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 · see citing works

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 · see citing works

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 4,216 · see citing works

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 · see citing works

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 1,536 · see citing works

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 1,311 · see citing works

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 1,170 · see citing works

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 · see citing works

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 1,056 · see citing works

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 · see citing works

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Connell, P. M., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., & Patterson, C. (2000) · Nature Cell Biology · doi:10.1038/35050618 · Cited by 1,002 · see citing works

Cellular Defenses against Unfolded Proteins

Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 984 · see citing works

Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions

Ballinger, C. A., Connell, P. M., Wu, Y., Hu, Z., Thompson, L. J., Yin, L.-Y., & Patterson, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4535 · Cited by 943 · see citing works

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., & Cyr, D. (2000) · Nature Cell Biology · doi:10.1038/35050509 · Cited by 839 · see citing works

Hsp90

Young, J. C., Moarefi, I., & Hartl, F. U. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104079 · Cited by 826 · see citing works

Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway

Isaacs, J. S., Jung, Y.-J., Mimnaugh, E. G., Martinez, A., Cuttitta, F., & Neckers, L. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204733200 · Cited by 663 · see citing works

Multiple Associated Proteins Regulate Proteasome Structure and Function

Leggett, D., Hanna, J. W., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R. T., Walz, T., Ploegh, H. L., & Finley, D. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00638-x · Cited by 631 · see citing works

Hsp90 & Co. – a holding for folding

Büchner, J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01373-0 · Cited by 625 · see citing works

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 · see citing works

The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome

Lüders, J., Demand, J., & Höhfeld, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4613 · Cited by 491 · see citing works

The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the Chaperone*

Marcu, M., Chadli, A., Bouhouche, I., Catelli, M., & Neckers, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003701200 · Cited by 481 · see citing works

CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase Activity

Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K. I., & Takahashi, R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00583-x · Cited by 473 · see citing works

Proteasome subunit Rpn1 binds ubiquitin-like protein domains

Elsasser, S., Gali, R. R., Schwickart, M., Larsen, C. N., Leggett, D., Mueller, B., Feng, M. T., Tübing, F., Dittmar, G. A. G., & Finley, D. J. (2002) · Nature Cell Biology · doi:10.1038/ncb845 · Cited by 468 · see citing works

Amyotrophic Lateral Sclerosis

Julien, J. (2001) · Cell · doi:10.1016/s0092-8674(01)00244-6 · Cited by 435 · see citing works

Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu

Xu, W., Marcu, M. G., Yuan, X., Mimnaugh, E. G., Patterson, C., & Neckers, L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202365899 · Cited by 433 · see citing works

The U box is a modified RING finger — a common domain in ubiquitination

Aravind, L., & Koonin, E. V. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00398-5 · Cited by 429 · see citing works

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

Demand, J., Alberti, S., Patterson, C., & Höhfeld, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00487-0 · Cited by 377 · see citing works

Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70

Bercovich, B., Stancovski, I., Mayer, A., Blumenfeld, N., Laszlo, A., Schwartz, A. L., & Ciechanover, A. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9002 · Cited by 298 · see citing works

Resistance to cadmium mediated by ubiquitin-dependent proteolysis

Jungmann, J., Reins, H., Schobert, C., & Jentsch, S. (1993) · Nature · doi:10.1038/361369a0 · Cited by 261 · see citing works

Ubiquitylation of BAG-1 Suggests a Novel Regulatory Mechanism during the Sorting of Chaperone Substrates to the Proteasome

Alberti, S., Demand, J., Esser, C., Emmerich, N., Schild, H., & Höhfeld, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204196200 · Cited by 190 · see citing works

Opportunism knocks?

Schubert, I. A., & Wobus, U. (2000) · Nature · doi:10.1038/35004754 · Cited by 170 · see citing works

Involvement of the Molecular Chaperone Ydj1 in the Ubiquitin-Dependent Degradation of Short-Lived and Abnormal Proteins in Saccharomyces cerevisiae

Lee, D. H., Sherman, M. Y., & Goldberg, A. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4773 · Cited by 149 · see citing works

Both the N‐ and C‐terminal chaperone sites of Hsp90 participate in protein refolding

Minami, M., Nakamura, M., Emori, Y., & Minami, Y. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02145.x · Cited by 43 · see citing works

Induction of heat shock proteins for protection against oxidative stress

Kalmár, B., & Greensmith, L. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.02.003 · Cited by 519 · see citing works

Mechanisms and functions of ribosome-associated protein quality control

Joazeiro, C. A. P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0118-2 · Cited by 456 · see citing works

Aβ inhibits the proteasome and enhances amyloid and tau accumulation

Tseng, B. P., Green, K. N., Chan, J. L., Blurton-Jones, M., & LaFerla, F. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.014 · Cited by 384 · see citing works

Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes

Grünblatt, E., Mandel, S. A., Jacob‐Hirsch, J., Zeligson, S., Amariglo, N., Rechavi, G., Li, J., Ravid, R., Roggendorf, W., Riederer, P. F., et al. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0212-1 · Cited by 358 · see citing works

Hsp90: Structure and Function

Jackson, S. (2012) · Topics in current chemistry · doi:10.1007/128_2012_356 · Cited by 334 · see citing works

Altered neuronal gene expression in brain regions differentially affected by Alzheimer's disease: a reference data set

Liang, W. S., Dunckley, T., Beach, T. G., Grover, A., Mastroeni, D., Ramsey, K., Caselli, R. J., Kukull, W. A., McKeel, D., Morris, J. C., et al. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.00242.2007 · Cited by 309 · see citing works

Multiubiquitylation by E4 enzymes: ‘one size’ doesn't fit all

Hoppe, T. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.02.004 · Cited by 237 · see citing works

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226 · see citing works

Broad action of Hsp90 as a host chaperone required for viral replication

Geller, R., Taguwa, S., & Frydman, J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.007 · Cited by 220 · see citing works

The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications

Burger, A. M., & Seth, A. K. (2004) · European Journal of Cancer · doi:10.1016/j.ejca.2004.07.006 · Cited by 224 · see citing works

CHIP Protects from the Neurotoxicity of Expanded and Wild-type Ataxin-1 and Promotes Their Ubiquitination and Degradation

Al‐Ramahi, I., Lam, Y. C., Chen, H.-K., Gouyon, B., Zhang, M., Perez, A. M., Branco, J., de Haro, M., Patterson, C., Zoghbi, H. Y., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601603200 · Cited by 198 · see citing works

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll, M., Dattenböck, C., Carreras-Villaseñor, N., Mendoza‐Mendoza, A., Tisch, D., Alemán-Duarte, M. I., Baker, S., Brown, C. M., Cervantes-Badillo, M. G., Cetz-Chel, J. E., et al. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-15 · Cited by 190 · see citing works

Antigen Presentation and the Ubiquitin‐Proteasome System in Host–Pathogen Interactions

Loureiro, J., & Ploegh, H. L. (2006) · Advances in immunology · doi:10.1016/s0065-2776(06)92006-9 · Cited by 171 · see citing works

Gene Expression Profiling of Sporadic Parkinson's Disease Substantia Nigra Pars Compacta Reveals Impairment of Ubiquitin-Proteasome Subunits, SKP1A, Aldehyde Dehydrogenase, and Chaperone HSC-70

Mandel, S. A., Grünblatt, E., Riederer, P. F., Amariglio, N., Hirsch, J. J., Rechavi, G., & Youdim, M. B. H. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1344.031 · Cited by 158 · see citing works

CHIP Overexpression Reduces Mutant Androgen Receptor Protein and Ameliorates Phenotypes of the Spinal and Bulbar Muscular Atrophy Transgenic Mouse Model

Adachi, H., Waza, M., Tokui, K., Katsuno, M., Minamiyama, M., Tanaka, F., Doyu, M., & Sobue, G. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1242-07.2007 · Cited by 156 · see citing works

Tetratricopeptide repeat cochaperones in steroid receptor complexes

Smith, D. F. (2004) · Cell stress & chaperones (Print) · doi:10.1379/csc-31.1 · Cited by 156 · see citing works

A Caspase Cleaved Form of Tau Is Preferentially Degraded through the Autophagy Pathway

Dolan, P. J., & Johnson, G. V. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110940 · Cited by 147 · see citing works

CHIP and HSPs interact with β-APP in a proteasome-dependent manner and influence Aβ metabolism

Kumar, P., Ambasta, R. K., Veereshwarayya, V., Rosen, K. M., Kosik, K. S., Band, H., Mestril, R., Patterson, C., & Querfurth, H. W. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm030 · Cited by 145 · see citing works

Regulation of the Myosin-Directed Chaperone UNC-45 by a Novel E3/E4-Multiubiquitylation Complex in C. elegans

Hoppe, T., Cassata, G., Barral, J. M., Springer, W., Hutagalung, A. H., Epstein, H. F., & Baumeister, R. (2004) · Cell · doi:10.1016/j.cell.2004.07.014 · Cited by 141 · see citing works

Dilated cardiomyopathy-associatedBAG3mutations impair Z-disc assembly and enhance sensitivity to apoptosis in cardiomyocytes

Arimura, T., Ishikawa, T., Nunoda, S., Kawai, S., & Kimura, A. (2011) · Human Mutation · doi:10.1002/humu.21603 · Cited by 134 · see citing works

The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover

Tawo, R., Pokrzywa, W., Kevei, É., Akyuz, M. E., Balaji, V., Adrian, S., Höhfeld, J., & Hoppe, T. (2017) · Cell · doi:10.1016/j.cell.2017.04.003 · Cited by 134 · see citing works

The Chaperone-Dependent Ubiquitin Ligase CHIP Targets HIF-1α for Degradation in the Presence of Methylglyoxal

Bento, C. F., Fernandes, R., Ramalho, J. S., Marques, C., Shang, F., Taylor, A., & Pereira, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015062 · Cited by 132 · see citing works

The role of heat shock proteins in Amyotrophic Lateral Sclerosis: The therapeutic potential of Arimoclomol

Kalmár, B., Lu, C., & Greensmith, L. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.08.003 · Cited by 130 · see citing works

Critical regulation of TGFβ signaling by Hsp90

Wrighton, K. H., Lin, X., & Feng, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800163105 · Cited by 131 · see citing works

Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease

Salminen, A., Ojala, J. O., Kaarniranta, K., Hiltunen, M., & Soininen, H. S. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.006 · Cited by 129 · see citing works

Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes

Xu, Z., Kohli, E., Devlin, K. I., Bold, M. S., Nix, J. C., & Misra, S. (2008) · BMC Structural Biology · doi:10.1186/1472-6807-8-26 · Cited by 124 · see citing works

The phosphorylation of the androgen receptor by TFIIH directs the ubiquitin/proteasome process

Chymkowitch, P., May, N. L., Charneau, P., Compe, E., & Egly, J. (2011) · EMBO Journal · doi:10.1038/emboj.2010.337 · Cited by 135 · see citing works

Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90

Yan, S., Sun, X., Xiang, B., Cang, H., Kang, X., Chen, Y., Li, H., Shi, G., Yeh, E. T. H., Wang, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.245 · Cited by 123 · see citing works

The role of heat shock proteins and co-chaperones in heart failure

Ranek, M. J., Stachowski, M. J., Kirk, J. A., & Willis, M. S. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0530 · Cited by 121 · see citing works

Human Sgt1 Binds HSP90 through the CHORD-Sgt1 Domain and Not the Tetratricopeptide Repeat Domain*

Lee, Y.-T., Jacob, J., Michowski, W., Nowotny, M., Kuźnicki, J., & Chazin, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400215200 · Cited by 136 · see citing works

Deciphering the Ubiquitin-Mediated Pathway in Apicomplexan Parasites: A Potential Strategy to Interfere with Parasite Virulence

Ponts, N., Yang, J., Chung, D.-W. D., Prudhomme, J. G., Girke, T., Horrocks, P., & Roch, K. G. L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002386 · Cited by 117 · see citing works

Parkin and relatives: the RBR family of ubiquitin ligases

Marı́n, I., Lucas‐Lledó, J. I., Gradilla, A., & Ferrús, A. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00226.2003 · Cited by 116 · see citing works

A molecular signature in blood identifies early Parkinson’s disease

Molochnikov, L., Rabey, J. M., Dobronevsky, E., Bonuccelli, U., Ceravolo, R., Frosini, D., Grünblatt, E., Riederer, P. F., Jacob, C., Aharon‐Peretz, J., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-26 · Cited by 113 · see citing works

Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva, N. V., Bobkova, I. N., & Shilov, E. M. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0790-0 · Cited by 112 · see citing works

Molecular Chaperones as Rational Drug Targets for Parkinsons Disease Therapeutics

Kalia, S. K., Kalia, L. V., & McLean, P. J. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237386 · Cited by 104 · see citing works

Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2

Xu, Z., Page, R. C., Gomes, M. M., Kohli, E., Nix, J. C., Herr, A. B., Patterson, C., & Misra, S. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1518 · Cited by 101 · see citing works

Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate

Zhang, P., Leu, J. I.-J., Murphy, M. E., George, D. L., & Marmorstein, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103518 · Cited by 99 · see citing works

CHIP: A Co-chaperone for Degradation by the Proteasome

Edkins, A. L. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_11 · Cited by 97 · see citing works

In Silico Identification of Carboxylate Clamp Type Tetratricopeptide Repeat Proteins in Arabidopsis and Rice As Putative Co-Chaperones of Hsp90/Hsp70

Prasad, B. D., Goel, S., & Krishna, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012761 · Cited by 93 · see citing works

Geldanamycin and its derivatives as Hsp90 inhibitors

Górska‐Ponikowska, M. (2012) · Frontiers in bioscience · doi:10.2741/4050 · Cited by 93 · see citing works

Advances in targeted degradation of endogenous proteins

Röth, S., Fulcher, L. J., & Sapkota, G. P. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03112-6 · Cited by 92 · see citing works

SIRT1 overexpression ameliorates a mouse model of SOD1-linked amyotrophic lateral sclerosis via HSF1/HSP70i chaperone system

Watanabe, S., Ageta‐Ishihara, N., Nagatsu, S., Takao, K., Komine, O., Endo, F., Miyakawa, T., Misawa, H., Takahashi, R., Kinoshita, M., et al. (2014) · Molecular Brain · doi:10.1186/s13041-014-0062-1 · Cited by 90 · see citing works

Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes

Zhang, X., & Qian, S. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-05-0388 · Cited by 84 · see citing works

Hectd1 regulates intracellular localization and secretion of Hsp90 to control cellular behavior of the cranial mesenchyme

Sarkar, A. A., & Zohn, I. E. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201105101 · Cited by 85 · see citing works

Differential Regulation of Rad18 through Rad6-dependent Mono- and Polyubiquitination

Miyase, S., Tateishi, S., Watanabe, K., Tomita, K., Suzuki, K., Inoue, H., & Yamaizumi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409219200 · Cited by 79 · see citing works

Derivitization of the C‐Terminus of Ubiquitin and Ubiquitin‐like Proteins Using Intein Chemistry: Methods and Uses

Wilkinson, K. D., Gan‐Erdene, T., & Kolli, N. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99003-4 · Cited by 79 · see citing works

Co-translational protein aggregation after transient cerebral ischemia

Liu, C. L., Ge, P., Zhang, F., & Hu, B. R. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.05.015 · Cited by 77 · see citing works

The Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging

Tsakiri, E. N., & Trougakos, I. P. (2014) · International review of cytology · doi:10.1016/bs.ircmb.2014.09.002 · Cited by 78 · see citing works

The network interaction of the human cytosolic 90kDa heat shock protein Hsp90: A target for cancer therapeutics

da Silva, V. C. H., & Ramos, C. H. I. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2011.12.028 · Cited by 76 · see citing works

Bag1 directly routes immature BCR-ABL for proteasomal degradation

Tsukahara, F., & Maru, Y. (2010) · Blood · doi:10.1182/blood-2009-10-249623 · Cited by 73 · see citing works

Genome-wide RNAi screen and in vivo protein aggregation reporters identify degradation of damaged proteins as an essential hypertonic stress response

Choe, K. P., & Strange, K. B. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00450.2008 · Cited by 73 · see citing works

A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?

Joshi, V., Amanullah, A., Upadhyay, A., Mishra, R., Kumar, A., & Mishra, A. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00093 · Cited by 74 · see citing works

The role of the UPS in cystic fibrosis

Turnbull, E. L., Rosser, M. F. N., & Cyr, D. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-s1-s11 · Cited by 73 · see citing works

Essential Role of Endogenous Heat Shock Protein 90 of Dendritic Cells in Antigen Cross-Presentation

Ichiyanagi, T., Imai, T., Kajiwara, C., Mizukami, S., Nakai, A., Nakayama, T., & Udono, H. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000821 · Cited by 73 · see citing works

The E3 ubiquitin ligase CHIP mediates ubiquitination and proteasomal degradation of PRMT5

Zhang, H., Zeng, L., He, Q., Tao, W. A., Zha, Z., & Hu, C. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.001 · Cited by 70 · see citing works

Functional interaction of DYX1C1 with estrogen receptors suggests involvement of hormonal pathways in dyslexia

Massinen, S., Tammimies, K., Tapia‐Páez, I., Matsson, H., Hokkanen, M., Söderberg, O., Landegren, U. D., Ċastrén, E., Gustafsson, J.-Α., Treuter, E., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp215 · Cited by 68 · see citing works

Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p

Tu, D., Li, W., Ye, Y., & Brünger, A. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701369104 · Cited by 68 · see citing works

Role of the proteasome in the regulation of estrogen receptor α turnover and function in MCF-7 breast carcinoma cells

Laı̈os, I., Journé, F., Nonclercq, D., Vidal, D. S., Toillon, R., Laurent, G., & Leclercq, G. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2005.02.005 · Cited by 67 · see citing works

STUB1/CHIP mutations cause Gordon Holmes syndrome as part of a widespread multisystemic neurodegeneration: evidence from four novel mutations

Hayer, S. N., Deconinck, T., Bender, B., Smets, K., Zuchner, S. L., Reich, S., Schöls, L. J., Schüle, R., Jonghe, P. D., Baets, J., et al. (2017) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-017-0580-x · Cited by 66 · see citing works

Protein quality control gets muscle into shape

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Molecular Mechanism of the Negative Regulation of Smad1/5 Protein by Carboxyl Terminus of Hsc70-interacting Protein (CHIP)

Wang, L., Liu, Y., Hao, R., Chen, L., Chang, Z., Wang, H., Wang, Z., & Wu, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.201814 · Cited by 64 · see citing works

Cross‐functional E3 ligases Parkin and C‐terminus Hsp70‐interacting protein in neurodegenerative disorders

Kumar, P., Pradhan, K., Ramani, K., Ambasta, R. K., & Querfurth, H. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07588.x · Cited by 61 · see citing works

Irreversible aggregation of protein synthesis machinery after focal brain ischemia

Zhang, F., Liu, C., & Hu, B. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03838.x · Cited by 60 · see citing works

Structure and Interactions of the Helical and U-Box Domains of CHIP, the C Terminus of HSP70 Interacting Protein ,

Xu, Z., Devlin, K. I., Ford, M. G., Nix, J. C., Qin, J., & Misra, S. (2006) · Biochemistry · doi:10.1021/bi0601508 · Cited by 60 · see citing works

Physiological and pathological role of the ubiquitin-proteasome system in the vascular smooth muscle cell

Demasi, M., & Laurindo, F. R. M. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs128 · Cited by 60 · see citing works

Methylglyoxal Alters the Function and Stability of Critical Components of the Protein Quality Control

Bento, C. F., Marques, F., Fernandes, R., & Pereira, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013007 · Cited by 58 · see citing works

Covalent ISG15 conjugation to CHIP promotes its ubiquitin E3 ligase activity and inhibits lung cancer cell growth in response to type I interferon

Yoo, L., Yoon, A. R., Yun, C., & Chung, K. C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0138-9 · Cited by 58 · see citing works

Mineralocorticoid receptor degradation is promoted by Hsp90 inhibition and the ubiquitin-protein ligase CHIP

Faresse, N., Ruffieux-Daidié, D., Salamin, M., Gómez-Sánchez, C. E., & Staub, O. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00285.2010 · Cited by 58 · see citing works

Chaperone-assisted E3 ligase CHIP: A double agent in cancer

Kumar, S., Basu, M., & Ghosh, M. K. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.003 · Cited by 57 · see citing works

CYTOCHROME P450 UBIQUITINATION: Branding for the Proteolytic Slaughter?

Correia, M. A., Sadeghi, S. J., & Mundo-Paredes, E. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.100127 · Cited by 57 · see citing works

Molecular Mechanism of 17-Allylamino-17-demethoxygeldanamycin (17-AAG)-induced AXL Receptor Tyrosine Kinase Degradation

Krishnamoorthy, G. P., Guida, T., Alfano, L., Avilla, E., Santoro, M. M., Carlomagno, F., & Melillo, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439422 · Cited by 55 · see citing works

HRD1-mediated ERAD tuning of ER-bound E2 is conserved between plants and mammals

Chen, Q., Zhong, Y., Wu, Y., Liu, L., Wang, P., Liu, R., Cui, F., Li, Q., Yang, X., Fang, S., et al. (2016) · Nature Plants · doi:10.1038/nplants.2016.94 · Cited by 55 · see citing works

CHIP functions an E3 ubiquitin ligase of Runx1

Shang, Y., Zhao, X., Xu, X., Xin, H., Li, X., Zhai, Y., He, D., Jia, B., Chen, W., & Chang, Z. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.043 · Cited by 53 · see citing works

Repair or destruction—an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis

Kevei, É., Pokrzywa, W., & Hoppe, T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12750 · Cited by 52 · 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

DPM1, the Catalytic Subunit of Dolichol-phosphate Mannose Synthase, Is Tethered to and Stabilized on the Endoplasmic Reticulum Membrane by DPM3

Ashida, H., Maeda, Y., & Kinoshita, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511311200 · Cited by 52 · see citing works

P42 Ebp1 regulates the proteasomal degradation of the p85 regulatory subunit of PI3K by recruiting a chaperone-E3 ligase complex HSP70/CHIP

Ko, H. R., Kim, C.-H., Lee, S. B., Song, J., Lee, K.-H., Kim, K. K., Park, K. W., Cho, S.-W., & Ahn, J.-Y. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.79 · Cited by 50 · see citing works

Protein stability and aggregation in Parkinson's disease

Robinson, P. A. (2008) · Biochemical Journal · doi:10.1042/bj20080295 · Cited by 50 · see citing works

CHIP‐dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic response

Maruyama, T., Kadowaki, H., Okamoto, N., Nagai, A., Naguro, I., Matsuzawa, A., Shibuyà, H., Tanaka, K., Murata, S., Takeda, K., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.141 · Cited by 48 · see citing works

Expression of α-hemoglobin stabilizing protein gene during human erythropoiesis

dos Santos, C. O., Duarte, A. S. S., Saad, S. T. O., & Costa, F. F. (2004) · Experimental Hematology · doi:10.1016/j.exphem.2003.11.002 · Cited by 48 · see citing works

A Sporadic Parkinson Disease Model via Silencing of the Ubiquitin-Proteasome/E3 Ligase Component SKP1A

Fishman-Jacob, T., Reznichenko, L., Youdim, M. B. H., & Mandel, S. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034223 · Cited by 49 · see citing works

Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1

Gaude, H., Aznar, N., Delay, A., Brès, A., Buchet-Poyau, K., Caillat, C., Vigouroux, A., Rogon, C., Woods, A., Vanacker, J.-M., et al. (2011) · Oncogene · doi:10.1038/onc.2011.342 · Cited by 47 · see citing works

Fibroblast Growth Factor Receptor 3 (FGFR3) Is a Strong Heat Shock Protein 90 (Hsp90) Client

Laederich, M. B., Degnin, C., Lunstrum, G. P., Holden, P. K., & Horton, W. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206151 · Cited by 46 · see citing works

What we know about ST13, a co-factor of heat shock protein, or a tumor suppressor?

Shi, Z.-Z., Zhang, J.-W., & Zheng, S. S. (2007) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.2007.b0170 · Cited by 46 · see citing works

Connecting chaperone-mediated autophagy dysfunction to cellular senescence

Moreno-Blas, D., Gorostieta-Salas, E., & Castro‐Obregón, S. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.11.001 · Cited by 42 · see citing works

Co-chaperone CHIP associates with mutant Cu/Zn-superoxide dismutase proteins linked to familial amyotrophic lateral sclerosis and promotes their degradation by proteasomes

Choi, J.-S., Cho, S., Park, S. G., Park, B. C., & Lee, D. H. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.07.010 · Cited by 43 · see citing works

Dorfin-CHIP chimeric proteins potently ubiquitylate and degrade familial ALS-related mutant SOD1 proteins and reduce their cellular toxicity

Ishigaki, S., Niwa, J., Yamada, S.-I., Takahashi, M., Ito, T., Sone, J., Doyu, M., Urano, F., & Sobue, G. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.09.017 · Cited by 42 · see citing works

LRRK 2 gene mutations in the pathophysiology of the ROCO domain and therapeutic targets for Parkinson’s disease: a review

Chen, M., & Wu, R. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0454-0 · Cited by 40 · see citing works

Oxidative Stress and Protein Quality Control Systems in the Aged Canine Brain as a Model for Human Neurodegenerative Disorders

Romanucci, M., & Salda, L. D. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/940131 · Cited by 40 · see citing works

Co-chaperone CHIP Stabilizes Aggregate-prone Malin, a Ubiquitin Ligase Mutated in Lafora Disease

Rao, S. N. R., Sharma, J., Maity, R., & Jana, N. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.006312 · Cited by 40 · see citing works

ALS-related misfolded protein management in motor neurons and muscle cells

Galbiati, M., Crippa, V., Rusmini, P., Cristofani, R., Cicardi, M. E., Giorgetti, E., Onesto, E., Messi, E., & Poletti, A. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.10.007 · Cited by 40 · see citing works

Ubiquitin‐dependent and ‐independent mitochondrial protein quality controls: implications in ageing and neurodegenerative diseases

Germain, D. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06502.x · Cited by 40 · see citing works

Ubiquitin Proteasome pathway proteins as potential drug targets in parasite Trypanosoma cruzi

Gupta, I., Aggarwal, S., Singh, K., Yadav, A. K., & Khan, S. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-26532-z · Cited by 38 · see citing works

Functional analysis of tomato CHIP ubiquitin E3 ligase in heat tolerance

Zhang, Y., Lai, X., Yang, S., Ren, H., Yuan, J., Jin, H., Shi, C., Lai, Z., & Xia, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-81372-8 · Cited by 38 · see citing works

Gene and protein signatures in sporadic Parkinson's disease and a novel genetic model of PD

Mandel, S. A., Fishman-Jacob, T., & Youdim, M. B. H. (2007) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(08)70009-9 · Cited by 38 · see citing works

Protein Quality Control System in Neurodegeneration: A Healing Company Hard to Beat but Failure is Fatal

Chhangani, D., & Mishra, A. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8411-0 · Cited by 37 · see citing works

Ubc13 and COOH Terminus of Hsp70-interacting Protein (CHIP) Are Required for Growth Hormone Receptor Endocytosis

Slotman, J. A., Almeida, A. C. D. S., Hassink, G. C., van de Ven, R. A. H., van Kerkhof, P., Kuiken, H. J., & Strous, G. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302521 · Cited by 36 · see citing works

Sculpting ion channel functional expression with engineered ubiquitin ligases

Kanner, S. A., Morgenstern, T. J., & Colecraft, H. M. (2017) · eLife · doi:10.7554/elife.29744 · Cited by 36 · see citing works

Ubiquitin–proteasome degradation of serum- and glucocorticoid-regulated kinase-1 (SGK-1) is mediated by the chaperone-dependent E3 ligase CHIP

Belova, L., Sharma, S., Brickley, D. R., Nicolarsen, J. R., Patterson, C., & Conzen, S. D. (2006) · Biochemical Journal · doi:10.1042/bj20060905 · Cited by 36 · see citing works

Ca2+/S100 Proteins Act as Upstream Regulators of the Chaperone-associated Ubiquitin Ligase CHIP (C Terminus of Hsc70-interacting Protein)

Shimamoto, S., Kubota, Y., Yamaguchi, F., Tokumitsu, H., & Kobayashi, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.436758 · Cited by 35 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works