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204 Initiation factors

Find the optimum response for the response surface in Figure 14.7 using the fixed-sized simplex searching algorithm. Use (0, 0) for the initial factor levels, and set the step size for each factor to 1.0. [Pg.672]

Each row is formed by representing aU possible assignments of electron i to all orbital-spin combinations. The initial factor is necessary for normalization. Swapping two electrons corresponds to interchanging two rows of the determinant, which will have the effect of changing its sign. [Pg.260]

Increased protein synthesis Increased amino acid uptake/increased translation of mRNA Akt-mediated stimulation of system A amino acid transporter and stimulation of mRNA-translation through activation of p70S6kinase and elongation initiation factor 4 (elF4). Possible involvement of atypical PKCs... [Pg.634]

Rarely has any research area so continuously been in the focus of scientific interest as organosilicon chemistry. A rapidly increasing number of publications, review articles, and scientific conferences reflects this development. The initiating factor was the spectacular discovery of stable molecules with SiSi double bonds, disilaethenes (disilenes) by R. West and S. Masamune in 1981 and 1982 [1-7]. [Pg.3]

Initiation of protein synthesis requires that an mRNA molecule be selected for translation by a ribosome. Once the mRNA binds to the ribosome, the latter finds the correct reading frame on the mRNA, and translation begins. This process involves tRNA, rRNA, mRNA, and at least ten eukaryotic initiation factors (elFs), some of which have multiple (three to eight) subunits. Also involved are GTP, ATP, and amino acids. Initiation can be divided into four steps (1) dissociation of the ribosome into its 40S and 60S subunits (2) binding of a ternary complex consisting of met-tRNAf GTP, and eIF-2 to the 40S ribosome to form a preinitiation complex (3) binding of mRNA to the 40S preinitiation complex to form a 43S initiation complex and (4) combination of the 43S initiation complex with the 60S ribosomal subunit to form the SOS initiation complex. [Pg.365]

Two initiation factors, eIF-3 and elF-lA, bind to the newly dissociated 40S ribosomal subunit. This delays its reassociation with the 60S subunit and allows other translation initiation factors to associate with the 40S subunit. [Pg.365]

Previously, it has been reported that the amounts of eukaryotic initiation factors in wheat germ extract prepared by a common method were deficient for the translation of some kinds of mRNAs including a-amylase mRNA and (i-globin mRNA [2]. Therefore, it can be expected that the activity of wheat germ extract prepared by a common method can be enhanced by the simple addition of extract containing deficient initiation factors. In this study, a wheat germ extract was further purified partially by ammonium sulfate fractionation... [Pg.169]

The catalytic activities of the fortified wheat germ cell-free systems supplemented with each fraction were investigated (Fig. 2). As shown in Fig. 2, only 0 - 40 % ammonium sulfate fraction showed an enhancement in DHFR protein synthesis. This enhancement of protein experimental results and the fact that the various eukaryotic initiation factors are contained in synthesis was also confirmed by SDS-PAGE and autoradiography (Fig. 3). From the above 0-40 % ammonium sulfate fraction [5, 6], it can be concluded that the amount of initiation factors in a conventionally prepared wheat germ cell-fi extract is deficient for the translation of DHFR with internal ribosome entry site. Therefore, it needs to supplement a wheat germ cell-free extract with the fraction containing the limited initiation factors for the efficient protein translation, and this fortified cell-free system can be easily made by simple... [Pg.171]

Initiation factors, which directly cause CKD. These factors are modifiable by pharmacologic therapy. [Pg.375]

Roy, A. L., Meisteremst, M., Pognonec, P., and Roeder, R. G. (1991). Cooperative interaction of an initiator-binding transcription initiation factor and helix-loop-helix activator USF. Nature 354 245-248. [Pg.147]

Schmidt More specifically, most people in the translation field would say that it is translation and initiation factors. [Pg.40]

Nurse Do you think that initiation factors are the limiting component for translation ... [Pg.40]

Figure 7.5 Model of ferritin (and erythroid a-aminolaevulinate synthase) translation/ribosome binding regulation by IRP. In (a), with IRP not bound to the IRE (1) binding of the 43S preinitiation complex (consisting of the small ribosomal 40S subunit, GTP and Met-tRNAMet) to the mRNA is assisted by initiation factors associated with this complex, as well as additional eukaryotic initiation factors (elFs) that interact with the mRNA to facilitate 43S association. Subsequently (2), the 43S preinitiation complex moves along the 5 -UTR towards the AUG initiator codon, (3) GTP is hydrolysed, initiation factors are released and assembly of the 80S ribosome occurs. Protein synthesis from the open reading frame (ORF) can now proceed. In (b) With IRP bound to the IRE, access of the 43S preinitiation complex to the mRNA is sterically blocked. From Gray and Hentze, 1994, by permission of Oxford University Press. Figure 7.5 Model of ferritin (and erythroid a-aminolaevulinate synthase) translation/ribosome binding regulation by IRP. In (a), with IRP not bound to the IRE (1) binding of the 43S preinitiation complex (consisting of the small ribosomal 40S subunit, GTP and Met-tRNAMet) to the mRNA is assisted by initiation factors associated with this complex, as well as additional eukaryotic initiation factors (elFs) that interact with the mRNA to facilitate 43S association. Subsequently (2), the 43S preinitiation complex moves along the 5 -UTR towards the AUG initiator codon, (3) GTP is hydrolysed, initiation factors are released and assembly of the 80S ribosome occurs. Protein synthesis from the open reading frame (ORF) can now proceed. In (b) With IRP bound to the IRE, access of the 43S preinitiation complex to the mRNA is sterically blocked. From Gray and Hentze, 1994, by permission of Oxford University Press.
Isolation and Identification of Eukaryotic Initiation Factor 4A as a Molecular Target for the Marine Natural Product Pateamine A 303... [Pg.6]

Purification of FLAG-Tagged Eukaryotic Initiation Factor 2B Complexes, Subcomplexes, and Fragments from Saccharomyces cerevisiae... [Pg.39]

Alone, P. V., and Dever, T. E. (2006). Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP—GTP exchange factors eIF5 and eIF2B epsilon. J. Biol. Client. 281, 12636—12644. [Pg.49]

Anthony, T. G., Fabian, J. R., Kimball, S. R., and Jefferson, L. S. (2000). Identification of domains within the epsilon-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation. Biochim. Biophys. Acta 1492, 56—62. [Pg.49]

Bieniossek, C., Schutz, P., Bumann, M., Limacher, A., Uson, I., and Baumann, U. (2006). The crystal stmcture of the carboxy-terminal domain of human translation initiation factor eIF5. /. Mol. Biol. 360, 457—465. [Pg.49]

Boesen, T., Mohammad, S. S., Pavitt, G. D., and Andersen, G. R. (2004). Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. /. Biol. Chem. 279, 10584—10592. [Pg.49]

Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., andTrachsel, H. (1977). Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis. Cell 11, 187-200. [Pg.49]


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