When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Ubiquitin D - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_D

    Ubiquitin is a protein composed of 76 amino acids. In order for ubiquitin to bind to other proteins, it must go through an activation process by E1, an ATP-dependent ubiquitin activating enzyme. The carboxyl terminal (C-terminus) of ubiquitin is linked to the cysteine residue of the E1 protein by a high energy thioester linkage and activated.

  3. Ubiquitin - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin

    Ubiquitin is a small protein that exists in all eukaryotic cells. It performs its myriad functions through conjugation to a large range of target proteins. A variety of different modifications can occur. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.6 kDa.

  4. Deubiquitinating enzyme - Wikipedia

    en.wikipedia.org/wiki/Deubiquitinating_enzyme

    These modifications are a post translational modification (addition to a protein after it has been made) where single ubiquitin proteins or chains of ubiquitin are added to lysines of a substrate protein. These ubiquitin modifications are added to proteins by the ubiquitination machinery; ubiquitin-activating enzymes (E1s), ubiquitin ...

  5. Ubiquitin-like protein - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-like_protein

    Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in a cell, usually with a regulatory function. The UBL protein family derives its name from the first member of the class to be discovered, ubiquitin (Ub), best known for its role in regulating protein degradation through covalent modification of other proteins.

  6. Ubiquitin-activating enzyme - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-activating_enzyme

    The ubiquitin-proteasome system is critical to appropriate protein degradation within cells. Dysfunctions of this system can disrupt cellular homeostasis and lead to a host of disorders. In normally functioning cells, the covalent linkage of ubiquitin or ubiquitin-like protein to a target protein changes the target protein's surface.

  7. UBE2D2 - Wikipedia

    en.wikipedia.org/wiki/UBE2D2

    Modifying proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s; ubiquitin-conjugating enzymes, or E2s; and ubiquitin-protein ligases, or E3s.

  8. AOL Mail - AOL Help

    help.aol.com/products/aol-webmail

    Get answers to your AOL Mail, login, Desktop Gold, AOL app, password and subscription questions. Find the support options to contact customer care by email, chat, or phone number.

  9. Ubiquitin-binding domain - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-binding_domain

    The NMR structure of a UBA domain, among the most common types of ubiquitin-binding domain, from the protein ubiquilin-1 (top, cyan) bound to ubiquitin (bottom, orange). ). Isoleucine 44, the center of a hydrophobic patch on the ubiquitin surface that interacts with a number of ubiquitin-binding domains, is highlighted i