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http://scihub22266oqcxt.onion/10.1074/jbc.M408913200
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  • Overlap of interaction domains indicates a central role of the P protein in assembly and regulation of the Borna disease virus polymerase complex #MMPMID15509569
  • Schneider U; Blechschmidt K; Schwemmle M; Staeheli P
  • J Biol Chem 2004[Dec]; 279 (53): 55290-6 PMID15509569garesp_yesshow ga
  • The active polymerase complex of Borna disease virus is composed of the viral proteins N, P, and L. The viral X (negative regulatory factor) protein acts as a regulator of polymerase activity. Interactions of P with N and X were previously studied, but interactions with L were poorly defined. Using a mammalian two-hybrid system, we observed that L specifically interacts with P but not with N, X, or itself. Mapping of the L-binding domain in the P molecule revealed that it overlaps with two adjacent domains required for multimerization and interaction with N. Competition experiments showed that the interaction between L and P was inefficient when N was present, indicating that L may preferentially interact with free P in infected cells. Interestingly, a multimerization-defective P mutant maintained the ability to interact with L, N, and X but failed to support reporter gene expression from an artificial Borna disease virus minigenome. Furthermore, dominant negative effects on minigenome activity were only observed when P mutants with an intact multimerization domain were used, suggesting that P multimers, rather than monomers, exhibit biological activity. P mutants lacking functional interaction domains for L or N still formed complexes with these viral proteins when wild-type P was available as a bridging molecule, indicating that P multimers have the potential to act as scaffolds on which the RNA polymerase complex is assembled.
  • |Binding, Competitive[MESH]
  • |Borna disease virus/*enzymology[MESH]
  • |Cell Line[MESH]
  • |Chromatography, Gel[MESH]
  • |DNA, Complementary/metabolism[MESH]
  • |DNA-Directed RNA Polymerases/*chemistry[MESH]
  • |Genes, Dominant[MESH]
  • |Humans[MESH]
  • |Mutation[MESH]
  • |Phosphoproteins[MESH]
  • |Plasmids/metabolism[MESH]
  • |Point Mutation[MESH]
  • |Protein Binding[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |Two-Hybrid System Techniques[MESH]
  • |Viral Proteins/*chemistry[MESH]
  • |Viral Structural Proteins/*chemistry/physiology[MESH]


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    55290 53.279 2004