. Interaction of the protein kinase Raf-1 with 14-3-3 proteins. , 1994, Science.
[31] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[32] N. Ahn,et al. Transformation of mammalian cells by constitutively active MAP kinase kinase. , 1994, Science.
[33] L Bibbs,et al. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. , 1994, Science.
[34] B. Kemp,et al. Insights into autoregulation from the crystal structure of twitchin kinase , 1994, Nature.
[35] J. Woodgett,et al. The stress-activated protein kinase subfamily of c-Jun kinases , 1994, Nature.
[36] M. Karin,et al. JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain , 1994, Cell.
[37] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[38] Elizabeth J. Goldsmith,et al. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution , 1994, Nature.
[39] A. Yoshimura,et al. Ligand-induced activation of chimeric receptors between the erythropoietin receptor and receptor tyrosine kinases. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[40] Hong Sun,et al. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo , 1993, Cell.
[41] M. Karin,et al. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. , 1993, Genes & development.
[42] K. Guan,et al. Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase. , 1993, The Journal of biological chemistry.
[43] R. Davis,et al. The mitogen-activated protein kinase signal transduction pathway. , 1993, The Journal of biological chemistry.
[44] Sung-Hou Kim,et al. Crystal structure of cyclin-dependent kinase 2 , 1993, Nature.
[45] S V Evans,et al. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. , 1993, Journal of molecular graphics.
[46] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[47] M. Cobb,et al. Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. , 1993, The Journal of biological chemistry.
[48] M. Cobb,et al. Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1 , 1993, Molecular and cellular biology.
[49] E. Krebs,et al. Human T-cell mitogen-activated protein kinase kinases are related to yeast signal transduction kinases. , 1992, The Journal of biological chemistry.
[50] T. Haystead,et al. Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. , 1992, Science.
[51] David L. Brautigan,et al. Raf-1 activates MAP kinase-kinase , 1992, Nature.
[52] E. Krebs,et al. ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[53] M. Cobb,et al. Extracellular signal-regulated kinases 2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: analysis by peptide mapping. , 1992, Molecular biology of the cell.
[54] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[55] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[56] S. Pelech,et al. Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase. , 1991, The Journal of biological chemistry.
[57] Sung-Hou Kim,et al. Sparse matrix sampling: a screening method for crystallization of proteins , 1991 .
[58] J. Zheng,et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. , 1991, Science.
[59] J. Zheng,et al. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. , 1991, Science.
[60] Nancy Y. Ip,et al. ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF , 1991, Cell.
[61] M. Cobb,et al. Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies. , 1991, Cell regulation.
[62] J. Shabanowitz,et al. Identification of the regulatory phosphorylation sites in pp42/mitogen‐activated protein kinase (MAP kinase). , 1991, The EMBO journal.
[63] J. Thornton,et al. Influence of proline residues on protein conformation. , 1991, Journal of molecular biology.
[64] E. Krebs,et al. Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase. , 1991, The Journal of biological chemistry.
[65] C. Slaughter,et al. An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. , 1990, Science.
[66] J. Maller,et al. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase , 1990, Nature.
[67] D. Bacon,et al. A fast algorithm for rendering space-filling molecule pictures , 1988 .
[68] T. Hunter. A tail of two src's: Mutatis mutandis , 1987, Cell.
[69] V. Stanton,et al. Activation of human raf transforming genes by deletion of normal amino-terminal coding sequences , 1987, Molecular and cellular biology.
[70] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[71] M. Day,et al. Protein structures. , 1998, Chemistry and Biology.
[72] Harry Hines Boulevard,et al. The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution , 1997 .
[73] T. Hunter,et al. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1 , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[74] Axel T. Brunger,et al. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .
[75] V. T. Platonenko,et al. Interaction of a , 1978 .