The SCF ubiquitin ligase: insights into a molecular machine

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840

CDK inhibitors: positive and negative regulators of G1-phase progression

Sherr, C. J., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.12.1501 · Cited by 6,115

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012

Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy

Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774

The leucine-rich repeat as a protein recognition motif

Kobe, B. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(01)00266-4 · Cited by 1,720

SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27

Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544

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

SKP1 Connects Cell Cycle Regulators to the Ubiquitin Proteolysis Machinery through a Novel Motif, the F-Box

Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M. G., Harper, J. W., & Elledge, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80098-7 · Cited by 1,421

The WD repeat: a common architecture for diverse functions

Smith, T. F., Gaitatzes, C. G., Saxena, K., & Neer, E. J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01384-5 · Cited by 1,256

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 1,233

Recycling the Cell Cycle

Murray, A. W. (2004) · Cell · doi:10.1016/s0092-8674(03)01080-8 · Cited by 1,079

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

Small molecule modulation of Smoothened activity

Chen, J., Taipale, J., Young, K. E., Maiti, T., & Beachy, P. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182542899 · Cited by 991

The SCFbeta -TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in Ikappa Balpha and beta -catenin and stimulates Ikappa Balpha ubiquitination in vitroPreprint

Winston, J. T., Strack, P. R., Beer‐Romero, P., Chu, C. Y., Elledge, S. J., & Harper, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.3.270 · Cited by 964

The Anaphase-Promoting Complex

Peters, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00540-3 · Cited by 928

Cyclin E-CDK2 is a regulator of p27Kip1.Preprint

Sheaff, R. J., Groudine, M. T., Gordon, M., Roberts, J., & Clurman, B. E. (1997) · Genes & Development · doi:10.1101/gad.11.11.1464 · Cited by 910

Crystal structure of the p27Kip1 cyclin-dependent-kinase inibitor bound to the cyclin A–Cdk2 complex

Russo, A. A., Jeffrey, P. D., Patten, A. K., Massagué, J., & Pavletich, N. P. (1996) · Nature · doi:10.1038/382325a0 · Cited by 899

Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function

Stebbins, C. E., Kaelin, W. G., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.284.5413.455 · Cited by 852

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

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 820

p27Kip1 ubiquitination and degradation is regulated by the SCFSkp2 complex through phosphorylated Thr187 in p27

Tsvetkov, L. M., Yeh, K., Lee, S.-J., Sun, H., & Zhang, H. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80290-5 · Cited by 791

Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

Min, J.-H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.1073440 · Cited by 765

Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCF Fbw7 Ubiquitin Ligase

Koepp, D. M., Schaefer, L. K., Ye, X., Keyomarsi, K., Chu, C., Harper, J. W., & Elledge, S. J. (2001) · Science · doi:10.1126/science.1065203 · Cited by 764

The F-box protein family.

Kipreos, E. T., & Pagano, M. (2000) · Genome biology · doi:10.1186/gb-2000-1-5-reviews3002 · Cited by 753

A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity

Baba, M., Nishimura, O., Kanzaki, N., Okamoto, M., Sawada, H., Iizawa, Y., Shiraishi, M., Aramaki, Y., Okonogi, K., Ogawa, Y., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5698 · Cited by 752

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751

Proteasomes and their kin: proteases in the machine age

Pickart, C. M., & Cohen, R. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1336 · Cited by 735

Targeted disruption of Skp2 results in accumulation of cyclin E and p27Kip1, polyploidy and centrosome overduplication

Nakayama, K., Nagahama, H., Minamishima, Y. A., 雅記, 松., Nakamichi, I., Kitagawa, K., Shirane, M., Tsunematsu, R., Tsukiyama, T., Ishida, N., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.9.2069 · Cited by 719

Back to the Future with Ubiquitin

Pickart, C. M. (2004) · Cell · doi:10.1016/s0092-8674(03)01074-2 · Cited by 706

p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells

Sutterlüty, H., Chatelain, E., Marti, A., Wirbelauer, C., Senften, M., Müller, U., & Krek, W. (1999) · Nature Cell Biology · doi:10.1038/12027 · Cited by 700

Phosphorylation‐dependent degradation of the cyclin‐dependent kinase inhibitor p27Kip1

Vlach, J., Hennecke, S., & Amati, B. B. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5334 · Cited by 680

The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell

Hart, M. J., Concordet, J., Lassot, I., Albert, I., Santos, R., Durand, H., Perret, C., Rubinfeld, B., Margottin-Goguet, F., Bénarous, R., et al. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80091-8 · Cited by 670

Whose end is destruction: cell division and the anaphase-promoting complexPreprint

Zachariae, W., & Nasmyth, K. (1999) · Genes & Development · doi:10.1101/gad.13.16.2039 · Cited by 667

Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex

Lepourcelet, M., Chen, Y.-N. P., France, D. S., Wang, H., Crews, P., Petersen, F., Bruseo, C. W., Wood, A. W., & Shivdasani, R. A. (2004) · Cancer Cell · doi:10.1016/s1535-6108(03)00334-9 · Cited by 667

The ubiquitin system

Hershko, A., Ciechanover, A. J., & Varshavsky, A. J. (2000) · Nature Medicine · doi:10.1038/80384 · Cited by 661

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

Insights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex

Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E., Finnin, M. S., Elledge, S. J., Harper, J. W., Pagano, M., & Pavletich, N. P. (2000) · Nature · doi:10.1038/35042620 · Cited by 610

Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formationPreprint

Montagnoli, A., FIORE, F., Eytan, E., Carrano, A. C., Draetta, G. F., Hershko, A., & Pagano, M. (1999) · Genes & Development · doi:10.1101/gad.13.9.1181 · Cited by 596

Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line

Strohmaier, H. M., Spruck, C., Kaiser, P., Won, K., Sangfelt, O., & Reed, S. I. (2001) · Nature · doi:10.1038/35095076 · Cited by 584

Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity.

Kriwacki, R. W., Hengst, L., Tennant, L. L., Reed, S. I., & Wright, P. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11504 · Cited by 576

Structure of an E6AP-UbcH7 Complex: Insights into Ubiquitination by the E2-E3 Enzyme Cascade

Huang, L., Kinnucan, E., Wang, G., Beaudenon, S. L., Howley, P. M., Huibregtse, J. M., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.286.5443.1321 · Cited by 562

The spindle checkpoint: structural insights into dynamic signalling

Musacchio, A., & Hardwick, K. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm929 · Cited by 532

An F‐box protein, FWD1, mediates ubiquitin‐dependent proteolysis of β‐catenin

Kitagawa, M., Hatakeyama, S., Shirane, M., Matsumoto, M., Ishida, N., Hattori, K., Nakamichi, I., Kikuchi, A., Nakayama, K.-I., & Nakayama, K. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2401 · Cited by 529

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 515

Role of the SCFSkp2 Ubiquitin Ligase in the Degradation of p21Cip1 in S Phase

Bornstein, G., Bloom, J., Sitry-Shevah, D., Nakayama, K., Pagano, M., & Hershko, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301774200 · Cited by 508

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

BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

Xu, L., Yue, W., Reboul, J., Vaglio, P., Shin, T.-H., Vidal, M., Elledge, S. J., & Harper, J. W. (2003) · Nature · doi:10.1038/nature01985 · Cited by 500

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

M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCF β-TrCP

Watanabe, N., Arai, H., Nishihara, Y., Taniguchi, M., Watanabe, N., Hunter, T., & Osada, H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307700101 · Cited by 472

The cell-cycle regulatory protein Cks1 is required for SCFSkp2-mediated ubiquitinylation of p27

Ganoth, D., Bornstein, G., Ko, T. K., Larsen, B. G., Tyers, M., Pagano, M., & Hershko, A. (2001) · Nature Cell Biology · doi:10.1038/35060126 · Cited by 468

Targeting of protein ubiquitination by BTB–Cullin 3–Roc1 ubiquitin ligases

Furukawa, M., He, Y. J., Borchers, C. H., & Xiong, Y. (2003) · Nature Cell Biology · doi:10.1038/ncb1056 · Cited by 461

Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage

Busino, L., Donzelli, M., Chiesa, M., Guardavaccaro, D., Ganoth, D., Valerio Dorrello, N., Hershko, A., Pagano, M., & Draetta, G. F. (2003) · Nature · doi:10.1038/nature02082 · Cited by 447

The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin

Latres, E., Chiaur, D. S., & Pagano, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202653 · Cited by 442

Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines

Moberg, K. H., Bell, D. W., Wahrer, D. C. R., Haber, D. A., & Hariharan, I. K. (2001) · Nature · doi:10.1038/35095068 · Cited by 438

Nedd8 on cullin: building an expressway to protein destruction

Pan, Z., Kentsis, A., Dias, D. C., Yamoah, K., & Wu, K. (2004) · Oncogene · doi:10.1038/sj.onc.1207414 · Cited by 436

The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

Pintard, L., Willis, J. H., Willems, A. R., Johnson, J.-L., Srayko, M., Kurz, T., Luke-Glaser, S., Mains, P. E., Tyers, M., Bowerman, B. A., et al. (2003) · Nature · doi:10.1038/nature01959 · Cited by 434

Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21 CIP1/WAF1 and cyclin D proteins

Yu, Z.-K., Gervais, J., & Zhang, H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11324 · Cited by 410

COP9 Signalosome

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

Emi1 Is a Mitotic Regulator that Interacts with Cdc20 and Inhibits the Anaphase Promoting Complex

Reimann, J. D. R., Freed, E., Hsu, J. Y., Kramer, E. R., Peters, J., & Jackson, P. K. (2001) · Cell · doi:10.1016/s0092-8674(01)00361-0 · Cited by 389

Binding of small molecules to an adaptive protein–protein interface

Arkin, M. R., Randal, M., DeLano, W. L., Hyde, J., Luong, T. N., Oslob, J. D., Raphael, D. R., Taylor, L., Wang, J., McDowell, R. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252756299 · Cited by 376

Multisite Phosphorylation by Cdk2 and GSK3 Controls Cyclin E Degradation

Welcker, M., Singer, J. D., Loeb, K. R., Grim, J. A., Bloecher, A., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00287-9 · Cited by 369

Identification of a family of human F-box proteins

Cenciarelli, C., Chiaur, D. S., Guardavaccaro, D., Parks, W. P., Vidal, M., & Pagano, M. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80020-2 · Cited by 365

Skp2-Mediated Degradation of p27 Regulates Progression into Mitosis

Nakayama, K., Nagahama, H., Minamishima, Y. A., Miyake, S., Ishida, N., Hatakeyama, S., Kitagawa, M., Iemura, S.-I., Natsume, T., & Nakayama, K. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00131-5 · Cited by 364

A family of mammalian F-box proteins

Winston, J. T., Koepp, D. M., Zhu, C., Elledge, S. J., & Harper, J. W. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80021-4 · Cited by 357

A CDK-Independent Function of Mammalian Cks1

Spruck, C., Strohmaier, H. M., Watson, M. H., Smith, A. P. L., Ryan, A., Krek, W., & Reed, S. I. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00210-6 · Cited by 355

Control of Meiotic and Mitotic Progression by the F Box Protein β-Trcp1 In Vivo

Guardavaccaro, D., Kudo, Y., Boulaire, J., Barchi, M., Busino, L., Donzelli, M., Margottin-Goguet, F., Jackson, P. K., Yamasaki, L., & Pagano, M. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00154-0 · Cited by 355

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

BTB/POZ Domain Proteins Are Putative Substrate Adaptors for Cullin 3 Ubiquitin Ligases

Geyer, R. K., Wee, S., Anderson, S., Yates, J. R., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00341-1 · Cited by 342

SCFβ-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase

Jin, J., Shirogane, T., Xu, L., Nalepa, G., Qin, J., Elledge, S. J., & Harper, J. W. (2003) · Genes & Development · doi:10.1101/gad.1157503 · Cited by 340

Prophase Destruction of Emi1 by the SCFβTrCP/Slimb Ubiquitin Ligase Activates the Anaphase Promoting Complex to Allow Progression beyond Prometaphase

Margottin-Goguet, F., Hsu, J. Y., Loktev, A. V., Hsieh, H.-M., Reimann, J. D. R., & Jackson, P. K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00153-9 · Cited by 337

E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APCCdh1

Hsu, J. Y., Reimann, J. D. R., Sørensen, C. S., Lukas, J., & Jackson, P. K. (2002) · Nature Cell Biology · doi:10.1038/ncb785 · Cited by 337

Small-molecule antagonists of Myc/Max dimerization inhibit Myc-induced transformation of chicken embryo fibroblasts

Berg, T., Cohen, S. B., Desharnais, J., Sonderegger, C. K., Maslyar, D. J., Goldberg, J., Boger, D. L., & Vogt, P. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062036999 · Cited by 326

Proteasome-Mediated Degradation of p21 via N-Terminal Ubiquitinylation

Bloom, J., Amador, V., Bartolini, F., Demartino, G., & Pagano, M. (2003) · Cell · doi:10.1016/s0092-8674(03)00755-4 · Cited by 322

p27 binds cyclin–CDK complexes through a sequential mechanism involving binding-induced protein folding

Lacy, E. R., Filippov, I. V., Lewis, W. S., Otieno, S. B., Xiao, L., Weiß, S. B., Hengst, L., & Kriwacki, R. W. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb746 · Cited by 305

Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT Domain E3 Ligase

Verdecia, M. A., Joazeiro, C. A. P., Wells, N. J., Ferrer, J.-L., Bowman, M. E., Hunter, T. R., & Noel, J. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00774-8 · Cited by 288

Split-Hand/Split-Foot Malformation Is Caused by Mutations in the p63 Gene on 3q27

Ianakiev, P., Kilpatrick, M. W., Toudjarska, I., Basel, D., Beighton, P., & Tsipouras, P. (2000) · The American Journal of Human Genetics · doi:10.1086/302972 · Cited by 288

Ubiquitin Ligases and the Immune Response

Liu, Y. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104813 · Cited by 286

Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover

Reed, S. I. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1246 · Cited by 282

Inhibition of Protein−Protein Association by Small Molecules: Approaches and Progress

Toogood, P. L. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010468s · Cited by 281

Ubiquitination and Degradation of the Substrate Recognition Subunits of SCF Ubiquitin–Protein Ligases

Zhou, P., & Howley, P. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80156-2 · Cited by 258

Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis

Risseeuw, E. P., Daskalchuk, T. E., Banks, T. W., Liu, E., Cotelesage, J. H., Hellmann, H. A., Estelle, M. A., Somers, D. E., & Crosby, W. L. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01768.x · Cited by 255

Structural principles of leucine‐rich repeat (LRR) proteins

Enkhbayar, P., Kamiya, M., Osaki, M., Takeshi Matsumoto, A., & Matsushima, N. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10605 · Cited by 243

Crystal Structure and Mutational Analysis of the Human CDK2 Kinase Complex with Cell Cycle–Regulatory Protein CksHs1

Bourne, Y., Watson, M. H., Hickey, M. J., Holmes, W., Rocque, W. J., Reed, S. I., & Tainer, J. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81065-x · Cited by 235

Rapid Degradation of the G 1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation

Lanker, S., Valdivieso, M. ‐., & Wittenberg, C. (1996) · Science · doi:10.1126/science.271.5255.1597 · Cited by 232

Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome

Moshe, Y., Boulaire, J., Pagano, M., & Hershko, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402442101 · Cited by 213

Inhibition of tubulin-microtubule polymerization by drugs of the Vinca alkaloid class.

Owellen, R. J., Hartke, C., Dickerson, R. M., & Hains, F. O. (1976) · PubMed · Cited by 207

Human cyclin F.

Bai, C., Richman, R., & Elledge, S. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06955.x · Cited by 200

Dual mode of degradation of Cdc25 A phosphatase

Donzelli, M., Squatrito, M., Ganoth, D., Hershko, A., Pagano, M., & Draetta, G. F. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf491 · Cited by 199

Emi1 regulates the anaphase-promoting complex by a different mechanism than Mad2 proteinsPreprint

Reimann, J. D. R., Gardner, B., Margottin-Goguet, F., & Jackson, P. K. (2001) · Genes & Development · doi:10.1101/gad.945701 · Cited by 185

Tome-1, a Trigger of Mitotic Entry, Is Degraded during G1 via the APC

Ayad, N. G., Rankin, S., Murakami, M. S., Jebanathirajah, J. A., Gygi, S. P., & Kirschner, M. W. (2003) · Cell · doi:10.1016/s0092-8674(03)00232-0 · Cited by 179

Fbs2 Is a New Member of the E3 Ubiquitin Ligase Family That Recognizes Sugar Chains

Yoshida, Y., Tokunaga, F., Chiba, T., Iwaï, K., Tanaka, K., & Tai, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304157200 · Cited by 176

Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase.

Mayer, B. J., & Baltimore, D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.5.2883 · Cited by 175

The F‐box protein Skp2 is a ubiquitylation target of a Cul1‐based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts

Wirbelauer, C., Sutterlüty, H., Blondel, M., Gstaiger, M., Peter, M., Reymond, F., & Krek, W. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5362 · Cited by 172

CUL7: A DOC domain-containing cullin selectively binds Skp1⋅Fbx29 to form an SCF-like complex

Dias, D. C., Dolios, G., Wang, R., & Pan, Z. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252646399 · Cited by 170

Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation

Petroski, M. D., & Deshaies, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00221-1 · Cited by 148

Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis

Arai, T., Kasper, J. S., Skaar, J. R., Ali, S. H., Takahashi, C., & DeCaprio, J. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1733908100 · Cited by 145

Functional Consequences of Preorganized Helical Structure in the Intrinsically Disordered Cell-Cycle Inhibitor p27Kip1

Bienkiewicz, E. A., Adkins, J., & Lumb, K. J. (2001) · Biochemistry · doi:10.1021/bi015763t · Cited by 143

Protein–protein interfaces: mimics and inhibitors

Cochran, A. G. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(01)00262-9 · Cited by 133

The Caenorhabditis elegans Skp1-Related Gene Family

Nayak, S., Santiago, F. E., Jin, H., Lin, D., Schedl, T., & Kipreos, E. T. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00682-6 · Cited by 129

The Small Heat-shock Protein αB-Crystallin Promotes FBX4-dependent Ubiquitination

den Engelsman, J., Keijsers, V., JONG, W. W. D., & Boelens, W. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211403200 · Cited by 127

Dynamics of the Cell Cycle: Checkpoints, Sizers, and Timers

Qu, Z., MacLellan, W. R., & Weiss, J. N. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74778-x · Cited by 123

IκBα Ubiquitination Is Catalyzed by an SCF-like Complex Containing Skp1, Cullin-1, and Two F-Box/WD40-Repeat Proteins, βTrCP1 and βTrCP2

Suzuki, H., Chiba, T., Kobayashi, M., Takeuchi, M., Suzuki, T., Ichiyama, A., Ikenoue, T., Omata, M., Furuichi, K., & Tanaka, K. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0289 · Cited by 122

Loss of the anaphase-promoting complex in quiescent cells causes unscheduled hepatocyte proliferationPreprint

Wirth, K. G., Ricci, R., Giménez-Abián, J. F., Taghybeeglu, S., Kudo, N. R., Jochum, W., Vasseur-Cognet, M., & Nasmyth, K. (2004) · Genes & Development · doi:10.1101/gad.285404 · Cited by 102

Mathematical Modeling Suggests Cooperative Interactions between a Disordered Polyvalent Ligand and a Single Receptor Site

Klein, P., Pawson, T. J., & Tyers, M. (2003) · Current Biology · doi:10.1016/j.cub.2003.09.027 · Cited by 93

A novel member of the F-box/WD40 gene family, encoding dactylin, is disrupted in the mouse dactylaplasia mutant

Sidow, A., Bulotsky, M. S., Kerrebrock, A. W., Birren, B. W., Altshuler, D., Jaenisch, R., Johnson, K. R., & Lander, E. S. (1999) · Nature Genetics · doi:10.1038/12709 · Cited by 91

Three Different Binding Sites of Cks1 Are Required for p27-Ubiquitin Ligation

Sitry-Shevah, D., Seeliger, M. A., Ko, T. K., Ganoth, D., Breward, S. E., Itzhaki, L. S., Pagano, M., & Hershko, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205254200 · Cited by 90

When protein destruction runs amok, malignancy is on the loose

Pagano, M., & Benmaamar, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00243-5 · Cited by 89

Oncogenic aberrations of cullin-dependent ubiquitin ligases

Guardavaccaro, D., & Pagano, M. (2004) · Oncogene · doi:10.1038/sj.onc.1207413 · Cited by 84

Structural basis of sugar-recognizing ubiquitin ligase

Mizushima, T., Hirao, T., Yoshida, Y., Lee, S. J., Chiba, T., Iwaï, K., Yamaguchi, Y., Kato, K., Tomitake Tsukihara, A., & Tanaka, K. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb732 · Cited by 83

Culprits in the degradation of cyclin E apprehendedPreprint

Winston, J. T., Chu, C., & Harper, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.21.2751 · Cited by 82

Release of Ubiquitin-Charged Cdc34-S∼Ub from the RING Domain Is Essential for Ubiquitination of the SCFCdc4-Bound Substrate Sic1

Deffenbaugh, A. E., Scaglione, K. M., Zhang, L., Moore, J. M., Buranda, T., Sklar, L. A., & Skowyra, D. (2003) · Cell · doi:10.1016/s0092-8674(03)00641-x · Cited by 81

Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2

Adkins, J., & Lumb, K. J. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10018 · Cited by 75

Aberrant ubiquitin-mediatedproteolysis of cell cycle regulatory proteins and oncogenesis

Bashir, T., & Pagano, M. (2003) · Advances in cancer research · doi:10.1016/s0065-230x(03)88305-7 · Cited by 73

The F Box Protein AFR Is a Positive Regulator of Phytochrome A-Mediated Light Signaling

Harmon, F. G., & Kay, S. A. (2003) · Current Biology · doi:10.1016/j.cub.2003.11.019 · Cited by 73

Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro

Kus, B., Caldon, C. E., Andorn‐Broza, R., & Edwards, A. M. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10620 · Cited by 72

Multiple Skp1-Related Proteins in Caenorhabditis elegans

Yamanaka, A., Yada, M., Imaki, H., Koga, M., Ohshima, Y., & Nakayama, K. I. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00657-7 · Cited by 71

F-Box Protein Grr1 Interacts with Phosphorylated Targets via the Cationic Surface of Its Leucine-Rich Repeat

Hsiung, Y. G., Chang, H.-C., Pellequer, J., Valle, R. L., Lanker, S., & Wittenberg, C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.7.2506-2520.2001 · Cited by 71

Stability of Homologue of Slimb F-box Protein Is Regulated by Availability of Its Substrate

Li, Y., Gazdoiu, S., Pan, Z., & Fuchs, S. Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312301200 · Cited by 69

Proviral insertions in the zebrafish hagoromo gene, encoding an F-box/WD40-repeat protein, cause stripe pattern anomalies

Kawakami, K., Amsterdam, A., Shimoda, N., Becker, T. S., Mugg, J., Shima, A., & Hopkins, N. H. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00444-9 · Cited by 63

Kip1 meets SKP2: new links in cell-cycle control

Amati, B. B., & Vlach, J. (1999) · Nature Cell Biology · doi:10.1038/12087 · Cited by 59

Cdc34 Self-Association Is Facilitated by Ubiquitin Thiolester Formation and Is Required for Its Catalytic Activity

Varelas, X., Ptak, C. P., & Ellison, M. J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5388-5400.2003 · Cited by 52

Molecular profile of synovial fibroblasts in rheumatoid arthritis depends on the stage of proliferation

Masuda, K., Masuda, R., Neidhart, M., Simmen, B. R., Michel, B. A., Müller‐Ladner, U., Gay, R. E., & Gay, S. (2002) · Arthritis Research & Therapy · doi:10.1186/ar427 · Cited by 51

The Arabidopsis SKP1-like genes present a spectrum of expression profiles

Marrocco, K., Lécureuil, A., Nicolas, P., & Guerche, P. (2003) · Plant Molecular Biology · doi:10.1023/a:1025056008926 · Cited by 41

Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase

Xu, K., Belunis, C. J., Wei, C. H. U., Weber, D. V., Podlaski, F., Huang, K., Reed, S. I., & Vassilev, L. T. (2003) · Biochemical Journal · doi:10.1042/bj20021722 · Cited by 30

A Negatively Charged Amino Acid in Skp2 Is Required for Skp2-Cks1 Interaction and Ubiquitination of p27Kip1

Wang, W., Ungermannova, D., Chen, L., & Liu, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305241200 · Cited by 25

Cooperative organization in a macromolecular complex

Seeliger, M. A., Breward, S. E., Friedler, A., Schön, O., & Itzhaki, L. S. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb962 · Cited by 20

Split hand foot malformation is associated with a reduced level of Dactylin gene expression

Basel, D., Depaepe, A., Kilpatrick, M. W., & Tsipouras, P. (2003) · Clinical Genetics · doi:10.1034/j.1399-0004.2003.00153.x · Cited by 20

A Novel Cyclin Gene (CCNF) in the Region of the Polycystic Kidney Disease Gene (PKD1)

Kraus, B., Pohlschmidt, M., Leung, A. L. S., Germino, G. G., Snarey, A., Schneider, M. C., Reeders, S. T., & Frischauf, A.-M. (1994) · Genomics · doi:10.1006/geno.1994.1578 · Cited by 15

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

The F-box protein TIR1 is an auxin receptor

Dharmasiri, N., Dharmasiri, S., & Estelle, M. (2005) · Nature · doi:10.1038/nature03543 · Cited by 2,083

Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications

Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501023 · Cited by 1,654

Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1

Bodine, S. C., & Baehr, L. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2014 · Cited by 1,159

The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition

Meloche, S., & Pouysségur, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210414 · Cited by 1,091

The F-box: a new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction

Craig, K. L., & Tyers, M. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00010-3 · Cited by 298

The Biology of F-box Proteins: The SCF Family of E3 Ubiquitin Ligases

Nguyen, K. M., & Busino, L. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_8 · Cited by 108

F-box protein substrate recognition

Chen, B. B., & Mallampalli, R. K. (2013) · Cell Cycle · doi:10.4161/cc.23071 · Cited by 11

Identification of novel F-box proteins in Xenopus laevis

Reimann, J. D. R., Duong, Q. V., & Jackson, P. K. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80006-8 · Cited by 21

A family of mammalian F-box proteins

Winston, J. T., Koepp, D. M., Zhu, C., Elledge, S. J., & Harper, J. W. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80021-4 · Cited by 357