Mechanisms underlying ubiquitination.

By C. Pickart. Annual Review of Biochemistry, 2001

3,851 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/3e3da579177db5b560be0579b83ac627a552d2f1

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In Molecular Biology

1. Donna D. Zhang
2. D. Komander
3. Ivan Dikic
4. M. Hochstrasser
5. Aaron Ciechanover
6. W. Gu
7. M. Estelle
8. C. Brooks

In Oncology

1. D. Komander
2. Donna D. Zhang
3. M. Hochstrasser
4. W. Gu
5. Ivan Dikic
6. C. Brooks
7. M. Estelle
8. Aaron Ciechanover

Citations in the corpus

• The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “Most E2s interact with several E3s (Fig.”
• Ubiquitin: structures, functions, mechanisms. (2004, background): “[29]) and the E6AP locus is mutated in a human disease known as Angelman syndrome (see Ref.”
• Metabolic rate depression in animals: transcriptional and translational controls (2004, background): “Ubiquitindependent proteolysis is one of the major modes of cellular proteolysis ; conjugation with a polymer of ubiquitin tags proteins for degradation by the 26S proteasome whereas monoubiquitylated proteins are targeted for endocytosis and degradation in lysosomes (Pickart, 2001).”
• Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex (2002, background): “Ubiquitin-protein ligases (also known as E3s) act at the last step of a three-enzyme cascade involving the ubiquitin-activating (E1) and ubiquitin-conjugating (E2) enzyme”
• Reading protein modifications with interaction domains (2006, background): “Ubiquitylation is inducible (for example, by growth factors, cytokines, DNA damage and cell-cycle transitions), reversible, and occurs through the regulated function of ubiquitin-activating (E1), ubiquitin-conjugating (E2) and ubiquitin-ligase (E3) enzyme”
• The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif (2003, background): “Proteins that are selected for proteasomal degradation are covalently marked by polyubiquitinatio”
• IAPs, RINGs and ubiquitylation (2005, background): “Conjugation of the 76-amino-acid ubiquitin peptide to a protein substrate involves a cascade of three, sometimes four, enzymes that are known as E1, E2, E3 and E4 (see Box 2 ; reviewed in Ref”
• Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. (2004, background): “Using antisera to the PRC2 proteins Suz12 or Eed to identify Xi domains, we ob-characteristic of ubiquitin and SUMO E3 ligases (re- viewed in Pickart, 2001). served Xi enrichment of Ring1B (Figure 1A) and also Mel18 and Mph2 (not shown).”
• Auxin receptors and plant development: a new signaling paradigm. (2008, background): “A third protein or protein complex called the Ub-protein ligase (E3) interacts with both the Ub-E2 and specific substrate proteins, thus promoting the transfer of Ub to the substrate (Hershko & Ciechanover 1998, Pickart 2001).”
• Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains (2009, background): “Ubiquitination involves the formation of an isopeptide linkage between the carboxy terminus of ubiquitin and the amino group of a substrate lysine side chain (Pickart, 2001).”
• Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation (2004, background): “Polyubiquitin chains may be formed in vivo by three linkages within ubiquitin: K29, K48, and K63 (45).”