CHIP: a quality-control E3 ligase collaborating with molecular chaperones

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,304

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024

Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Schubert, U., Antón, L. C., Gibbs, J. S., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,567

Glutamine Repeats and Neurodegeneration

Zoghbi, H. Y., & Orr, H. T. (2000) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.23.1.217 · Cited by 1,314

Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones

Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,184

A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly

Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,074

Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

Wickner, S., Maurizi, M. R., & Gottesman, S. (1999) · Science · doi:10.1126/science.286.5446.1888 · Cited by 1,071

An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin

Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050

HDAC Inhibitor Modulation of Proteotoxicity as a Therapeutic Approach in Cancer

McConkey, D. J., White, M. C., & Yan, W. (2012) · Advances in cancer research · doi:10.1016/b978-0-12-394387-3.00004-5 · Cited by 35

FGFR3 biology and skeletal disease

Narayana, J., & Horton, W. A. (2015) · Connective Tissue Research · doi:10.3109/03008207.2015.1051224 · Cited by 36

Regulation of Proto-Oncogenic Dbl by Chaperone-Controlled, Ubiquitin-Mediated Degradation

Kamynina, E., Kauppinen, K. P., Duan, F., Muakkassa, N., & Manor, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01051-06 · Cited by 35

The co-chaperone CHIP is induced in various stresses and confers protection to cells

Dikshit, P., & Jana, N. R. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.018 · Cited by 34

Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic Fibrosis

Chanoux, R. A., & Rubenstein, R. C. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00137 · Cited by 40

Mode of Action of Heat Shock Protein (HSP) Inhibitors against Viruses through Host HSP and Virus Interactions

Wu, S., Zhao, Y., Wang, D., & Chen, Z. (2023) · Genes · doi:10.3390/genes14040792 · Cited by 33

CHIP interacts with heat shock factor 1 during heat stress

Kim, S., Yoon, J., Kim, D. K., Kim, S.-G., & Ahn, S. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.10.043 · Cited by 33

Metastatic Lymph Node CHIP Expression is a Potential Prognostic Marker for Resected Esophageal Squamous Cell Carcinoma Patients

Wen, J., Luo, K., Hu, Y., Yang, H., & Fu, J. (2013) · Annals of Surgical Oncology · doi:10.1245/s10434-012-2733-4 · Cited by 32

Molecular Chaperone HSP90 Is Necessary to Prevent Cellular Senescence via Lysosomal Degradation of p14ARF

Han, S. Y., Ko, A., Kitano, H., Choi, C. H., Lee, M.-S., Seo, J., Fukuoka, J., Kim, S., Hewitt, S. M., Chung, J., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0613 · Cited by 33

Heat Shock Proteins at the Crossroads between Cancer and Alzheimer’s Disease

Wang, H., Tan, M., Lu, R.-C., Yu, J., & Tan, L. (2014) · BioMed Research International · doi:10.1155/2014/239164 · Cited by 32

Nuclear Protein Quality Is Regulated by the Ubiquitin-Proteasome System through the Activity of Ubc4 and San1 in Fission Yeast

Matsuo, Y., Kishimoto, H., Tanae, K., Kitamura, K., Katayama, S., & Kawamukai, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.169953 · Cited by 29

The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation

Gao, X.-C., Zhou, C.-J., Zhou, Z., Wu, M., Cao, C., & Hu, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.294728 · Cited by 29

It Takes 15 to Tango: Making Sense of the Many Ubiquitin Ligases of p53

Love, I. M., & Grossman, S. R. (2012) · Genes & Cancer · doi:10.1177/1947601912455198 · Cited by 28

CHIP-dependent p53 regulation occurs specifically during cellular senescence

Sisoula, C., Trachana, V., Patterson, C., & Gonos, E. S. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.701 · Cited by 29

Potential roles of natural products in the targeting of proteinopathic neurodegenerative diseases

Dash, R., Jahan, I., Ali, M. C., Mitra, S., Munni, Y. A., Timalsina, B., Hannan, M. A., & Moon, I. S. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105011 · Cited by 28

Protein profile changes in the human breast cancer cell line MCF‐7 in response to SEL1L gene induction

Bianchi, L., Canton, C., Bini, L., Orlandi, R., Ménard, S., Armini, A., Cattaneo, M., PALLINI, V., Bernardi, L. R., & Biunno, I. (2005) · PROTEOMICS · doi:10.1002/pmic.200401283 · Cited by 28

Clinical and pathologic phenotype of a large family with heterozygous STUB1 mutation

Mol, M. O., van Rooij, J., Brusse, E., Verkerk, A. J. M. H., Melhem, S., den Dunnen, W. F. A., Rizzu, P., Cupidi, C., Swieten, J. C. V., & Kaat, L. D. (2020) · Neurology Genetics · doi:10.1212/nxg.0000000000000417 · Cited by 29

Direct Identification of Ubiquitination Sites on Ubiquitin-Conjugated CHIP Using MALDI Mass Spectrometry

Wang, D., Xu, W., McGrath, S. C., Patterson, C., Neckers, L., & Cotter, R. J. (2005) · Journal of Proteome Research · doi:10.1021/pr050104e · Cited by 26

Inefficient Quality Control of Thermosensitive Proteins on the Plasma Membrane

Lewis, M., & Pelham, H. R. B. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005038 · Cited by 25

Ligand-independent and agonist-mediated degradation of estrogen receptor-α in breast carcinoma cells: evidence for distinct degradative pathways

Nonclercq, D., Journé, F., Body, J., Leclercq, G., & Laurent, G. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.07.003 · Cited by 26

Hsp90 Cochaperone Aha1 Is a Negative Regulator of the Saccharomyces MAL Activator and Acts Early in the Chaperone Activation Pathway

Ran, F., Gadura, N., & Michels, C. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040600 · Cited by 24

The co‐chaperone p23 is degraded by caspases and the proteasome during apoptosis

Mollerup, J., & Berchtold, M. W. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.06.045 · Cited by 25

Dimer formation and conformational flexibility ensure cytoplasmic stability and nuclear accumulation of Elk-1

Evans, E. L., Saxton, J., Shelton, S. J., Begitt, A., Holliday, N. D., Hipskind, R. A., & Shaw, P. E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr266 · Cited by 24

E3 ligase CHIP and Hsc70 regulate Kv1.5 protein expression and function in mammalian cells

Li, P., Kurata, Y., Maharani, N., Mahati, E., Higaki, K., Hasegawa, A., Shirayoshi, Y., Yoshida, A., Kondo, T., Kurozawa, Y., et al. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.07.018 · Cited by 23

Heat shock proteins in antigen trafficking–Implications on antigen presentation to T cells

Udono, H., Ichiyanagi, T., Mizukami, S., & Imai, T. (2009) · International Journal of Hyperthermia · doi:10.3109/02656730902902183 · Cited by 23

CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome

Chakraborty, A., & Edkins, A. L. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_12 · Cited by 24

Phosphorylation of IRS4 by CK1γ2 promotes its degradation by CHIP through the ubiquitin/lysosome pathway

Li, X., Zhong, L., Wang, Z., Chen, H., Liao, D., Zhang, R., Zhang, H., & Kang, T. (2018) · Theranostics · doi:10.7150/thno.26021 · Cited by 22

The E3 ubiquitin ligase CHIP protects against sepsis-induced myocardial dysfunction by inhibiting NF-κB-mediated inflammation via promoting ubiquitination and degradation of karyopherin-α 2

Liao, J., Su, X., Wang, M., Jiang, L., Chen, X., Liu, Z., Tang, G., Zhou, L., Li, H., Lv, X., et al. (2022) · Translational research · doi:10.1016/j.trsl.2022.11.006 · Cited by 21

Characterization of the protein ubiquitination response induced by Doxorubicin

Mandili, G., Khadjavi, A., Gallo, V., Minero, V. G., Bessone, L., Carta, F., Giribaldi, G., & Turrini, F. M. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08602.x · Cited by 21

CHIP attenuates lipopolysaccharide‐induced cardiac hypertrophy and apoptosis by promoting NFATc3 proteasomal degradation

Chao, C., Lai, C., Badrealam, K. F., Lo, J., Shen, C.-Y., Chen, C., Chen, R., Viswanadha, V. P., Kuo, W., & Huang, C. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28614 · Cited by 21

Arctigenin promotes degradation of inducible nitric oxide synthase through CHIP-associated proteasome pathway and suppresses its enzyme activity

Yao, X., Li, G., Lü, C., Xu, H., & Yin, Z. (2012) · International Immunopharmacology · doi:10.1016/j.intimp.2012.06.017 · Cited by 20

Carboxyl terminus of heat-shock cognate 70-interacting protein degrades tau regardless its phosphorylation status without affecting the spatial memory of the rats

Zhang, Y.-J., Xu, Y., Liu, X., Li, D., Yin, J., Liu, Y.-H., Chen, X., & Wang, J. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-007-0857-7 · Cited by 20

Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis

Ferreira, J. V., Soares, A. R., Ramalho, J. S., Ribeiro‐Rodrigues, T., Carvalho, C. M., Zuzarte, M., Girão, H., & Pereira, P. (2019) · PLoS ONE · doi:10.1371/journal.pone.0223790 · Cited by 21

Differential expression of circulating miRNAs as a novel tool to assess BAG3-associated familial dilated cardiomyopathy

Zaragoza, C., Saura, M., Hernández, I., Ramírez-Carracedo, R., Garcia‐García, F., Zamorano, J. L., Mangas, A., & Toro, R. (2019) · Bioscience Reports · doi:10.1042/bsr20180934 · Cited by 19

CHIP E3 ligase regulates mammalian senescence by modulating the levels of oxidized proteins

Sisoula, C., & Gonos, E. S. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.04.003 · Cited by 18

Carboxy-terminus Hsc70 interacting protein exerts a tumor inhibition function in head and neck cancer

Xiao, M., Yan, M., Zhang, J., Xu, Q., & Chen, W. (2017) · Oncology Reports · doi:10.3892/or.2017.5827 · Cited by 18

Regulation of FSP27 protein stability by AMPK and HSC70

Zhang, X., Heckmann, B. L., Xie, X., Saarinen, A. M., & Liu, J. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00125.2014 · Cited by 18

Age-related modifications of egr1 expression and ubiquitin-proteasome components in pet dog hippocampus

Ghi, P., Brisco, F. D., Dallorto, D., Osella, M. C., & Orsetti, M. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.01.007 · Cited by 18

Modeling sporadic Parkinson's disease by silencing the ubiquitin E3 ligase component, SKP1A

Mandel, S. A., Fishman-Jacob, T., & Youdim, M. B. H. (2009) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(09)70803-x · Cited by 18

Proteome oxidative carbonylation during oxidative stress-induced premature senescence of WI-38 human fibroblasts

Boulch, M. L., Ahmed, E. K., Rogowska-Wrzesińska, A., Baraibar, M. A., & Friguet, B. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.07.005 · Cited by 18

Expression of the Orphan Cytosolic Sulfotransferase SULT4A1 and Its Major Splice Variant in Human Tissues and Cells: Dimerization, Degradation and Polyubiquitination

Sidharthan, N. P., Butcher, N. J., Mitchell, D. J., & Minchin, R. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101520 · Cited by 17

UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP

Teng, Y., Rezvani, K. S., & Biasi, M. D. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.08.084 · Cited by 18

Covalent Modifications of RUNX Proteins: Structure Affects Function

Blumenthal, E., Greenblatt, S., Huang, G., Ando, K., Xu, Y., & Nimer, S. D. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-10-3233-2_3 · Cited by 16

The E3 Ligases in Cervical Cancer and Endometrial Cancer

Zhai, F., Wang, J., Yang, W., Ye, M., & Jin, X. (2022) · Cancers · doi:10.3390/cancers14215354 · Cited by 16

Toll-Like Receptor-2 Ligand Peptidoglycan Upregulates Expression and Ubiquitin Ligase Activity of CHIP through JNK Pathway

Meng, Y., Chen, C., Wang, L., Wang, X., Tian, C., Du, J., & Li, H. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000354509 · Cited by 16

The Evolutionarily Conserved E3 Ubiquitin Ligase AtCHIP Contributes to Plant Immunity

Copeland, C., Ao, K., Huang, Y., Tong, M., & Li, X. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00309 · Cited by 16

Heat shock protein magic in antigen trafficking within dendritic cells: implications in antigen cross-presentation in immunity.

Udono, H. (2012) · PubMed · doi:10.18926/amo/48075 · Cited by 15

Hsp90 inhibition renders iNOS aggregation and the clearance of iNOS aggregates by proteasomes requires SPSB2

Wang, T., Luo, S., Qin, H., & Xia, Y. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.021 · Cited by 15

Protein Ubiquitination: CHIPping Away the Symmetry

Schulman, B. A., & Chen, Z. J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.11.019 · Cited by 16

Quality control pathways of tail-anchored proteins

Jiang, H. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118922 · Cited by 16

Pairs of Vp1 Cysteine Residues Essential for Simian Virus 40 Infection

Li, P. P., Nakanishi, A., Fontanes, V., & Kasamatsu, H. (2005) · Journal of Virology · doi:10.1128/jvi.79.6.3859-3864.2005 · Cited by 14

Nkx3.2 induces oxygen concentration-independent and lysosome-dependent degradation of HIF-1α to modulate hypoxic responses in chondrocytes

Im, S., & Kim, D. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.05.001 · Cited by 15

Tumorous imaginal disc 1 (TID1) inhibits isoproterenol-induced cardiac hypertrophy and apoptosis by regulating c-terminus of hsc70-interacting protein (CHIP) mediated degradation of Gαs

Feng, C.-C., Liao, P., Tsai, H.-I., Cheng, S., Yang, L., PadmaViswanadha, V., Pan, L.-F., Chen, R., Lo, J., & Huang, C. (2018) · International Journal of Medical Sciences · doi:10.7150/ijms.24296 · Cited by 14

Cytoplasmic expression of c-erbB2 in non-small cell lung cancers

Cheng, C., Tsuneyama, K., Matsui, K., Takahashi, H., Ishizawa, S., & Takano, Y. (2005) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-005-1258-7 · Cited by 14

CHIP-overexpressing Wharton's jelly-derived mesenchymal stem cells attenuate hyperglycemia-induced oxidative stress-mediated kidney injuries in diabetic rats

Ali, A., Shibu, M. A., Kuo, C., Lo, J., Chen, R., Day, C. H., Ho, T., PadmaViswanadha, V., Kuo, W., & Huang, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.026 · Cited by 13

Monte Carlo cross-validation analysis screens pathway cross-talk associated with Parkinson’s disease

Li, T., Tang, W., & Zhang, L. (2016) · Neurological Sciences · doi:10.1007/s10072-016-2595-9 · Cited by 13

Putting human Tid-1 in context: an insight into its role in the cell and in different disease states

Banerjee, S., Chaturvedi, R., Singh, A. T., & Kushwaha, H. R. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00912-5 · Cited by 13

Chaperone-E3 Ligase Complex HSP70-CHIP Mediates Ubiquitination of Ribosomal Protein S3

Hwang, I., Cho, S., & Ahn, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092723 · Cited by 12

Perspectives on the Development of First-in-Class Protein Degraders

Rambacher, K. M., Calabrese, M. F., & Yamaguchi, M. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0033 · Cited by 11

Exploiting the potential of the ubiquitin-proteasome system in overcoming tyrosine kinase inhibitor resistance in chronic myeloid leukemia

Li, X., Li, W., Zhang, Y., Xu, L., & Song, Y. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.101150 · Cited by 11

Mutant γPKC that causes spinocerebellar ataxia type 14 upregulates Hsp70, which protects cells from the mutant’s cytotoxicity

Ogawa, K., Seki, T., Onji, T., Adachi, N., Tanaka, S., Hide, I., Saito, N., & Sakai, N. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.013 · Cited by 10

Structural Insights into Functional Modes of Proteins Involved in Ubiquitin Family Pathways

Hänzelmann, P., Schäfer, A., Völler, D., & Schindelin, H. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_39 · Cited by 10

Ubiquitin/Proteasome System in Plant Pathogen Responses

Sorel, M., Mooney, B., de Marchi, R., & Graciet, E. (2019) · Annual Plant Reviews online · doi:10.1002/9781119312994.apr0665 · Cited by 10

Natural Products Targeting Hsp90 for a Concurrent Strategy in Glioblastoma and Neurodegeneration

Mitra, S., Dash, R., Munni, Y. A., Selsi, N. J., Akter, N., Uddin, M. N., Mazumder, K., & Moon, I. S. (2022) · Metabolites · doi:10.3390/metabo12111153 · Cited by 9

CHIP inhibits odontoblast differentiation through promoting DLX3 polyubiquitylation and degradation

Zheng, H., Zhang, X., Fu, J., Xue, Y., Chen, Z., Yang, G., Chen, Y., Chen, D., & Yuan, G. (2023) · Development · doi:10.1242/dev.200848 · Cited by 9

CHIP mutations affect the heat shock response differently in human fibroblasts and iPSC-derived neurons

Schuster, S., Heuten, E., Velić, A., Admard, J., Synofzik, M., Ossowski, S., Maček, B., Hauser, S., & Schöls, L. J. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.045096 · Cited by 9

Molecular determinants of the response of cancer cells towards geldanamycin and its derivatives

Seo, E., Khelifi, D., Fayez, S., Feineis, D., Bringmann, G., Efferth, T., & Dawood, M. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110677 · Cited by 8

Cyclin-dependent kinase 5-mediated phosphorylation of CHIP promotes the tAIF-dependent death pathway in rotenone-treated cortical neurons

Kim, C., Lee, J., Ko, Y. U., & Oh, Y. J. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.10.053 · Cited by 8

A Global View of the Proteome Perturbations by Hsp90 Inhibitors

Echeverría, P. C., & Picard, D. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_6 · Cited by 8

Enhancement of Ubiquitin Conjugation Activity Reduces Intracellular Aggregation of V76D Mutant γD-Crystallin

Liu, Z., Taylor, A., Liu, Y., Wu, M., Gong, X., & Shang, F. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-9744 · Cited by 8

A sporadic Parkinson’s disease model via silencing of the ubiquitin–proteasome/E3 ligase component, SKP1A

Fishman-Jacob, T., & Youdim, M. B. H. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02687-6 · Cited by 7

E3 Ubiquitin Ligase CHIP Inhibits Haemocyte Proliferation and Differentiation via the Ubiquitination of Runx in the Pacific Oyster

Dong, M., Song, Y., Wang, W., Song, X., Wu, W., Wang, L., & Song, L. (2024) · Cells · doi:10.3390/cells13181535 · Cited by 7

Subunits of an E3 Ligase Complex as Degrons for Efficient Degradation of Cytosolic, Nuclear, and Membrane Proteins

Verbič, A., Lebar, T., Praznik, A., & Jerala, R. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00588 · Cited by 6

Lafora Progressive Myoclonus Epilepsy: Recent Insights into Cell Degeneration

Spuch, C., Ortolano, S., & Navarro, C. (2012) · Recent Patents on Endocrine Metabolic & Immune Drug Discovery · doi:10.2174/187221412800604617 · Cited by 6

A Novel Heat Shock Element (HSE) in Entamoeba histolytica that Regulates the Transcriptional Activation of the EhPgp5 Gene in the Presence of Emetine Drug

Nieto, A., Pérez-Ishiwara, D. G., Orozco, E., Monroy, V. S., & Gómez-García, M. D. C. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00492 · Cited by 6

LRSAM1 E3 ubiquitin ligase promotes proteasomal clearance of E6-AP protein

Mishra, R., Joshi, V., Upadhyay, A., Amanullah, A., Dubey, A. R., Singh, S., Dubey, V. K., Poluri, K. M., Jana, N. R., & Mishra, A. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109836 · Cited by 6

Ubiquitin-Dependent Protein Degradation

Hegde, A. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.02826-2 · Cited by 7

Physiological and molecular response of soybean to combined drought and heat stresses during flowering

Xia, C., Huang, Z., Lu, B., Geng, Z., Wang, S., & Xu, C. (2026) · BMC Plant Biology · doi:10.1186/s12870-025-08081-6 · Cited by 5

Molecular mechanism of the carboxyl terminus of Hsc70-interacting protein in TAU hyperphosphorylation induced by AlCl3 in N2a cells

Lu, X., Pan, B.-L., Gao, D., Ju, X. F., 宦佳平, Han, X., Lu, X., & Wang, L. (2023) · Toxicology · doi:10.1016/j.tox.2023.153610 · Cited by 6

Degradation of caspase-activated DNase by the ubiquitin–proteasome system

Tsuruta, T., Oh‐hashi, K., Kiuchi, K., & Hirata, Y. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.003 · Cited by 5

Regulation of HSF Activation and Repression

Takaki, E., & Nakai, A. (2016) · Springer eBooks · doi:10.1007/978-4-431-55852-1_3 · Cited by 4

Protein Aggregation and Multiple Organelle Damage After Brain Ischemia

Liu, C. H., Zhang, F., Krisrian, T., Polster, B. M., Fiskum, G. M., & Hu, B. R. (2012) · Springer eBooks · doi:10.1007/978-1-4419-9530-8_5 · Cited by 4

Ubiquitin-Dependent Protein Degradation

Hegde, A. N. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00697-3 · Cited by 4

Cytochrome P450 Degradation and Its Clinical Relevance

Liao, M., Kang, P., Murray, B. P., & Correia, M. A. (2009) · Wiley eBooks · doi:10.1002/9780470538951.ch11 · Cited by 4

Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H

Shankar, S., Liu, Y., Tulsian, N. K., Low, B. C., Lin, Q., & Sivaraman, J. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae536 · Cited by 3

Structural Characterization of Heat Shock Protein 90β and Molecular Interactions with Geldanamycin and Ritonavir: A Computational Study

Lima, C. R., Antunes, D., Caffarena, E. R., & Carels, N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168782 · Cited by 3

Cotranslational Protein Folding and Aggregation After Brain Ischemia

Hu, B. R. (2006) · Springer eBooks · doi:10.1007/978-0-387-30383-3_7 · Cited by 3

Heat Shock Proteins as Therapeutic Targets in Amyotrophic Lateral Sclerosis

Kalmár, B., & Greensmith, L. (2008) · Springer eBooks · doi:10.1007/978-1-4020-8231-3_4 · Cited by 3

17-AAG promotes the degradation of HSP90 client METTL3 to suppress MYC RNA m6A modification and expression in colorectal cancer

Meng, H., Jalal, M., Wang, H., Wang, Y., Feng, Y., Zheng, P., Liu, X., & Huang, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149421 · Cited by 2

E3 ubiquitin ligases in nasopharyngeal carcinoma and implications for therapies

Zhou, Z., Zheng, K., Zhou, S., Yang, Y., Chen, J., & Jin, X. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02376-7 · Cited by 3

Less Is More: How Protein Degradation Regulates Muscle Development

Hoppe, T. (2008) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2008_101 · Cited by 2

Chaperone Suppression of Aggregated Protein Toxicity

Wacker, J. L., & Muchowski, P. J. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_8 · Cited by 2

Up and Down Regulation of the Stress Response by the Co-Chaperone Ubiquitin Ligase CHIP

Qian, S., & Patterson, C. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_13 · Cited by 2

Chaperone-directed ubiquitylation maintains proteostasis at the expense of longevity

Pokrzywa, W., Lorenz, R., & Hoppe, T. (2017) · Worm · doi:10.1080/21624054.2017.1371403 · Cited by 2

The Ubiquitin Ligase CHIP Accelerates Papillary Thyroid Carcinoma Metastasis via the Transgelin–Matrix Metalloproteinase-9 Axis

Zhan, S., Yang, Y., Deng, S., Liu, X., Cui, L., & Wang, T. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00726 · Cited by 1

Ubiquitin Ligases and Cancer

Burger, A. M., & Seth, A. K. (2009) · Springer eBooks · doi:10.1007/978-0-387-69147-3_1 · Cited by 1

Defining the role of HSP90 in the stability of FGFR3 and as a drug target for the treatment of skeletal diseases and cancer

Laederich, M. B. (2011) · doi:10.6083/m4rf5s10 · Cited by 1

7 Putting genetics into optogenetics: knocking out proteins with light

LaBella, M. L., Sigrist, S. J., & Jørgensen, E. M. (2013) · De Gruyter eBooks · doi:10.1515/9783110270723.79 · Cited by 1

Mammalian HSP40/DnaJ Chaperone Proteins in Cytosol

Terada, K., & Mori, M. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_11 · Cited by 1

The Ubiquitin Proteasome System and Muscle Development

Kim, J., & Hoppe, T. (2006) · doi:10.1002/9783527620227.ch2 · Cited by 1

Purification and Assay of the Chaperone‐Dependent Ubiquitin Ligase of the Carboxyl Terminus of Hsc70‐Interacting Protein

Murata, S., Minami, M., & Minami, Y. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)98022-1 · Cited by 8

CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein

Murata, S., Minami, Y., Minami, M., Chiba, T., & Tanaka, K. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve246 · Cited by 574

CHIP: a link between the chaperone and proteasome systems

McDonough, H., & Patterson, C. (2003) · BioOne Complete (BioOne) · doi:10.1379/1466-1268(2003)008<0303:calbtc>2.0.co;2 · Cited by 5

A CHIPotle in physiology and disease

Paul, I., & Ghosh, M. K. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.10.027 · Cited by 45

Endoplasmic Reticulum Protein Quality Control Is Determined by Cooperative Interactions between Hsp/c70 Protein and the CHIP E3 Ligase

Matsumura, Y., Sakai, J., & Skach, W. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479345 · Cited by 69