A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins
Open accessAbstract
The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the tetratricopeptide repeat (TPR) domain of CHIP in complex with the α-helical lid subdomain and unstructured tail of Hsc70. Surprisingly, the CHIP-TPR interacts with determinants within both the Hsc70-lid subdomain and the C-terminal PTIEEVD motif of the tail, exhibiting an atypical mode of interaction between chaperones and TPR domains. We demonstrate that the interaction between CHIP and the Hsc70-lid subdomain is required for proper ubiquitination of Hsp70/Hsc70 or Hsp70/Hsc70-bound substrate proteins. Posttranslational modifications of the Hsc70 lid and tail disrupt key contacts with the CHIP-TPR and may regulate CHIP-mediated ubiquitination. Our study shows how CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Hsp70 likewise has an unstructured EEVD-connecting linker that may not take part directly in cochaperone interactions.
“Hsp70 similarly contains an unstructured EEVD-connecting linker that may not participate directly in cochaperone interactions”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Zhang et al., 2015
The Introduction describes an unstructured tail preceding Hsp70’s EEVD-containing motif, and the Results report that most residues between the lid and motif are disordered. But the Results also show that the first few tail residues directly contact CHIP’s TPR domain, so the suggestion that the linker may not participate directly needs that qualification. Page numbers are unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
<i>Phaser</i> crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
<i>MolProbity</i> : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
Scaling and assessment of data quality
Evans, P. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905036693 · Cited by 4,391 · see citing works
Hsp70 chaperones: Cellular functions and molecular mechanism
Mayer, M. P., & Bukau, B. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4464-6 · Cited by 2,857 · see citing works
Purification and Characterization
Tsai, C. S. (2006) · Biomacromolecules · doi:10.1002/0470080124.ch3 · Cited by 2,368 · see citing works
Molecular Chaperone Functions in Protein Folding and Proteostasis
Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,468 · see citing works
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188 · see citing works
TPR proteins: the versatile helix
D’Andrea, L. D. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.007 · Cited by 1,154 · 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
New insights into ubiquitin E3 ligase mechanism
Berndsen, C., & Wolberger, C. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2780 · Cited by 706 · 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
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521 · see citing works
Molecular evolution of the HSP70 multigene family
Boorstein, W. R., Ziegelhoffer, T., & Craig, E. A. (1994) · Journal of Molecular Evolution · doi:10.1007/bf00175490 · Cited by 510 · see citing works
Molina, H., Horn, D. M., Tang, N., Mathivanan, S., & Pandey, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611217104 · Cited by 502 · see citing works
SOLVE and RESOLVE: Automated Structure Solution and Density Modification
Terwilliger, T. C. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)74002-6 · Cited by 466 · see citing works
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
Bertelsen, E., Chang, L., Gestwicki, J., & Zuiderweg, E. (2009) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0903503106 · Cited by 461 · see citing works
Kim, H. T., Kim, K. P., Lledı́as, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., Gygi, S. P., & Goldberg, A. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609659200 · Cited by 438 · see citing works
Self-citationChaperone-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
Structure, Function and Regulation of the Hsp90 Machinery
Büchner, J., & Li, J. (2013) · Biomedical Journal · doi:10.4103/2319-4170.113230 · Cited by 421 · see citing works
Zhang, M., Windheim, M., Roe, S. M., Peggie, M. W., Cohen, P., Prodromou, C., & Pearl, L. H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.023 · Cited by 420 · see citing works
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
Kityk, R., Kopp, J., Sinning, I., & Mayer, M. P. (2012) · Molecules and Cells · doi:10.1016/j.molcel.2012.09.023 · Cited by 412 · see citing works
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
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
Bukau, B., Mayer, M. P., Schröder, H., Rüdiger, S., Paal, K., & Laufen, T. (2000) · Nature Structural Biology · doi:10.1038/76819 · Cited by 374 · see citing works
CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
Qian, S., McDonough, H., Boellmann, F., Cyr, D., & Patterson, C. (2006) · Nature · doi:10.1038/nature04600 · Cited by 369 · see citing works
Structural and Functional Discussion of the Tetra-Trico-Peptide Repeat, a Protein Interaction Module
Zeytuni, N., & Zarivach, R. (2012) · Structure · doi:10.1016/j.str.2012.01.006 · Cited by 344 · see citing works
Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
Cyr, D., Höhfeld, J., & Patterson, C. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02125-4 · Cited by 338 · see citing works
Structure of an E3:E2∼Ub Complex Reveals an Allosteric Mechanism Shared among RING/U-box Ligases
Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., & Klevit, R. E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.001 · Cited by 333 · see citing works
Building and remodelling Cullin–RING E3 ubiquitin ligases
Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327 · see citing works
Benchmarking and Analysis of Protein Docking Performance in Rosetta v3.2
Chaudhury, S., Berrondo, M., Weitzner, B. D., Muthu, P., Bergman, H., & Gray, J. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022477 · Cited by 326 · see citing works
BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2379 · Cited by 319 · see citing works
Structure of the TPR Domain of p67phox in Complex with Rac·GTP
Lapouge, K., Smith, S. J. M., Walker, P. A., Gamblin, S. J., Smerdon, S. J., & Rittinger, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00091-2 · Cited by 311 · see citing works
The chaperone Hsp90: changing partners for demanding clients
Röhl, A., Rohrberg, J., & Büchner, J. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.02.003 · Cited by 268 · see citing works
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Qi, R., Sarbeng, E. B., Liu, Q., Le, K. Q., Xu, X., Xu, H., Wong, J. L., Wong, J. L., Vorvis, C., Hendrickson, W. A., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2583 · Cited by 252 · see citing works
Versatile TPR domains accommodate different modes of target protein recognition and function
Allan, R. K., & Ratajczak, T. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0248-0 · Cited by 245 · see citing works
Molecular basis for TPR domain‐mediated regulation of protein phosphatase 5
Yang, J., Roe, S. M., Cliff, M. J., Williams, M. A., Ladbury, J. E., Cohen, P. T. W., & Barford, D. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600496 · Cited by 239 · see citing works
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
Schmid, A. B., Lagleder, S., Gräwert, M. A., Röhl, A., Hagn, F., Wandinger, S. K., Cox, M. B., Demmer, O., Richter, K., Groll, M., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.472 · Cited by 229 · see citing works
Müller, P., Růčková, E., Halada, P., Coates, P. J., Hrstka, R., Lane, D. P., & Vojtěšek, B. (2012) · Oncogene · doi:10.1038/onc.2012.314 · Cited by 226 · see citing works
Mechanics of Hsp70 chaperones enables differential interaction with client proteins
Schlecht, R., Erbse, A. H., Bukau, B., & Mayer, M. P. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2006 · Cited by 194 · see citing works
Kleiger, G., Saha, A., Lewis, S. M., Kuhlman, B. A., & Deshaies, R. J. (2009) · Cell · doi:10.1016/j.cell.2009.10.030 · Cited by 194 · see citing works
Wu, B., Li, P., Liu, Y., Lou, Z., Ding, Y., Shu, C., Ye, S., Bartlam, M., Shen, B., & Rao, Z. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305969101 · Cited by 165 · see citing works
Substrate Transfer from the Chaperone Hsp70 to Hsp90
Wegele, H., Wandinger, S. K., Schmid, A. B., Reinstein, J., & Büchner, J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.008 · Cited by 162 · see citing works
Cloutier, P., Lavallée‐Adam, M., Faubert, D., Blanchette, M., & Coulombe, B. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003210 · Cited by 156 · see citing works
Ube2w and Ataxin-3 Coordinately Regulate the Ubiquitin Ligase CHIP
Scaglione, K. M., Zavodszky, E., Todi, S. V., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.036 · Cited by 156 · see citing works
Self-citationGAPDH regulates cellular heme insertion into inducible nitric oxide synthase
Chakravarti, R., Aulak, K. S., Fox, P. L., & Stuehr, D. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008133107 · Cited by 146 · see citing works
Self-citationChaperone Functions of the E3 Ubiquitin Ligase CHIP
Rosser, M. F. N., Washburn, E. K., Muchowski, P. J., Patterson, C., & Cyr, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700513200 · Cited by 144 · see citing works
He, B., Bai, S., Hnat, A. T., Kalman, R. I., Minges, J. T., Patterson, C., & Wilson, E. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403117200 · Cited by 137 · see citing works
Two Structures of Cyclophilin 40
Taylor, P., Dornan, J., Carrello, A., Minchin, R. F., Ratajczak, T., & Walkinshaw, M. D. (2001) · Structure · doi:10.1016/s0969-2126(01)00603-7 · Cited by 136 · see citing works
Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity
Nikolay, R., Wiederkehr, T., Rist, W., Krämer, G., Mayer, M. P., & Bukau, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311112200 · Cited by 130 · 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
Self-citationAlvira, S., Cuéllar, J., Röhl, A., Yamamoto, S., Itoh, H., Alfonso, C., Rivas, G., Büchner, J., & Valpuesta, J. (2014) · Nature Communications · doi:10.1038/ncomms6484 · Cited by 121 · see citing works
Stankiewicz, M., Nikolay, R., Rybin, V., & Mayer, M. P. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07737.x · Cited by 120 · see citing works
Cho, H., Shimazu, T., Toyokawa, G., Daigo, Y., Maehara, Y., Hayami, S., Ito, A., Masuda, K., Ikawa, N., Field, H. I., et al. (2012) · Nature Communications · doi:10.1038/ncomms2074 · Cited by 119 · see citing works
Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP
Kundrat, L., & Regan, L. (2010) · Biochemistry · doi:10.1021/bi100386w · Cited by 114 · see citing works
Jakobsson, M. E., Moen, A. R., Bousset, L., Egge-Jacobsen, W. M., Kernstock, S., Melki, R., & Falnes, P. Ø. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483248 · Cited by 106 · see citing works
Identification of Residues on Hsp70 and Hsp90 Ubiquitinated by the Cochaperone CHIP
Kundrat, L., & Regan, L. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.017 · Cited by 106 · 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
Self-citationEffect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock Protein
Greene, L. E., Zinner, R., Naficy, S., & Eisenberg, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2967 · Cited by 89 · see citing works
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle
Li, Z., Hartl, F. U., & Bracher, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2608 · Cited by 87 · see citing works
Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
Priya, S., Sharma, S., & Goloubinoff, P. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.014 · Cited by 86 · see citing works
Multiple Domains of the Co-chaperone Hop Are Important for Hsp70 Binding
Carrigan, P. E., Nelson, G. M., Roberts, P. J., Stoffer, J. B., Riggs, D. L., & Smith, D. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314130200 · Cited by 80 · see citing works
Flom, G. A., Behal, R. H., Rosen, L., Cole, D. G., & Johnson, J. L. (2007) · Biochemical Journal · doi:10.1042/bj20070084 · Cited by 80 · see citing works
Wu, S., Fu-Hwa, L. I. U., Hu, S., & Chung, W. A. N. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590419 · Cited by 74 · see citing works
Ubiquitylation of Neuronal Nitric-oxide Synthase by CHIP, a Chaperone-dependent E3 Ligase
Peng, H., Morishima, Y., Jenkins, G. J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406926200 · Cited by 73 · see citing works
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
Motif-Specific Sampling of Phosphoproteomes
Ruse, C. I., McClatchy, D. B., Lu, B., Cociorva, D., Motoyama, A., Park, S. K., & Yates, J. R. (2008) · Journal of Proteome Research · doi:10.1021/pr800147u · Cited by 60 · see citing works
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
Self-citationThe E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex
Smith, M. C. P., Scaglione, K. M., Assimon, V. A., Patury, S., Thompson, A. D., Dickey, C. A., Southworth, D. R., Paulson, H. L., Gestwicki, J. E., & Zuiderweg, E. R. P. (2013) · Biochemistry · doi:10.1021/bi4009209 · Cited by 59 · see citing works
Self-citationEngineering a Ubiquitin Ligase Reveals Conformational Flexibility Required for Ubiquitin Transfer
Qian, S., Wasson, L. K., Choudhary, N. R., Klevit, R. E., Chazin, W., & Patterson, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032334 · Cited by 53 · see citing works
Graf, C., Stankiewicz, M., Nikolay, R., et al. (2010) · Biochemistry · doi:10.1021/bi901829f · Cited by 51 · see citing works
Connarn, J. N., Assimon, V. A., Reed, R. A., Tse, E., Southworth, D. R., Zuiderweg, E. R. P., Gestwicki, J. E., & Sun, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.519421 · Cited by 48 · see citing works
Wu, S., Fu-Hwa, L. I. U., Hu, S., et al. (2001) · Biochemical Journal · doi:10.1042/bj3590419 · Cited by 48 · see citing works
Dutta, S., & Tan, Y. (2008) · Biochemistry · doi:10.1021/bi800758a · Cited by 44 · see citing works
Topology and dynamics of the 10 kDa C‐terminal domain of DnaK in solution
Bertelsen, E. B., Zhou, H., Lowry, D. F., Flynn, G. C., & Dahlquist, F. W. (1999) · Protein Science · doi:10.1110/ps.8.2.343 · Cited by 36 · see citing works
Chen, L., Kong, X., Fu, J., Xu, Y., Fang, S., Hua, P., Luo, L., & Yin, Z. (2009) · Cellular Immunology · doi:10.1016/j.cellimm.2009.03.009 · Cited by 31 · see citing works
Pan, Z., Zhu, J., Shang, Y., Wei, Z., Jia, M. Z., Xia, C., Wen, W., Wang, W., & Zhang, M. (2013) · Structure · doi:10.1016/j.str.2013.04.005 · Cited by 29 · see citing works
Chakravarti, R., & Stuehr, D. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342758 · Cited by 28 · see citing works
Self-citationMaeda, H., Sahara, H., Mori, Y., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703436200 · Cited by 25 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Assimon, V. A., Southworth, D. R., & Gestwicki, J. E. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00801 · Cited by 112 · see citing works
Lee, K., Thwin, A. C., Nadel, C. M., Tse, E., Gates, S. N., Gestwicki, J. E., & Southworth, D. R. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.023 · Cited by 76 · see citing works
Kumar, R., Moche, M., Winblad, B., & Pavlov, P. F. (2017) · Scientific Reports · doi:10.1038/s41598-017-14731-z · Cited by 40 · see citing works
Wang, C., Arrington, J., Ratliff, A. C., Chen, J., Horton, H. E., Nie, Y., Yue, F., Hrycyna, C. A., Tao, W. A., & Kuang, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008430 · Cited by 33 · see citing works
Hidden information on protein function in censuses of proteome foldedness
Cox, D., Ang, C.-S., Nillegoda, N. B., Reid, G. E., & Hatters, D. M. (2022) · Nature Communications · doi:10.1038/s41467-022-29661-2 · Cited by 16 · see citing works
- Authors
- Zhang, H., Amick, J., Chakravarti, R., Santarriaga, S., Schlanger, S., McGlone, C., Dare, M., Nix, J. C., Scaglione, K. M., Stuehr, D. J., Misra, S., & Page, R. C.
- Affiliations
- Miami University (US)
- Cleveland Clinic (US)
- Medical College of Wisconsin (US)
- Lawrence Berkeley National Laboratory (US)
- Corresponding author
- Misra, Saurav
- Page, Richard C.
- ORCID
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2015-03
- Volume
- 23
- Issue
- 3
- Pages
- 472-482
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC4351142
- OpenAlex
- W2075239233
- Cited by
- 98
- References
- 81
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 8 · 2023: 8 · 2022: 14 · 2021: 9 · 2020: 8 · 2019: 7 · 2018: 7 · 2017: 8 · 2016: 12 · 2015: 2
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 368 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- US NIH (R01-GM080271, R00-NS073936, T32-HL007914)
- Burroughs Wellcome Foundation Collaborative Research Travel (1014031)
- Miami University
- Research and Education Program
- Medical College of Wisconsin
- US Department of Energy (DE-AC03-76SF00098)
- Lawrence Berkeley National Laboratory
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- CHIP, HSP70, Hsc70, tetratricopeptide repeat domain, ubiquitination, chaperone-client interactions, protein quality control, protein degradation, post-translational modification, protein complex structure
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Crystallography, X-Ray, Ubiquitin-Protein Ligases, HSC70 Heat-Shock Proteins, Mice, Protein Interaction Domains and Motifs, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
