enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Sirtuin 4 - Wikipedia

    en.wikipedia.org/wiki/Sirtuin_4

    Sirtuin 4, also known as SIRT4, is a mitochondrial protein which in humans is encoded by the SIRT4 gene. [5] [6] SIRT4 is member of the mammalian sirtuin family of proteins, which are homologs to the yeast Sir2 protein. SIRT4 exhibits NAD+-dependent deacetylase activity.

  3. Sirtuin - Wikipedia

    en.wikipedia.org/wiki/Sirtuin

    [2] [3] They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. [2] Chemically, sirtuins are a class of proteins that possess either mono- ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase , demalonylase , demyristoylase and depalmitoylase activity.

  4. 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]

  5. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.

  6. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]

  7. Neuraminidase - Wikipedia

    en.wikipedia.org/wiki/Neuraminidase

    Exo-α-sialidase (EC 3.2.1.18, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids: Hydrolysis of α-(2→3)-, α-(2→6)-, α-(28)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids ...

  8. AOL Mail

    mail.aol.com

    Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!

  9. 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 −