Gravin is a transitory effector of polo-like kinase 1 during cell division.

[1]  Xiao-wei Zhu,et al.  Clinicopathological significance of Polo-like kinase 1 (PLK1) expression in human malignant glioma. , 2012, Acta histochemica.

[2]  D. Fabbro,et al.  Targeting cancer with small-molecular-weight kinase inhibitors. , 2012, Methods in molecular biology.

[3]  M. Yaffe,et al.  14-3-3 proteins as signaling integration points for cell cycle control and apoptosis. , 2011, Seminars in cell & developmental biology.

[4]  Christopher D. Putnam,et al.  Aneuploidy Drives a Mutator Phenotype in Cancer , 2011, Science.

[5]  M. Schuler,et al.  Polo-like kinase 1 inhibitors in mono- and combination therapies: a new strategy for treating malignancies , 2011, Expert review of anticancer therapy.

[6]  Otto Hudecz,et al.  Spatial Exclusivity Combined with Positive and Negative Selection of Phosphorylation Motifs Is the Basis for Context-Dependent Mitotic Signaling , 2011, Science Signaling.

[7]  T. Pawson,et al.  AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade , 2010, Nature Cell Biology.

[8]  I. Gelman,et al.  Emerging Roles for SSeCKS/Gravin/AKAP12 in the Control of Cell Proliferation, Cancer Malignancy, and Barriergenesis. , 2010, Genes & cancer.

[9]  Hae-Ock Lee,et al.  Inhibition of Plk1 induces mitotic infidelity and embryonic growth defects in developing zebrafish embryos. , 2010, Developmental biology.

[10]  Richard D Kolodner,et al.  An overview of Cdk1-controlled targets and processes , 2010, Cell Division.

[11]  Erwin G. Van Meir,et al.  Exciting New Advances in Neuro‐Oncology: The Avenue to a Cure for Malignant Glioma , 2010, CA: a cancer journal for clinicians.

[12]  A. Newton,et al.  Interaction with AKAP79 modifies the cellular pharmacology of PKC. , 2010, Molecular cell.

[13]  T. Pawson,et al.  Cell Signaling in Space and Time: Where Proteins Come Together and When They’re Apart , 2009, Science.

[14]  N. Ahn PORE-ing over ERK substrates , 2009, Nature Structural &Molecular Biology.

[15]  T. Veenstra,et al.  KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals. , 2009, Molecular cell.

[16]  S. Carr,et al.  Plk1 Self-Organization and Priming Phosphorylation of HsCYK-4 at the Spindle Midzone Regulate the Onset of Division in Human Cells , 2009, PLoS biology.

[17]  B. Foster,et al.  Loss of the SSeCKS/Gravin/AKAP12 gene results in prostatic hyperplasia. , 2008, Cancer research.

[18]  Péter Lénárt,et al.  Polo on the Rise-from Mitotic Entry to Cytokinesis with Plk1. , 2008, Developmental cell.

[19]  Kyung S. Lee,et al.  Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-versus non-self-priming , 2008, Cell cycle.

[20]  P. Cohen,et al.  The selectivity of protein kinase inhibitors: a further update. , 2007, The Biochemical journal.

[21]  Gabriele Schackert,et al.  Long-term survival with glioblastoma multiforme. , 2007, Brain : a journal of neurology.

[22]  Jan-Michael Peters,et al.  Polo-like kinase 1 triggers the initiation of cytokinesis in human cells by promoting recruitment of the RhoGEF Ect2 to the central spindle. , 2007, Developmental cell.

[23]  S. Gammeltoft,et al.  Proteomic screen defines the Polo‐box domain interactome and identifies Rock2 as a Plk1 substrate , 2007, The EMBO journal.

[24]  A. Straight,et al.  Substance Abuse: Resurgence of Teen Inhalant Use , 2005, Environmental health perspectives.

[25]  Chao Zhang,et al.  Chemical genetics reveals the requirement for Polo-like kinase 1 activity in positioning RhoA and triggering cytokinesis in human cells , 2007, Proceedings of the National Academy of Sciences.

[26]  D. Cooper,et al.  An anchored PKA and PDE4 complex regulates subplasmalemmal cAMP dynamics , 2006, The EMBO journal.

[27]  A. Ullrich,et al.  Targeting polo-like kinase 1 for cancer therapy , 2006, Nature Reviews Cancer.

[28]  E. Nigg,et al.  Purification of mitotic spindles from cultured human cells. , 2006, Methods.

[29]  Takeshi Ono,et al.  Regulation of the Expression of Caspase-9 by the Transcription Factor Activator Protein-4 in Glucocorticoid-induced Apoptosis* , 2005, Journal of Biological Chemistry.

[30]  Yanping Sun,et al.  Volume Reconstruction Techniques Improve the Correlation Between Histological and in vivo Tumor Volume Measurements in Mouse Models of Human Gliomas , 2004, Journal of Neuro-Oncology.

[31]  Hsien-yu Wang,et al.  Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2‐adrenergic receptor , 2003, The EMBO journal.

[32]  D. Morrison,et al.  Regulation of MAP kinase signaling modules by scaffold proteins in mammals. , 2003, Annual review of cell and developmental biology.

[33]  Michael B. Yaffe,et al.  The Molecular Basis for Phosphodependent Substrate Targeting and Regulation of Plks by the Polo-Box Domain , 2003, Cell.

[34]  Michael B. Yaffe,et al.  Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs , 2003, Nucleic Acids Res..

[35]  K. Vermeulen,et al.  The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer , 2003, Cell proliferation.

[36]  J. Kere,et al.  Investigatory and analytical approaches to differential gene expression profiling in mantle cell lymphoma , 2002, British journal of haematology.

[37]  P. Unger,et al.  The Src-suppressed C kinase substrate, SSeCKS, is a potential metastasis inhibitor in prostate cancer. , 2001, Cancer research.

[38]  D. Meyer,et al.  Mixed lineage kinase‐dependent JNK activation is governed by interactions of scaffold protein JIP with MAPK module components , 2001, The EMBO journal.

[39]  G. Semenza,et al.  V-SRC induces expression of hypoxia-inducible factor 1 (HIF-1) and transcription of genes encoding vascular endothelial growth factor and enolase 1: involvement of HIF-1 in tumor progression. , 1997, Cancer research.

[40]  X. Lin,et al.  Reexpression of the major protein kinase C substrate, SSeCKS, suppresses v-src-induced morphological transformation and tumorigenesis. , 1997, Cancer research.

[41]  L. Langeberg,et al.  Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein , 1997, Current Biology.

[42]  X. Lin,et al.  A Novel src- and ras-suppressed Protein Kinase C Substrate Associated with Cytoskeletal Architecture* , 1996, The Journal of Biological Chemistry.

[43]  J. Lindstrom,et al.  Molecular cloning and preliminary characterization of a novel cytoplasmic antigen recognized by myasthenia gravis sera. , 1992, The Journal of clinical investigation.