919 resultados para Ostergren, Robert C.: The Europeans: a geography of people, culture and environment
On the relation between extremes of midlatitude cyclones and the atmospheric circulation using ERA40
Resumo:
We have previously identified a cellular protein kinase activity termed TAK that specifically associates with the HIV types 1 and 2 Tat proteins. TAK hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II in vitro in a manner believed to activate transcription [Herrmann, C. H. & Rice, A. P. (1995) J. Virol. 69, 1612–1620]. We show here that the catalytic subunit of TAK is a known human kinase previously named PITALRE, which is a member of the cyclin-dependent family of proteins. We also show that TAK activity is elevated upon activation of peripheral blood mononuclear cells and peripheral blood lymphocytes and upon differentiation of U1 and U937 promonocytic cell lines to macrophages. Therefore, in HIV-infected individuals TAK may be induced in T cells following activation and in macrophages following differentiation, thus contributing to high levels of viral transcription and the escape from latency of transcriptionally silent proviruses.
Resumo:
The replication terminator protein (RTP) of Bacillus subtilis causes polar fork arrest at replication termini by sequence-specific interaction of two dimeric proteins with the terminus sequence. The crystal structure of the RTP protein has been solved, and the structure has already provide valuable clues regarding the structural basis of its function. However, it provides little information as to the surface of the protein involved in dimer-dimer interaction. Using site-directed mutagenesis, we have identified three sites on the protein that appear to mediate the dimer-dimer interaction. Crystallographic analysis of one of the mutant proteins (Y88F) showed that its structure is unaltered when compared to the wild-type protein. The locations of the three sites suggested a model for the dimer-dimer interaction that involves an association between two beta-ribbon motifs. This model is supported by a fourth mutation that was predicted to disrupt the interaction and was shown to do so. Biochemical analyses of these mutants provide compelling evidence that cooperative protein-protein interaction between two dimers of RTP is essential to impose polar blocks to the elongation of both DNA and RNA chains.
Resumo:
Dedication signed by Robert Samber, who seems to have been the translator.
Resumo:
Mode of access: Internet.
Resumo:
Includes index.
Resumo:
Mode of access: Internet.
Resumo:
"A publication of the National Bureau of Economic Research, inc., in cooperation with the Committee on Recent Economic Changes."
Resumo:
Description based on: 1962.
Resumo:
Robert E. Whitmoyer, OARDC Historical Records Officer.
Resumo:
Mode of access: Internet.
Resumo:
Lists of club's members : [3] p. at end.
Resumo:
Mode of access: Internet.
Resumo:
Mode of access: Internet.