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10.1074/jbc.273.15.9007 http://scihub22266oqcxt.onion/10.1074/jbc.273.15.9007 9535888!ä!9535888 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 1998 ; 273 (15): 9007-12 Nephropedia Template TP {{tp|p=9535888|t=1998. Interactions of the borna disease virus P, N, and X proteins and their functional implications |pdf=|usr=}}{{9535888}} gab.com Text Interactions of the borna disease virus P, N, and X proteins and their functional implications JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=9535888 #FOAvip Borna disease virus (BDV) causes persistent central nervous system infection and behavioral disturbances in warm-blooded animals. Protein interaction studies were pursued to gain insight into the functions of the putative nucleoprotein (N), phosphoprotein (P), atypical glycoprotein (gp18), and X protein (X) of BDV. Coimmunoprecipitation experiments indicated that N and P, and P and X, form complexes in infected cells. Two-hybrid analyses confirmed interactions between P and P, P and X, and P and N, but not between P and gp18, N and gp18, X and gp18, or X and N. Analysis of P truncation mutants identified three nonoverlapping regions important for oligomerization (amino acids (aa) 135-172), and binding to X (aa 33-115) or N (aa 197-201). Coexpression of X stimulated oligomerization of P but decreased N-P complex formation. Immunocytochemistry of transfected noninfected CHO cells demonstrated that the distribution of X is dependent upon the presence of P-X expressed alone was found predominantly in the cytoplasm whereas coexpression of X and P resulted in nuclear localization. Immunocytochemistry of infected cells revealed nuclear colocalization of P and X. Interactions of P, N, and X may have implications for regulation of BDV transcription/replication and ribonucleoprotein assembly. Twit Text FOAVip Interactions of the borna disease virus P, N, and X proteins and their functional implications ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=9535888 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=9535888 #FOAvip English Wikipedia <ref>{{Cite pmid|9535888}}</ref> Interactions of the borna disease virus P, N, and X proteins and their functional implications #MMPMID9535888 Schwemmle M; Salvatore M; Shi L; Richt J; Lee CH; Lipkin WI J Biol Chem 1998[Apr]; 273 (15): 9007-12 PMID9535888show ga Borna disease virus (BDV) causes persistent central nervous system infection and behavioral disturbances in warm-blooded animals. Protein interaction studies were pursued to gain insight into the functions of the putative nucleoprotein (N), phosphoprotein (P), atypical glycoprotein (gp18), and X protein (X) of BDV. Coimmunoprecipitation experiments indicated that N and P, and P and X, form complexes in infected cells. Two-hybrid analyses confirmed interactions between P and P, P and X, and P and N, but not between P and gp18, N and gp18, X and gp18, or X and N. Analysis of P truncation mutants identified three nonoverlapping regions important for oligomerization (amino acids (aa) 135-172), and binding to X (aa 33-115) or N (aa 197-201). Coexpression of X stimulated oligomerization of P but decreased N-P complex formation. Immunocytochemistry of transfected noninfected CHO cells demonstrated that the distribution of X is dependent upon the presence of P-X expressed alone was found predominantly in the cytoplasm whereas coexpression of X and P resulted in nuclear localization. Immunocytochemistry of infected cells revealed nuclear colocalization of P and X. Interactions of P, N, and X may have implications for regulation of BDV transcription/replication and ribonucleoprotein assembly. |*Saccharomyces cerevisiae Proteins[MESH] |*Transcription Factors[MESH] |Animals[MESH] |Borna disease virus/genetics/*physiology[MESH] |CHO Cells[MESH] |COS Cells[MESH] |Cell Line[MESH] |Cell Nucleus/metabolism/ultrastructure[MESH] |Cricetinae[MESH] |Cysteine/metabolism[MESH] |DNA-Binding Proteins[MESH] |Fungal Proteins/biosynthesis[MESH] |Macromolecular Substances[MESH] |Methionine/metabolism[MESH] |Open Reading Frames[MESH] |Protein Biosynthesis[MESH] |Protein Multimerization[MESH] |Recombinant Fusion Proteins/biosynthesis[MESH] |Transfection[MESH] |Two-Hybrid System Techniques[MESH]Interactions of the borna disease virus P, N, and X proteins and their(epmc).pdf DeepDyve Pubget Overpricing