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Sequences nature

Determining the Amino Acid Sequence Nature of Amino Acid Sequences Synthe.sis of Polypeptides in the Laboratory... [Pg.107]

FI. Faik, P., Walker, J. I. H., Redmill, A. A. M., and Morgan, M. J Mouse glucose-6-phosphate iso-merase and neuroleukin have identical 3 sequences. Nature 332,455-457 (1988). [Pg.40]

Sieber, V., Martinez, C.A. and Arnold, F.H. (2001) Libraries of hybrid proteins from distantly related sequences. Nature Biotechnology, 19, 456-460. [Pg.77]

Fraser CM, Eisen JA, Saizberg SL. Microbial genome sequencing. Nature 2000 406[6797] 799-803. [Pg.33]

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998 393[6685] 537—544. [Pg.33]

Chakravarti A. Population geneticsmaking sense out of sequence. Nature Genet 1999 21[1 Suppl) 56-60. [Pg.35]

Pennacchio LA, Rubin EM. Genomic strategies to identify mammalian regulatory sequences. Nature Rev Genet 2001 2 100-109. [Pg.56]

Roest Croellius H et al. Estimate of human gene number provided by genomewide analysis using Tetradon nigroviridis DNA sequence. Nature Genet 2000 25 235-238. [Pg.112]

Cole, S.T., et al., "Deciphering the Biology of Mycobacterium tuberculosis from the Complete Genome Sequence," Nature, 393, 537-544 (1998). [Pg.161]

Normal biochemical events surrounding the maintenance and functions of the nervous system centers around energy metabolism, biosynthesis of macromolecules, and neurotransmitter synthesis, storage, release, uptake, and degradation. Measurement of these events is complicated by the sequenced nature of the components of the nervous system and the transient and labile nature of the moieties involved. Use of measurements of alterations in these functions as indicators of neurotoxicity is further complicated by our lack of a complete understanding of the normal operation of these systems and by the multitude of day-to-day occurrences (such as diurnal cycle, diet, temperature, age, sex, and endocrine status) which are constantly modulating the baseline system. For detailed discussions of these difficulties, the reader is advised to see Damstra and Bondy (1980, 1982). [Pg.756]

Adams, M. D., Kerlavage, A. R., Fleischmann, R. D., Fuldner, R. A., Bult, C. J., Lee, N. H., Kirkness, E. F., Weinstock, K. G., Gocayne,J. D., White, O., etal. (1995). Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. Nature 377, 3S-174S. [Pg.270]

Schumacher, M. Camp, S. Maulet, Y. Newton, M. MacPhee-Quigley, K. Taylor, S. S. Friedmann, T. Taylor, P. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature 1986, 319, 407 09. [Pg.196]

S Sabbah, GKE Scriba. Separation of dipeptide and tripeptide enantiomers in capillary electrophoresis using carboxymethyl-beta-cyclodextrin and succinyl-beta-cyclodextrin. Influence of the amino acid sequence, nature of the cyclodextrin and pH. Electrophoresis 22 1385-1393, 2001. [Pg.113]

Claesson-Welsh, L. (1994). Platelet-derived growth factor receptor signals. J. Biol. Chem. 269(51), 32023-32026. Downward, J. et al. (1984). Close similarity of EGF receptor and V-erb-B oncogene protein sequences. Nature 307, 521-527. [Pg.300]

M. Noda, H. Takahashi, T. Tanabe, M. Toyosato, Y. Enrutani, T. Hirose, M. Asak, S. Inayama, T. Miyata, S. Numa (1982). Primary structure of a-subunit precursor of Torpedo califomica acetylchohne receptor from cDNA sequence. Nature 299 793-802. [Pg.300]

M. Noda, S. Shimizu, T. Tanabe, T, Takai, T. Kayano, T. Ikeda, H. Takahashi, H. Nakayama, Y. Kanaoka, N. Minamino (1984). Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence. Nature 312 121-127. [Pg.464]

Parkhill, J. Wren, B.W. Mungall, K. et al. The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature, 403, 665-668 (2000)... [Pg.473]

Noda, M. et al. (1982). primary structure of the a subunit precursor of Torpedo acetylcholine receptor deduced from cDNA sequence. Nature (London) 299, 793-797. [Pg.265]

Wilson, T. and Treisman, R. (1988) Removal of poly (A) and consequent degradation of c-fos mRNA facilitated by AU-rich sequences. Nature, 336, 396-399. [Pg.12]

ST Cole, R Brosch, J Parkhill, T Gamier, C Churcher, D Harris, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 537-544, 1998. [Pg.282]

MacLennan, D.H., Brandi, C.J., Korczak, B., Green, N.M. (1985). Amino-add sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature (London) 316,696-700. [Pg.63]

Before cloning and routine sequence analysis, DNA renaturation provided the only method for comparing nucleic acid sequences. Naturally, for a time, the importance of this approach decreased as the newer methods became routine. However, the availability of oligonucleotides for use as hybridization probes and PCR primers has reinvigorated the usefulness of nucleic acid hybridization as a complement to DNA sequence analysis. [Pg.232]

Polypeptide lengths refer to mature proteins, as predicted from cDNA sequences, after removal of cleavable signal peptide sequences. Natural IFN proteins may undergo C-terminal processing so that shorter forms may be generated. [Pg.3]

P.S., Context-dependent secondary structnre formation of a designed peptide sequence. Nature 380, 730-734, 1996 Mezei, M., Chameleon sequences in the PDB, Protein. Eng. 11,411 14,1998 Tidow, H. etal.. The solution structure of a chimeric LEKTI domain reveals a chameleon sequence. Biochemistry 43, 11238-11247, 2004. [Pg.69]

Minor DL Jr, Kim PS. Context-dependent secondary structure formation of a designed protein sequence. Nature 1996 380 730-734. [Pg.26]

Noda M, Takahashi H, Tanabe T, Toyosato M, Eurutani Y, Hirose T, Asai M, Inayama S, Miyata T, Numa S. Primary structure of alpha-subunit precursor of Torpedo califomica acetylchoUne receptor deduced from cDNA sequence. Nature 1982 299 793-797. [Pg.808]

Schneider C, Owen MJ, Banville D, Williams JG. 1984. Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature 311 675-78... [Pg.654]


See other pages where Sequences nature is mentioned: [Pg.32]    [Pg.204]    [Pg.720]    [Pg.11]    [Pg.282]    [Pg.22]    [Pg.377]    [Pg.609]    [Pg.46]    [Pg.4]    [Pg.406]    [Pg.164]    [Pg.244]    [Pg.307]    [Pg.14]   
See also in sourсe #XX -- [ Pg.67 ]




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