Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

By N. Zheng, Brenda A. Schulman, Langzhou Song, Julie J. Miller, Philip D. Jeffrey, Ping Wang, C. Chu, D. M. Koepp, Stephen J. Elledge, M. Pagano and 4 more. Nature, 2002

1,528 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/d8bbdeb33e01e07dda32273e678953905d9816cb

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In Molecular Biology

1. Masayuki Yamamoto
2. Donna D. Zhang
3. A. Dinkova-Kostova
4. Liam Baird
5. K. I. Tong
6. Mark Hannink
7. A. Kobayashi
8. Moon-Il Kang

In Oncology

1. Donna D. Zhang
2. M. Estelle
3. Mark Hannink
4. M. Eddins
5. J. Harper
6. J. Peters
7. A. Dinkova-Kostova
8. A. Rustgi

Citations in the corpus

• Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsis1[w] (2005, background): “1; Kamura et al., 1999; Chen et al., 2000; Zheng et al., 2002).”
• Identification, Analysis and Prediction of Protein Ubiquitination Sites (2010, background): “The structures of ubiquitin ligases contain large cavities and gaps13,14,17,18,97 that may serve to accommodate unstructured substrates.”
• RING domain E3 ubiquitin ligases. (2009, background): “RING-HC Cys - X2 - Cys - X(9-39) - Cys - X(1-3) - His - X(2-3) - Cys - X2 - Cys - X(4-48) - Cys - X2 - Cys RING-H2 Cys - X2 - Cys - X(9-39) - Cys - X(1-3) - His - X(2-3) - His - X2 - Cys - X(4-48) - Cys - X2 - Cys C2H2C4 (Mdm2) Cys - X2 - Cys - X10 - His - X4 - His - X3 - Cys - X2 - Cys - X10 - Cys ”
• Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials (2020, background): “The crystal structure of the Skp2–SCF complex shows that Skp2 interacts directly with Skp1 through its F-box domain and indirectly binds to Cul1 and Rbx1.”
• Sequence and structural analysis of BTB domain proteins (2005, methodology): “In Skp1, this region includes a large disordered segment followed by a unique helix α4, but it is not involved in any protein-protein interactions [23-26].”
• A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. (2006, background): “All cullins interact with an E2 binding RING finger protein (Rbx1 or Rbx2) through their C-terminal domain and with substrate receptors via the N terminus (Zheng et al., 2002; Petroski and Deshaies, 2005).”
• Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway (2006, background): “SCF (Skp1-Cullin-F-box protein) is the best studied class of E3 ubiquitin ligases (Zheng et al., 2002).”
• Modeling the CRL4A ligase complex to predict target protein ubiquitination induced by cereblon-recruiting PROTACs (2022, background): “To generate CRL4A ligase complex model, CUL4A (PDBID: 2HYE, with DDB1) was aligned to CUL1 (PDBID: 6TTU) based on partial CTD region (residues 416 – 672).”
• Phosphorylation-Dependent Ubiquitination of Cyclin D1 by the SCFFBX4-αB Crystallin Complex (2006, background): “F-box deletion abrogates SKP1 binding (Zheng et al., 2002), but not substrate or αB crystallin recognition (Fig.”