The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

Zhang, Qi; Wang, Zhongduo; Hou, Feng; Harding, Rachel; Huang, Xinyi; Dong, Aiping; Walker, John R.; Tong, Yufeng

doi:10.1016/j.bbagen.2016.10.019

Title: The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

Journal Article · Sun Jan 01 00:00:00 UTC 2017 · Biochimica et Biophysica Acta - General Subjects

DOI: https://doi.org/10.1016/j.bbagen.2016.10.019 · OSTI ID:1414337

Zhang, Qi; Wang, Zhongduo; Hou, Feng; Harding, Rachel;

; Dong, Aiping; Walker, John R.;

Not Available

View Accepted Manuscript (Publisher)

Cite

Export

Save

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1414337

Journal Information:: Biochimica et Biophysica Acta - General Subjects, Journal Name: Biochimica et Biophysica Acta - General Subjects Journal Issue: 1 PA Vol. 1861; ISSN 0304-4165

Publisher:: ElsevierCopyright Statement

Country of Publication:: Netherlands

Language:: English

References (85)

The expression of SIAH1 is downregulated and associated with Bim and apoptosis in human breast cancer tissues and cells: EXPRESSION OF SIAH1 THE BREAST CARCINOGENESIS Wen, Yuan-Yuan; Yang, Zhi-Qiang; Song, Min Molecular Carcinogenesis, Vol. 49, Issue 5 https://doi.org/10.1002/mc.20615	journal	January 2010
Modulation of multidrug resistance in cancer cells by the E3 ubiquitin ligase seven-in-absentia homologue 1 Liu, M.; Aneja, R.; Wang, H. The Journal of Pathology, Vol. 214, Issue 4 https://doi.org/10.1002/path.2312	journal	December 2007
RING domains: master builders of molecular scaffolds? Borden, Katherine L. B. Journal of Molecular Biology, Vol. 295, Issue 5 https://doi.org/10.1006/jmbi.1999.3429	journal	February 2000
Homology modeling and in silico screening of inhibitors for the substrate binding domain of human Siah2: implications for hypoxia-induced cancers Anupriya, Gopalsamy; Roopa, Kothapalli; Basappa, S. Journal of Molecular Modeling, Vol. 17, Issue 12 https://doi.org/10.1007/s00894-011-1025-4	journal	March 2011
Downregulation of SIAH2, an ubiquitin E3 ligase, is associated with resistance to endocrine therapy in breast cancer Jansen, Maurice P. H. M.; Ruigrok-Ritstier, Kirsten; Dorssers, Lambert C. J. Breast Cancer Research and Treatment, Vol. 116, Issue 2 https://doi.org/10.1007/s10549-008-0125-z	journal	July 2008
Regulators and Effectors of Siah Ubiquitin Ligases Qi, Jianfei; Kim, Hyungsoo; Scortegagna, Marzia Cell Biochemistry and Biophysics, Vol. 67, Issue 1 https://doi.org/10.1007/s12013-013-9636-2	journal	May 2013
The SPOT-synthesis technique Frank, Ronald Journal of Immunological Methods, Vol. 267, Issue 1 https://doi.org/10.1016/S0022-1759(02)00137-0	journal	September 2002
Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content Singer, Gregory A. C.; Hickey, Donal A. Gene, Vol. 317 https://doi.org/10.1016/S0378-1119(03)00660-7	journal	October 2003
An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19 Velasco, Kelly; Zhao, Bin; Callegari, Simone Biochemical and Biophysical Research Communications, Vol. 433, Issue 4 https://doi.org/10.1016/j.bbrc.2013.02.094	journal	April 2013
HDACi – Targets beyond chromatin Buchwald, Marc; Krämer, Oliver H.; Heinzel, Thorsten Cancer Letters, Vol. 280, Issue 2 https://doi.org/10.1016/j.canlet.2009.02.028	journal	August 2009
The E3 Ubiquitin Ligase Siah2 Contributes to Castration-Resistant Prostate Cancer by Regulation of Androgen Receptor Transcriptional Activity Qi, Jianfei; Tripathi, Manisha; Mishra, Rajeev Cancer Cell, Vol. 23, Issue 3 https://doi.org/10.1016/j.ccr.2013.02.016	journal	March 2013
Siah2 Regulates Stability of Prolyl-Hydroxylases, Controls HIF1α Abundance, and Modulates Physiological Responses to Hypoxia Nakayama, Koh; Frew, Ian J.; Hagensen, Mette Cell, Vol. 117, Issue 7 https://doi.org/10.1016/j.cell.2004.06.001	journal	June 2004
Defining the Human Deubiquitinating Enzyme Interaction Landscape Sowa, Mathew E.; Bennett, Eric J.; Gygi, Steven P. Cell, Vol. 138, Issue 2 https://doi.org/10.1016/j.cell.2009.04.042	journal	July 2009
Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications Brahimi-Horn, Christiane; Mazure, Nathalie; Pouysségur, Jacques Cellular Signalling, Vol. 17, Issue 1 https://doi.org/10.1016/j.cellsig.2004.04.010	journal	January 2005
Structure-Based Design of Covalent Siah Inhibitors Stebbins, John L.; Santelli, Eugenio; Feng, Yongmei Chemistry & Biology, Vol. 20, Issue 8 https://doi.org/10.1016/j.chembiol.2013.06.008	journal	August 2013
Hypoxic Regulation of Glutamine Metabolism through HIF1 and SIAH2 Supports Lipid Synthesis that Is Necessary for Tumor Growth Sun, Ramon C.; Denko, Nicholas C. Cell Metabolism, Vol. 19, Issue 2 https://doi.org/10.1016/j.cmet.2013.11.022	journal	February 2014
The inducible E3 ubiquitin ligases SIAH1 and SIAH2 perform critical roles in breast and prostate cancers Knauer, Shirley K.; Mahendrarajah, Nisintha; Roos, Wynand P. Cytokine & Growth Factor Reviews, Vol. 26, Issue 4 https://doi.org/10.1016/j.cytogfr.2015.04.002	journal	August 2015
A SPOT on the chromatin landscape? Histone peptide arrays as a tool for epigenetic research Nady, Nataliya; Min, Jinrong; Kareta, Michael S. Trends in Biochemical Sciences, Vol. 33, Issue 7 https://doi.org/10.1016/j.tibs.2008.04.014	journal	July 2008
Role of Quinones in Toxicology ^† Bolton, Judy L.; Trush, Michael A.; Penning, Trevor M. Chemical Research in Toxicology, Vol. 13, Issue 3 https://doi.org/10.1021/tx9902082	journal	March 2000
Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation Buchwald, M.; Pietschmann, K.; Müller, J. P. Leukemia, Vol. 24, Issue 8 https://doi.org/10.1038/leu.2010.114	journal	May 2010
SIAH proteins: critical roles in leukemogenesis Krämer, O. H.; Stauber, R. H.; Bug, G. Leukemia, Vol. 27, Issue 4 https://doi.org/10.1038/leu.2012.284	journal	October 2012
High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy Hasson, Samuel A.; Kane, Lesley A.; Yamano, Koji Nature, Vol. 504, Issue 7479 https://doi.org/10.1038/nature12748	journal	November 2013
Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR Winter, Melanie; Sombroek, Dirk; Dauth, Ilka Nature Cell Biology, Vol. 10, Issue 7 https://doi.org/10.1038/ncb1743	journal	June 2008
Hypoxia regulates Hippo signalling through the SIAH2 ubiquitin E3 ligase Ma, Biao; Chen, Yan; Chen, Ling Nature Cell Biology, Vol. 17, Issue 1 https://doi.org/10.1038/ncb3073	journal	December 2014
The molecular programme of tumour reversion: the steps beyond malignant transformation Telerman, Adam; Amson, Robert Nature Reviews Cancer, Vol. 9, Issue 3 https://doi.org/10.1038/nrc2589	journal	January 2009
RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis Lipkowitz, Stanley; Weissman, Allan M. Nature Reviews Cancer, Vol. 11, Issue 9 https://doi.org/10.1038/nrc3120	journal	August 2011
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling Polekhina, Galina; House, Colin M.; Traficante, Nadia Nature Structural Biology, Vol. 9, Issue 1 https://doi.org/10.1038/nsb743	journal	December 2001
Molecular recognition of p53 and MDM2 by USP7/HAUSP Sheng, Yi; Saridakis, Vivian; Sarkari, Feroz Nature Structural & Molecular Biology, Vol. 13, Issue 3 https://doi.org/10.1038/nsmb1067	journal	February 2006
SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation Buchwald, M.; Pietschmann, K.; Brand, P. Oncogene, Vol. 32, Issue 41 https://doi.org/10.1038/onc.2012.515	journal	December 2012
CHK2 stability is regulated by the E3 ubiquitin ligase SIAH2 García-Limones, C.; Lara-Chica, M.; Jiménez-Jiménez, C. Oncogene, Vol. 35, Issue 33 https://doi.org/10.1038/onc.2015.495	journal	January 2016
New Insights into the RNA-Binding and E3 Ubiquitin Ligase Activities of Roquins Zhang, Qi; Fan, Lixin; Hou, Feng Scientific Reports, Vol. 5, Issue 1 https://doi.org/10.1038/srep15660	journal	October 2015
To ubiquitinate or to deubiquitinate: it all depends on the partners Marfany, Gemma; Denuc, Amanda Biochemical Society Transactions, Vol. 36, Issue 5 https://doi.org/10.1042/BST0360833	journal	September 2008
Estrogen down-regulation of the corepressor N-CoR: Mechanism and implications for estrogen derepression of N-CoR-regulated genes Frasor, J.; Danes, J. M.; Funk, C. C. Proceedings of the National Academy of Sciences, Vol. 102, Issue 37 https://doi.org/10.1073/pnas.0502782102	journal	September 2005
Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: activation of the vertebrate homologue of the drosophila seven in absentia gene. Amson, R. B.; Nemani, M.; Roperch, J. P. Proceedings of the National Academy of Sciences, Vol. 93, Issue 9 https://doi.org/10.1073/pnas.93.9.3953	journal	April 1996
Regulation of Synaptophysin Degradation by Mammalian Homologues of Seven in Absentia Wheeler, Tiffany C.; Chin, Lih-Shen; Li, Yankun Journal of Biological Chemistry, Vol. 277, Issue 12 https://doi.org/10.1074/jbc.M107857200	journal	March 2002
USP13 Enzyme Regulates Siah2 Ligase Stability and Activity via Noncatalytic Ubiquitin-binding Domains* Scortegagna, Marzia; Subtil, Tony; Qi, Jianfei Journal of Biological Chemistry, Vol. 286, Issue 31 https://doi.org/10.1074/jbc.M111.218214	journal	August 2011
Ubiquitin-specific Protease 19 (USP19) Regulates Hypoxia-inducible Factor 1α (HIF-1α) during Hypoxia* Altun, Mikael; Zhao, Bin; Velasco, Kelly Journal of Biological Chemistry, Vol. 287, Issue 3 https://doi.org/10.1074/jbc.M111.305615	journal	January 2012
Seven in Absentia Homolog 2 (Siah2) Protein Is a Regulator of NF-E2-related Factor 2 (Nrf2)* Baba, Kazunobu; Morimoto, Haruka; Imaoka, Susumu Journal of Biological Chemistry, Vol. 288, Issue 25 https://doi.org/10.1074/jbc.M112.438762	journal	June 2013
Tight Control of Hypoxia-inducible Factor-α Transient Dynamics Is Essential for Cell Survival in Hypoxia Bagnall, James; Leedale, Joseph; Taylor, Sarah E. Journal of Biological Chemistry, Vol. 289, Issue 9 https://doi.org/10.1074/jbc.M113.500405	journal	February 2014
Role of Apoptosis Signal-regulating Kinase 1 (ASK1) as an Activator of the GAPDH-Siah1 Stress-Signaling Cascade Tristan, Carlos A.; Ramos, Adriana; Shahani, Neelam Journal of Biological Chemistry, Vol. 290, Issue 1 https://doi.org/10.1074/jbc.M114.596205	journal	January 2015
Structural Analysis of Siah1-Siah-interacting Protein Interactions and Insights into the Assembly of an E3 Ligase Multiprotein Complex Santelli, Eugenio; Leone, Marilisa; Li, Chenlong Journal of Biological Chemistry, Vol. 280, Issue 40 https://doi.org/10.1074/jbc.M506707200	journal	October 2005
Siah1 Interacts with the Scaffold Protein POSH to Promote JNK Activation and Apoptosis* Xu, Zhiheng; Sproul, Andrew; Wang, Wenyi Journal of Biological Chemistry, Vol. 281, Issue 1 https://doi.org/10.1074/jbc.M509060200	journal	January 2006
Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8) Avvakumov, George V.; Walker, John R.; Xue, Sheng Journal of Biological Chemistry, Vol. 281, Issue 49 https://doi.org/10.1074/jbc.M606704200	journal	October 2006
Up-regulation of Tumor Susceptibility Gene 101 Protein in Ovarian Carcinomas Revealed by Proteomics Analyses Young, Travis W.; Mei, Fang C.; Rosen, Daniel G. Molecular & Cellular Proteomics, Vol. 6, Issue 2 https://doi.org/10.1074/mcp.M600305-MCP200	journal	February 2007
SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status Adam, M. Gordian; Matt, Sonja; Christian, Sven Cell Cycle, Vol. 14, Issue 23 https://doi.org/10.1080/15384101.2015.1104441	journal	December 2015
MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling Liang, Jian; Saad, Yasser; Lei, Tianhua Journal of Experimental Medicine, Vol. 207, Issue 13 https://doi.org/10.1084/jem.20092641	journal	November 2010
Geneious Basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data Kearse, M.; Moir, R.; Wilson, A. Bioinformatics, Vol. 28, Issue 12 https://doi.org/10.1093/bioinformatics/bts199	journal	April 2012
Stress-induced decrease in TRAF2 stability is mediated by Siah2 Habelhah, H. The EMBO Journal, Vol. 21, Issue 21 https://doi.org/10.1093/emboj/cdf576	journal	November 2002
Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways Pérez, Moisés; García-Limones, Carmen; Zapico, Inés Journal of Molecular Cell Biology, Vol. 4, Issue 5 https://doi.org/10.1093/jmcb/mjs047	journal	August 2012
Effect of Disrupting Seven-in-Absentia Homolog 2 Function on Lung Cancer Cell Growth Ahmed, Atique U.; Schmidt, Rebecca L.; Park, Cheol Hong JNCI: Journal of the National Cancer Institute, Vol. 100, Issue 22 https://doi.org/10.1093/jnci/djn365	journal	November 2008
Structural classification of zinc fingers: SURVEY AND SUMMARY Krishna, S. S. Nucleic Acids Research, Vol. 31, Issue 2 https://doi.org/10.1093/nar/gkg161	journal	January 2003
SWISS-MODEL: an automated protein homology-modeling server Schwede, T. Nucleic Acids Research, Vol. 31, Issue 13 https://doi.org/10.1093/nar/gkg520	journal	July 2003
MUSCLE: multiple sequence alignment with high accuracy and high throughput Edgar, R. C. Nucleic Acids Research, Vol. 32, Issue 5, p. 1792-1797 https://doi.org/10.1093/nar/gkh340	journal	March 2004
RAPIDO: a web server for the alignment of protein structures in the presence of conformational changes Mosca, R.; Schneider, T. R. Nucleic Acids Research, Vol. 36, Issue Web Server https://doi.org/10.1093/nar/gkn197	journal	May 2008
UniProt: a hub for protein information Consortium, UniPot Nucleic Acids Research, Vol. 43, Issue D1, p. D204-D212 https://doi.org/10.1093/nar/gku989	journal	October 2014
Multiple Comparisons of Log-Likelihoods with Applications to Phylogenetic Inference Shimodaira, H.; Hasegawa, M. Molecular Biology and Evolution, Vol. 16, Issue 8 https://doi.org/10.1093/oxfordjournals.molbev.a026201	journal	August 1999
An analysis of protein domain linkers: their classification and role in protein folding George, Richard A.; Heringa, Jaap Protein Engineering, Design and Selection, Vol. 15, Issue 11 https://doi.org/10.1093/protein/15.11.871	journal	November 2002
Mechanism for ubiquitylation of the leukemia fusion proteins AML1‐ETO and PML‐RARα Krämer, Oliver H.; Müller, Sylvia; Buchwald, Marc The FASEB Journal, Vol. 22, Issue 5 https://doi.org/10.1096/fj.06-8050com	journal	December 2007
Overexpression of Siah2 Is Associated With Poor Prognosis in Patients With Epithelial Ovarian Carcinoma Gao, Ya; Liu, Yunduo; Meng, Fanling International Journal of Gynecologic Cancer, Vol. 26, Issue 1 https://doi.org/10.1097/IGC.0000000000000574	journal	January 2016
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
Coot model-building tools for molecular graphics Emsley, Paul; Cowtan, Kevin Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 12, p. 2126-2132 https://doi.org/10.1107/S0907444904019158	journal	November 2004
HKL -3000: the integration of data reduction and structure solution – from diffraction images to an initial model in minutes Minor, Wladek; Cymborowski, Marcin; Otwinowski, Zbyszek Acta Crystallographica Section D Biological Crystallography, Vol. 62, Issue 8 https://doi.org/10.1107/S0907444906019949	journal	July 2006
MolProbity : all-atom structure validation for macromolecular crystallography Chen, Vincent B.; Arendall, W. Bryan; Headd, Jeffrey J. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 1 https://doi.org/10.1107/S0907444909042073	journal	December 2009
Refinement of Macromolecular Structures by the Maximum-Likelihood Method Murshudov, G. N.; Vagin, A. A.; Dodson, E. J. Acta Crystallographica Section D Biological Crystallography, Vol. 53, Issue 3 https://doi.org/10.1107/S0907444996012255	journal	May 1997
Two high-resolution structures of the human E3 ubiquitin ligase Siah1 Rimsa, Vadim; Eadsforth, Thomas C.; Hunter, William N. Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 69, Issue 12 https://doi.org/10.1107/S1744309113031448	journal	November 2013
GRAIL: a unique mediator of CD4 T-lymphocyte unresponsiveness: GRAIL maintains CD4 T cell unresponsiveness Whiting, Chan C.; Su, Leon L.; Lin, Jack T. FEBS Journal, Vol. 278, Issue 1 https://doi.org/10.1111/j.1742-4658.2010.07922.x	journal	November 2010
Inhibition of Siah2 ubiquitin ligase by vitamin K3 (menadione) attenuates hypoxia and MAPK signaling and blocks melanoma tumorigenesis Shah, Meera; Stebbins, John L.; Dewing, Antimone Pigment Cell & Melanoma Research, Vol. 22, Issue 6 https://doi.org/10.1111/j.1755-148X.2009.00628.x	journal	December 2009
TIN2 Stability Is Regulated by the E3 Ligase Siah2 Bhanot, M.; Smith, S. Molecular and Cellular Biology, Vol. 32, Issue 2 https://doi.org/10.1128/MCB.06227-11	journal	November 2011
Siah-1 N-Terminal RING Domain Is Required for Proteolysis Function, and C-Terminal Sequences Regulate Oligomerization and Binding to Target Proteins Hu, Gang; Fearon, Eric R. Molecular and Cellular Biology, Vol. 19, Issue 1 https://doi.org/10.1128/MCB.19.1.724	journal	January 1999
RING Domain E3 Ubiquitin Ligases Deshaies, Raymond J.; Joazeiro, Claudio A. P. Annual Review of Biochemistry, Vol. 78, Issue 1 https://doi.org/10.1146/annurev.biochem.78.101807.093809	journal	June 2009
Siah Proteins: Novel Drug Targets in the Ras and Hypoxia Pathways: Figure 1. House, Colin M.; Möller, Andreas; Bowtell, David D. L. Cancer Research, Vol. 69, Issue 23 https://doi.org/10.1158/0008-5472.CAN-09-1676	journal	November 2009
Vascular Normalization by Loss of Siah2 Results in Increased Chemotherapeutic Efficacy Wong, Christina S. F.; Sceneay, Jaclyn; House, Colin M. Cancer Research, Vol. 72, Issue 7 https://doi.org/10.1158/0008-5472.CAN-11-3310	journal	February 2012
Siah: A Promising Anticancer Target Wong, Christina S. F.; Möller, Andreas Cancer Research, Vol. 73, Issue 8 https://doi.org/10.1158/0008-5472.CAN-12-4348	journal	March 2013
The Ubiquitin Ligase Siah2 and the Hypoxia Response Nakayama, Koh; Qi, Jianfei; Ronai, Ze'ev Molecular Cancer Research, Vol. 7, Issue 4 https://doi.org/10.1158/1541-7786.MCR-08-0458	journal	April 2009
Screening for Ligands Using a Generic and High-Throughput Light-Scattering-Based Assay Senisterra, Guillermo A.; Markin, Eugene; Yamazaki, Ken Journal of Biomolecular Screening, Vol. 11, Issue 8 https://doi.org/10.1177/1087057106294699	journal	December 2006
NeEMO: a method using residue interaction networks to improve prediction of protein stability upon mutation Giollo, Manuel; Martin, Alberto JM; Walsh, Ian BMC Genomics, Vol. 15, Issue Suppl 4 https://doi.org/10.1186/1471-2164-15-S4-S7	journal	January 2014
The expression of the ubiquitin ligase SIAH2 (seven in absentia homolog 2) is mediated through gene copy number in breast cancer and is associated with a basal-like phenotype and p53 expression Chan, Peter; Möller, Andreas; Liu, Mira CP Breast Cancer Research, Vol. 13, Issue 1 https://doi.org/10.1186/bcr2828	journal	February 2011
DUBs at a glance Wilkinson, K. D. Journal of Cell Science, Vol. 122, Issue 14 https://doi.org/10.1242/jcs.041046	journal	July 2009
Fine Tuning of the UPR by the Ubiquitin Ligases Siah1/2 Scortegagna, Marzia; Kim, Hyungsoo; Li, Jian-Liang PLoS Genetics, Vol. 10, Issue 5 https://doi.org/10.1371/journal.pgen.1004348	journal	May 2014
Investigating the Molecular Basis of Siah1 and Siah2 E3 Ubiquitin Ligase Substrate Specificity Gopalsamy, Anupriya; Hagen, Thilo; Swaminathan, Kunchithapadam PLoS ONE, Vol. 9, Issue 9 https://doi.org/10.1371/journal.pone.0106547	journal	September 2014
USP 19 modulates autophagy and antiviral immune responses by deubiquitinating Beclin‐1 Jin, Shouheng; Tian, Shuo; Chen, Yamei The EMBO Journal, Vol. 35, Issue 8 https://doi.org/10.15252/embj.201593596	journal	March 2016
Enhanced Expression of EHMT2 Is Involved in the Proliferation of Cancer Cells through Negative Regulation of SIAH1 Cho, Hyun-Soo; Kelly, John D.; Hayami, Shinya Neoplasia, Vol. 13, Issue 8 https://doi.org/10.1593/neo.11512	journal	August 2011
The Siah2-HIF-FoxA2 axis in prostate cancer - new markers and therapeutic opportunities Qi, Jianfei; Pellecchia, Maurizio; Ronai, Ze’ev A. Oncotarget, Vol. 1, Issue 5 https://doi.org/10.18632/oncotarget.171	journal	September 2010
SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells Müller, Sylvia; Chen, Yuan; Ginter, Torsten Oncotarget, Vol. 5, Issue 10 https://doi.org/10.18632/oncotarget.1899	journal	April 2014
Siah: New Players in the Cellular Response to Hypoxia Nakayama, Koh; Ronai, Ze’ev Cell Cycle, Vol. 3, Issue 11 https://doi.org/10.4161/cc.3.11.1207	journal	November 2004

Similar Records

The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

Journal Article · Sun Jan 01 04:00:00 UTC 2017 · Biochimica et Biophysica Acta - General Subjects · OSTI ID:1373767

Zhang, Qi; Wang, Zhongduo; Hou, Feng; +5 more

STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1

Journal Article · Thu Jan 12 00:00:00 UTC 2017 · Structure · OSTI ID:1419805

Durzynska, Izabela; Xu, Xiang; Adelmant, Guillaume; +5 more

Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity

Journal Article · Tue Mar 24 04:00:00 UTC 2020 · Biochem. J. · OSTI ID:1606453

Singh, Sunil; Sivaraman, J.

Title: The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

Citation Formats

References (85)

Similar Records

Related Subjects