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  2. Sirtuin 4 - Wikipedia

    en.wikipedia.org/wiki/Sirtuin_4

    75387 Ensembl ENSG00000089163 ENSMUSG00000029524 UniProt Q9Y6E7 Q8R216 RefSeq (mRNA) NM_012240 NM_001385733 NM_001385734 NM_001385735 NM_001167691 NM_133760 RefSeq (protein) NP_036372 NP_001161163 NP_598521 Location (UCSC) Chr 12: 120.3 – 120.31 Mb Chr 5: 115.48 – 115.48 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Sirtuin 4, also known as SIRT4, is a mitochondrial protein ...

  3. Sirtuin - Wikipedia

    en.wikipedia.org/wiki/Sirtuin

    In yeast, roundworms, and fruitflies, sir2 is the name of one of the sirtuin-type proteins (see table below). [16] Mammals possess seven sirtuins (SIRT1–7) that occupy different subcellular compartments: SIRT1, SIRT6 and SIRT7 are predominantly in the nucleus, SIRT2 in the cytoplasm, and SIRT3, SIRT4 and SIRT5 in the mitochondria. [2]

  4. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − NH +3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −

  5. Cytochrome c - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c

    In more than thirty species tested in one study, 34 of the 104 amino acids were conserved (identical at their characteristic position). [11] For example, human cytochrome oxidase reacted with wheat cytochrome c, in vitro; which held true for all pairs of species tested. [11] In addition, the redox potential of +0.25 volts is the same in all ...

  6. Pleckstrin homology domain - Wikipedia

    en.wikipedia.org/wiki/Pleckstrin_homology_domain

    Pleckstrin homology domain (PH domain) or (PHIP) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.

  7. Apamin - Wikipedia

    en.wikipedia.org/wiki/Apamin

    Apamin selectively blocks SK channels, a type of Ca 2+-activated K + channel expressed in the central nervous system. Toxicity is caused by only a few amino acids, in particular cysteine 1, lysine 4, arginine 13, arginine 14 and histidine 18. These amino acids are involved in the binding of apamin to the Ca 2+-activated K + channel.

  8. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids with the structure NH + 3 −CXY−CXY−CO − 2, such as β-alanine, a component of carnosine and a few other peptides, are β-amino acids. Ones with the structure NH + 3 −CXY−CXY−CXY−CO − 2 are γ-amino acids, and so on, where X and Y are two substituents (one of which is normally H). [7]

  9. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature.

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