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Al-DNA complexes

ACS Symposium Series American Chemical Society Washington, DC, 1980. [Pg.77]

It has previously been shown that Cu ions produce crosslinks between DNA strands (12. 13. 14. 15). Al also produces [Pg.78]

Metal Ions, Genetic Information Transfer and Aging [Pg.78]

The possible Involvement of aluminum in Alzheimer s disease is of Interest in aging because senile dementia is sometimes associated with aging. Metal Ions may be Involved in the aging process in more general ways, as we shall try to demonstrate. [Pg.78]


The interaction of divalent cations with DNA is extensively studied, DNA complexation with trivalent cations is less understood. It was shown that the interaction of Al with DNA produces several types of Al-DNA complexes depending on pH and metal ion concentration. However, the exact cation binding site and the effect of Al interactions on the DNA secondary structure are not determined, particularly at low cation concentrations. Martin [8]... [Pg.95]

Figure 9.12 Schematic diagram of the structure of the heterodimeric yeast transcription factor Mat a2-Mat al bound to DNA. Both Mat o2 and Mat al are homeodomains containing the helix-turn-helix motif. The first helix in this motif is colored blue and the second, the recognition helix, is red. (a) The assumed structure of the Mat al homeodomain in the absence of DNA, based on Its sequence similarity to other homeodomains of known structure, (b) The structure of the Mat o2 homeodomain. The C-terminal tail (dotted) is flexible in the monomer and has no defined structure, (c) The structure of the Mat a 1-Mat a2-DNA complex. The C-terminal domain of Mat a2 (yellow) folds into an a helix (4) in the complex and interacts with the first two helices of Mat a2, to form a heterodimer that binds to DNA. (Adapted from B.J. Andrews and M.S. Donoviel, Science 270 251-253, 1995.)... Figure 9.12 Schematic diagram of the structure of the heterodimeric yeast transcription factor Mat a2-Mat al bound to DNA. Both Mat o2 and Mat al are homeodomains containing the helix-turn-helix motif. The first helix in this motif is colored blue and the second, the recognition helix, is red. (a) The assumed structure of the Mat al homeodomain in the absence of DNA, based on Its sequence similarity to other homeodomains of known structure, (b) The structure of the Mat o2 homeodomain. The C-terminal tail (dotted) is flexible in the monomer and has no defined structure, (c) The structure of the Mat a 1-Mat a2-DNA complex. The C-terminal domain of Mat a2 (yellow) folds into an a helix (4) in the complex and interacts with the first two helices of Mat a2, to form a heterodimer that binds to DNA. (Adapted from B.J. Andrews and M.S. Donoviel, Science 270 251-253, 1995.)...
Billeter, M., et al. Determination of the nuclear magnetic resonance solution structure of an Antennapedia home-odomain DNA complex. /. Mol. Biol. 234 1084-1097, 1993. [Pg.173]

Cho, Y., et al. Crystal structure of a p53 tumor suppres-sor DNA complex understanding tumorigenic mutations. Science 265 346-355, 1994. [Pg.173]

Kissinger, C.R., et al. Crystal structure of an engrailed homeodomain DNA complex at 2.8 A resolution a framework for understanding homeodomain-DNA interactions. Cell 63 579-590, 1990. [Pg.173]

Ellenberger, T.E., et al. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted a helices crystal structure of the protein-DNA complex. Cell 71 1223-1237, 1992. [Pg.203]

According to Barbieri et al., it can not be excluded that some of the coordination sites are occupied by (Nj atoms of the nucleic acid constituents. The precipitate obtained from [Ph2Sn(IV)] would contain both the [R2Sn(IV)] -DNA complex and distannoxane [(Ph2SnCl)20]. The main products of the... [Pg.382]

The large subunit pUL56 is stably associated with the capsid, represents a structural component and forms a dimer with C-2 symmetry (Beard et al. 2004 Catalano 2000 Sheaffer et al. 2001 Yu and Weller 1998 Savva et al. 2004). This structure is the prerequisite for the formation of a protein-DNA complex required for packaging into the procapsid. [Pg.166]

Barton and coworkers have shown that proteins can in fact modulate the DNA electron transfer [168]. Methyltransferases are enzymes that recognize distinct DNA sequences, e.g., 5 -G CGC-3, and effect methylation by extrading the target base cytosine ( C) completely out of the DNA duplex while the remainder of the double helix is left intact. The methyltransferase Hha 1-DNA complex is a well-characterized example, revealing that the structure of the DNA is significantly but locally distorted [169,170]. In a recent study, Raj ski et al. used DNA duplex 20 containing the M.Hha I binding site between two oxidizable 5 -GG-3 sites [168] (Fig. 20). The duplex contains a complementary strand, selectively 5 -modified with a Rh intercalator that can function as a photooxidant. Upon... [Pg.421]

In 1985, it was reported by Hsiang et al. [43] that the cytotoxic activity of 20-(S)-camptothecin (CPT III) was attributed to a novel mechanism of action involving the nuclear enzyme topo I, and this discovery of unique mechanism of action revived the interest in CPT and its analogues as anticancer agents. CPT stabilizes the covalent, reversible topo I-DNA complex leading to the inhibition of DNA synthesis in mammalian cells and interferes with the topo I breakage-reunion reaction [44]. Clinical trials and structure-activity relationships have demonstrated the requirement of the a-hydroxy group, the... [Pg.49]

The DNA forms stable complexes with doxorubicin (Adriamycin, ADR) and daunorubicin (DNR). Doxorubicin and DNR, although structurally similar, show distinctly different properties ADR is more toxic and active than DNR in the treatment of various human solid tumors the apparent binding affinity of ADR to DNA is about 1.8 times higher than that of DNR to DNA. Trouet et al. [229] found the ADR-DNA complex to be more active than ADR, DNR, or DNR-DNA in subcutaneously inoculated leukemic mice, whereas the DNR-DNA complex showed the highest... [Pg.570]

Chamber J et al. DNA microarrays of the complex human cytomegalovirus genome profiling kinetic class with drug sensitivity of viral gene expression. J Virol 1999 73 5757-5766... [Pg.115]

Tousignan JD, Gates AL, Ingram LA et al (2002) Comprehensive analysis of the acute toxicities induced by systemic administration of cationic lipid Plasmid DNA complexes in mice. Hum Gene Ther 11 2493-2513... [Pg.59]

Chollet P, Favrot MC, Hurbin A et al (2002) Side-effects of a systemic injection of linear polyethylenimine-DNA complexes. J Gene Med 4 84—91... [Pg.59]

Peng SF, Yang MJ, Su CJ et al (2009) Effects of incorporation of poly(y-glutamic acid) in chitosan/DNA complex nanoparticles on cellular uptake and transfection efficiency. Biomaterials 30 1797-1808... [Pg.62]


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See also in sourсe #XX -- [ Pg.77 ]




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