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Basic domain

Vivi-s, E., Brodin, P., and Lebleu, B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 1997, 272, 16010-16017. [Pg.29]

Robbins, J., Dilworth, S., Laskey, R., and Dingwall, C. (1991). Two interdependent basic domains in nucleoplasmin nuclear targeting sequence identification of a class of bipartite nuclear targeting sequences. Cell 64, 615-623. [Pg.340]

The domains (as we have defined them) within a subunit very often resemble each other (as discussed in Section IV,B), and those similar domains are frequently related by an approximate 2-fold axis. The 2-fold relationship often occurs even in cases in which it involves considerable inconvenience because the start and end of the chain are on opposite sides of the basic domain structure, so that a long additional... [Pg.249]

Ignatovich lA, Dizhe EB, Pavlotskaya AV, et al. Complexes of plasmid DNA with basic domain 47-57 of the HlV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways. J Biol Chem 2003 278(43) 42625-42636. [Pg.312]

Rusnati M, Tulipano G, Urbinati C, et al. The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists. J Biol Chem 1998 273(26) 16027-16037. [Pg.313]

Filikov, A.V. and James, T.L. Structure-based design ofligands for protein basic domains application to the HIV-1 Tat protein./.Comput.-Aided Mol. Des. 1998, 12, 229-240. [Pg.113]

Detert H, Seifert R, Schunack W (1996) Cationic amphiphiles with G-protein-stimulatory activity studies on the role of the basic domain in the activation process. Pharmazie 51 67-72 DeVries L, Farquhar MG (1999) RGS proteins more than just GAPs for heterotrimeric G proteins. Trends Cell Biol 9 138-144... [Pg.75]

The point group P C PBL and when P = PBL (which is so for a holosymmetric space group) the points and lines of symmetry mark out the basic domain il of the Brillouin zone. When... [Pg.331]

Figure 16.14. Brillouin zone of the reciprocal lattice of the strictly 2-D square lattice. The symmetry points mark out the basic domain Z and Z are equivalent points. Figure 16.14. Brillouin zone of the reciprocal lattice of the strictly 2-D square lattice. The symmetry points mark out the basic domain Z and Z are equivalent points.
DNA binding domains called basic domains (rich in basic amino acids), occur in transcription factors in combination with leucine zipper or helix-loop-helix (HLH) dimerization domains (see below). The combination of basic domain and dimerization domain gives these proteins their names of basic leucine zipper proteins (bZIP) or basic HLH proteins, respectively. In each case the dimerization means that two basic domains (one from each monomer) interact with the target DNA. [Pg.192]

Fig. 5. (a) A bZIP protein dimer showing the leucine zipper dimerization domain and the two basic domains (b) folded structure of a bZIP protein showing the basic domains binding in the major groove of the target DNA. Reprinted from A. Travers, DNA-Protein Interactions, Chapman Hall, 1993. With permission from A. Travers. [Pg.193]

Figure 13.12. The Nrf family and Maf family transcription factors. The basic domain is involved in DNA binding and the leucine zipper domain is a dimerization module with other basic-leucine zipper transcription factors. Small Maf proteins such as MafK and MafG het-erodimerize with Nrf2 for binding and activation of the ARE. Figure 13.12. The Nrf family and Maf family transcription factors. The basic domain is involved in DNA binding and the leucine zipper domain is a dimerization module with other basic-leucine zipper transcription factors. Small Maf proteins such as MafK and MafG het-erodimerize with Nrf2 for binding and activation of the ARE.
The incorporation of a weak-acid and a weak-base resin into a crosslinked inert matrix or adjustment of the polymerization procedure of a mixture of weak-acid and weak-base monomers (or their derivatives) so that discrete acidic and basic domains would be formed has led to the development of a new class of ion-exchange resins known as thermally regenerable resins which will be discussed in the next section. [Pg.94]

The electron micrographs of no-matrix resins prepared by the precursor method show that there are discrete acidic and basic domains in which the acidic groups are in effect, embedded in a matrix of the polyamine. A possible mode of polymerization is one in which block copolymers are formed as a result of the formation, initially, of a macroradical. The marked dependence of the thermally regenerable capacity of a resin on the solvent suggests that a macroradical may be involved, since their formation and stability are also greatly dependent on the solvent. However, a study of some linear analogues suggests that this is an oversimplified picture. [Pg.107]

It should be clear from the above that there are a number of variations of the basic domain decomposition algorithm for short-range interaction and there is still a lot of room for improvement both in the methods and the implementations. [Pg.255]

When using these formal tools, there are four basic domains of bioethics wherein they are applied. These are the following ... [Pg.590]

The C terminus of p53 contains a basic domain where DNA can be bound in a nonspecific way. Furthermore, the C-terminal domain contains several sites for post-translational modifications, including Ser-phosphorylation, Lys-acetylation, ubiquitination, and Lys-sumoylation. Futhermore, sequence signals for nuclear localization, sequence sections for tetramerization, and binding sites for transcription factors are found in the C-terminal part. Overall, the C-terminal domain has an important function for the regulation of p53. There is experimental evidence that specific DNA binding of the core domain is controlled by phosphorylation of the C-terminal domain. [Pg.496]

Kjems, J. and Sharp, P.A. (1993). The basic domain of Rev from human immunodeficiency virus type 1 specifically blocks the entry of U4/U6.U5... [Pg.231]


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See also in sourсe #XX -- [ Pg.331 ]




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