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  1. Tools From Wikipedia, the free encyclopedia Selenocysteine (symbol Sec or U, [2] in older publications also as Se-Cys) [3] is the 21st proteinogenic amino acid. Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in place of the sulfur .

    • C₃H₇NO₂Se
    • .mw-parser-output .plainlist ol,.mw-parser-output .plainlist ul{line-height:inherit;list-style:none;margin:0;padding:0}.mw-parser-output .plainlist ol li,.mw-parser-output .plainlist ul li{margin-bottom:0}10236-58-5
  2. Oct 9, 2012 · Emerging evidence suggests that enzymes responsible for selenocysteine formation and decoding the selenocysteine UGA codon, which by extension are critical for synthesis of the entire selenoproteome, are essential for the development and health of the human organism.

    • Rachel L. Schmidt, Miljan Simonović
    • Rachel L. Schmidt, Miljan Simonović
    • 2012
    • 10.3325/cmj.2012.53.535
  3. General Principle The selenocysteine insertion activity of the computer-selected SECIS candidates can be assayed in vivo by using a suitable reporter system. The DNAs of the SECIS candidates are obtained by polymerase chain reaction (PCR) amplification of genomic DNA, or constructed with oligonucleotide cassettes.

  4. Jun 11, 2018 · We recently discovered allo-tRNAs, tRNA species with unusual structure, that are as efficient serine acceptors as E. coli tRNA Ser. Ser-allo-tRNA was converted into Sec-allo-tRNA by Aeromonas salmonicida selenocysteine synthase (SelA).

    • Takahito Mukai, Anastasia Sevostyanova, Tateki Suzuki, Xian Fu, Dieter Söll
    • 2018
  5. A selenocysteine residue could be embedded within a peptide that has an N-terminal cysteine residue such that the selenocysteine does not participate directly in the ligation reaction. From: Methods in Enzymology, 2002 Related terms: Molybdenum Selenium Cysteine Residue Selenocysteine Cysteine Peroxidase Thioredoxin Amino Acid Glutathione

  6. Jun 6, 2018 · The SelA N-terminal domain binds the elbow region of Ser-tRNA to bring the Ser moiety into the catalytic site of the SelA core domain, and is fixed to the core domain by hydrophobic interactions with a few residues ( We expected that engineering of this inter-domain interaction would fine-tune the orientation of the N-terminal domain and consequ...

  7. A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). [From DeltaMass: Average Mass: 64.] Although selenocysteine-charged tRNA (Sec) is biosynthesized from serine-charged tRNA (Sec), in peptide work selenocysteine is usually considered as either ...

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