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Gene sequence conservation

Holland, P.W.H., Holland, L.Z., Williams, N.A., and Holland, N.D., An amphioxus homeobox gene sequence conservation, spatial expression during development and insights into vertebrate evolution. Development, 116, 653-661, 1992. [Pg.273]

Toumier-Lasserve, E, Odenwald, W. F Garbem, J., Trojanowski, J., and Lazzarini, R. A. (1989). Remarkable intron and exon sequence conservation in human and mouse homeobox 1.3 genes. Mol. Cell Biol. 9 2273-2278. [Pg.124]

ExPASy (Expert Protein Analysis System, www.expasy.ch) or the National Centre for Biotechnology Information (NCBI, www.ncbi.nlm.gov) websites. Both websites provide bioinformatics tools, links to sequence databases and extensive bibliographic resources. As an example of the wealth of information available on individual enzymes, at the time of writing a search based on nitrilase in the Entrez protein section of NCBI will recover more than 10000 references to nitrilase enzyme amino acid sequences. These can be rapidly screened online by organism, and the individual entries will have links to amino acid and gene sequence, relevant literature and information on protein features (such as conserved domains). [Pg.90]

Benveniste, R., Callahan, R., Sherr, C., Chapman, V. and Todaro, G. (1977) Two distinct endogenous type C viruses isolated from the Asian rodent Mus cervicolor. Conservation of viral gene sequences in related rodent species. J Virol 21, 849-862. [Pg.242]

Figure 2 Order and organization of enniatin synthetase and cyclosporin synthetase as deduced from gene sequence and biochemical characterization. Symbols in the adenylateforming modules (black boxes) indicate the corresponding activated amino acids. M stands for A -methyltransferase domain. Condensation domains are represented by white boxes. (A) Top Structure of enniatin synthetase. EA represents the D-Hiv-activating module EB represents the L-valine-activating module D-Ehv is D-2-hydroxyisovaleric acid. Bottom Structural features of the wild-type A -methyltransferase domain M of esynl. The black boxes indicate conserved motifs which can be found within methyltransferases and A -methyltransferase domains of peptide synthetases (see also Fig. 3). The numbers indicate the amino acid position in the sequence of Esyn. (B) Structure of cyclosporin synthetase. Abu = L-a-aminobutyric acid Bmt = (4A)-4-[(E)-2-butenyl]-4-methyl-L-threonine. Figure 2 Order and organization of enniatin synthetase and cyclosporin synthetase as deduced from gene sequence and biochemical characterization. Symbols in the adenylateforming modules (black boxes) indicate the corresponding activated amino acids. M stands for A -methyltransferase domain. Condensation domains are represented by white boxes. (A) Top Structure of enniatin synthetase. EA represents the D-Hiv-activating module EB represents the L-valine-activating module D-Ehv is D-2-hydroxyisovaleric acid. Bottom Structural features of the wild-type A -methyltransferase domain M of esynl. The black boxes indicate conserved motifs which can be found within methyltransferases and A -methyltransferase domains of peptide synthetases (see also Fig. 3). The numbers indicate the amino acid position in the sequence of Esyn. (B) Structure of cyclosporin synthetase. Abu = L-a-aminobutyric acid Bmt = (4A)-4-[(E)-2-butenyl]-4-methyl-L-threonine.
Eukaryotic homology, gene-orientated clusters of transcript sequences, conserved protein domain, markers and mapping, population study (PopSet), expression and molecular abundance profiles (GEO), and GEO data sets and cancer chromosomes. [Pg.498]


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See also in sourсe #XX -- [ Pg.28 ]




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Gene sequences

Sequence conservation

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