RING Domain E3 Ubiquitin Ligases

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O ₂ -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · see citing works

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O ₂ Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · see citing works

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · see citing works

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148 · see citing works

Role of histone H2A ubiquitination in Polycomb silencing

Wang, H., Wang, L., Erdjument‐Bromage, H., Vidal, M., Tempst, P., Jones, R. S., & Zhang, Y. (2004) · Nature · doi:10.1038/nature02985 · Cited by 1,770 · see citing works

Recognition of the polyubiquitin proteolytic signal

Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,718 · see citing works

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688 · see citing works

A proteomics approach to understanding protein ubiquitination

Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D. J., & Gygi, S. P. (2003) · Nature Biotechnology · doi:10.1038/nbt849 · Cited by 1,601 · see citing works

A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535 · see citing works

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

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507 · see citing works

The anaphase promoting complex/cyclosome: a machine designed to destroy

Peters, J.-M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1988 · Cited by 1,315 · see citing works

MOLECULAR PATHOPHYSIOLOGY OF PARKINSON'S DISEASE

Moore, D. J., West, A. B., Dawson, V. L., & Dawson, T. M. (2005) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.28.061604.135718 · Cited by 1,274 · see citing works

SCF and Cullin/RING H2-Based Ubiquitin Ligases

Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238 · see citing works

F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,227 · see citing works

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11364 · Cited by 1,151 · see citing works

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53

Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works

The Tyrosine Kinase Negative Regulator c-Cbl as a RING-Type, E2-Dependent Ubiquitin-Protein Ligase

Joazeiro, C. A. P., Wing, S. S., Huang, H.-K., Leverson, J. D., Hunter, T. R., & Liu, Y. (1999) · Science · doi:10.1126/science.286.5438.309 · Cited by 1,036 · see citing works

Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade

Scheffner, M., Nuber, U. A., & Huibregtse, J. M. (1995) · Nature · doi:10.1038/373081a0 · Cited by 1,017 · see citing works

Ubiquitin Ligase Activity and Tyrosine Phosphorylation Underlie Suppression of Growth Factor Signaling by c-Cbl/Sli-1

Levkowitz, G., Waterman, H., Ettenberg, S. A., Katz, M., Tsygankov, A. Y., Alroy, I., Lavi, S., Iwaï, K., Reiss, Y., Ciechanover, A. J., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80231-2 · Cited by 1,003 · see citing works

Ubiquitin Protein Ligase Activity of IAPs and Their Degradation in Proteasomes in Response to Apoptotic Stimuli

Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M., & Ashwell, J. D. (2000) · Science · doi:10.1126/science.288.5467.874 · Cited by 981 · see citing works

A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.

Feldman, R. M. R., Correll, C. C., Kaplan, K. B., & Deshaies, R. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80404-3 · Cited by 872 · see citing works

Structure of a c-Cbl–UbcH7 Complex

Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839 · see citing works

Genome-Wide and Functional Annotation of Human E3 Ubiquitin Ligases Identifies MULAN, a Mitochondrial E3 that Regulates the Organelle's Dynamics and Signaling

Li, W., Bengtson, M. H., Ulbrich, A., Matsuda, A., Reddy, V. A., Orth, A. P., Chanda, S. K., Batalov, S., & Joazeiro, C. A. P. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001487 · Cited by 839 · see citing works

Diversity of degradation signals in the ubiquitin–proteasome system

Ravid, T., & Hochstrasser, M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2468 · Cited by 825 · see citing works

Noncanonical MMS2-Encoded Ubiquitin-Conjugating Enzyme Functions in Assembly of Novel Polyubiquitin Chains for DNA Repair

Hofmann, R. M., & Pickart, C. M. (1999) · Cell · doi:10.1016/s0092-8674(00)80575-9 · Cited by 815 · see citing works

Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation

Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Fiore, P. P. D., & Đikić, I. (2003) · Nature Cell Biology · doi:10.1038/ncb983 · Cited by 813 · see citing works

Ubiquitin-binding domains

Hicke, L., Schubert, H., & Hill, C. P. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1701 · Cited by 795 · see citing works

Rbx1, a Component of the VHL Tumor Suppressor Complex and SCF Ubiquitin Ligase

Kamura, T., Koepp, D. M., Conrad, M. N., Skowyra, D., Moreland, R. J., Iliopoulos, O., Lane, W. S., Kaelin, W. G., Elledge, S. J., Conaway, R. C., et al. (1999) · Science · doi:10.1126/science.284.5414.657 · Cited by 786 · see citing works

A ubiquitin ligase complex assembles linear polyubiquitin chains

Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., & Iwaï, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601360 · Cited by 772 · see citing works

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767 · see citing works

Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication

Nash, P., Tang, X., Orlicky, S. M., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T. J., & Tyers, M. (2001) · Nature · doi:10.1038/35107009 · Cited by 761 · see citing works

TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases

Meroni, G., & Diez‐Roux, G. (2005) · BioEssays · doi:10.1002/bies.20304 · Cited by 731 · see citing works

Back to the Future with Ubiquitin

Pickart, C. M. (2004) · Cell · doi:10.1016/s0092-8674(03)01074-2 · Cited by 699 · see citing works

A dynamic role of HAUSP in the p53-Mdm2 pathway

Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679 · see citing works

The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation

Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., & Ohta, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000881200 · Cited by 634 · see citing works

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612 · see citing works

Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination.

Scherer, D. C., Brockman, J. A., Chen, Z., Maniatis, T., & Ballard, D. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.11259 · Cited by 554 · see citing works

A novel gysteine-rich sequence motif

Freemont, P. S., Hanson, I. M., & Trowsdale, J. (1991) · Cell · doi:10.1016/0092-8674(91)90229-r · Cited by 545 · see citing works

Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex

Jin, L., Williamson, A. P., Banerjee, S., Philipp, I., & Rapé, M. (2008) · Cell · doi:10.1016/j.cell.2008.04.012 · Cited by 536 · see citing works

Bre1, an E3 Ubiquitin Ligase Required for Recruitment and Substrate Selection of Rad6 at a Promoter

Wood, A., Krogan, N. J., Dover, J., Schneider, J., Heidt, J. W., Boateng, M. A., Dean, K., Golshani, A., Zhang, Y., Greenblatt, J., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00802-x · Cited by 530 · see citing works

Physiological Significance of Reactive Cysteine Residues of Keap1 in Determining Nrf2 Activity

Yamamoto, T., Suzuki, T., Kobayashi, A., Wakabayashi, J., Maher, J. M., Motohashi, H., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01704-07 · Cited by 515 · see citing works

Control of Cyclin Ubiquitination by CDK-Regulated Binding of Hct1 to the Anaphase Promoting Complex

Zachariae, W., Schwab, M., Nasmyth, K., & Seufert, W. (1998) · Science · doi:10.1126/science.282.5394.1721 · Cited by 511 · see citing works

Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase

Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works

Control of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase

Bashir, T., Dorrello, N. V., Amador, V., Guardavaccaro, D., & Pagano, M. (2004) · Nature · doi:10.1038/nature02330 · Cited by 504 · see citing works

Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex

Wei, W., Ayad, N. G., Wan, Y., Zhang, G.-J., Kirschner, M. W., & Kaelin, W. G. (2004) · Nature · doi:10.1038/nature02381 · Cited by 495 · see citing works

Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex

Reverter, D., & Lima, C. D. (2005) · Nature · doi:10.1038/nature03588 · Cited by 493 · see citing works

The COP9 Signalosome

Wei, N., & Deng, X. W. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.112449 · Cited by 492 · see citing works

The anaphase-promoting complex: it's not just for mitosis any morePreprint

Harper, J. W., Burton, J. L., & Solomon, M. J. (2002) · Genes & Development · doi:10.1101/gad.1013102 · Cited by 490 · see citing works

The RING finger domain: a recent example of a sequence—structure family

Borden, K. L. B., & Freemont, P. S. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80060-1 · Cited by 472 · see citing works

Structure of a Fbw7-Skp1-Cyclin E Complex: Multisite-Phosphorylated Substrate Recognition by SCF Ubiquitin Ligases

Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W., & Pavletich, N. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.022 · Cited by 464 · see citing works

ROC1, a Homolog of APC11, Represents a Family of Cullin Partners with an Associated Ubiquitin Ligase Activity

Ohta, T., Michel, J. J. C., Schottelius, A. J. G., & Xiong, Y. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80482-7 · Cited by 461 · see citing works

DCAFs, the Missing Link of the CUL4-DDB1 Ubiquitin Ligase

Lee, J., & Zhou, P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.001 · Cited by 460 · see citing works

Phosphorylation of Sic1p by G 1 Cdk Required for Its Degradation and Entry into S Phase

Verma, R., Annan, R. S., Huddleston, M. J., Carr, S. A., Reynard, G. J., & Deshaies, R. J. (1997) · Science · doi:10.1126/science.278.5337.455 · Cited by 449 · see citing works

A Conserved RING Finger Protein Required for Histone H2B Monoubiquitination and Cell Size Control

Hwang, W. W., Venkatasubrahmanyam, S., Ianculescu, A. G., Tong, A. H. Y., Boone, C. M., & Madhani, H. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00826-2 · Cited by 439 · see citing works

Certain Pairs of Ubiquitin-conjugating Enzymes (E2s) and Ubiquitin-Protein Ligases (E3s) Synthesize Nondegradable Forked Ubiquitin Chains Containing All Possible Isopeptide Linkages

Kim, H. T., Kim, K. P., Lledı́as, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., Gygi, S. P., & Goldberg, A. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609659200 · Cited by 438 · see citing works

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

Kirkpatrick, D. S., Hathaway, N. A., Hanna, J. W., Elsasser, S., Rush, A. J., Finley, D. J., King, R. W., & Gygi, S. P. (2006) · Nature Cell Biology · doi:10.1038/ncb1436 · Cited by 431 · see citing works

The U box is a modified RING finger — a common domain in ubiquitination

Aravind, L., & Koonin, E. V. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00398-5 · Cited by 429 · see citing works

Chaperoned Ubiquitylation—Crystal Structures of the CHIP U Box E3 Ubiquitin Ligase and a CHIP-Ubc13-Uev1a Complex

Zhang, M., Windheim, M., Roe, S. M., Peggie, M. W., Cohen, P., Prodromou, C., & Pearl, L. H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.023 · Cited by 420 · see citing works

COP9 Signalosome

Cope, G. A., & Deshaies, R. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00722-0 · Cited by 409 · see citing works

Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34Preprint

Seol, J. H., Feldman, R. M. R., Zachariae, W., Shevchenko, A., Correll, C. C., Lyapina, S., Chi, Y., Gálová, M., Claypool, J. T., Sandmeyer, S. B., et al. (1999) · Genes & Development · doi:10.1101/gad.13.12.1614 · Cited by 403 · see citing works

Multimodal Activation of the Ubiquitin Ligase SCF by Nedd8 Conjugation

Saha, A., & Deshaies, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.021 · Cited by 396 · see citing works

Reconstitution of G 1 Cyclin Ubiquitination with Complexes Containing SCF Grr1 and Rbx1

Skowyra, D., Koepp, D. M., Kamura, T., Conrad, M. N., Conaway, R. C., Conaway, J. W., Elledge, S. J., & Harper, J. W. (1999) · Science · doi:10.1126/science.284.5414.662 · Cited by 377 · see citing works

Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins

Bordallo, J., Plemper, R. K., Finger, A., & Wolf, D. H. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.1.209 · Cited by 374 · see citing works

Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms

Yoo, S. J., Huh, J. R., Muro, I., Yu, H., Wang, L., Wang, S. L., Feldman, R. M. R., Clem, R. J., Müller, H. ‐. J., & Hay, B. A. (2002) · Nature Cell Biology · doi:10.1038/ncb793 · Cited by 373 · see citing works

Site-specific Lys-63-linked Tumor Necrosis Factor Receptor-associated Factor 6 Auto-ubiquitination Is a Critical Determinant of IκB Kinase Activation

Lamothe, B., Besse, A., Campos, A. D., Webster, W. K., Wu, H., & Darnay, B. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609503200 · Cited by 369 · see citing works

Gp78, a Membrane-Anchored Ubiquitin Ligase, Associates with Insig-1 and Couples Sterol-Regulated Ubiquitination to Degradation of HMG CoA Reductase

Song, B., Sever, N., & DeBose‐Boyd, R. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.009 · Cited by 368 · see citing works

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53

Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361 · see citing works

Structural basis for self-association and receptor recognition of human TRAF2

Park, Y. C., Burkitt, V., Villa, A. R., Tong, L., & Wu, H. (1999) · Nature · doi:10.1038/19110 · Cited by 359 · see citing works

A Bacterial Inhibitor of Host Programmed Cell Death Defenses Is an E3 Ubiquitin Ligase

Janjusevic, R., Abramovitch, R. B., Martin, G. B., & Stebbins, C. E. (2005) · Science · doi:10.1126/science.1120131 · Cited by 354 · see citing works

Mms2–Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation

Eddins, M. J., Carlile, C., Gomez, K. M., Pickart, C. M., & Wolberger, C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1148 · Cited by 352 · see citing works

E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages

Christensen, D. E., Brzovic, P. S., & Klevit, R. E. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1295 · Cited by 351 · see citing works

E3 ubiquitin ligase that recognizes sugar chains

Yoshida, Y., Chiba, T., Tokunaga, F., Kawasaki, H., Iwaï, K., Suzuki, T., Ito, Y., Matsuoka, K., Yoshida, M., Tanaka, K., et al. (2002) · Nature · doi:10.1038/nature00890 · Cited by 351 · see citing works

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346 · see citing works

Recruitment of a ROC1–CUL1 Ubiquitin Ligase by Skp1 and HOS to Catalyze the Ubiquitination of IκBα

Tan, P., Fuchs, S. Y., Chen, A., Wu, K. K.-Y., Gomez, C., Ronai, Z. A., & Pan, Z. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80481-5 · Cited by 345 · see citing works

NEDD8 recruits E2‐ubiquitin to SCF E3 ligase

Kawakami, T., Chiba, T., Suzuki, T., Iwai, K., Yamanaka, K., Minato, N., Suzuki, H., Shimbara, N., Hidaka, Y., Osaka, F., et al. (2001) · EMBO Journal · doi:10.1093/emboj/20.15.4003 · Cited by 344 · see citing works

SUMO‐targeted ubiquitin ligases in genome stability

Prudden, J., Kaeser-Pebernard, S., Raffa, G. D., Slavin, D. A., Perry, J. J. P., Tainer, J. A., McGowan, C. H., & Boddy, M. N. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601838 · Cited by 334 · see citing works

The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto‐oncoprotein PML.

Borden, K. L. B., Boddy, M. N., Lally, J., O’Reilly, N., Martin, S. R., Howe, K. M., Solomon, E., & Freemont, P. S. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07139.x · Cited by 328 · see citing works

Mass Spectrometric Analysis of the Anaphase-Promoting Complex from Yeast: Identification of a Subunit Related to Cullins

Zachariae, W., Shevchenko, A., Andrews, P. D., Ciosk, R., Gálová, M., Stark, M. J. R., Mann, M., & Nasmyth, K. (1998) · Science · doi:10.1126/science.279.5354.1216 · Cited by 326 · see citing works

Ligand-induced Ubiquitination of the Epidermal Growth Factor Receptor Involves the Interaction of the c-Cbl RING Finger and UbcH7

Yokouchi, M., Kondo, T., Houghton, A., Bartkiewicz, M., Horne, W. C., Zhang, H., Yoshimura, A., & Baron, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31707 · Cited by 321 · see citing works

NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases

Liu, J., Furukawa, M., Matsumoto, T., & Xiong, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00783-9 · Cited by 319 · see citing works

Ubiquitin-dependent Proteolytic Control of SUMO Conjugates

Uzunova, K., Göttsche, K., Miteva, M., Weisshaar, S. R., Glanemann, C., Schnellhardt, M., Niessen, M. T., Scheel, H., Hofmann, K., Johnson, E. S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706505200 · Cited by 314 · see citing works

A UbcH5/Ubiquitin Noncovalent Complex Is Required for Processive BRCA1-Directed Ubiquitination

Brzović, P. S., Lissounov, A., Christensen, D. E., Hoyt, D. W., & Klevit, R. E. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.02.008 · Cited by 311 · see citing works

CAND1 Binds to Unneddylated CUL1 and Regulates the Formation of SCF Ubiquitin E3 Ligase Complex

Zheng, J., Yang, X., Harrell, J. M., Ryzhikov, S., Shim, E., Lykke‐Hartmann, K., Wei, N., Sun, H., Kobayashi, R., & Zhang, H. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00784-0 · Cited by 309 · see citing works

Structural Basis of the Cks1-Dependent Recognition of p27Kip1 by the SCFSkp2 Ubiquitin Ligase

Hao, B., Zheng, N., Schulman, B. A., Wu, G., Miller, J. J., Pagano, M., & Pavletich, N. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.003 · Cited by 306 · see citing works

Getting into position: the catalytic mechanisms of protein ubiquitylation

Passmore, L. A., & Barford, D. (2004) · Biochemical Journal · doi:10.1042/bj20040198 · Cited by 305 · see citing works

Mechanism of Lysine 48-Linked Ubiquitin-Chain Synthesis by the Cullin-RING Ubiquitin-Ligase Complex SCF-Cdc34

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