The SCF ubiquitin ligase: insights into a molecular machine
Abstract
Ubiquitin ligases are well suited to regulate molecular networks that operate on a post-translational timescale. The F-box family of proteins - which are the substrate-recognition components of the Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase - are important players in many mammalian functions. Here we explore a unifying and structurally detailed view of SCF-mediated proteolytic control of cellular processes that has been revealed by recent studies.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Phosphorylation of both serines in the degron sequence is needed to allow recognition by βTRCP.
“The phosphorylation of both serines in the degron sequence is needed to allow recognition by βTRCP [69].”
From Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions (2019) · cites this paper as [69]
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 1,669 · see citing works
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 · see citing works
Self-citationStructure 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
Self-citationBai, 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 · see citing works
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 · see citing works
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
Murray, A. W. (2004) · Cell · doi:10.1016/s0092-8674(03)01080-8 · Cited by 1,054 · 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
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 · see citing works
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 949 · see citing works
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 · see citing works
The Anaphase-Promoting Complex
Peters, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00540-3 · Cited by 909 · see citing works
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 · see citing works
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 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 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Kipreos, E. T., & Pagano, M. (2000) · Genome biology · doi:10.1186/gb-2000-1-5-reviews3002 · Cited by 743 · see citing works
Self-citationProteasomes 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 · see citing works
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 · see citing works
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 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 653 · see citing works
Hershko, A., Ciechanover, A. J., & Varshavsky, A. J. (2000) · Nature Medicine · doi:10.1038/80384 · Cited by 649 · 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
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 · see citing works
Self-citationUbiquitination 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 · see citing works
Self-citationStrohmaier, H. M., Spruck, C., Kaiser, P., Won, K., Sangfelt, O., & Reed, S. I. (2001) · Nature · doi:10.1038/35095076 · Cited by 584 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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
Self-citationXu, 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 497 · see citing works
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 496 · see citing works
Self-citationDegradation 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
M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCF <sup>β-TrCP</sup>
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 · see citing works
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 · see citing works
Self-citationTargeting 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 459 · see citing works
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 · see citing works
Self-citationLatres, E., Chiaur, D. S., & Pagano, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202653 · Cited by 442 · see citing works
Self-citationArchipelago 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 · see citing works
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 431 · see citing works
Nedd8 on cullin: building an expressway to protein destruction
Pan, Z., Kentsis, A., Dias, D. C., Yamoah, K., & Wu, K. K.-Y. (2004) · Oncogene · doi:10.1038/sj.onc.1207414 · Cited by 430 · see citing works
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 · see citing works
Cope, G. A., & Deshaies, R. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00722-0 · Cited by 409 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationMultisite 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 364 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationE3 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
SCF<sup>β-TRCP</sup> 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 · see citing works
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 339 · see citing works
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 · see citing works
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 331 · see citing works
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 · see citing works
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 · see citing works
Self-citationLacy, 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 · see citing works
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 · see citing works
Ubiquitin Ligases and the Immune Response
Liu, Y. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104813 · Cited by 283 · see citing works
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 282 · see citing works
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 · see citing works
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 280 · see citing works
Zhou, P., & Howley, P. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80156-2 · Cited by 259 · see citing works
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 258 · see citing works
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 237 · see citing works
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 236 · see citing works
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 · see citing works
Moshe, Y., Boulaire, J., Pagano, M., & Hershko, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402442101 · Cited by 213 · see citing works
Self-citationInhibition 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 · see citing works
Bai, C., Richman, R., & Elledge, S. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06955.x · Cited by 200 · see citing works
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 194 · see citing works
Self-citationEmi1 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 165 · see citing works
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 149 · see citing works
Targeted disruption of <i>p185/Cul7</i> 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 · see citing works
Bienkiewicz, E. A., Adkins, J., & Lumb, K. J. (2001) · Biochemistry · doi:10.1021/bi015763t · Cited by 143 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Klein, P., Pawson, T. J., & Tyers, M. (2003) · Current Biology · doi:10.1016/j.cub.2003.09.027 · Cited by 96 · see citing works
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 · see citing works
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 90 · see citing works
Self-citationThree 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 · see citing works
Self-citationOncogenic aberrations of cullin-dependent ubiquitin ligases
Guardavaccaro, D., & Pagano, M. (2004) · Oncogene · doi:10.1038/sj.onc.1207413 · Cited by 82 · see citing works
Self-citationCulprits 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 · see citing works
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 82 · see citing works
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 79 · see citing works
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 · see citing works
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 · see citing works
Self-citationThe 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 70 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Wang, W., Ungermannova, D., Chen, L., & Liu, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305241200 · Cited by 25 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Flagged first, then by citations
1 of the 131 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
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 · see citing works
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 1,609 · see citing works
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 1,117 · see citing works
Meloche, S., & Pouysségur, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210414 · Cited by 1,091 · see citing works
The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond
Hunter, T. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.019 · Cited by 946 · see citing works
Kobayashi, A., Kang, M.-I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.221-229.2006 · Cited by 933 · see citing works
Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer
Frescas, D., & Pagano, M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2396 · Cited by 886 · see citing works
Self-citationTebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works
Sustained proliferation in cancer: Mechanisms and novel therapeutic targets
Feitelson, M. A., Arzumanyan, A. L., Kulathinal, R. J., Blain, S. W., Holcombe, R. F., Mahajna, J. A., Marino, M., Martínez‐Chantar, M. L., Nawroth, R., Sánchez-Garcı́a, I., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.02.006 · Cited by 783 · see citing works
DNA damage checkpoints: from initiation to recovery or adaptation
Bartek, J., & Lukas, J. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.009 · Cited by 784 · see citing works
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
The ubiquitin-proteasome system
Nandi, D., Tahiliani, P., Kumar, A., & Chandu, D. (2006) · Journal of Biosciences · doi:10.1007/bf02705243 · Cited by 767 · see citing works
S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth
Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731 · see citing works
Self-citationSystematic analysis and nomenclature of mammalian F-box proteinsPreprint
Jin, J., Cardozo, T. J., Lovering, R. C., Elledge, S. J., Pagano, M., & Harper, J. W. (2004) · Genes & Development · doi:10.1101/gad.1255304 · Cited by 716 · see citing works
Self-citationStructure and function of WD40 domain proteins
Xu, C., & Min, J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1018-1 · Cited by 644 · see citing works
Lateral root development in Arabidopsis: fifty shades of auxin
Lavenus, J., Goh, T., Roberts, I., Guyomarc’h, S., Lucas, M., Smet, I. D., Fukaki, H., Beeckman, T., Bennett, M. J., & Laplaze, L. (2013) · Trends in Plant Science · doi:10.1016/j.tplants.2013.04.006 · Cited by 639 · see citing works
Genetics of Circadian Rhythms in Mammalian Model Organisms
Lowrey, P. L., & Takahashi, J. S. (2011) · Advances in genetics · doi:10.1016/b978-0-12-387690-4.00006-4 · Cited by 578 · see citing works
Siepka, S. M., Yoo, S. H., Park, J., Song, W., Kumar, V., Hu, Y., Lee, C., & Takahashi, J. S. (2007) · Cell · doi:10.1016/j.cell.2007.04.030 · Cited by 536 · see citing works
The Cullin-RING Ubiquitin-Protein Ligases
Hua, Z., & Vierstra, R. D. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112256 · Cited by 509 · see citing works
Controlling nuclear receptors: the circular logic of cofactor cycles
Perissi, V., & Rosenfeld, M. G. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1680 · Cited by 507 · see citing works
Busino, L., Bassermann, F. C., Maiolica, A., Lee, C., Nolan, P. M., Godinho, S. I. H., Draetta, G. F., & Pagano, M. (2007) · Science · doi:10.1126/science.1141194 · Cited by 509 · see citing works
Self-citationMammalian iron metabolism and its control by iron regulatory proteins
Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works
McMahon, M. J., Thomas, N., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601119200 · Cited by 489 · see citing works
Zhuang, M., Calabrese, M. F., Liu, J., Waddell, M. B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.022 · Cited by 486 · see citing works
Kong, H., Landherr, L. L., Frohlich, M. W., Leebens‐Mack, J., Mā, H., & dePamphilis, C. W. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03097.x · Cited by 479 · see citing works
G Protein–Coupled Receptor Sorting to Endosomes and Lysosomes
Marchese, A., Paing, M. M., Temple, B. R. S., & Trejo, J. (2007) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094646 · Cited by 456 · see citing works
Sundqvist, A., Bengoechea-Alonso, M. T., Ye, X., Lukiyanchuk, V., Jin, J., Harper, J. W., & Ericsson, J. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.04.010 · Cited by 444 · see citing works
Modulation of Host Cell Function byLegionella pneumophilaType IV Effectors
Hubber, A. M., & Roy, C. R. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104034 · Cited by 427 · see citing works
Control of iron homeostasis by an iron-regulated ubiquitin ligase
Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429 · see citing works
MAX2 participates in an SCF complex which acts locally at the node to suppress shoot branching
Stirnberg, P., Furner, I. J., & Ottoline Leyser, H. M. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03032.x · Cited by 429 · see citing works
Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
Hoeller, D., Hecker, C.-M., & Đikić, I. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1994 · Cited by 409 · 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
D’Angiolella, V., Donato, V., Forrester, F. M., Jeong, Y., Pellacani, C., Kudo, Y., Saraf, A., Florens, L. A., Washburn, M. P., & Pagano, M. (2012) · Cell · doi:10.1016/j.cell.2012.03.043 · Cited by 396 · see citing works
Self-citationFoxM1: At the crossroads of ageing and cancer
Laoukili, J., Stahl, M., & Medema, R. H. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.006 · Cited by 377 · see citing works
Nuclear PTEN Regulates the APC-CDH1 Tumor-Suppressive Complex in a Phosphatase-Independent Manner
Song, M. S., Carracedo, A., Salmena, L., Song, S. J., Egia, A., Malumbres, M., & Pandolfi, P. P. (2011) · Cell · doi:10.1016/j.cell.2010.12.020 · Cited by 375 · see citing works
The Drosophila IMD pathway in the activation of the humoral immune response
Kleino, A., & Silverman, N. S. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.05.014 · Cited by 366 · see citing works
Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364 · see citing works
Genomic stability and tumour suppression by the APC/C cofactor Cdh1
García-Higuera, I., Manchado, E., Dubus, P. R., Cañamero, M., Méndez, J., Moreno, S., & Malumbres, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1742 · Cited by 357 · see citing works
Targeting cell cycle regulation in cancer therapy
Díaz‐Moralli, S., Tarrado‐Castellarnau, M., Miranda, A., & Cascante, M. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.011 · Cited by 361 · see citing works
A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons
Tasaki, T., Mulder, L. C. F., Iwamatsu, A., Lee, M. J., Davydov, I. V., Varshavsky, A. J., Muesing, M. A., & Kwon, Y. T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7120-7136.2005 · Cited by 348 · see citing works
Dehan, E., & Pagano, M. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.02.014 · Cited by 353 · see citing works
Self-citationGearhart, M. D., Corcoran, C. M., Wamstad, J. A., & Bardwell, V. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00630-06 · Cited by 352 · see citing works
Male gametophyte development: a molecular perspective
Borg, M., Brownfield, L. R., & David Twell, B. (2009) · Journal of Experimental Botany · doi:10.1093/jxb/ern355 · Cited by 349 · see citing works
Ubiquitin signaling in cell cycle control and tumorigenesis
Dang, F., Nie, L., & Wei, W. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00648-0 · Cited by 343 · see citing works
Xu, G., Mā, H., Nei, M., & Kong, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812043106 · Cited by 343 · see citing works
Silencing by small RNAs is linked to endosomal trafficking
Lee, Y. S., Pressman, S., Andress, A. P., Kim, K., White, J. L., Cassidy, J. J., Li, X., Lubell, K., Lim, D., Cho, I. S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1930 · Cited by 338 · see citing works
SCF ubiquitin ligase-targeted therapies
Skaar, J. R., Pagan, J. K., & Pagano, M. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4432 · Cited by 336 · see citing works
Self-citationRegulation of NF‐κB by ubiquitination and degradation of the IκBs
Kanarek, N., & Ben‐Neriah, Y. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01098.x · Cited by 326 · see citing works
Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom)Preprint
Mohan, M., Herz, H., Takahashi, Y.-H., Lin, C., Lai, K. C., Zhang, Y., Washburn, M. P., Florens, L. A., & Shilatifard, A. (2010) · Genes & Development · doi:10.1101/gad.1898410 · Cited by 312 · see citing works
Wang, C., Gale, M., Keller, B. C., Huang, H., Brown, M. S., Goldstein, J. L., & Ye, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.004 · Cited by 293 · see citing works
F-box-like domain in the polerovirus protein P0 is required for silencing suppressor function
Pazhouhandeh, M., Dieterle, M., Marrocco, K., Lechner, E., Berry, B., Brault, V., Hemmer, O., Kretsch, T., Richards, K., Genschik, P., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510784103 · Cited by 299 · see citing works
FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas
Duan, S., C̆ermák, L., Pagan, J. K., Rossi, M., Martinengo, C., di Celle, P. F., Chapuy, B., Shipp, M. A., Chiarle, R., & Pagano, M. (2011) · Nature · doi:10.1038/nature10688 · Cited by 295 · see citing works
Self-citationJETLAG Resets the Drosophila Circadian Clock by Promoting Light-Induced Degradation of TIMELESS
Koh, K., Zheng, X., & Sehgal, A. (2006) · Science · doi:10.1126/science.1124951 · Cited by 293 · see citing works
Peschiaroli, A., Dorrello, N. V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N. E., & Pagano, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.013 · Cited by 289 · see citing works
Self-citationAuxin signaling: Research advances over the past 30 years
Yu, Z., Zhang, F., Friml, J., & Ding, Z. (2022) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13225 · Cited by 284 · see citing works
E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification
Huang, D. T. C., Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G. A. M., Murray, P. J., Roussel, M. F., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.011 · Cited by 282 · see citing works
SCFCyclin F controls centrosome homeostasis and mitotic fidelity through CP110 degradation
D’Angiolella, V., Donato, V., Vijayakumar, S., Saraf, A., Florens, L. A., Washburn, M. P., Dynlacht, B. D., & Pagano, M. (2010) · Nature · doi:10.1038/nature09140 · Cited by 281 · see citing works
Self-citationThe Processivity of Multiubiquitination by the APC Determines the Order of Substrate Degradation
Rapé, M., Reddy, S., & Kirschner, M. W. (2006) · Cell · doi:10.1016/j.cell.2005.10.032 · Cited by 280 · see citing works
Gene networks controlling A rabidopsis thaliana flower development
Ó’Maoiléidigh, D. S., Graciet, E., & Wellmer, F. (2013) · New Phytologist · doi:10.1111/nph.12444 · Cited by 272 · see citing works
Hirano, A., Yumimoto, K., Tsunematsu, R., Matsumoto, M., Oyama, M., Kozuka‐Hata, H., Nakagawa, T., Lanjakornsiripan, D., Nakayama, K. I., & Fukada, Y. (2013) · Cell · doi:10.1016/j.cell.2013.01.054 · Cited by 274 · see citing works
Evidence for the direct involvement of βTrCP in Gli3 protein processing
Wang, B., & Li, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509927103 · Cited by 273 · see citing works
Bassermann, F. C., Eichner, R., & Pagano, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.028 · Cited by 268 · see citing works
Self-citationGao, D., Inuzuka, H., Tseng, A., Chin, Y. R., Toker, A., & Wei, W. (2009) · Nature Cell Biology · doi:10.1038/ncb1847 · Cited by 267 · see citing works
Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response
Reinhardt, H. C., & Yaffe, M. B. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3640 · Cited by 260 · see citing works
Phylogenetic and structural analysis of centromeric DNA and kinetochore proteins
Meraldi, P., McAinsh, A. D., Rheinbay, E., & Sorger, P. K. (2006) · Genome biology · doi:10.1186/gb-2006-7-3-r23 · Cited by 262 · see citing works
Chen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Ding, M., Peng, H. B., & Shao, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.004 · Cited by 270 · see citing works
Protein damage, repair and proteolysis
Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 254 · see citing works
Ubiquitin Ligases and Cell Cycle Control
Teixeira, L. K., & Reed, S. I. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060410-105307 · Cited by 253 · see citing works
mTOR Drives Its Own Activation via SCFβTrCP-Dependent Degradation of the mTOR Inhibitor DEPTOR
Gao, D., Inuzuka, H., Tan, M.-K. M., Fukushima, H., Locasale, J. W., Liu, P., Wan, L., Zhai, B., Chin, Y. R., Shaik, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.030 · Cited by 248 · see citing works
Nishitani, H., Shiomi, Y., Iida, H., Michishita, M., Takami, T., & Tsurimoto, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806045200 · Cited by 241 · see citing works
Tarpey, P. S., Raymond, F. L., O’Meara, S., Edkins, S., Teague, J. W., Butler, A. P., Dicks, E., Stevens, C., Tofts, C., Avis, T., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/511134 · Cited by 232 · see citing works
The ubiquitous role of ubiquitin in the DNA damage response
Al-Hakim, A., Escribano‐Diaz, C., Landry, M.-C., O’Donnell, L., Panier, S., Szilard, R. K., & Durocher, D. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.09.011 · Cited by 224 · see citing works
Emerging Roles for Ubiquitin and Protein Degradation in Neuronal Function
Yi, J. J., & Ehlers, M. D. (2007) · Pharmacological Reviews · doi:10.1124/pr.59.1.4 · Cited by 224 · see citing works
Acetylation-Dependent Regulation of Skp2 Function
Inuzuka, H., Gao, D., Finley, L. W. S., Yang, W., Wan, L., Fukushima, H., Chin, Y. R., Zhai, B., Shaik, S., Lau, A. W., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.038 · Cited by 218 · see citing works
Dynamic Allostery: Linkers Are Not Merely Flexible
Ma, B., Tsai, C.-J., Haliloğlu, T., & Nussinov, R. (2011) · Structure · doi:10.1016/j.str.2011.06.002 · Cited by 222 · see citing works
Specific Small Molecule Inhibitors of Skp2-Mediated p27 Degradation
Wu, L. I., Grigoryan, A. V., Li, Y., Hao, B., Pagano, M., & Cardozo, T. J. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.09.015 · Cited by 220 · see citing works
Self-citationZheng, H., Shen, M., Zha, Y.-L., Li, W., Wei, Y., Blanco, M. A., Ren, G., Zhou, T., Störz, P., Wang, H., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.022 · Cited by 218 · see citing works
Gan, W., Dai, X., Lunardi, A., Li, Z., Inuzuka, H., Liu, P., Varmeh, S., Zhang, J., Liang Cheng, C., Sun, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.026 · Cited by 214 · see citing works
Cyclins and Cell Cycle Control in Cancer and Disease
Casimiro, M., Crosariol, M., Loro, E., Li, Z., & Pestell, R. G. (2012) · Genes & Cancer · doi:10.1177/1947601913479022 · Cited by 219 · see citing works
Peschel, N., Chen, K., Szabo, G., & Stanewsky, R. (2009) · Current Biology · doi:10.1016/j.cub.2008.12.042 · Cited by 215 · see citing works
Control of plant germline proliferation by SCFFBL17 degradation of cell cycle inhibitors
Kim, H. J., Oh, S. A., Brownfield, L. R., Hong, S. H., Ryu, H., Hwang, I., David Twell, B., & Nam, H. G. (2008) · Nature · doi:10.1038/nature07289 · Cited by 213 · see citing works
Genetics and Cell Biology of Building Specific Synaptic Connectivity
Shen, K., & Scheiffele, P. (2010) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.051508.135302 · Cited by 212 · see citing works
Identification of SCF Ubiquitin Ligase Substrates by Global Protein Stability Profiling
Yen, H.-C. S., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1160462 · Cited by 209 · see citing works
FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity
Abida, W. M., Nikolaev, A. Y., Zhao, W., Zhang, W., & Gu, W. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609001200 · Cited by 201 · see citing works
Inuzuka, H., Tseng, A., Gao, D., Zhai, B., Zhang, Q. H., Shaik, S., Wan, L., Cambronne, X. A., Mock, C. S., Yin, H., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.06.015 · Cited by 205 · see citing works
SCRAPPER-Dependent Ubiquitination of Active Zone Protein RIM1 Regulates Synaptic Vesicle Release
Yao, I., Takagi, H., Ageta, H., Kahyo, T., Sato, S., Hatanaka, K., Fukuda, Y., Chiba, T., Morone, N., Yuasa, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.052 · Cited by 200 · see citing works
Han, S., Lear, T., Jerome, J. A., Rajbhandari, S., Snavely, C. A., Gulick, D. L., Gibson, K. F., Zou, C., Chen, B. B., & Mallampalli, R. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645549 · Cited by 202 · see citing works
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
A Critical Role for FBXW8 and MAPK in Cyclin D1 Degradation and Cancer Cell Proliferation
Okabe, H., Lee, S., Phuchareon, J., Albertson, D. G., McCormick, F. P., & Tetsu, O. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000128 · Cited by 195 · see citing works
Duan, S., Skaar, J. R., Kuchay, S., Toschi, A., Kanarek, N., Ben‐Neriah, Y., & Pagano, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.005 · Cited by 194 · see citing works
Self-citationRegulation of Abiotic Stress Signal Transduction by E3 Ubiquitin Ligases in Arabidopsis
Lee, J., & Kim, W. T. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0031-9 · Cited by 191 · see citing works
Control of chromosome stability by the β-TrCP–REST–Mad2 axis
Guardavaccaro, D., Frescas, D., Dorrello, N. V., Peschiaroli, A., Multani, A. S., Cardozo, T. J., Lasorella, A., Iavarone, A., Chang, S. S., Hernando, E., et al. (2008) · Nature · doi:10.1038/nature06641 · Cited by 188 · see citing works
Self-citationThe Skp2 Pathway: A Critical Target for Cancer Therapy
Cai, Z., Moten, A., Peng, D., Hsu, C.-C., Pan, B., Manne, R., Li, H., & Lin, H. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.01.013 · Cited by 183 · see citing works
Olson, B. L., Hock, M. B., Ekholm‐Reed, S., Wohlschlegel, J. A., Dev, K. K., Kralli, A., & Reed, S. I. (2008) · Genes & Development · doi:10.1101/gad.1624208 · Cited by 185 · see citing works
The F Box Protein Fbx6 Regulates Chk1 Stability and Cellular Sensitivity to Replication Stress
Zhang, Y.-W., Brognard, J., Coughlin, C., You, Z., Dolled-Filhart, M. P., Aslanian, A., Manning, G., Abraham, R. T., & Hunter, T. R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.030 · Cited by 186 · see citing works
ERK1 and ERK2 regulate embryonic stem cell self-renewal through phosphorylation of Klf4
Kim, M. O., Kim, S.-H., Cho, Y., Nadas, J., Jeong, C., Yao, K., Kim, D. J., Yu, D.-H., Keum, Y.-S., Lee, K.-Y., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2217 · Cited by 179 · see citing works
Luo, K., Xiao, Z., Ehrlich, E. S., Yu, Y., Liu, B., Zheng, S. S., & Yu, X.-F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502440102 · Cited by 178 · see citing works
Auxin Perception--Structural Insights
Calderon-Villalobos, L. I., Tan, X., Zheng, N., & Estelle, M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005546 · Cited by 177 · see citing works
miR‐124 inhibits cell proliferation in gastric cancer through down‐regulation of SPHK1
Xia, J., Wu, Z., Yu, C., He, W., Zheng, H., He, Y., Jian, W., Chen, L., Zhang, L., & Li, W. (2012) · The Journal of Pathology · doi:10.1002/path.4030 · Cited by 177 · see citing works
- Authors
- Cardozo, T., & Pagano, M.
- Affiliations
- NYU Langone Health (US)
- Corresponding author
- Pagano, Michele
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2004-09-01
- Volume
- 5
- Issue
- 9
- Pages
- 739-751
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2061156149
- Cited by
- 1,114
- References
- 131
- Citations by year
- 2026: 29 · 2025: 33 · 2024: 31 · 2023: 50 · 2022: 39 · 2021: 44 · 2020: 43 · 2019: 34 · 2018: 38 · 2017: 54 · 2016: 35 · 2015: 61 · 2014: 64 · 2013: 73 · 2012: 74
- FWCI
- 4.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- SCF ubiquitin ligase, F-box protein, substrate recognition, ubiquitination, proteolytic regulation, post-translational regulation, protein degradation, molecular machines
- MeSH terms
- Animals, Cell Cycle, Humans, Models, Molecular, Drug Design, Protein Structure, Tertiary, Cyclin-Dependent Kinases, Evolution, Molecular, F-Box Proteins, SKP Cullin F-Box Protein Ligases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review