Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 129

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Molecular Mechanism of Mutant p53 Stabilization: The Role of HSP70 and MDM2

Wiech, Milena, Olszewski, Maciej B., Tracz-Gaszewska, Zuzanna, Wawrzynow, Bartosz, Zylicz, Maciej, Zylicz, Alicja·2012·PLoS ONE
DOI 10.1371/journal.pone.0051426
Open this paper in CoChat — free account

Overview

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1371/journal.pone.0051426

Cites

9 of 9 references verified0 citation errors · 0 not checkable

Statistics

Verification

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.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 9 references

Research works printed but not linked: 80

  1. M Oren, 2003, Decision making by p53: life, death and cancer, Cell Death Differ, 10, 431, 10.1038/sj.cdd.4401183 · DOI · Paper page
  2. X Wu, 1993, The p53-mdm-2 autoregulatory feedback loop, Genes Dev, 7, 1126, 10.1101/gad.7.7a.1126 · DOI · Paper page
  3. M Gajjar, 2012, The p53 mRNA-Mdm2 interaction controls Mdm2 nuclear trafficking and is required for p53 activation following DNA damage, Cancer Cell, 21, 25, 10.1016/j.ccr.2011.11.016 · DOI · Paper page
  4. J Bartek, 1991, Aberrant expression of the p53 oncoprotein is a common feature of a wide spectrum of human malignancies, Oncogene, 6, 1699
  5. PA Muller, 2009, Mutant p53 drives invasion by promoting integrin recycling, Cell, 139, 1327, 10.1016/j.cell.2009.11.026 · DOI · Paper page
  6. GA Lang, 2004, Gain of function of a p53 hot spot mutation in a mouse model of Li-Fraumeni syndrome, Cell, 119, 861, 10.1016/j.cell.2004.11.006 · DOI · Paper page
  7. G Blandino, 1999, Mutant p53 gain of function: differential effects of different p53 mutants on resistance of cultured cells to chemotherapy, Oncogene, 18, 477, 10.1038/sj.onc.1202314 · DOI · Paper page
  8. L Weisz, 2004, Transactivation of the EGR1 gene contributes to mutant p53 gain of function, Cancer Res, 64, 8318, 10.1158/0008-5472.CAN-04-1145 · DOI
  9. S Strano, 2007, Mutant p53: an oncogenic transcription factor, Oncogene, 26, 2212, 10.1038/sj.onc.1210296 · DOI · Paper page
  10. MM Maslon, 2010, Drug discovery and mutant p53, Trends Cell Biol, 20, 542, 10.1016/j.tcb.2010.06.005 · DOI
  11. PA Muller, 2011, p53 and its mutants in tumor cell migration and invasion, J Cell Biol, 192, 209, 10.1083/jcb.201009059 · DOI · Paper page
  12. S Strano, 2000, Physical and functional interaction between p53 mutants and different isoforms of p73, J Biol Chem, 275, 29503, 10.1074/jbc.M003360200 · DOI · Paper page
  13. C Gaiddon, 2001, A subset of tumor-derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain, Mol Cell Biol, 21, 1874, 10.1128/MCB.21.5.1874-1887.2001 · DOI · Paper page
  14. Y Li, 2007, Are interactions with p63 and p73 involved in mutant p53 gain of oncogenic function?, Oncogene, 26, 2220, 10.1038/sj.onc.1210311 · DOI · Paper page
  15. J Xu, 2011, Gain of function of mutant p53 by coaggregation with multiple tumor suppressors, Nat Chem Biol, 7, 285, 10.1038/nchembio.546 · DOI · Paper page
  16. S Acin, 2011, Gain-of-function mutant p53 but not p53 deletion promotes head and neck cancer progression in response to oncogenic K-ras, J Pathol, 225, 479, 10.1002/path.2971 · DOI
  17. M Trbusek, 2011, Missense mutations located in structural p53 DNA-binding motifs are associated with extremely poor survival in chronic lymphocytic leukemia, J Clin Oncol, 29, 2703, 10.1200/JCO.2011.34.7872 · DOI
  18. C Lo Nigro, 2012, High frequency of complex TP53 mutations in CNS metastases from breast cancer, Br J Cancer, 106, 397, 10.1038/bjc.2011.464 · DOI
  19. C Dai, 2007, Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis, Cell, 130, 1005, 10.1016/j.cell.2007.07.020 · DOI · Paper page
  20. FW King, 2001, Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53, Embo J, 20, 6297, 10.1093/emboj/20.22.6297 · DOI · Paper page
  21. M Zylicz, 2001, Hsp70 interactions with the p53 tumour suppressor protein, Embo J, 20, 4634, 10.1093/emboj/20.17.4634 · DOI · Paper page
  22. SK Calderwood, 2006, Heat shock proteins in cancer: chaperones of tumorigenesis, Trends Biochem Sci, 31, 164, 10.1016/j.tibs.2006.01.006 · DOI · Paper page
  23. C Garrido, 2006, Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties, Cell Cycle, 5, 2592, 10.4161/cc.5.22.3448 · DOI · Paper page
  24. K Steiner, 2006, High HSP70-membrane expression on leukemic cells from patients with acute myeloid leukemia is associated with a worse prognosis, Leukemia, 20, 2076, 10.1038/sj.leu.2404391 · doi:10.1038/sj.leu.2404391
  25. S Tsutsumi, 2009, Impact of heat-shock protein 90 on cancer metastasis, Future Oncol, 5, 679, 10.2217/fon.09.30 · DOI
  26. VZ Volloch, 1999, Oncogenic potential of Hsp72, Oncogene, 18, 3648, 10.1038/sj.onc.1202525 · doi:10.1038/sj.onc.1202525
  27. M Rohde, 2005, Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms, Genes Dev, 19, 570, 10.1101/gad.305405 · DOI · Paper page
  28. T Langer, 1992, Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding, Nature, 356, 683, 10.1038/356683a0 · DOI · Paper page
  29. FU Hartl, 2011, Molecular chaperones in protein folding and proteostasis, Nature, 475, 324, 10.1038/nature10317 · DOI · Paper page
  30. J Jiang, 2001, CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation, J Biol Chem, 276, 42938, 10.1074/jbc.M101968200 · DOI · Paper page
  31. J Hohfeld, 2001, From the cradle to the grave: molecular chaperones that may choose between folding and degradation, EMBO Rep, 2, 885, 10.1093/embo-reports/kve206 · DOI · Paper page
  32. C Esser, 2004, Cooperation of molecular chaperones with the ubiquitin/proteasome system, Biochim Biophys Acta, 1695, 171, 10.1016/j.bbamcr.2004.09.020 · DOI · Paper page
  33. F Kriegenburg, 2012, Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation, Febs J, 279, 532, 10.1111/j.1742-4658.2011.08456.x · DOI
  34. D Skowyra, 1990, The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner, Cell, 62, 939, 10.1016/0092-8674(90)90268-J · DOI · Paper page
  35. A Ziemienowicz, 1993, Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity, J Biol Chem, 268, 25425, 10.1016/S0021-9258(19)74409-3 · doi:10.1016/s0021-9258(19)74409-3
  36. DA Parsell, 1994, Protein disaggregation mediated by heat-shock protein Hsp104, Nature, 372, 475, 10.1038/372475a0 · DOI · Paper page
  37. S Zietkiewicz, 2004, Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation, J Biol Chem, 279, 44376, 10.1074/jbc.M402405200 · DOI
  38. S Zietkiewicz, 2006, Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation, J Biol Chem, 281, 7022, 10.1074/jbc.M507893200 · DOI
  39. EA Nollen, 2001, Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection, Proc Natl Acad Sci U S A, 98, 12038, 10.1073/pnas.201112398 · DOI
  40. D Walerych, 2009, Hsp70 molecular chaperones are required to support p53 tumor suppressor activity under stress conditions, Oncogene, 28, 4284, 10.1038/onc.2009.281 · DOI
  41. L Ravagnan, 2001, Heat-shock protein 70 antagonizes apoptosis-inducing factor, Nat Cell Biol, 3, 839, 10.1038/ncb0901-839 · DOI · Paper page
  42. M Zylicz, 1983, The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system, Proc Natl Acad Sci U S A, 80, 6431, 10.1073/pnas.80.21.6431 · DOI · Paper page
  43. K Liberek, 1991, Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK, Proc Natl Acad Sci U S A, 88, 2874, 10.1073/pnas.88.7.2874 · DOI · Paper page
  44. K Liberek, 1991, The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein, J Biol Chem, 266, 14491, 10.1016/S0021-9258(18)98713-2 · DOI · Paper page
  45. HR Pelham, 1986, Speculations on the functions of the major heat shock and glucose-regulated proteins, Cell, 46, 959, 10.1016/0092-8674(86)90693-8 · DOI · Paper page
  46. M Dreiseidler, 2012, Analysis of chaperone-assisted ubiquitylation, Methods Mol Biol, 832, 473, 10.1007/978-1-61779-474-2_34 · doi:10.1007/978-1-61779-474-2_34
  47. Y Peng, 2001, Inhibition of MDM2 by hsp90 contributes to mutant p53 stabilization, J Biol Chem, 276, 40583, 10.1074/jbc.M102817200 · DOI · Paper page
  48. Esser C, Scheffner M, Hohfeld J (2005) The chaperone associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J Biol Chem. · DOI · Paper page
  49. P Muller, 2008, Chaperone-dependent stabilization and degradation of p53 mutants, Oncogene, 27, 3371, 10.1038/sj.onc.1211010 · DOI · Paper page
  50. D Li, 2011, Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cells, Mol Cancer Res, 9, 577, 10.1158/1541-7786.MCR-10-0534 · DOI · Paper page
  51. R Bagatell, 2000, Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents, Clin Cancer Res, 6, 3312
  52. KF Winklhofer, 2001, Geldanamycin restores a defective heat shock response in vivo, J Biol Chem, 276, 45160, 10.1074/jbc.M104873200 · DOI
  53. F Guo, 2005, Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin, Cancer Res, 65, 10536, 10.1158/0008-5472.CAN-05-1799 · DOI · Paper page
  54. AK McCollum, 2006, Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism, Cancer Res, 66, 10967, 10.1158/0008-5472.CAN-06-1629 · DOI
  55. T Terzian, 2008, The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss, Genes Dev, 22, 1337, 10.1101/gad.1662908 · DOI · Paper page
  56. YA Suh, 2011, Multiple stress signals activate mutant p53 in vivo, Cancer Res, 71, 7168, 10.1158/0008-5472.CAN-11-0459 · DOI
  57. C Esser, 2005, The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation, J Biol Chem, 280, 27443, 10.1074/jbc.M501574200 · DOI · Paper page
  58. PJ Coates, 2006, Regulating p73 isoforms in human tumours, J Pathol, 210, 385, 10.1002/path.2080 · DOI
  59. J Fortun, 2003, Emerging role for autophagy in the removal of aggresomes in Schwann cells, J Neurosci, 23, 10672, 10.1523/JNEUROSCI.23-33-10672.2003 · DOI · Paper page
  60. CB Levy, 2011, Co-localization of mutant p53 and amyloid-like protein aggregates in breast tumors, Int J Biochem Cell Biol, 43, 60, 10.1016/j.biocel.2010.10.017 · DOI · Paper page
  61. AP Bom, 2010, The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure, J Biol Chem, 285, 2857, 10.1074/jbc.M109.075861 · DOI
  62. JL Silva, 2010, Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins, Acc Chem Res, 43, 271, 10.1021/ar900179t · DOI
  63. J Milner, 1991, Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation, Cell, 65, 765, 10.1016/0092-8674(91)90384-B · DOI · Paper page
  64. J Momand, 1998, The MDM2 gene amplification database, Nucleic Acids Res, 26, 3453, 10.1093/nar/26.15.3453 · DOI · Paper page
  65. MS Sheikh, 1993, The p53-binding protein MDM2 gene is differentially expressed in human breast carcinoma, Cancer Res, 53, 3226
  66. A Brekman, 2011, A p53-independent role of Mdm2 in estrogen-mediated activation of breast cancer cell proliferation, Breast Cancer Res, 13, R3, 10.1186/bcr2804 · DOI · Paper page
  67. C Cordon-Cardo, 1994, Molecular abnormalities of mdm2 and p53 genes in adult soft tissue sarcomas, Cancer Res, 54, 794
  68. M Ladanyi, 1993, MDM2 gene amplification in metastatic osteosarcoma, Cancer Res, 53, 16
  69. R Mathew, 2002, Alterations in p53 and pRb pathways and their prognostic significance in oesophageal cancer, Eur J Cancer, 38, 832, 10.1016/S0959-8049(02)00007-2 · DOI
  70. H Shimizu, 2002, The conformationally flexible S9–S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo, J Biol Chem, 277, 28446, 10.1074/jbc.M202296200 · DOI
  71. J Ma, 2006, A second p53 binding site in the central domain of Mdm2 is essential for p53 ubiquitination, Biochemistry, 45, 9238, 10.1021/bi060661u · DOI
  72. M Wallace, 2006, Dual-site regulation of MDM2 E3-ubiquitin ligase activity, Mol Cell, 23, 251, 10.1016/j.molcel.2006.05.029 · DOI
  73. J Gu, 2001, Identification of p53 sequence elements that are required for MDM2-mediated nuclear export, Mol Cell Biol, 21, 8533, 10.1128/MCB.21.24.8533-8546.2001 · DOI
  74. SK Sharma, 2010, The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase, Nat Chem Biol, 6, 914, 10.1038/nchembio.455 · DOI · Paper page
  75. D Walerych, 2010, ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein, J Biol Chem, 285, 32020, 10.1074/jbc.M110.112110 · DOI
  76. KL Lim, 2005, Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation, J Neurosci, 25, 2002, 10.1523/JNEUROSCI.4474-04.2005 · DOI · Paper page
  77. Q Zhu, 2001, Mdm2 mutant defective in binding p300 promotes ubiquitination but not degradation of p53: evidence for the role of p300 in integrating ubiquitination and proteolysis, J Biol Chem, 276, 29695, 10.1074/jbc.M102634200 · DOI
  78. B Wawrzynow, 2009, A function for the RING finger domain in the allosteric control of MDM2 conformation and activity, J Biol Chem, 284, 11517, 10.1074/jbc.M809294200 · DOI
  79. S Bolte, 2006, A guided tour into subcellular colocalization analysis in light microscopy, J Microsc, 224, 213, 10.1111/j.1365-2818.2006.01706.x · DOI · Paper page
  80. PM Neilsen, 2011, Mutant p53 uses p63 as a molecular chaperone to alter gene expression and induce a pro-invasive secretome, Oncotarget, 2, 1203, 10.18632/oncotarget.382 · DOI

Cited by

See all 129

Metadata

Authors
Wiech, M., Olszewski, M. B., Tracz-Gaszewska, Z., Wawrzynow, B., Zylicz, M., & Zylicz, A.
Venue
PLoS ONE
Publisher
Public Library of Science (PLoS)
Published
2012-12-12
Volume
7
Issue
12
Pages
e51426
ISSN
1932-6203
DOI
10.1371/journal.pone.0051426
Cited by
129
References
9
Language
en
Update notices
Licence
creativecommons.org/licenses/by/4.0/ (unspecified)

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

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Molecular Mechanism of Mutant p53 Stabilization: The Role of HSP70 and MDM2. https://app.cochat.ai/papers/10.1371/journal.pone.0051426
The paper
Wiech, M., Olszewski, M. B., Tracz-Gaszewska, Z., Wawrzynow, B., Zylicz, M., & Zylicz, A. (2012). Molecular Mechanism of Mutant p53 Stabilization: The Role of HSP70 and MDM2. PLoS ONE. https://doi.org/10.1371/journal.pone.0051426

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.