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

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

Cellular Defenses against Unfolded Proteins

Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 996

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

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

Hsp90

Young, J. C., Moarefi, I., & Hartl, F. U. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104079 · Cited by 838

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

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

Hsp90 & Co. – a holding for folding

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

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

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

Marcu, M. G., Chadli, A., Bouhouche, I., CATELLI, M. G., & Neckers, L. Μ. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003701200 · Cited by 506

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

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 477

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

Amyotrophic Lateral Sclerosis

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

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 431

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 431

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

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

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

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

Opportunism knocks?

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

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

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

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

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

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

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 355

Hsp90: Structure and Function

Jackson, S. (2012) · Topics in current chemistry · doi:10.1007/128_2012_356 · Cited by 347

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