A binding motif for Siah ubiquitin ligase

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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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

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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 ubiquitin–proteasome pathway: on protein death and cell life

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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

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

HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation

Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181341498 · Cited by 796 · see citing works

Siah-1, SIP, and Ebi Collaborate in a Novel Pathway for β-Catenin Degradation Linked to p53 Responses

Matsuzawa, S.-I., & Reed, J. C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00242-8 · Cited by 587 · see citing works

Siah-1 Mediates a Novel β-Catenin Degradation Pathway Linking p53 to the Adenomatous Polyposis Coli Protein

Liu, J., Stevens, J., Rote, C. A., Yost, H. J., Hu, Y., Neufeld, K. L., White, R. L., & Matsunami, N. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00241-6 · Cited by 422 · see citing works

Emerging Roles of Ubiquitin in Transcription Regulation

Conaway, R. C., Brower, C. S., & Conaway, J. W. (2002) · Science · doi:10.1126/science.1067466 · Cited by 391 · see citing works

seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye

Carthew, R. W., & Rubin, G. M. (1990) · Cell · doi:10.1016/0092-8674(90)90452-k · Cited by 310 · see citing works

Siah-1 N-Terminal RING Domain Is Required for Proteolysis Function, and C-Terminal Sequences Regulate Oligomerization and Binding to Target Proteins

Hu, G., & Fearon, E. R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.724 · Cited by 241 · see citing works

PHYL Acts to Down-Regulate TTK88, a Transcriptional Repressor of Neuronal Cell Fates, by a SINA-Dependent Mechanism

Tang, A., Neufeld, T. P., Kwan, E., & Rubin, G. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80506-1 · Cited by 230 · see citing works

Proteasomal regulation of nuclear receptor corepressor-mediated repressionPreprint

Zhang, J., Guenther, M. G., Carthew, R. W., & Lazar, M. A. (1998) · Genes & Development · doi:10.1101/gad.12.12.1775 · Cited by 223 · see citing works

Photoreceptor Cell Differentiation Requires Regulated Proteolysis of the Transcriptional Repressor Tramtrack

Li, S., Li, Y., Carthew, R. W., & Lai, Z.-C. (1997) · Cell · doi:10.1016/s0092-8674(00)80507-3 · Cited by 218 · see citing works

Mammalian homologs of seven in absentia regulate DCC via the ubiquitin–proteasome pathwayPreprint

Hu, G., Zhang, S., Vidal, M., Baer, J. L., Xu, T., & Fearon, E. R. (1997) · Genes & Development · doi:10.1101/gad.11.20.2701 · Cited by 191 · see citing works

Regulation of Synaptophysin Degradation by Mammalian Homologues of Seven in Absentia

Wheeler, T. C., Chin, L., Li, Y., Roudabush, F. L., & Li, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107857200 · Cited by 167 · see citing works

Unusual 5' Transcript Complexity of Plectin Isoforms: Novel Tissue-Specific Exons Modulate Actin Binding Activity

FUCHS, P. C., Zörer, M., Rezniczek, G. A., Spazierer, D., Oehler, S., Castañón, M. J., Hauptmann, R., & Wiche, G. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.13.2461 · Cited by 158 · see citing works

Biophysical Characterization of Interactions Involving Importin-α during Nuclear Import

Catimel, B., Teh, T., Fontes, M. R. M., Jennings, I. G., Jans, D. A., Howlett, G. J., Nice, E. C., & Kobe, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103531200 · Cited by 155 · see citing works

Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling

Polekhina, G., House, C. M., Traficante, N., Mackay, J. P., Relaix, F., Sassoon, D. A., Parker, M. W., & Bowtell, D. D. L. (2001) · Nature Structural Biology · doi:10.1038/nsb743 · Cited by 137 · see citing works

Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24).

Liu, C. G., Maercker, C., Castañón, M. J., Hauptmann, R., & Wiche, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4278 · Cited by 129 · see citing works

Ras1 signaling and transcriptional competence in the R7 cell of Drosophila.Preprint

Kauffmann, R. C., Li, S., Gallagher, P., Zhang, J., & Carthew, R. W. (1996) · Genes & Development · doi:10.1101/gad.10.17.2167 · Cited by 121 · see citing works

Siah-1 binds and regulates the function of Numb

Susini, L., Passer, B. J., Amzallag, N., Juven‐Gershon, T., Prieur, S., Privat, N., Tuynder, M., Gendron, M., Israël, A., Amson, R. B., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261571998 · Cited by 95 · see citing works

ebi regulates epidermal growth factor receptor signaling pathways in DrosophilaPreprint

Dong, X., Tsuda, L., Zavitz, K. H., Lin, M. Z., Li, S., Carthew, R. W., & Zipursky, S. L. (1999) · Genes & Development · doi:10.1101/gad.13.8.954 · Cited by 90 · see citing works

Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor

Catimel, B., Nerrie, M., Lee, F.-T., Scott, A. M., Ritter, G., Welt, S., Old, L. J., Burgess, A. W., & Nice, E. C. (1997) · Journal of Chromatography A · doi:10.1016/s0021-9673(97)00087-3 · Cited by 86 · see citing works

SIAH-1 interacts with α-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis

Germani, A., Bruzzoni‐Giovanelli, H., Fellous, A., Gisselbrecht, S., Varin‐Blank, N., & Calvo, F. M. (2000) · Oncogene · doi:10.1038/sj.onc.1204002 · Cited by 84 · see citing works

Modulation of Transforming Growth Factor β (TGFβ)/Smad Transcriptional Responses through Targeted Degradation of TGFβ-inducible Early Gene-1 by Human Seven in Absentia Homologue

Johnsen, S. A., Subramaniam, M., Monroe, D. G., Janknecht, R., & Spelsberg, T. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204812200 · Cited by 78 · see citing works

Regulation of BOB.1/OBF.1 stability by SIAH

Boehm, J., He, Y., Greiner, A., Staudt, L. M., & Wirth, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4153 · Cited by 74 · see citing works

The RING finger protein Siah‐1 regulates the level of the transcriptional coactivator OBF‐1

Tiedt, R., Bartholdy, B. A., Matthias, G., Newell, J. W., & Matthias, P. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4143 · Cited by 74 · see citing works

Competitive interaction of Seven in absentia homolog‐1A and Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic glutamate receptors

Ishikawa, K., Nash, S. R., Nishimune, A., Neki, A., Kaneko, S., & Nakanishi, S. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00269.x · Cited by 72 · see citing works

Phyllopod Acts as an Adaptor Protein To Link the Sina Ubiquitin Ligase to the Substrate Protein Tramtrack

Li, S., Xu, C., & Carthew, R. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.19.6854-6865.2002 · Cited by 62 · see citing works

A role for Ebi in neuronal cell cycle control

Boulton, S. J., Brook, A., Staehling‐Hampton, K., Heitzler, P., & Dyson, N. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5376 · Cited by 56 · see citing works

hSiah2 Is a New Vav Binding Protein Which Inhibits Vav-Mediated Signaling Pathways

Germani, A., Romero, F., Houlard, M., Camonis, J., Gisselbrecht, S., Fischer, S., & Varin‐Blank, N. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3798 · Cited by 41 · see citing works

The enigmatic megakaryocyte gradually reveals its secrets

Kaushansky, K. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199904)21:4 · Cited by 38 · see citing works

Direct immobilization of gangliosides onto gold-carboxymethyldextran sensor surfaces by hydrophobic interaction: applications to antibody characterization

Catimel, B., Scott, A. M., Lee, F.-T., Hanai, N., Ritter, G., Welt, S., Old, L. J., Burgess, A. W., & Nice, E. C. (1998) · Glycobiology · doi:10.1093/glycob/8.9.927 · Cited by 26 · see citing works

Reading between the lines: SH3 recognition of an intact protein

Lim, W. A. (1996) · Structure · doi:10.1016/s0969-2126(96)00071-8 · Cited by 24 · see citing works

Synthesis, conformational studies and biological activity of Να‐mono‐biotinylated rat relaxin*

Mathieu, M. N., Wade, J. D., Tregear, G. W., BOND, C. P., Summers, R. J., Catimel, B., Nice, E. C., & Otvos, L. P. (2001) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2001.00853.x · Cited by 18 · see citing works

S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding

Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,071 · see citing works

A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin

Willems, A. R., Schwab, M. G., & Tyers, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.027 · Cited by 461 · see citing works

Molecular traces of alternative social organization in a termite genome

Terrapon, N., Li, C., Robertson, H. M., Ji, L., Meng, X., Booth, W., Chen, Z., Childers, C. P., Glastad, K. M., Gokhale, K., et al. (2014) · Nature Communications · doi:10.1038/ncomms4636 · Cited by 395 · see citing works

Thiol-based redox switches in eukaryotic proteins

Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works

Small-molecule-induced polymerization triggers degradation of BCL6

Słabicki, M., Yoon, H., Koeppel, J., Nitsch, L., Roy Burman, S. S., Di Genua, C., Donovan, K. A., Sperling, A. S., Hunkeler, M., Tsai, J. M., et al. (2020) · Nature · doi:10.1038/s41586-020-2925-1 · Cited by 270 · see citing works

Siah2-Dependent Concerted Activity of HIF and FoxA2 Regulates Formation of Neuroendocrine Phenotype and Neuroendocrine Prostate Tumors

Qi, J., Nakayama, K., Cardiff, R. D., Borowsky, A. D., Kaul, K. L., Williams, R. M., Krajewski, S., Mercola, D., Carpenter, P. M., Bowtell, D. D. L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.024 · Cited by 236 · see citing works

GAPDH as a sensor of NO stress

Hara, M. R., Cascio, M. B., & Sawa, A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.01.012 · Cited by 220 · see citing works

Ubiquitylation of synphilin-1 and α-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease

Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Rieß, O., Ross, C. A., Rott, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401081101 · Cited by 192 · see citing works

Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR

Winter, M., Sombroek, D., Dauth, I., Moehlenbrink, J., Scheuermann, K., Crone, J., & Hofmann, T. G. (2008) · Nature Cell Biology · doi:10.1038/ncb1743 · Cited by 190 · see citing works

The molecular programme of tumour reversion: the steps beyond malignant transformation

Telerman, A., & Amson, R. B. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2589 · Cited by 185 · see citing works

Mechanisms of leukemogenesis by MLL fusion proteins

Marschalek, R. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08459.x · Cited by 185 · see citing works

Ubiquitination of -synuclein by Siah-1 promotes -synuclein aggregation and apoptotic cell death

Lee, J. T., Wheeler, T. C., Li, L., & Chin, L. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm363 · Cited by 169 · see citing works

Plectin–intermediate filament partnership in skin, skeletal muscle, and peripheral nerve

Castañón, M. J., Walko, G., Winter, L., & Wiche, G. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1102-0 · Cited by 157 · see citing works

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation

Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 144 · see citing works

Anchoring Junctions As Drug Targets: Role in Contraceptive Development

Mruk, D. D., Silvestrini, B., & Cheng, C. Y. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.07105 · Cited by 138 · see citing works

Functional role of KLF10 in multiple disease processes

Subramaniam, M., Hawse, J. R., Rajamannan, N. M., Ingle, J. N., & Spelsberg, T. C. (2010) · BioFactors · doi:10.1002/biof.67 · Cited by 115 · see citing works

Siah-1 Facilitates Ubiquitination and Degradation of Synphilin-1

Nagano, Y., Yamashita, H., Takahashi, T., Kishida, S., Nakamura, T., Iseki, E., Hattori, N., Mizuno, Y., Kikuchi, A., & Matsumoto, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306347200 · Cited by 113 · see citing works

Plectin-RACK1 (Receptor for Activated C Kinase 1) Scaffolding

Osmanagic‐Myers, S., & Wiche, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312382200 · Cited by 110 · see citing works

TIEG1 Null Mouse-Derived Osteoblasts Are Defective in Mineralization and in Support of Osteoclast Differentiation In Vitro

Subramaniam, M., Gorny, G., Johnsen, S. A., Monroe, D. G., Evans, G. L., Fraser, D. G., Rickard, D. J., Rasmussen, K., van Deursen, J. M. A., Turner, R. T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1191-1199.2005 · Cited by 110 · see citing works

Structural Analysis of Siah1-Siah-interacting Protein Interactions and Insights into the Assembly of an E3 Ligase Multiprotein Complex

Santelli, E., Leone, M., Chenlong, L., Fukushima, T., Preece, N. E., Olson, A. J., Ely, K. R., Reed, J. C., Pellecchia, M., Liddington, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506707200 · Cited by 106 · see citing works

The ubiquitin ligase Siah2 regulates tumorigenesis and metastasis by HIF-dependent and -independent pathways

Qi, J., Nakayama, K., Gaitonde, S., Goydos, J. S., Krajewski, S., Eroshkin, A. M., Bar‐Sagi, D., Bowtell, D. D. L., & Ronai, Z. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804063105 · Cited by 102 · see citing works

The SIAH E3 ubiquitin ligases promote Wnt/β-catenin signaling through mediating Wnt-induced Axin degradation

Ji, L., Jiang, B., Jiang, X., Charlat, O., Chen, A., Mickanin, C., Bauer, A., Xu, W., Yan, X., & Cong, F. (2017) · Genes & Development · doi:10.1101/gad.300053.117 · Cited by 89 · see citing works

Role of TIEG1 in biological processes and disease states

Subramaniam, M., Hawse, J. R., Johnsen, S. A., & Spelsberg, T. C. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21492 · Cited by 85 · see citing works

Siah Proteins: Novel Drug Targets in the Ras and Hypoxia Pathways

House, C. M., Möller, A., & Bowtell, D. D. L. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1676 · Cited by 80 · see citing works

Elucidation of the Substrate Binding Site of Siah Ubiquitin Ligase

House, C. M., Hancock, N. C., Möller, A., Cromer, B. A., Fedorov, V., Bowtell, D. D. L., Parker, M. W., & Polekhina, G. (2006) · Structure · doi:10.1016/j.str.2005.12.013 · Cited by 79 · see citing works

Inhibition of Siah ubiquitin ligase function

Möller, A., House, C., Wong, C. S. F., Scanlon, D. B., Liu, M. C. P., Ronai, Z. A., & Bowtell, D. D. L. (2008) · Oncogene · doi:10.1038/onc.2008.382 · Cited by 78 · see citing works

Interaction of AF4 wild-type and AF4·MLL fusion protein with SIAH proteins: indication for t(4;11) pathobiology?

Bursen, A., Moritz, S., Anne, G., Moritz, S., Dingermann, T., & Marschalek, R. (2004) · Oncogene · doi:10.1038/sj.onc.1207837 · Cited by 78 · see citing works

Mechanism for ubiquitylation of the leukemia fusion proteins AML1‐ETO and PML‐RARα

Krämer, O. H., Müller, S., Buchwald, M., Reichardt, S., & Heinzel, T. (2007) · The FASEB Journal · doi:10.1096/fj.06-8050com · Cited by 72 · see citing works

The Ubiquitin Ligase Siah2 Regulates PPARγ Activity in Adipocytes

Kilroy, G. E., Kirk-Ballard, H., Carter, L. E., & Floyd, Z. E. (2012) · Endocrinology · doi:10.1210/en.2011-1725 · Cited by 68 · see citing works

siah-1 Protein Is Necessary for High Glucose-induced Glyceraldehyde-3-phosphate Dehydrogenase Nuclear Accumulation and Cell Death in Müller Cells

Yego, E. C. K., & Mohr, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083907 · Cited by 66 · see citing works

The Coiled-coil Domain Is the Structural Determinant for Mammalian Homologues of Drosophila Sina-mediated Degradation of Promyelocytic Leukemia Protein and Other Tripartite Motif Proteins by the Proteasome

Fanelli, M., Fantozzi, A., Luca, P. D., Caprodossi, S., Matsuzawa, S.-I., Lazar, M. A., Pelicci, P. G., & Minucci, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306407200 · Cited by 65 · see citing works

CacyBP/SIP — Structure and variety of functions

Topolska‐Woś, A. M., Chazin, W., & Filipek, A. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.10.012 · Cited by 64 · see citing works

The ubiquitin ligase SEVEN IN ABSENTIA ( SINA ) ubiquitinates a defense‐related NAC transcription factor and is involved in defense signaling

Miao, M., Niu, X., Kud, J., Du, X., Ávila-Pacheco, J., Devarenne, T. P., Kuhl, J. C., Liu, Y., & Xiao, F. (2016) · New Phytologist · doi:10.1111/nph.13890 · Cited by 64 · see citing works

cAMP perturbs inter‐sertoli tight junction permeability barrier in vitro via its effect on proteasome‐sensitive ubiquitination of occludin

Lui, W., & Lee, W. M. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20254 · Cited by 62 · see citing works

Ca2+-promoted cyclin B1 degradation in mouse oocytes requires the establishment of a metaphase arrest

Hyslop, L., Nixon, V. L., Levasseur, M., Chapman, F., Chiba, K., McDougall, A., Venables, J. P., Elliott, D. J., & Jones, K. T. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.01.030 · Cited by 62 · see citing works

Identification of a Src Tyrosine Kinase/SIAH2 E3 Ubiquitin Ligase Pathway That Regulates C/EBPδ Expression and Contributes to Transformation of Breast Tumor Cells

Sarkar, T. R., Sharan, S., Wang, J., Pawar, S. A., Cantwell, C. A., Johnson, P. F., Morrison, D. K., Wang, J., & Sterneck, E. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05790-11 · Cited by 61 · see citing works

Roles for the ubiquitin–proteasome pathway in protein quality control and signaling in the retina: Implications in the pathogenesis of age-related macular degeneration

Shang, F., & Taylor, A. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.04.001 · Cited by 60 · see citing works

Seven in Absentia Homolog 2 (Siah2) Protein Is a Regulator of NF-E2-related Factor 2 (Nrf2)*

Baba, K., Morimoto, H., & Imaoka, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.438762 · Cited by 59 · see citing works

Siah1 Interacts with the Scaffold Protein POSH to Promote JNK Activation and Apoptosis

Xu, Z., Sproul, A. A., Wang, W., Kukekov, N. V., & Greene, L. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509060200 · Cited by 58 · see citing works

ARTS and Siah Collaborate in a Pathway for XIAP Degradation

Garrison, J. B., Correa, R. G., Gerlic, M., Yip, K. W., Krieg, A. H., Tamble, C. M., Shi, R., Welsh, K., Duggineni, S., Huang, Z., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.002 · Cited by 56 · see citing works

Targeted ablation of plectin isoform 1 uncovers role of cytolinker proteins in leukocyte recruitment

Abrahamsberg, C., FUCHS, P. C., Osmanagic‐Myers, S., Fischer, I., Propst, F., Elbe‐Bürger, A., & Wiche, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505380102 · Cited by 56 · see citing works

Siah: A Promising Anticancer Target

Wong, C. S. F., & Möller, A. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4348 · Cited by 56 · see citing works

Structure-Based Design of Covalent Siah Inhibitors

Stebbins, J. L., Santelli, E., Feng, Y., De, S. K., Purves, A., Motamedchaboki, K., Wu, B., Ronai, Z. A., Liddington, R., & Pellecchia, M. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.06.008 · Cited by 56 · see citing works

D1/D5 receptors and histone deacetylation mediate the Gateway Effect of LTP in hippocampal dentate gyrusPreprint

Huang, Y. Y., Levine, A. A., Kandel, D. B., Yin, D., Colnaghi, L., Drisaldi, B., & Kandel, E. R. (2014) · Learning & Memory · doi:10.1101/lm.032292.113 · Cited by 56 · see citing works

Function of the ubiquitin proteolytic pathway in the eye

Shang, F., & Taylor, A. (2003) · Experimental Eye Research · doi:10.1016/j.exer.2003.10.003 · Cited by 55 · see citing works

Vascular Normalization by Loss of Siah2 Results in Increased Chemotherapeutic Efficacy

Wong, C. S. F., Sceneay, J., House, C. M., Halse, H. M., Liu, M. C. P., George, J., Hunnam, T. C. U. P., Parker, B. S., Haviv, I., Ronai, Z. A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3310 · Cited by 54 · see citing works

SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome

Venables, J. P., Dalgliesh, C., Paronetto, M. P., Skitt, L., Thornton, J. K., Saunders, P. T. K., Sette, C., Jones, K. T., & Elliott, D. J. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh165 · Cited by 54 · see citing works

Up-regulation of β-catenin by a viral oncogene correlates with inhibition of the seven in absentia homolog 1 in B lymphoma cells

Jang, K. L., Shackelford, J., Seo, S. Y., & Pagano, J. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504054102 · Cited by 54 · see citing works

Mediation of Af4 protein function in the cerebellum by Siah proteins

Oliver, P. L., Bitoun, E., Clark, J., Jones, E. L., & Davies, K. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406196101 · Cited by 53 · see citing works

The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies,

Bhattacharya, S., Lee, Y., Michowski, W., Jastrzębska, B., Filipek, A., Kuźnicki, J., & Chazin, W. (2005) · Biochemistry · doi:10.1021/bi0502689 · Cited by 52 · see citing works

Plectin isoform 1-dependent nuclear docking of desmin networks affects myonuclear architecture and expression of mechanotransducers

Staszewska-Daca, I., Fischer, I., & Wiche, G. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv438 · Cited by 52 · see citing works

Mitotic Regulation of the Stability of Microtubule Plus-end Tracking Protein EB3 by Ubiquitin Ligase SIAH-1 and Aurora Mitotic Kinases

Ban-Ishihara, R., Matsuzaki, H., Akashi, T., Sakashita, G., Taniguchi, H., Park, S., Tanaka, H., Furukawa, K., & Urano, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000273 · Cited by 51 · see citing works

Hacking the Code of Amyloid Formation

Pastor, M. T., Esteras‐Chopo, A., & Serrano, L. G. (2007) · Prion · doi:10.4161/pri.1.1.4100 · Cited by 51 · see citing works

TIEG1/KLF10 Modulates Runx2 Expression and Activity in Osteoblasts

Hawse, J. R., Cicek, M., Grygo, S. B., Bruinsma, E. S., Rajamannan, N. M., van Wijnen, A. J., Lian, J. B., Stein, G. S., Oursler, M. J., Subramaniam, M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019429 · Cited by 50 · see citing works

Peptide‐based covalent inhibitors of protein–protein interactions

Paulussen, F. M., & Grossmann, T. N. (2022) · Journal of Peptide Science · doi:10.1002/psc.3457 · Cited by 49 · see citing works

DeSUMOylase SENP7-Mediated Epithelial Signaling Triggers Intestinal Inflammation via Expansion of Gamma-Delta T Cells

Suhail, A., Rizvi, Z. A., Mujagond, P., Ali, S. A., Gaur, P., Singh, M. K., Ahuja, V., Awasthi, A., & Srikanth, C. V. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.028 · Cited by 47 · see citing works

PKC Phosphorylation Regulates mGluR5 Trafficking by Enhancing Binding of Siah-1A

Ko, S. J., Isozaki, K., Kim, I., Lee, J. H., Cho, H., Sohn, S. Y., Oh, S. R., Park, S., Kim, D. G., Kim, C. H., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1964-12.2012 · Cited by 41 · see citing works

Variants in the degron of AFF3 are associated with intellectual disability, mesomelic dysplasia, horseshoe kidney, and epileptic encephalopathy

Voisin, N., Schnur, R. E., Douzgou, S., Hiatt, S. M., Rustad, C. F., Brown, N. J., Earl, D., Keren, B., Levchenko, O. A., Geuer, S., et al. (2021) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2021.04.001 · Cited by 40 · see citing works

Polycystins as components of large multiprotein complexes of polycystin interactors

Hardy, E. P., & Tsiokas, L. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109640 · Cited by 37 · see citing works

Central role of SIAH inhibition in DCC-dependent cardioprotection provoked by netrin-1/NO

Li, Q., Wang, P., Ye, K., & Cai, H. “. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420695112 · Cited by 36 · see citing works

Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth

Park, S. H., Jeong, J. S., Yu, Z., Mustafa, N. F. B., & Chua, N. (2022) · Plant Communications · doi:10.1016/j.xplc.2022.100348 · Cited by 36 · see citing works

Siah1/SIP regulates p27kip1stability and cell migration under metabolic stress

Nagano, Y., Fukushima, T., Okemoto, K., Tanaka, K., Bowtell, D. D. L., Ronai, Z. A., Reed, J. C., & Matsuzawa, S. (2011) · Cell Cycle · doi:10.4161/cc.10.15.16912 · Cited by 35 · see citing works

Synphilin-1A Inhibits Seven in Absentia Homolog (SIAH) and Modulates α-Synuclein Monoubiquitylation and Inclusion Formation

Szargel, R., Rott, R., Eyal, A., Haskin, J., Shani, V., Balan, L., Wolosker, H., & Engelender, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805990200 · Cited by 34 · see citing works

The Siah2-HIF-FoxA2 axis in prostate cancer - new markers and therapeutic opportunities

Qi, J., Pellecchia, M., & Ronai, Z. A. (2010) · Oncotarget · doi:10.18632/oncotarget.171 · Cited by 33 · see citing works

Plectin

Rezniczek, G. A., Janda, Ľ., & Wiche, G. (2004) · Methods in cell biology · doi:10.1016/s0091-679x(04)78025-5 · Cited by 32 · see citing works

SIAH-mediated ubiquitination and degradation of acetyl-transferases regulate the p53 response and protein acetylation

Grishina, I., Debus, K., Garcı́a-Limones, C., Schneider, C., Shresta, A., García, C., Calzado, M. A., & Schmitz, M. L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.09.011 · Cited by 32 · see citing works

Herpes Simplex Virus Immediate-Early Protein ICP0 Is Targeted by SIAH-1 for Proteasomal Degradation

Nagel, C., Albrecht, N., Milovic-Holm, K., Lakshmikanth, M., Keyser, B., Abel, B., Weseloh, B., Hofmann, T. G., Eibl, M. M., & Hauber, J. (2011) · Journal of Virology · doi:10.1128/jvi.02207-10 · Cited by 31 · see citing works

Role of the Ubiquitin–Proteasome in Protein Quality Control and Signaling

Shang, F., & Taylor, A. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00010-9 · Cited by 28 · see citing works

TIN2 Stability Is Regulated by the E3 Ligase Siah2

Bhanot, M., & Smith, S. H. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06227-11 · Cited by 27 · see citing works

SIAH-1 Interacts with the Kaposi's Sarcoma-Associated Herpesvirus-Encoded ORF45 Protein and Promotes Its Ubiquitylation and Proteasomal Degradation

Abada, R., Dreyfuss-Grossman, T., Herman-Bachinsky, Y., Geva, H., Masa, S.-R., & Sarid, R. (2007) · Journal of Virology · doi:10.1128/jvi.02285-07 · Cited by 27 · see citing works

Breaking Bad Proteins—Discovery Approaches and the Road to Clinic for Degraders

Bouvier, C., Lawrence, R., Cavallo, F., Xolalpa, W., Jordan, A. M., Hjerpe, R., & Rodríguez, M. S. (2024) · Cells · doi:10.3390/cells13070578 · Cited by 27 · see citing works

Identifying Plectin Isoform Functions through Animal Models

Castañón, M. J., & Wiche, G. (2021) · Cells · doi:10.3390/cells10092453 · Cited by 26 · see citing works

Regulation of MYPT1 stability by the E3 ubiquitin ligase SIAH2

Twomey, E. C., Li, Y., Lei, J. X., Sodja, C., Ribecco‐Lutkiewicz, M., Smith, B., Fang, H., Bani‐Yaghoub, M., McKinnell, I. W., & Sikorska, M. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.09.001 · Cited by 25 · see citing works

The robotic mouse: Unravelling the function of AF4 in the cerebellum

Bitoun, E., & Davies, K. E. (2005) · The Cerebellum · doi:10.1080/14734220500325897 · Cited by 25 · see citing works

Plectin regulates the signaling and trafficking of the HIV-1 co-receptor CXCR4 and plays a role in HIV-1 infection

Ding, Y., Zhang, L., Goodwin, J. S., Wang, Z., Liu, B., Zhang, J., & Fan, G.-H. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.10.032 · Cited by 25 · see citing works

Polo-like kinase 3, hypoxic responses, and tumorigenesis

Xu, D., Dai, W. H., & Li, C. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1373224 · Cited by 25 · see citing works

Siah2 integrates mitogenic and extracellular matrix signals linking neuronal progenitor ciliogenesis with germinal zone occupancy

Ong, T., Trivedi, N., Wakefield, R., Frase, S., & Solecki, D. J. (2020) · Nature Communications · doi:10.1038/s41467-020-19063-7 · Cited by 24 · see citing works

Siah2 regulates tight junction integrity and cell polarity through control of ASPP2 stability

Kim, H., Claps, G., Möller, A., Bowtell, D. D. L., Lü, X., & Ronai, Z. A. (2013) · Oncogene · doi:10.1038/onc.2013.149 · Cited by 24 · see citing works

Regulation of the SIAH2-HIF-1 Axis by Protein Kinases and Its Implication in Cancer Therapy

Xu, D., & Li, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.646687 · Cited by 23 · see citing works

E2F1 represses β‐catenin/TCF activity by direct up‐regulation of Siah1

Xie, W., Jin, L., Mei, Y., & Wu, M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00423.x · Cited by 23 · see citing works

Mutual regulation between Polo-like kinase 3 and SIAH2 E3 ubiquitin ligase defines a regulatory network that fine-tunes the cellular response to hypoxia and nickel

Li, C., Park, S., Zhang, X., Dai, W. H., & Xu, D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767178 · Cited by 23 · see citing works

HIF Prolyl-4-hydroxylase Interacting Proteins: Consequences for Drug Targeting

Wenger, R. H., Camenisch, G., Stiehl, D. P., & Katschinski, D. M. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789649411 · Cited by 21 · see citing works

A crosstalk between hSiah2 and Pias E3-ligases modulates Pias-dependent activation

Depaux, A., Régnier, F., Germani, A., & Varin‐Blank, N. (2007) · Oncogene · doi:10.1038/sj.onc.1210486 · Cited by 22 · see citing works

DDX6 transfers P-TEFb kinase to the AF4/AF4N (AFF1) super elongation complex.

Mück, F., Bracharz, S., & Marschalek, R. (2016) · PubMed Central · Cited by 20 · see citing works

Identification and characterization of small molecule inhibitors of the ubiquitin ligases Siah1/2 in melanoma and prostate cancer cells

Feng, Y., Sessions, E. H., Zhang, F., Ban, F., Placencio-Hickok, V., Ma, C.-T., Zeng, F., Pass, I., Terry, D. B., Cadwell, G. W., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.012 · Cited by 22 · see citing works

E3 ubiquitin ligases SIAH1/2 regulate hypoxia-inducible factor-1 (HIF-1)-mediated Th17 cell differentiation

Matsui-Hasumi, A., Sato, Y., Uto-Konomi, A., Yamashita, S., Uehori, J., Yoshimura, A., Yamashita, M., Asahara, H., Suzuki, S., & Kubo, M. (2017) · International Immunology · doi:10.1093/intimm/dxx014 · Cited by 21 · see citing works

Ubiquitin-mediated proteasome degradation regulates optic fissure fusion

Piedade, W. P., Veith, S., & Famulski, J. K. (2019) · Biology Open · doi:10.1242/bio.044974 · Cited by 20 · see citing works

The role of E3 ubiquitin ligase seven in absentia homolog in the innate immune system: An overview

Siswanto, F. M., Jawi, I. M., & Kartiko, B. H. (2018) · Veterinary World · doi:10.14202/vetworld.2018.1551-1557 · Cited by 20 · see citing works

Polycystin-1 regulates the stability and ubiquitination of transcription factor Jade-1

Foy, R. L., Chitalia, V. C., Panchenko, M. V., Zeng, L., Lopez, D., Lee, J. W., Rana, S. V., Boletta, A., Qian, F., Tsiokas, L., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds391 · Cited by 19 · see citing works

The Bin/Amphiphysin/Rvs (BAR) Domain Protein Endophilin B2 Interacts with Plectin and Controls Perinuclear Cytoskeletal Architecture

Vannier, C., Pesty, A., Jouve, M. J., & Schmidt, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.485482 · Cited by 17 · see citing works

Investigating the Molecular Basis of Siah1 and Siah2 E3 Ubiquitin Ligase Substrate Specificity

Gopalsamy, A., Hagen, T., & Swaminathan, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106547 · Cited by 17 · see citing works

Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks

Outla, Z., Přechová, M., Korelova, K., Gemperle, J., & Gregor, M. (2025) · Open Biology · doi:10.1098/rsob.240208 · Cited by 15 · see citing works

Analysis of human neurological disorders using mutagenesis in the mouse

Oliver, P. L., & Davies, K. E. (2005) · Clinical Science · doi:10.1042/cs20050041 · Cited by 16 · see citing works

Structure of the SCAN Domain of Human Paternally Expressed Gene 3 Protein

Rimsa, V., Eadsforth, T. C., & Hunter, W. N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069538 · Cited by 15 · see citing works

FRK inhibits glioblastoma progression via phosphorylating YAP and inducing its ubiquitylation and degradation by Siah1

Wang, Y., Wang, K., Fu, J., Zhang, Y., Mao, Y., Wang, X., Wang, X., Yu, R., & Zhou, X. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac156 · Cited by 15 · see citing works

The Robotic Mouse: Understanding the Role of AF4, a Cofactor of Transcriptional Elongation and Chromatin Remodelling, in Purkinje Cell Function

Bitoun, E., & Davies, K. E. (2009) · The Cerebellum · doi:10.1007/s12311-009-0101-0 · Cited by 15 · see citing works

Proteolysis-targeting influenza vaccine strains induce broad-spectrum immunity and in vivo protection

Shen, J., Li, J., Shen, Q., Hou, J., Zhang, C., Bai, H., Ai, X., Su, Y., Wang, Z., Zhang, Y., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01908-2 · Cited by 14 · see citing works

E3 ubiquitin ligase-mediated regulation of vertebrate ocular development; new insights into the function of SIAH enzymes

Piedade, W. P., & Famulski, J. K. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200613 · Cited by 14 · see citing works

Two high-resolution structures of the human E3 ubiquitin ligase Siah1

Rimsa, V., Eadsforth, T. C., & Hunter, W. N. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113031448 · Cited by 14 · see citing works

Nuclear GAPDH: changing the fate of Müller cells in diabetes

Jayaguru, P., & Mohr, S. (2011) · Journal of ocular biology, diseases, and informatics · doi:10.1007/s12177-012-9085-y · Cited by 13 · see citing works

Elucidation of the Substrate Binding Site of Siah Ubiquitin Ligase

House, C. M., Hancock, N. C., Möller, A., Cromer, B. A., Fedorov, V., Bowtell, D. D. L., Parker, M. W., & Polekhina, G. (2006) · Structure · doi:10.1016/j.str.2005.12.013 · Cited by 79 · see citing works

I Siah Substrate!

Briant, D. J., Ceccarelli, D. F. J., & Sicheri, F. (2006) · Structure · doi:10.1016/j.str.2006.03.003 · Cited by 1 · see citing works

Degrading liaisons: Siah structure revealed

Reed, J. C., & Ely, K. R. (2002) · Nature Structural Biology · doi:10.1038/nsb0102-8 · Cited by 50 · see citing works

Structural Analysis of Siah1 and Its Interactions with Siah-interacting Protein (SIP)

Matsuzawa, S., Li, C., Ni, C., Takayama, S.-I. J., Reed, J. C., & Ely, K. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210263200 · Cited by 45 · see citing works

Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling

Polekhina, G., House, C. M., Traficante, N., Mackay, J. P., Relaix, F., Sassoon, D. A., Parker, M. W., & Bowtell, D. D. L. (2001) · Nature Structural Biology · doi:10.1038/nsb743 · Cited by 137 · see citing works