Crossref
journal-article
Springer Science and Business Media LLC
Nature (297)
References
22
Referenced
204
-
Thrower, J. S. et al. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94–102 (2000)
(
10.1093/emboj/19.1.94
) / EMBO J. by JS Thrower (2000) -
Dye, B. T. & Schulman, B. Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu. Rev. Biophys. Biomol. Struct. 36, 131–150 (2007)
(
10.1146/annurev.biophys.36.040306.132820
) / Annu. Rev. Biophys. Biomol. Struct. by BT Dye (2007) -
Petroski, M. & Deshaies, R. Function and regulation of cullin–RING ubiquitin ligases. Nature Rev. Mol. Cell Biol. 6, 9–20 (2005)
(
10.1038/nrm1547
) / Nature Rev. Mol. Cell Biol. by M Petroski (2005) -
Saha, A. & Deshaies, R. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 32, 21–31 (2008)
(
10.1016/j.molcel.2008.08.021
) / Mol. Cell by A Saha (2008) -
Petroski, M. & Deshaies, R. Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34. Cell 123, 1107–1120 (2005)
(
10.1016/j.cell.2005.09.033
) / Cell by M Petroski (2005) -
Ravid, T. & Hochstrasser, M. Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue. Nature Cell Biol. 9, 422–427 (2007)
(
10.1038/ncb1558
) / Nature Cell Biol. by T Ravid (2007) -
Li, W. et al. A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. Nature 446, 333–337 (2007)
(
10.1038/nature05542
) / Nature by W Li (2007) -
Hochstrasser, M. Lingering mysteries of ubiquitin-chain assembly. Cell 124, 27–34 (2006)
(
10.1016/j.cell.2005.12.025
) / Cell by M Hochstrasser (2006) -
Li, W. et al. Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc. Natl Acad. Sci. USA 106, 3722–3727 (2009)
(
10.1073/pnas.0808564106
) / Proc. Natl Acad. Sci. USA by W Li (2009) -
Deshaies, R. J. & Joazeiro, C. A. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 78, 399–434 (2009)
(
10.1146/annurev.biochem.78.101807.093809
) / Annu. Rev. Biochem. by RJ Deshaies (2009) - Fersht, A. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding Ch. 14 (Freeman, 1999) / Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding by A Fersht (1999)
-
Nash, P. et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514–521 (2001)
(
10.1038/35107009
) / Nature by P Nash (2001) -
Orlicky, S. et al. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 112, 243–256 (2003)
(
10.1016/S0092-8674(03)00034-5
) / Cell by S Orlicky (2003) -
Strohmaier, H. et al. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316–322 (2001)
(
10.1038/35095076
) / Nature by H Strohmaier (2001) - Kleiger, G., Saha, A., Lewis, S., Kuhlman, B. & Deshaies, R. Rapid E2–E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell (in the press)
-
Kati, W. M. et al. Mechanism and fidelity of HIV reverse transcriptase. J. Biol. Chem. 267, 25988–25997 (1992)
(
10.1016/S0021-9258(18)35706-5
) / J. Biol. Chem. by WM Kati (1992) -
Petroski, M. et al. Evaluation of a diffusion-driven mechanism for substrate ubiquitination by the SCF-Cdc34 ubiquitin ligase complex. Mol. Cell 24, 523–534 (2006)
(
10.1016/j.molcel.2006.10.010
) / Mol. Cell by M Petroski (2006) -
Feldman, R. M. et al. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221–230 (1997)
(
10.1016/S0092-8674(00)80404-3
) / Cell by RM Feldman (1997) -
Kamura, T. et al. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 13, 2928–2933 (1999)
(
10.1101/gad.13.22.2928
) / Genes Dev. by T Kamura (1999) -
Petroski, M. & Deshaies, R. In vitro reconstitution of SCF substrate ubiquitination with purified proteins. Methods Enzymol. 398, 143–158 (2005)
(
10.1016/S0076-6879(05)98013-0
) / Methods Enzymol. by M Petroski (2005) -
Hao, B. et al. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol. Cell 26, 131–143 (2007)
(
10.1016/j.molcel.2007.02.022
) / Mol. Cell by B Hao (2007) -
Wu, G. et al. Structure of a β-TrCP1-Skp1-β-catenin complex. Mol. Cell 11, 1445–1456 (2003)
(
10.1016/S1097-2765(03)00234-X
) / Mol. Cell by G Wu (2003)
Dates
Type | When |
---|---|
Created | 15 years, 8 months ago (Dec. 1, 2009, 3:19 p.m.) |
Deposited | 2 years, 3 months ago (May 18, 2023, 2:29 p.m.) |
Indexed | 1 week, 1 day ago (Aug. 19, 2025, 6:52 a.m.) |
Issued | 15 years, 8 months ago (Dec. 1, 2009) |
Published | 15 years, 8 months ago (Dec. 1, 2009) |
Published Print | 15 years, 8 months ago (Dec. 1, 2009) |
@article{Pierce_2009, title={Detection of sequential polyubiquitylation on a millisecond timescale}, volume={462}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature08595}, DOI={10.1038/nature08595}, number={7273}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Pierce, Nathan W. and Kleiger, Gary and Shan, Shu-ou and Deshaies, Raymond J.}, year={2009}, month=dec, pages={615–619} }