Identification of protein kinase CK2 as a potent kinase of Epstein-Barr virus latent membrane protein 1.

[1]  A. Rickinson Epstein-Barr virus. , 2001, Virus research.

[2]  R. Cardiff,et al.  Protein kinase CK2 in mammary gland tumorigenesis , 2001, Oncogene.

[3]  S. Davies,et al.  Selectivity of 4,5,6,7‐tetrabromobenzotriazole, an ATP site‐directed inhibitor of protein kinase CK2 (‘casein kinase‐2’) , 2001, FEBS letters.

[4]  Marco Antonio Boschetti,et al.  Unique features of HIV‐1 Rev protein phosphorylation by protein kinase CK2 (‘casein kinase‐2’) , 2000, FEBS letters.

[5]  D. Seldin,et al.  Endogenous Protein Kinase CK2 Participates in Wnt Signaling in Mammary Epithelial Cells* , 2000, The Journal of Biological Chemistry.

[6]  A. Ciechanover,et al.  Degradation of the Epstein-Barr Virus Latent Membrane Protein 1 (LMP1) by the Ubiquitin-Proteasome Pathway , 2000, The Journal of Biological Chemistry.

[7]  S. Leung,et al.  CTL Control of EBV in Nasopharyngeal Carcinoma (NPC): EBV-Specific CTL Responses in the Blood and Tumors of NPC Patients and the Antigen-Processing Function of the Tumor Cells1 , 2000, The Journal of Immunology.

[8]  K. Ahmed,et al.  Antisense oligonucleotides against protein kinase CK2‐α inhibit growth of squamous cell carcinoma of the head and neck in vitro , 2000, Head & neck.

[9]  U. Wirkner,et al.  Transcription Factors Ets1, NF-κB, and Sp1 Are Major Determinants of the Promoter Activity of the Human Protein Kinase CK2α Gene* , 2000, The Journal of Biological Chemistry.

[10]  D. Schmitt,et al.  The disruption of adherens junctions is associated with a decrease of E-cadherin phosphorylation by protein kinase CK2. , 2000, Experimental cell research.

[11]  R. Everett,et al.  The Multifunctional Herpes Simplex Virus IE63 Protein Interacts with Heterogeneous Ribonucleoprotein K and with Casein Kinase 2* , 1999, The Journal of Biological Chemistry.

[12]  E. Kieff,et al.  The Epstein-Barr Virus Oncoprotein Latent Membrane Protein 1 Engages the Tumor Necrosis Factor Receptor-Associated Proteins TRADD and Receptor-Interacting Protein (RIP) but Does Not Induce Apoptosis or Require RIP for NF-κB Activation , 1999, Molecular and Cellular Biology.

[13]  L. Young,et al.  Activation of the p38 mitogen-activated protein kinase pathway by Epstein-Barr virus-encoded latent membrane protein 1 coregulates interleukin-6 and interleukin-8 production. , 1999, The Journal of biological chemistry.

[14]  M. Ueffing,et al.  Latent membrane protein 1 of Epstein–Barr virus interacts with JAK3 and activates STAT proteins , 1999, The EMBO journal.

[15]  W. Hammerschmidt,et al.  LMP1 signal transduction differs substantially from TNF receptor 1 signaling in the molecular functions of TRADD and TRAF2 , 1999, The EMBO journal.

[16]  L. Young,et al.  Epstein-Barr Virus-Encoded Latent Membrane Protein 1 Activates the JNK Pathway through Its Extreme C Terminus via a Mechanism Involving TRADD and TRAF2 , 1999, Journal of Virology.

[17]  V. Godfrey,et al.  Expression of the Epstein-Barr virus latent membrane protein 1 induces B cell lymphoma in transgenic mice. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[18]  S. Yang,et al.  Identification of the regulatory autophosphorylation site of autophosphorylation-dependent protein kinase (auto-kinase). Evidence that auto-kinase belongs to a member of the p21-activated kinase family. , 1998, The Biochemical journal.

[19]  P. Farrell Signal transduction from the Epstein-Barr virus LMP-1 transforming protein. , 1998, Trends in microbiology.

[20]  E. Kieff,et al.  The Epstein–Barr virus oncogene product latent membrane protein 1 engages the tumor necrosis factor receptor-associated death domain protein to mediate B lymphocyte growth transformation and activate NF-κB , 1997 .

[21]  E. Kieff,et al.  Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation , 1996, Molecular and cellular biology.

[22]  E. Kieff,et al.  Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[23]  R. Garcea,et al.  In Vitro Phosphorylation of the Polyomavirus Major Capsid Protein VP1 on Serine 66 by Casein Kinase II (*) , 1995, The Journal of Biological Chemistry.

[24]  P. Leder,et al.  Association of Elevated Protein Kinase CK2 Activity with Aggressive Behavior of Squamous Cell Carcinoma of the Head and Neck , 1995, Molecular medicine.

[25]  C. Ware,et al.  The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family , 1995, Cell.

[26]  E. Kieff,et al.  The Epstein-Barr virus LMP1 cytoplasmic carboxy terminus is essential for B-lymphocyte transformation; fibroblast cocultivation complements a critical function within the terminal 155 residues , 1995, Journal of virology.

[27]  G. Klein Epstein-Barr virus strategy in normal and neoplastic B cells , 1994, Cell.

[28]  S. Goueli,et al.  Nuclear casein kinase 2 (CK‐2) activity in human normal, benign hyperplastic, and cancerous prostate , 1994, The Prostate.

[29]  D. Marshak,et al.  Serine-173 of the Epstein-Barr virus ZEBRA protein is required for DNA binding and is a target for casein kinase II phosphorylation. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[30]  E. Kieff,et al.  Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[31]  D. Thorley-Lawson,et al.  Biochemical, genetic, and functional analyses of the phosphorylation sites on the Epstein-Barr virus-encoded oncogenic latent membrane protein LMP-1 , 1993, Journal of virology.

[32]  S. T. Liu,et al.  Cloning and characterization of the latent membrane protein (LMP) of a specific Epstein-Barr virus variant derived from the nasopharyngeal carcinoma in the Taiwanese population. , 1992, Oncogene.

[33]  Chin-Tarng Lin,et al.  Establishment and characterization of two nasopharyngeal carcinoma cell lines. , 1990, Laboratory investigation; a journal of technical methods and pathology.

[34]  D. Thorley-Lawson,et al.  Processing of the Epstein-Barr virus-encoded latent membrane protein p63/LMP , 1990, Journal of virology.

[35]  I. Kameshita,et al.  A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. , 1989, Analytical biochemistry.

[36]  V. Baichwal,et al.  Transformation of Balb 3T3 cells by the BNLF-1 gene of Epstein-Barr virus. , 1988, Oncogene.

[37]  V. Baichwal,et al.  Posttranslational processing of an Epstein-Barr virus-encoded membrane protein expressed in cells transformed by Epstein-Barr virus , 1987, Journal of virology.

[38]  E. Kieff,et al.  Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus , 1986, Journal of virology.

[39]  E. Kieff,et al.  An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells , 1985, Cell.

[40]  D. Staunton,et al.  Epstein-Barr virus-encoded protein found in plasma membranes of transformed cells , 1985, Journal of virology.

[41]  E. Kieff Epstein-Barr virus and its replication , 1996 .

[42]  O. Issinger,et al.  Casein kinases: pleiotropic mediators of cellular regulation. , 1993, Pharmacology & therapeutics.

[43]  D. Thorley-Lawson,et al.  Mutational analysis of the transforming function of the EBV encoded LMP-1. , 1992, Current topics in microbiology and immunology.

[44]  B. Sefton,et al.  Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. , 1989, Analytical biochemistry.