The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation

The membrane-cytoskeleton linker ezrin is necessary for osteosarcoma metastasis

Khanna, C., Wan, X., Bose, S., Cassaday, R., Olomu, O., Mendoza, A., Yeung, C., Gorlick, R., Hewitt, S. M., & Helman, L. J. (2004) · Nature Medicine · doi:10.1038/nm982 · Cited by 705 · see citing works

Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein.

Baek, S. H., Ohgi, K., Rose, D., Koo, E., Glass, C., & Rosenfeld, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00809-7 · Cited by 591 · see citing works

The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum

Fang, S., Ferrone, M. L., Yang, C., Jensen, J. P., Tiwari, S., & Weissman, A. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251401598 · Cited by 413 · see citing works

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

Song, B., Sever, N., & DeBose‐Boyd, R. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.009 · Cited by 371 · see citing works

Transcriptional regulation of a metastasis suppressor gene by Tip60 and β-catenin complexes

Kim, J. H., Kim, B., Cai, L., Choi, H. J., Ohgi, K. A., Tran, C., Chen, C., Chung, C. H., Huber, O., Rose, D. W., et al. (2005) · Nature · doi:10.1038/nature03452 · Cited by 291 · see citing works

Interaction of KAI1 on tumor cells with DARC on vascular endothelium leads to metastasis suppression

Bandyopadhyay, S., Zhan, R., Chaudhuri, A., Watabe, M., Pai, S. K., Hirota, S., Hosobe, S., Tsukada, T., Miura, K., Takano, Y., et al. (2006) · Nature Medicine · doi:10.1038/nm1444 · Cited by 237 · see citing works

The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

Chen, B., Mariano, J. M., Tsai, Y. C., Chan, A. H., Cohen, M. M., & Weissman, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506618103 · Cited by 213 · see citing works

AAA ATPase p97/Valosin-containing Protein Interacts with gp78, a Ubiquitin Ligase for Endoplasmic Reticulum-associated Degradation

Zhong, X., Shen, Y., Ballar, P., Apostolou, A., Agami, R., & Fang, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409034200 · Cited by 209 · see citing works

Metastasis Suppression: The Evolving Role of Metastasis Suppressor Genes for Regulating Cancer Cell Growth at the Secondary Site

KAUFFMAN, E. C., ROBINSON, V. L., Stadler, W. M., Sokoloff, M. H., & Rinker-Schaeffer, C. W. (2003) · The Journal of Urology · doi:10.1097/01.ju.0000051580.89109.4b · Cited by 183 · see citing works

Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor

Watanabe, H., Carmi, P., Hogan, V. A., Raz, T., Silletti, S., Nabi, I. R., & Raz, A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98859-9 · Cited by 178 · see citing works

Sterol-regulated Degradation of Insig-1 Mediated by the Membrane-bound Ubiquitin Ligase gp78

Lee, J. N., Song, B., DeBose‐Boyd, R. A., & Ye, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608999200 · Cited by 170 · see citing works

The Tetraspan Protein CD82 Is a Resident of MHC Class II Compartments Where It Associates with HLA-DR, -DM, and -DO Molecules

Hammond, C., Denzin, L. K., Pan, M., Griffith, J. M., Geuze, H. J., & Cresswell, P. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.7.3282 · Cited by 165 · see citing works

Roles of sumoylation of a reptin chromatin-remodelling complex in cancer metastasis

Kim, J. H., Choi, H. J., Kim, B., Kim, M. H., Lee, J. M., Kim, I. S., Lee, M. H., Choi, S. J., Kim, K. I., Kim, S., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1415 · Cited by 148 · see citing works

Motility inhibition and apoptosis are induced by metastasis-suppressing gene product CD82 and its analogue CD9, with concurrent glycosylation.

Ono, M., Handa, K., Withers, D. A., & Hakomori, S. (1999) · PubMed · Cited by 141 · see citing works

Identification of B16-F1 melanoma autocrine motility-like factor receptor.

Nabi, I. R., Watanabe, H., & Raz, A. (1990) · PubMed · Cited by 134 · see citing works

Expression of the cytoskeleton linker protein ezrin in human cancers

Bruce, B. G., Khanna, G., Ren, L., Landberg, G., Jirström, K., Powell, C. A., Borczuk, A., Keller, E. T., Wojno, K. J., Meltzer, P. S., et al. (2007) · Clinical & Experimental Metastasis · doi:10.1007/s10585-006-9050-x · Cited by 133 · see citing works

Tetraspanin CD82 regulates compartmentalisation and ligand-induced dimerization of EGFR

Odintsova, E., Voortman, J., Gilbert, E., & Berditchevski, F. (2003) · Journal of Cell Science · doi:10.1242/jcs.00793 · Cited by 132 · see citing works

Overexpression of the Tumor Autocrine Motility Factor Receptor Gp78, a Ubiquitin Protein Ligase, Results in Increased Ubiquitinylation and Decreased Secretion of Apolipoprotein B100 in HepG2 Cells

Liang, J.-S., Kim, T. K., Fang, S., Yamaguchi, J., Weissman, A. M., Fisher, E. A. A., & Ginsberg, H. N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302683200 · Cited by 128 · see citing works

The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein1

Shimizu, K., Tani, M., Watanabe, H., Nagamachi, Y., Niinaka, Y., Shiroishi, T., Ohwada, S., Raz, A., & Yokota, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00966-7 · Cited by 119 · see citing works

CD82 metastasis suppressor gene: a potential target for new therapeutics?

Tonoli, H., & Barrett, J. C. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.10.002 · Cited by 104 · see citing works

Loss of Expression and Altered Localization of KAI1 and CD9 Protein Are Associated with Epithelial Ovarian Cancer Progression

Houle, C. D., Ding, X., Foley, J. F., Afshari, C. A., Barrett, J. C., & Davis, B. J. (2002) · Gynecologic Oncology · doi:10.1006/gyno.2002.6729 · Cited by 82 · see citing works

KAI1 promoter activity is dependent on p53, junB and AP2: evidence for a possible mechanism underlying loss of KAI1 expression in cancer cells

Marreiros, A., Dudgeon, K., Dao, V. A., Grimm, M., Czolij, R., Crossley, M., & Jackson, P. (2004) · Oncogene · doi:10.1038/sj.onc.1208216 · Cited by 73 · see citing works

Regulation of Urokinase Receptor Proteolytic Function by the Tetraspanin CD82

Bass, R., Werner, F., Odintsova, E., Sugiura, T., Berditchevski, F., & Ellis, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414189200 · Cited by 66 · see citing works

Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of α-1-antitrypsin

Shen, Y., Ballar, P., & Fang, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.173 · Cited by 60 · see citing works

Metastasis suppressor genes: From gene identification to protein function and regulation

Berger, J. C., Griend, D. J. V., Robinson, V. L., Hickson, J. A., & Rinker-Schaeffer, C. W. (2005) · Cancer Biology & Therapy · doi:10.4161/cbt.4.8.1865 · Cited by 59 · see citing works

The metastasis suppressor gene C33/CD82/KAI1 induces apoptosis through reactive oxygen intermediates

Schoenfeld, N., Bauer, M. K. A., & Grimm, S. (2003) · The FASEB Journal · doi:10.1096/fj.03-0420fje · Cited by 45 · see citing works

Absence of p53-dependent induction of the metastatic suppressor KAI1 gene after DNA damage

Duriez, C., Falette, N., Cortes, U., Moyret‐Lalle, C., & Puisieux, A. (2000) · Oncogene · doi:10.1038/sj.onc.1203580 · Cited by 25 · see citing works

Tetraspanins: push and pull in suppressing and promoting metastasis

Zöller, M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2543 · Cited by 668 · see citing works

Osteosarcoma

Beird, H. C., Bielack, S. S., Flanagan, A. M., Gill, J., Heymann, D., Janeway, K. A., Livingston, J. A., Roberts, R. D., Strauss, S. J., & Gorlick, R. (2022) · Nature Reviews Disease Primers · doi:10.1038/s41572-022-00409-y · Cited by 660 · see citing works

HECT and RING finger families of E3 ubiquitin ligases at a glance

Metzger, M. B., Hristova, V. A., & Weissman, A. M. (2012) · Journal of Cell Science · doi:10.1242/jcs.091777 · Cited by 622 · see citing works

RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination

Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.026 · Cited by 608 · see citing works

Lateral organization of membrane proteins: tetraspanins spin their web

Charrin, S., Naour, F. L., Silvie, O., Milhiet, P., Boucheix, C., & Rubinstein, E. (2009) · Biochemical Journal · doi:10.1042/bj20082422 · Cited by 440 · see citing works

RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis

Lipkowitz, S., & Weissman, A. M. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3120 · Cited by 415 · see citing works

Tetraspanin proteins promote multiple cancer stages

Hemler, M. E. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3640 · Cited by 403 · see citing works

The E3 Ubiquitin Ligase AMFR and INSIG1 Bridge the Activation of TBK1 Kinase by Modifying the Adaptor STING

Wang, Q., Liu, X., Cui, Y., Tang, Y., Chen, W., Li, S., Yu, H., Pan, Y., & Wang, C. (2014) · Immunity · doi:10.1016/j.immuni.2014.11.011 · Cited by 363 · see citing works

The ubiquitylation machinery of the endoplasmic reticulum

Hirsch, C., Gauss, R., Horn, S. C., Neuber, O., & Sommer, T. (2009) · Nature · doi:10.1038/nature07962 · Cited by 351 · see citing works

Targeting of tetraspanin proteins — potential benefits and strategies

Hemler, M. E. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2659 · Cited by 345 · see citing works

Stress-Induced Phosphorylation and Proteasomal Degradation of Mitofusin 2 Facilitates Mitochondrial Fragmentation and Apoptosis

Leboucher, G. P., Tsai, Y. C., Yang, M., Shaw, K. C., Zhou, M., Veenstra, T. D., Glickman, M. H., & Weissman, A. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.041 · Cited by 334 · see citing works

The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation

Weissman, A. M., Shabek, N., & Ciechanover, A. J. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3173 · Cited by 318 · see citing works

Tetraspanins as Regulators of Protein Trafficking

Berditchevski, F., & Odintsova, E. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00515.x · Cited by 296 · see citing works

Ubiquitination: Friend and foe in cancer

Mansour, M. A. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.06.001 · Cited by 273 · see citing works

The Unfolded Protein Response, Degradation from the Endoplasmic Reticulum, and Cancer

Tsai, Y. C., & Weissman, A. M. (2010) · Genes & Cancer · doi:10.1177/1947601910383011 · Cited by 267 · see citing works

Ubiquitination and the Regulation of Membrane Proteins

Foot, N. J., Henshall, T. L., & Kumar, S. (2016) · Physiological Reviews · doi:10.1152/physrev.00012.2016 · Cited by 257 · see citing works

Osteosarcoma: Accelerating Progress Makes for a Hopeful Future

Saraf, A. J., Fenger, J. M., & Roberts, R. D. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00004 · Cited by 237 · see citing works

Differences in the Tumor Microenvironment between African-American and European-American Breast Cancer Patients

Martin, D. N., Boersma, B. J., Yi, M., Reimers, M., Howe, T. M., Yfantis, H. G., Tsai, Y. C., Williams, E. H., Lee, D. H., Stephens, R. M., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004531 · Cited by 221 · see citing works

Regulation of mitophagy by the Gp78 E3 ubiquitin ligase

Fu, M., St-Pierre, P., Shankar, J., Wang, P. T. C., Joshi, B., & Nabi, I. R. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-08-0607 · Cited by 204 · see citing works

Computational identification of hepatitis C virus associated microRNA-mRNA regulatory modules in human livers

Peng, X., Li, Y., Walters, K., Rosenzweig, E., Lederer, S., Aicher, L. D., Proll, S. C., & Katze, M. G. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-373 · Cited by 186 · see citing works

CD82/KAI1 Maintains the Dormancy of Long-Term Hematopoietic Stem Cells through Interaction with DARC-Expressing Macrophages

Hur, J., Choi, J.-I., Lee, H., Nham, P., Kim, T., Chae, C.-W., Yun, J.-Y., Kang, J.-A., Kang, J., Lee, S. E., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.01.013 · Cited by 177 · see citing works

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

Bernasconi, R., Galli, C., Calanca, V., Nakajima, T., & Molinari, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200910042 · Cited by 176 · see citing works

The importance of regulatory ubiquitination in cancer and metastasis

Gallo, L. H., Ko, J., & Donoghue, D. J. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1288326 · Cited by 171 · see citing works

Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets

Stipp, C. S. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001355 · Cited by 165 · see citing works

Allosteric Activation of E2-RING Finger-Mediated Ubiquitylation by a Structurally Defined Specific E2-Binding Region of gp78

Das, R., Mariano, J. M., Tsai, Y. C., Kalathur, R., Kostova, Z., Li, J., Tarasov, S. G., McFeeters, R. L., Altieri, A. S., Ji, X., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.010 · Cited by 160 · see citing works

The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation

Preston, G. M., & Brodsky, J. L. (2017) · Biochemical Journal · doi:10.1042/bcj20160582 · Cited by 138 · see citing works

Provocative questions in osteosarcoma basic and translational biology: A report from the Children's Oncology Group

Roberts, R. D., Lizardo, M. M., Reed, D. R., Hingorani, P., Glover, J., Allen‐Rhoades, W., Fan, T., Khanna, C., Sweet‐Cordero, E. A., Cash, T., et al. (2019) · Cancer · doi:10.1002/cncr.32351 · Cited by 127 · see citing works

Urban planning of the endoplasmic reticulum (ER): How diverse mechanisms segregate the many functions of the ER

Lynes, E. M., & Simmen, T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.011 · Cited by 126 · see citing works

The chemokine CCL1 triggers an AMFR-SPRY1 pathway that promotes differentiation of lung fibroblasts into myofibroblasts and drives pulmonary fibrosis

Liu, S., Liu, C., Lv, X., Cui, B., Yan, J., Li, Y., Li, K., Hua, F., Zhang, X., Yu, J., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.008 · Cited by 125 · see citing works

A genome-wide shRNA screen identifies GAS1 as a novel melanoma metastasis suppressor genePreprint

Gobeil, S., Zhu, X., Doillon, C. J., & Green, M. R. (2008) · Genes & Development · doi:10.1101/gad.1714608 · Cited by 122 · see citing works

Interactions among genes, tumor biology and the environment in cancer health disparities: examining the evidence on a national and global scale

Wallace, T. A., Martin, D., & Ambs, S. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr066 · Cited by 121 · see citing works

Distinct mechanisms controlling rough and smooth endoplasmic reticulum-mitochondria contacts

Wang, P. T. C., Garcin, P. O., Fu, M., Masoudi, M., St-Pierre, P., Panté, N., & Nabi, I. R. (2015) · Journal of Cell Science · doi:10.1242/jcs.171132 · Cited by 111 · see citing works

Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy

Liu, Y., & Ye, Y. (2011) · Cell Research · doi:10.1038/cr.2011.75 · Cited by 110 · see citing works

Controlling cell surface dynamics and signaling: How CD82/KAI1 suppresses metastasis

Miranti, C. K. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.08.023 · Cited by 100 · see citing works

Serine Residues in the Cytosolic Tail of the T-cell Antigen Receptor α-Chain Mediate Ubiquitination and Endoplasmic Reticulum-associated Degradation of the Unassembled Protein

Ishikura, S., Weissman, A. M., & Bonifacino, J. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.127936 · Cited by 97 · see citing works

Triggering of Toll-like receptor 4 on metastatic breast cancer cells promotes αvβ3-mediated adhesion and invasive migration

Liao, S., Zhou, Y., Yuan, Y., Li, D., Wu, F., Wang, Q., Zhu, J., Yan, B., Wei, J., Zhang, G., et al. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1844-0 · Cited by 93 · see citing works

Dissecting the diverse functions of the metastasis suppressor CD82/KAI1

Tsai, Y. C., & Weissman, A. M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.031 · Cited by 93 · see citing works

The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function

Nakamura, N. (2011) · Membranes · doi:10.3390/membranes1040354 · Cited by 92 · see citing works

Inhibition of the sterol regulatory element‐binding protein pathway suppresses hepatocellular carcinoma by repressing inflammation in mice

Li, N., Zhou, Z., Shen, Y., Xu, J., Miao, H., Xiong, Y., Xu, F., Li, B., Luo, J., & Song, B. (2016) · Hepatology · doi:10.1002/hep.29018 · Cited by 91 · see citing works

Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine

Das, R., Liang, Y., Mariano, J. M., Li, J., Huang, T., King, A., Tarasov, S. G., Weissman, A. M., Ji, X., & Byrd, R. A. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.174 · Cited by 90 · see citing works

Tetraspanins in human epithelial malignancies

Romańska, H., & Berditchevski, F. (2010) · The Journal of Pathology · doi:10.1002/path.2779 · Cited by 89 · see citing works

The complex biology of autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and its receptor, the gp78/AMFR E3 ubiquitin ligase

Fairbank, M., St-Pierre, P., & Nabi, I. R. (2009) · Molecular BioSystems · doi:10.1039/b820820b · Cited by 88 · see citing works

MiR-139-5p inhibits migration and invasion of colorectal cancer by downregulating AMFR and NOTCH1

Song, M., Yin, Y., Zhang, J., Zhang, B., Bian, Z., Quan, C., Zhou, L., Hu, Y., Wang, Q., Ni, S., et al. (2014) · Protein & Cell · doi:10.1007/s13238-014-0093-5 · Cited by 87 · see citing works

Melanoblast transcriptome analysis reveals pathways promoting melanoma metastasis

Marie, K. L., Sassano, A., Yang, H. H., Michalowski, A. M., Michael, H. T., Guo, T. W., Tsai, Y. C., Weissman, A. M., Lee, M. P., Jenkins, L. M. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14085-2 · Cited by 87 · see citing works

Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis

Hebert, D. N., & Molinari, M. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.005 · Cited by 84 · see citing works

Protein Quality Control in the Endoplasmic Reticulum and Cancer

Moon, H. W., Han, H. G., & Jeon, Y. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103020 · Cited by 83 · see citing works

Deacetylation of HSPA5 by HDAC6 leads to GP78-mediated HSPA5 ubiquitination at K447 and suppresses metastasis of breast cancer

Chang, Y.-W., Tseng, C.-F., Wang, M.-Y., Chang, W.-C., Lee, C.-C., Chen, L.-T., Hung, M.-C., & Su, J.-L. (2016) · Oncogene · doi:10.1038/onc.2015.214 · Cited by 82 · see citing works

Biological determinants of health disparities in prostate cancer

Martin, D. N., Starks, A. M., & Ambs, S. (2013) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32835eb5d1 · Cited by 78 · see citing works

Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system

Tsai, Y. C., Leichner, G. S., Pearce, M. M. P., Wilson, G. L., Wojcikiewicz, R. J. H., Roitelman, J., & Weissman, A. M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-08-0631 · Cited by 76 · see citing works

Unveiling the dark side of glucose-regulated protein 78 (GRP78) in cancers and other human pathology: a systematic review

Akinyemi, A. O., Simpson, K. E., Oyelere, S. F., Nur, M., Ngule, C. M., Owoyemi, B. C. D., Ayarick, V. A., Oyelami, F., Obaleye, O. E., Esoe, D.-P. I., et al. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00706-6 · Cited by 73 · see citing works

Ubiquitination of NLRP3 by gp78/Insig-1 restrains NLRP3 inflammasome activation

Xu, T., Yu, W., Fang, H., Wang, Z., Chi, Z., Guo, X., Jiang, D., Zhang, K., Chen, S., Li, M., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00947-8 · Cited by 72 · see citing works

Canalicular membrane MRP2/ABCC2 internalization is determined by Ezrin Thr567 phosphorylation in human obstructive cholestasis

Chai, J., Cai, S., Liu, X., Lian, W., Chen, S., Zhang, L., Feng, X., Cheng, Y., He, X., He, Y., et al. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.07.016 · Cited by 71 · see citing works

EGFR over-expression in non-small cell lung cancers harboring EGFR mutations is associated with marked down-regulation of CD82

Yang, C.-H., Chou, H.-C., Fu, Y.-N., Yeh, C.-L., Cheng, H.-W., Chang, I., Liu, K., Chang, G., Tsai, T., Tsai, S., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.020 · Cited by 67 · see citing works

Enhanced expression of SOS1 is detected in prostate cancer epithelial cells from African-American men

Dritschilo (2009) · International Journal of Oncology · doi:10.3892/ijo_00000388 · Cited by 67 · see citing works

gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum

Zhang, T., Xu, Y., Liu, Y., & Ye, Y. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-06-0354 · Cited by 66 · see citing works

Osteoblastic and Osteolytic Human Osteosarcomas can be Studied With a New Xenograft Mouse Model Producing Spontaneous Metastases

Yuan, J. J., Ossendorf, C., Szatkowski, J. P., Bronk, J. T., Maran, A., Yaszemski, M. J., Bolander, M. E., Sarkar, G., & Fuchs, B. (2009) · Cancer Investigation · doi:10.1080/07357900802491477 · Cited by 66 · see citing works

Functional Role of Cell Surface CUB Domain-Containing Protein 1 in Tumor Cell Dissemination

Deryugina, E. I., Conn, E. M., Wortmann, A., Partridge, J. J., Kupriyanova, T. A., Ardi, V. C., Hooper, J. D., & Quigley, J. P. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0100 · Cited by 63 · see citing works

Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3–SPOP E3 ubiquitin ligase complex

Kim, B., Nam, H. J., Pyo, K. E., Jang, M. J., Kim, I. S., Kim, D., Boo, K.-J., Lee, S., Yoon, J., Baek, S. H., et al. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.154 · Cited by 61 · see citing works

Different p97/VCP complexes function in retrotranslocation step of mammalian Er-associated degradation (ERAD)

Ballar, P., Pabuçcuoğlu, A., & Köse, F. A. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.12.021 · Cited by 61 · see citing works

Gp78 E3 Ubiquitin Ligase: Essential Functions and Contributions in Proteostasis

Joshi, V., Upadhyay, A., Kumar, A., & Mishra, A. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00259 · Cited by 61 · see citing works

MGAT3-mediated glycosylation of tetraspanin CD82 at asparagine 157 suppresses ovarian cancer metastasis by inhibiting the integrin signaling pathway

Li, J., Xu, J., Li, L., Ianni, A., Kumari, P., Liu, S., Sun, P., Braun, T. W., Tan, X., Xiang, R., et al. (2020) · Theranostics · doi:10.7150/thno.43865 · Cited by 60 · see citing works

Specificity and Regulation of the Endoplasmic Reticulum‐Associated Degradation Machinery

Merulla, J., Fasana, E., Soldà, T., & Molinari, M. (2013) · Traffic · doi:10.1111/tra.12068 · Cited by 59 · see citing works

Androgen Mediated Regulation of Endoplasmic Reticulum-Associated Degradation and its Effects on Prostate Cancer

Erzurumlu, Y., & Ballar, P. (2017) · Scientific Reports · doi:10.1038/srep40719 · Cited by 57 · see citing works

Viral and cellular MARCH ubiquitin ligases and cancer

Wang, X., Herr, R. A., & Hansen, T. H. (2008) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2008.09.002 · Cited by 56 · see citing works

Gp78, an E3 Ubiquitin Ligase Acts as a Gatekeeper Suppressing Nonalcoholic Steatohepatitis (NASH) and Liver Cancer

Zhang, T., Kho, D. H., Wang, Y., Harazono, Y., Nakajima, K., Xie, Y., & Raz, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118448 · Cited by 55 · see citing works

Autocrine motility factor receptor: a clinical review

Chiu, C. G., St-Pierre, P., Nabi, I. R., & Wiseman, S. M. (2008) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.8.2.207 · Cited by 55 · see citing works

Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: Cross-talk between E3s in the endoplasmic reticulum

Shmueli, A., Tsai, Y. C., Yang, M., Braun, M. A., & Weissman, A. M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.045 · Cited by 54 · see citing works

KAI-1/CD82, the molecule and clinical implication in cancer and cancer metastasis.

Malik, F. A., Sanders, A. J., & Jiang, W. G. (2009) · PubMed · doi:10.14670/hh-24.519 · Cited by 53 · see citing works

Dysregulation of Ezrin Phosphorylation Prevents Metastasis and Alters Cellular Metabolism in Osteosarcoma

Ren, L., Hong, S.-H., Chen, Q.-R., Briggs, J., Cassavaugh, J., Srinivasan, S., Lizardo, M. M., Mendoza, A., Xia, A. Y., Avadhani, N., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-0210 · Cited by 50 · see citing works

Roles of p97-Associated Deubiquitinases in Protein Quality Control at the Endoplasmic Reticulum

Liu, Y., & Ye, Y. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312802430608 · Cited by 50 · see citing works

Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration

Schaefer, A., Nethe, M., & Hordijk, P. L. (2012) · Biochemical Journal · doi:10.1042/bj20111815 · Cited by 50 · see citing works

The Endoplasmic Reticulum (ER)-associated Degradation System Regulates Aggregation and Degradation of Mutant Neuroserpin

Ying, Z., Wang, H., Fan, H., & Wang, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.200808 · Cited by 48 · see citing works

Role of HSPA1L as a cellular prion protein stabilizer in tumor progression via HIF-1α/GP78 axis

Lee, J. H., Han, Y.-S., Yoon, Y. M., Yun, C. W., Yun, S. P., Kim, S. M., Kwon, H. Y., Jeong, D., Baek, M. J., Lee, H., et al. (2017) · Oncogene · doi:10.1038/onc.2017.263 · Cited by 46 · see citing works

RNF-121 Is an Endoplasmic Reticulum-Membrane E3 Ubiquitin Ligase Involved in the Regulation of β-Integrin

Darom, A., Abu‐Shach, U. B., & Broday, L. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-09-0774 · Cited by 45 · see citing works

Tetraspanin CD82: a suppressor of solid tumors and a modulator of membrane heterogeneity

Feng, J., Huang, C., Wren, J. D., Wang, D. W., Yan, J., Zhang, J., Sun, Y., Han, X., & Zhang, X. A. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9585-x · Cited by 44 · see citing works

p38 MAP kinase–dependent phosphorylation of the Gp78 E3 ubiquitin ligase controls ER–mitochondria association and mitochondria motility

Li, L., Gao, G., Shankar, J., Joshi, B., Foster, L. J., & Nabi, I. R. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-02-0120 · Cited by 44 · see citing works

Fluorochrome-Labeled Inhibitors of Caspases: Convenient In Vitro and In Vivo Markers of Apoptotic Cells for Cytometric Analysis

Darżynkiewicz, Z., Pożarowski, P., Lee, B. W., & Johnson, G. L. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-409-8_9 · Cited by 44 · see citing works

The DSCs-Expressed CD82 Controls the Invasiveness of Trophoblast Cells via Integrinbeta1/MAPK/MAPK3/1 Signaling Pathway in Human First-Trimester Pregnancy1

Li, M., Hou, X.-F., Shao, J., Tang, C.-L., & Li, D. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.109.080739 · Cited by 41 · see citing works

A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation

Kostova, Z., Mariano, J. M., Scholz, S. L., Koenig, C., & Weissman, A. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.044255 · Cited by 41 · see citing works

Ganglioside GM2 mediates migration of tumor cells by interacting with integrin and modulating the downstream signaling pathway

Kundu, M., Mahata, B., Banerjee, A., Chakraborty, S., Debnath, S., Ray, S. S., Ghosh, Z., & Biswas, K. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.004 · Cited by 40 · see citing works

The metastasis suppressor CD82/KAI1 inhibits fibronectin adhesion-induced epithelial-to-mesenchymal transition in prostate cancer cells by repressing the associated integrin signaling

Lee, J., Byun, H.-J., Lee, M.-S., Jin, Y., Jeoung, D., Kim, Y., & Lee, H. (2016) · Oncotarget · doi:10.18632/oncotarget.13767 · Cited by 39 · see citing works

Fluorochrome-Labeled Inhibitors of Caspases: Expedient In Vitro and In Vivo Markers of Apoptotic Cells for Rapid Cytometric Analysis

Darżynkiewicz, Z., Zhao, H. L., Halicka, H. D., Pożarowski, P., & Lee, B. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7187-9_5 · Cited by 39 · see citing works

The Cellular Prion Protein: A Promising Therapeutic Target for Cancer

Go, G., & Lee, S. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239208 · Cited by 38 · see citing works

HMMR alleviates endoplasmic reticulum stress by promoting autophagolysosomal activity during endoplasmic reticulum stress‐driven hepatocellular carcinoma progression

He, L., Li, H., Li, C., Liu, Z., Lu, M., Zhang, R., Dong, W., Wei, D., Shao, J., Liu, M., et al. (2023) · 癌症：英文版 · doi:10.1002/cac2.12464 · Cited by 37 · see citing works

A Role for KAI1 in Promotion of Cell Proliferation and Mammary Gland Hyperplasia by the gp78 Ubiquitin Ligase

Joshi, B., Li, L., & Nabi, I. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.074344 · Cited by 37 · see citing works

Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity

Yoo, Y.-S., Han, H. G., & Jeon, Y. J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2969271 · Cited by 37 · see citing works

gp78: a Multifaceted Ubiquitin Ligase that Integrates a Unique Protein Degradation Pathway from the Endoplasmic Reticulum

Chen, Z., Du, S., & Fang, S. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312802430590 · Cited by 36 · see citing works

A VCP inhibitor substrate trapping approach (VISTA) enables proteomic profiling of endogenous ERAD substrates

Huang, E. Y., To, M., Tran, E., Dionisio, L. T. A., Cho, H. J., Baney, K. L. M., Pataki, C. I., & Olzmann, J. A. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-08-0514 · Cited by 36 · see citing works

KAI1/CD82 is a novel target of estrogen receptor‐mediated gene repression and downregulated in primary human breast cancer

Christgen, M., Bruchhardt, H., Ballmaier, M., Krech, T., Länger, F. P., Kreipe, H. H., & Lehmann, U. (2008) · International Journal of Cancer · doi:10.1002/ijc.23806 · Cited by 36 · see citing works

Liver Cytochrome P450 3A Ubiquitination in Vivo by gp78/Autocrine Motility Factor Receptor and C Terminus of Hsp70-interacting Protein (CHIP) E3 Ubiquitin Ligases

Kim, S., Acharya, P., Engel, J. C., & Correia, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167189 · Cited by 36 · see citing works

Calcium dependent regulation of protein ubiquitination – Interplay between E3 ligases and calcium binding proteins

Mukherjee, R., Das, A., Chakrabarti, S., & Chakrabarti, O. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.03.001 · Cited by 36 · see citing works

Basal Gp78-dependent mitophagy promotes mitochondrial health and limits mitochondrial ROS

Alan, P., Vandevoorde, K. R., Joshi, B., Cardoen, B., Gao, G., Mohammadzadeh, Y., Hamarneh, G., & Nabi, I. R. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04585-8 · Cited by 35 · see citing works

Protein Ubiquitination Research in Oncology

Faktor, J., Pjechová, M., Hernychová, L., & Vojtěšek, B. (2019) · Klinicka onkologie · doi:10.14735/amko20193s56 · Cited by 35 · see citing works

SYVN1, NEDD8, and FBXO2 Proteins Regulate ΔF508 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Ubiquitin-mediated Proteasomal Degradation

Ramachandran, S. S., Osterhaus, S. R., Parekh, K. R., Jacobi, A. M., Behlke, M. A., & McCray, P. B. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754283 · Cited by 32 · see citing works

Regulation of ER-associated degradation via p97/VCP-interacting motif

Ballar, P., & Fang, S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360818 · Cited by 32 · see citing works

The metastasis suppressor CD82/KAI1 represses the TGF‐β1 and Wnt signalings inducing epithelial‐to‐mesenchymal transition linked to invasiveness of prostate cancer cells

Lee, M., Lee, J., Kim, Y., & Lee, H. (2019) · The Prostate · doi:10.1002/pros.23837 · Cited by 32 · see citing works

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Liu, S., Chen, Y., Li, J., Huang, T., Tarasov, S. G., King, A., Weissman, A. M., Byrd, R. A., & Das, R. (2012) · Structure · doi:10.1016/j.str.2012.09.020 · Cited by 31 · see citing works

Silencing of ST6Gal I enhances colorectal cancer metastasis by down-regulating KAI1 via exosome-mediated exportation and thereby rescues integrin signaling

Jung, Y. R., Park, J.-J., Jin, Y. B., Cao, Y., Park, M. J., Kim, E. J., & Lee, M. (2016) · Carcinogenesis · doi:10.1093/carcin/bgw091 · Cited by 30 · see citing works

Tetraspanins: useful multifunction proteins for the possible design and development of small-molecule therapeutic tools

Robert, J.-M. H., Amoussou, N. G., Le, H., Logé, C., & Brouard, S. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.022 · Cited by 29 · see citing works

Abstract 990: Metastasis suppressor CD82/KAI1 expression is dependent on functional SWI/SNF ARID1A/B

Challa, R., Shoji, Y., Conrads, K. A., Hood, B. L., Wang, G., Darcy, K. M., Hamilton, C. A., Maxwell, G. L., Conrads, T. P., & Risinger, J. I. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-990 · Cited by 1 · see citing works

Upregulation of Glucose-Regulated Protein 78 in Metastatic Cancer Cells Is Necessary for Lung Metastasis Progression

Lizardo, M. M., Morrow, J. J., Miller, T. E., Hong, E. S., Ren, L., Mendoza, A., Halsey, C. H., Scacheri, P. C., Helman, L. J., & Khanna, C. (2016) · Neoplasia · doi:10.1016/j.neo.2016.09.001 · Cited by 50 · see citing works

Role of Metastasis Suppressor KAI1/CD82 in Different Cancers

Yan, W., Huang, J., Zhang, Q., & Zhang, J. (2021) · Journal of Oncology · doi:10.1155/2021/9924473 · Cited by 30 · see citing works

Interaction of KAI1 on tumor cells with DARC on vascular endothelium leads to metastasis suppression

Bandyopadhyay, S., Zhan, R., Chaudhuri, A., Watabe, M., Pai, S. K., Hirota, S., Hosobe, S., Tsukada, T., Miura, K., Takano, Y., et al. (2006) · Nature Medicine · doi:10.1038/nm1444 · Cited by 237 · see citing works

Frequent downregulation of the KAI1(CD82) metastasis suppressor protein in human cancer cell lines

White, A., Lamb, P. W., & Barrett, J. C. (1998) · Oncogene · doi:10.1038/sj.onc.1201852 · Cited by 82 · see citing works