| Year |
Citation |
Score |
| 2022 |
Friedlová N, Zavadil Kokáš F, Hupp TR, Vojtěšek B, Nekulová M. IFITM protein regulation and functions: Far beyond the fight against viruses. Frontiers in Immunology. 13: 1042368. PMID 36466909 DOI: 10.3389/fimmu.2022.1042368 |
0.308 |
|
| 2022 |
Padariya M, Jooste ML, Hupp T, Fåhraeus R, Vojtesek B, Vollrath F, Kalathiya U, Karakostis K. The Elephant Evolved p53 Isoforms that Escape MDM2-Mediated Repression and Cancer. Molecular Biology and Evolution. 39. PMID 35792674 DOI: 10.1093/molbev/msac149 |
0.413 |
|
| 2021 |
Salomao N, Karakostis K, Hupp T, Vollrath F, Vojtesek B, Fahraeus R. What do we need to know and understand about p53 to improve its clinical value? The Journal of Pathology. PMID 33826155 DOI: 10.1002/path.5677 |
0.352 |
|
| 2020 |
Bibi N, Hupp T, Kamal MA, Rashid S. Elucidation of PLK1 Linked Biomarkers in Oesophageal Cancer Cell Lines: A Step Towards Novel Signaling Pathways by p53 and PLK1- Linked Functions Crosstalk. Protein and Peptide Letters. PMID 32875973 DOI: 10.2174/0929866527999200901201837 |
0.416 |
|
| 2020 |
Faktor J, Grasso G, Zavadil F, Kurkowiak M, Mayordomo MY, Kote S, Singh A, Ruidong L, O'Neill JR, Muller P, Goodlett D, Vojtesek B, Hupp T. The effects of p53 gene inactivation on mutant proteome expression in a human melanoma cell model. Biochimica Et Biophysica Acta. General Subjects. 129722. PMID 32866596 DOI: 10.1016/J.Bbagen.2020.129722 |
0.399 |
|
| 2019 |
Delom F, Mohtar MA, Hupp T, Fessart D. The AGR2 interactome. American Journal of Physiology. Cell Physiology. PMID 31644305 DOI: 10.1152/Ajpcell.00532.2018 |
0.384 |
|
| 2019 |
Maurel M, Obacz J, Avril T, Ding YP, Papadodima O, Treton X, Daniel F, Pilalis E, Hörberg J, Hou W, Beauchamp MC, Tourneur-Marsille J, Cazals-Hatem D, Sommerova L, Samali A, ... Hupp T, et al. Control of anterior GRadient 2 (AGR2) dimerization links endoplasmic reticulum proteostasis to inflammation. Embo Molecular Medicine. PMID 31040128 DOI: 10.15252/Emmm.201810120 |
0.341 |
|
| 2019 |
Wang Q, Zhang X, Chen L, Weng S, Xia Y, Ye Y, Li K, Liao Z, Chen P, Alsamman K, Meng C, Stevens C, Hupp TR, Lin Y. Regulation of the Expression of DAPK1 by SUMO Pathway. Biomolecules. 9. PMID 30999631 DOI: 10.3390/biom9040151 |
0.304 |
|
| 2019 |
Bibi N, Niaz H, Hupp T, Kamal MA, Rashid S. Screening and Identification of PLK1-Polo Box binding peptides by high-throughput sequencing of phage-selected libraries. Protein and Peptide Letters. PMID 30887917 DOI: 10.2174/0929866526666190318101054 |
0.316 |
|
| 2019 |
Coufalova D, Remnant L, Hernychova L, Muller P, Healy A, Kannan S, Vojtesek B, Westwood N, Verma CS, Vojtesek B, Hupp TR, Houston DR. An inter-subunit protein-peptide interface that stabilizes the specific activity and oligomerization of the AAA+ chaperone Reptin. Journal of Proteomics. PMID 30862565 DOI: 10.1016/J.Jprot.2019.02.012 |
0.306 |
|
| 2019 |
Nguyen MN, Sen N, Lin MY, Joseph TL, Vaz C, Tanavde V, Way L, Hupp TR, Verma CS, Madhusudhan MS. Discovering Putative Protein Targets of Small Molecules: A Study of the p53 Activator Nutlin. Journal of Chemical Information and Modeling. PMID 30794402 DOI: 10.1021/Acs.Jcim.8B00762 |
0.433 |
|
| 2018 |
Mohtar MA, Hernychova L, O'Neill R, Lawrence M, Murray E, Vojtesek B, Hupp TR. The sequence-specific peptide-binding activity of the protein sulfide isomerase AGR2 directs its' stable binding to the oncogenic receptor EpCAM. Molecular & Cellular Proteomics : McP. PMID 29339412 DOI: 10.1074/mcp.RA118.000573 |
0.304 |
|
| 2017 |
Muller P, Chan JM, Simoncik O, Fojta M, Lane DP, Hupp T, Vojtesek B. Evidence for allosteric effects on p53 oligomerization induced by phosphorylation. Protein Science : a Publication of the Protein Society. PMID 29124793 DOI: 10.1002/Pro.3344 |
0.595 |
|
| 2017 |
Landré V, Revi B, Mir MG, Verma C, Hupp TR, Gilbert N, Ball KL. Regulation of transcriptional activators by DNA-binding domain ubiquitination. Cell Death and Differentiation. PMID 28362432 DOI: 10.1038/Cdd.2017.42 |
0.433 |
|
| 2016 |
Way L, Faktor J, Dvorakova P, Nicholson J, Vojtesek B, Graham D, Ball KL, Hupp T. Rearrangement of Mitochondrial Pyruvate Dehydrogenase Subunit Dihydrolipoamide Dehydrogenase Protein-Protein Interactions by the MDM2 Ligand Nutlin-3. Proteomics. PMID 27273042 DOI: 10.1002/Pmic.201500501 |
0.426 |
|
| 2015 |
Healy AR, Houston DR, Remnant L, Huart AS, Brychtova V, Maslon MM, Meers O, Muller P, Krejci A, Blackburn EA, Vojtesek B, Hernychova L, Walkinshaw MD, Westwood NJ, Hupp TR. Discovery of a novel ligand that modulates the protein-protein interactions of the AAA+ superfamily oncoprotein reptin. Chemical Science. 6: 3109-3116. PMID 28706685 DOI: 10.1039/c4sc03885a |
0.334 |
|
| 2015 |
Krejci A, Hupp TR, Lexa M, Vojtesek B, Muller P. Hammock: a hidden Markov model-based peptide clustering algorithm to identify protein-interaction consensus motifs in large datasets. Bioinformatics (Oxford, England). PMID 26342231 DOI: 10.1093/Bioinformatics/Btv522 |
0.345 |
|
| 2015 |
Dickinson ER, Jurneczko E, Nicholson J, Hupp TR, Zawacka-Pankau J, Selivanova G, Barran PE. The use of ion mobility mass spectrometry to probe modulation of the structure of p53 and of MDM2 by small molecule inhibitors. Frontiers in Molecular Biosciences. 2: 39. PMID 26217671 DOI: 10.3389/Fmolb.2015.00039 |
0.4 |
|
| 2015 |
Marcar L, Ihrig B, Hourihan J, Bray SE, Quinlan PR, Jordan LB, Thompson AM, Hupp TR, Meek DW. MAGE-A Cancer/Testis Antigens Inhibit MDM2 Ubiquitylation Function and Promote Increased Levels of MDM4. Plos One. 10: e0127713. PMID 26001071 DOI: 10.1371/journal.pone.0127713 |
0.331 |
|
| 2015 |
Dickinson ER, Jurneczko E, Pacholarz KJ, Clarke DJ, Reeves M, Ball KL, Hupp T, Campopiano D, Nikolova PV, Barran PE. Insights into the conformations of three structurally diverse proteins: cytochrome c, p53, and MDM2, provided by variable-temperature ion mobility mass spectrometry. Analytical Chemistry. 87: 3231-8. PMID 25629302 DOI: 10.1021/Ac503720V |
0.337 |
|
| 2015 |
Fraser JA, Worrall EG, Lin Y, Landre V, Pettersson S, Blackburn E, Walkinshaw M, Muller P, Vojtesek B, Ball K, Hupp TR. Phosphomimetic mutation of the N-terminal lid of MDM2 enhances the polyubiquitination of p53 through stimulation of E2-ubiquitin thioester hydrolysis. Journal of Molecular Biology. 427: 1728-47. PMID 25543083 DOI: 10.1016/J.Jmb.2014.12.011 |
0.312 |
|
| 2014 |
Gray TA, Alsamman K, Murray E, Sims AH, Hupp TR. Engineering a synthetic cell panel to identify signalling components reprogrammed by the cell growth regulator anterior gradient-2. Molecular Biosystems. 10: 1409-25. PMID 24710632 DOI: 10.1039/c4mb00113c |
0.325 |
|
| 2014 |
Nicholson J, Scherl A, Way L, Blackburn EA, Walkinshaw MD, Ball KL, Hupp TR. A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2. Cellular Signalling. 26: 1243-57. PMID 24583282 DOI: 10.1016/j.cellsig.2014.02.011 |
0.329 |
|
| 2014 |
Dejeans N, Manié S, Hetz C, Bard F, Hupp T, Agostinis P, Samali A, Chevet E. Addicted to secrete - novel concepts and targets in cancer therapy. Trends in Molecular Medicine. 20: 242-50. PMID 24456621 DOI: 10.1016/J.Molmed.2013.12.003 |
0.35 |
|
| 2014 |
Kofod-Olsen E, Pettersson S, Wallace M, Abduljabar AB, Oster B, Hupp T, Höllsberg P. Human herpesvirus-6B protein U19 contains a p53 BOX I homology motif for HDM2 binding and p53 stabilization. Virology. 448: 33-42. PMID 24314634 DOI: 10.1016/J.Virol.2013.10.002 |
0.489 |
|
| 2013 |
Huart AS, Saxty B, Merritt A, Nekulova M, Lewis S, Huang Y, Vojtesek B, Kettleborough C, Hupp TR. A Casein kinase 1/Checkpoint kinase 1 pyrazolo-pyridine protein kinase inhibitor as novel activator of the p53 pathway. Bioorganic & Medicinal Chemistry Letters. 23: 5578-85. PMID 24007918 DOI: 10.1016/j.bmcl.2013.08.046 |
0.31 |
|
| 2013 |
Hernychova L, Man P, Verma C, Nicholson J, Sharma CA, Ruckova E, Teo JY, Ball K, Vojtesek B, Hupp TR. Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry. Proteomics. 13: 2512-25. PMID 23776060 DOI: 10.1002/Pmic.201300029 |
0.339 |
|
| 2013 |
Kofod-Olsen E, Møller JM, Schleimann MH, Bundgaard B, Bak RO, Øster B, Mikkelsen JG, Hupp T, Höllsberg P. Inhibition of p53-dependent, but not p53-independent, cell death by U19 protein from human herpesvirus 6B. Plos One. 8: e59223. PMID 23555634 DOI: 10.1371/Journal.Pone.0059223 |
0.427 |
|
| 2013 |
Morgan HP, O'Reilly FJ, Wear MA, O'Neill JR, Fothergill-Gilmore LA, Hupp T, Walkinshaw MD. M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation. Proceedings of the National Academy of Sciences of the United States of America. 110: 5881-6. PMID 23530218 DOI: 10.1073/Pnas.1217157110 |
0.338 |
|
| 2013 |
Pettersson S, Sczaniecka M, McLaren L, Russell F, Gladstone K, Hupp T, Wallace M. Non-degradative ubiquitination of the Notch1 receptor by the E3 ligase MDM2 activates the Notch signalling pathway. The Biochemical Journal. 450: 523-36. PMID 23252402 DOI: 10.1042/Bj20121249 |
0.38 |
|
| 2013 |
Chevet E, Fessart D, Delom F, Mulot A, Vojtesek B, Hrstka R, Murray E, Gray T, Hupp T. Emerging roles for the pro-oncogenic anterior gradient-2 in cancer development. Oncogene. 32: 2499-509. PMID 22945652 DOI: 10.1038/Onc.2012.346 |
0.395 |
|
| 2013 |
Scotcher J, Clarke DJ, MacKay CL, Hupp T, Sadler PJ, Langridge-Smith PRR. Redox regulation of tumour suppressor protein p53: Identification of the sites of hydrogen peroxide oxidation and glutathionylation Chemical Science. 4: 1257-1269. DOI: 10.1039/C2Sc21702C |
0.467 |
|
| 2012 |
Ponnuswamy A, Hupp T, Fåhraeus R. Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops. Genes & Cancer. 3: 291-7. PMID 23150762 DOI: 10.1177/1947601912454140 |
0.526 |
|
| 2012 |
Nicholson J, Neelagandan K, Huart AS, Ball K, Molloy MP, Hupp T. An iTRAQ proteomics screen reveals the effects of the MDM2 binding ligand Nutlin-3 on cellular proteostasis. Journal of Proteome Research. 11: 5464-78. PMID 23039052 DOI: 10.1021/Pr300698D |
0.447 |
|
| 2012 |
Morelli X, Hupp T. Searching for the Holy Grail; protein-protein interaction analysis and modulation. Embo Reports. 13: 877-9. PMID 22986552 DOI: 10.1038/Embor.2012.137 |
0.352 |
|
| 2012 |
Hupp TR, Hayward RL, Vojtesek B. Strategies for p53 reactivation in human sarcoma. Cancer Cell. 22: 283-5. PMID 22975370 DOI: 10.1016/j.ccr.2012.08.020 |
0.314 |
|
| 2012 |
Huart AS, MacLaine NJ, Narayan V, Hupp TR. Exploiting the MDM2-CK1α protein-protein interface to develop novel biologics that induce UBL-kinase-modification and inhibit cell growth. Plos One. 7: e43391. PMID 22916255 DOI: 10.1371/journal.pone.0043391 |
0.384 |
|
| 2012 |
Robson AF, Hupp TR, Lickiss F, Ball KL, Faulds K, Graham D. Nanosensing protein allostery using a bivalent mouse double minute two (MDM2) assay. Proceedings of the National Academy of Sciences of the United States of America. 109: 8073-8. PMID 22556265 DOI: 10.1073/pnas.1116637109 |
0.348 |
|
| 2012 |
Gray TA, MacLaine NJ, Michie CO, Bouchalova P, Murray E, Howie J, Hrstka R, Maslon MM, Nenutil R, Vojtesek B, Langdon S, Hayward L, Gourley C, Hupp TR. Anterior Gradient-3: a novel biomarker for ovarian cancer that mediates cisplatin resistance in xenograft models. Journal of Immunological Methods. 378: 20-32. PMID 22361111 DOI: 10.1016/J.Jim.2012.01.013 |
0.403 |
|
| 2012 |
Frame S, Aspinall C, O'Neil R, Hollick J, Taylor S, Hupp T, Blake D, Zheleva DI. Abstract 2814: Potent and selective small molecule inhibitors of polo-like kinase 1: Biological characterization Cancer Research. 72: 2814-2814. DOI: 10.1158/1538-7445.Am2012-2814 |
0.401 |
|
| 2011 |
Clarke DJ, Murray E, Hupp T, Mackay CL, Langridge-Smith PR. Mapping a noncovalent protein-peptide interface by top-down FTICR mass spectrometry using electron capture dissociation. Journal of the American Society For Mass Spectrometry. 22: 1432-40. PMID 21953198 DOI: 10.1007/S13361-011-0155-3 |
0.407 |
|
| 2011 |
Hengel SM, Murray E, Langdon S, Hayward L, O'Donoghue J, Panchaud A, Hupp T, Goodlett DR. Data-independent proteomic screen identifies novel tamoxifen agonist that mediates drug resistance. Journal of Proteome Research. 10: 4567-78. PMID 21936522 DOI: 10.1021/Pr2004117 |
0.355 |
|
| 2011 |
Hollstein M, Hupp T. Chek2ing out the p53 pathway: can Puma lead the way? Cell Cycle (Georgetown, Tex.). 10: 1524. PMID 21478674 DOI: 10.4161/Cc.10.10.15514 |
0.396 |
|
| 2011 |
Scotcher J, Clarke DJ, Weidt SK, Mackay CL, Hupp TR, Sadler PJ, Langridge-Smith PR. Identification of two reactive cysteine residues in the tumor suppressor protein p53 using top-down FTICR mass spectrometry. Journal of the American Society For Mass Spectrometry. 22: 888-97. PMID 21472523 DOI: 10.1007/S13361-011-0088-X |
0.372 |
|
| 2011 |
Pang LY, Scott M, Hayward RL, Mohammed H, Whitelaw CB, Smith GC, Hupp TR. p21(WAF1) is component of a positive feedback loop that maintains the p53 transcriptional program. Cell Cycle (Georgetown, Tex.). 10: 932-50. PMID 21368573 |
0.375 |
|
| 2011 |
MacLaine NJ, Hupp TR. How phosphorylation controls p53. Cell Cycle (Georgetown, Tex.). 10: 916-21. PMID 21350334 DOI: 10.4161/cc.10.6.15076 |
0.4 |
|
| 2011 |
Narayan V, Halada P, Hernychová L, Chong YP, Žáková J, Hupp TR, Vojtesek B, Ball KL. A multiprotein binding interface in an intrinsically disordered region of the tumor suppressor protein interferon regulatory factor-1. The Journal of Biological Chemistry. 286: 14291-303. PMID 21245151 DOI: 10.1074/jbc.M110.204602 |
0.31 |
|
| 2011 |
Dastidar SG, Raghunathan D, Nicholson J, Hupp TR, Lane DP, Verma CS. Chemical states of the N-terminal "lid" of MDM2 regulate p53 binding: simulations reveal complexities of modulation. Cell Cycle (Georgetown, Tex.). 10: 82-9. PMID 21191186 DOI: 10.4161/Cc.10.1.14345 |
0.508 |
|
| 2011 |
Lin Y, Henderson P, Pettersson S, Satsangi J, Hupp T, Stevens C. Tuberous sclerosis-2 (TSC2) regulates the stability of death-associated protein kinase-1 (DAPK) through a lysosome-dependent degradation pathway. The Febs Journal. 278: 354-70. PMID 21134130 DOI: 10.1111/j.1742-4658.2010.07959.x |
0.343 |
|
| 2010 |
Marcar L, Maclaine NJ, Hupp TR, Meek DW. Mage-A cancer/testis antigens inhibit p53 function by blocking its interaction with chromatin. Cancer Research. 70: 10362-70. PMID 21056992 DOI: 10.1158/0008-5472.CAN-10-1341 |
0.428 |
|
| 2010 |
Maslon MM, Hrstka R, Vojtesek B, Hupp TR. A divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for Reptin. Journal of Molecular Biology. 404: 418-38. PMID 20888340 DOI: 10.1016/j.jmb.2010.09.035 |
0.339 |
|
| 2010 |
Fraser JA, Vojtesek B, Hupp TR. A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. Phosphorylation at SER269 in vivo is linked to inactivation of p53 function Journal of Biological Chemistry. 285: 37762-37772. PMID 20851891 DOI: 10.1074/jbc.M110.143099 |
0.41 |
|
| 2010 |
Fraser JA, Madhumalar A, Blackburn E, Bramham J, Walkinshaw MD, Verma C, Hupp TR. A novel p53 phosphorylation site within the MDM2 ubiquitination signal: II. A model in which phosphorylation at Ser269 induces a mutant conformation to p53 Journal of Biological Chemistry. 285: 37773-37786. PMID 20847049 DOI: 10.1074/Jbc.M110.143107 |
0.394 |
|
| 2010 |
Maslon MM, Hupp TR. Drug discovery and mutant p53. Trends in Cell Biology. 20: 542-55. PMID 20656489 DOI: 10.1016/j.tcb.2010.06.005 |
0.392 |
|
| 2010 |
Hrstka R, Nenutil R, Fourtouna A, Maslon MM, Naughton C, Langdon S, Murray E, Larionov A, Petrakova K, Muller P, Dixon MJ, Hupp TR, Vojtesek B. The pro-metastatic protein anterior gradient-2 predicts poor prognosis in tamoxifen-treated breast cancers. Oncogene. 29: 4838-47. PMID 20531310 DOI: 10.1038/Onc.2010.228 |
0.321 |
|
| 2010 |
Nicholson J, Hupp TR. The molecular dynamics of MDM2. Cell Cycle (Georgetown, Tex.). 9: 1878-81. PMID 20436290 DOI: 10.4161/cc.9.10.11597 |
0.33 |
|
| 2010 |
Worrall EG, Worrall L, Blackburn E, Walkinshaw M, Hupp TR. The effects of phosphomimetic lid mutation on the thermostability of the N-terminal domain of MDM2. Journal of Molecular Biology. 398: 414-28. PMID 20303977 DOI: 10.1016/j.jmb.2010.03.023 |
0.357 |
|
| 2010 |
Meek DW, Hupp TR. The regulation of MDM2 by multisite phosphorylation--opportunities for molecular-based intervention to target tumours? Seminars in Cancer Biology. 20: 19-28. PMID 19897041 DOI: 10.1016/j.semcancer.2009.10.005 |
0.403 |
|
| 2010 |
Lin Y, Hupp TR, Stevens C. Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death. The Febs Journal. 277: 48-57. PMID 19878313 DOI: 10.1111/j.1742-4658.2009.07411.x |
0.302 |
|
| 2009 |
Maclaine NJ, Hupp TR. The regulation of p53 by phosphorylation: a model for how distinct signals integrate into the p53 pathway. Aging. 1: 490-502. PMID 20157532 DOI: 10.18632/aging.100047 |
0.371 |
|
| 2009 |
Huart AS, MacLaine NJ, Meek DW, Hupp TR. CK1alpha plays a central role in mediating MDM2 control of p53 and E2F-1 protein stability. The Journal of Biological Chemistry. 284: 32384-94. PMID 19759023 DOI: 10.1074/jbc.M109.052647 |
0.373 |
|
| 2009 |
Worrall EG, Wawrzynow B, Worrall L, Walkinshaw M, Ball KL, Hupp TR. Regulation of the E3 ubiquitin ligase activity of MDM2 by an N-terminal pseudo-substrate motif. Journal of Chemical Biology. 2: 113-29. PMID 19568783 DOI: 10.1007/s12154-009-0019-5 |
0.372 |
|
| 2009 |
Lin Y, Stevens C, Harrison B, Pathuri S, Amin E, Hupp TR. The alternative splice variant of DAPK-1, s-DAPK-1, induces proteasome-independent DAPK-1 destabilization. Molecular and Cellular Biochemistry. 328: 101-7. PMID 19267229 DOI: 10.1007/s11010-009-0079-4 |
0.303 |
|
| 2009 |
Wawrzynow B, Pettersson S, Zylicz A, Bramham J, Worrall E, Hupp TR, Ball KL. A function for the RING finger domain in the allosteric control of MDM2 conformation and activity. The Journal of Biological Chemistry. 284: 11517-30. PMID 19188367 DOI: 10.1074/jbc.M809294200 |
0.312 |
|
| 2009 |
Stevens C, Lin Y, Harrison B, Burch L, Ridgway RA, Sansom O, Hupp T. Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling. The Journal of Biological Chemistry. 284: 334-44. PMID 18974095 DOI: 10.1074/Jbc.M805165200 |
0.415 |
|
| 2008 |
Stevens C, Pettersson S, Wawrzynow B, Wallace M, Ball K, Zylicz A, Hupp TR. ATP stimulates MDM2-mediated inhibition of the DNA-binding function of E2F1. The Febs Journal. 275: 4875-86. PMID 18754770 DOI: 10.1111/j.1742-4658.2008.06627.x |
0.364 |
|
| 2008 |
MacLaine NJ, Oster B, Bundgaard B, Fraser JA, Buckner C, Lazo PA, Meek DW, Höllsberg P, Hupp TR. A central role for CK1 in catalyzing phosphorylation of the p53 transactivation domain at serine 20 after HHV-6B viral infection. The Journal of Biological Chemistry. 283: 28563-73. PMID 18669630 DOI: 10.1074/jbc.M804433200 |
0.316 |
|
| 2008 |
Nelson L, Anderson S, Archibald AL, Rhind S, Lu ZH, Condie A, McIntyre N, Thompson J, Nenutil R, Vojtesek B, Whitelaw CBA, Little TJ, Hupp T. An animal model to evaluate the function and regulation of the adaptively evolving stress protein SEP53 in oesophageal bile damage responses Cell Stress and Chaperones. 13: 375-385. PMID 18465210 DOI: 10.1007/S12192-008-0037-1 |
0.344 |
|
| 2008 |
Lin Y, Stevens C, Hrstka R, Harrison B, Fourtouna A, Pathuri S, Vojtesek B, Hupp T. An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing. The Febs Journal. 275: 2574-84. PMID 18422656 DOI: 10.1111/J.1742-4658.2008.06404.X |
0.415 |
|
| 2008 |
Oster B, Bundgaard B, Hupp TR, Höllsberg P. Human herpesvirus 6B induces phosphorylation of p53 in its regulatory domain by a CK2- and p38-independent pathway. The Journal of General Virology. 89: 87-96. PMID 18089732 DOI: 10.1099/vir.0.83136-0 |
0.305 |
|
| 2007 |
Little TJ, Nelson L, Hupp T. Adaptive evolution of a stress response protein Plos One. 2. PMID 17925851 DOI: 10.1371/Journal.Pone.0001003 |
0.327 |
|
| 2007 |
Wawrzynow B, Zylicz A, Wallace M, Hupp T, Zylicz M. MDM2 chaperones the p53 tumor suppressor. The Journal of Biological Chemistry. 282: 32603-12. PMID 17848574 DOI: 10.1074/Jbc.M702767200 |
0.525 |
|
| 2007 |
Din S, Lennon AM, Arnott ID, Hupp T, Satsangi J. Technology insight: the application of proteomics in gastrointestinal disease. Nature Clinical Practice. Gastroenterology & Hepatology. 4: 372-85. PMID 17607293 DOI: 10.1038/Ncpgasthep0872 |
0.306 |
|
| 2007 |
Finlan LE, Hupp TR. p63: the phantom of the tumor suppressor. Cell Cycle (Georgetown, Tex.). 6: 1062-71. PMID 17426453 DOI: 10.4161/cc.6.9.4162 |
0.339 |
|
| 2007 |
Craig AL, Chrystal JA, Fraser JA, Sphyris N, Lin Y, Harrison BJ, Scott MT, Dornreiter I, Hupp TR. The MDM2 ubiquitination signal in the DNA-binding domain of p53 forms a docking site for calcium calmodulin kinase superfamily members. Molecular and Cellular Biology. 27: 3542-55. PMID 17339337 DOI: 10.1128/MCB.01595-06 |
0.596 |
|
| 2007 |
Lin Y, Stevens C, Hupp T. Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. The Journal of Biological Chemistry. 282: 16792-802. PMID 17324927 DOI: 10.1074/Jbc.M611559200 |
0.412 |
|
| 2007 |
Fraser JA, Hupp TR. Chemical genetics approach to identify peptide ligands that selectively stimulate DAPK-1 kinase activity. Biochemistry. 46: 2655-73. PMID 17297916 DOI: 10.1021/bi061562j |
0.309 |
|
| 2007 |
Stevens C, Lin Y, Sanchez M, Amin E, Copson E, White H, Durston V, Eccles DM, Hupp T. A germ line mutation in the death domain of DAPK-1 inactivates ERK-induced apoptosis. The Journal of Biological Chemistry. 282: 13791-803. PMID 17244621 DOI: 10.1074/Jbc.M605649200 |
0.344 |
|
| 2006 |
Finlan LE, Nenutil R, Ibbotson SH, Vojtesek B, Hupp TR. CK2-site phosphorylation of p53 is induced in DeltaNp63 expressing basal stem cells in UVB irradiated human skin. Cell Cycle (Georgetown, Tex.). 5: 2489-94. PMID 17106255 DOI: 10.4161/cc.5.21.3393 |
0.391 |
|
| 2006 |
Wallace M, Worrall E, Pettersson S, Hupp TR, Ball KL. Dual-site regulation of MDM2 E3-ubiquitin ligase activity. Molecular Cell. 23: 251-63. PMID 16857591 DOI: 10.1016/j.molcel.2006.05.029 |
0.367 |
|
| 2006 |
Shimizu H, Saliba D, Wallace M, Finlan L, Langridge-Smith PR, Hupp TR. Destabilizing missense mutations in the tumour suppressor protein p53 enhance its ubiquitination in vitro and in vivo. The Biochemical Journal. 397: 355-67. PMID 16579792 DOI: 10.1042/Bj20051521 |
0.41 |
|
| 2006 |
Cesková P, Chichger H, Wallace M, Vojtesek B, Hupp TR. On the mechanism of sequence-specific DNA-dependent acetylation of p53: the acetylation motif is exposed upon DNA binding. Journal of Molecular Biology. 357: 442-56. PMID 16438982 DOI: 10.1016/j.jmb.2005.12.026 |
0.349 |
|
| 2004 |
Dornan D, Eckert M, Wallace M, Shimizu H, Ramsay E, Hupp TR, Ball KL. Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53. Molecular and Cellular Biology. 24: 10083-98. PMID 15509808 DOI: 10.1128/MCB.24.22.10083-10098.2004 |
0.379 |
|
| 2004 |
Finlan L, Hupp TR. The N-terminal interferon-binding domain (IBiD) homology domain of p300 binds to peptides with homology to the p53 transactivation domain. The Journal of Biological Chemistry. 279: 49395-405. PMID 15337767 DOI: 10.1074/jbc.M405974200 |
0.369 |
|
| 2004 |
Burch L, Shimizu H, Smith A, Patterson C, Hupp TR. Expansion of protein interaction maps by phage peptide display using MDM2 as a prototypical conformationally flexible target protein. Journal of Molecular Biology. 337: 129-45. PMID 15001357 DOI: 10.1016/J.Jmb.2004.01.017 |
0.398 |
|
| 2004 |
Burch LR, Scott M, Pohler E, Meek D, Hupp T. Phage-peptide display identifies the interferon-responsive, death-activated protein kinase family as a novel modifier of MDM2 and p21WAF1. Journal of Molecular Biology. 337: 115-28. PMID 15001356 DOI: 10.1016/j.jmb.2003.10.081 |
0.343 |
|
| 2004 |
Pohler E, Craig AL, Cotton J, Lawrie L, Dillon JF, Ross P, Kernohan N, Hupp TR. The Barrett's antigen anterior gradient-2 silences the p53 transcriptional response to DNA damage. Molecular & Cellular Proteomics : McP. 3: 534-47. PMID 14967811 DOI: 10.1074/mcp.M300089-MCP200 |
0.343 |
|
| 2004 |
Pospísilová S, Brázda V, Kucharíková K, Luciani MG, Hupp TR, Skládal P, Palecek E, Vojtesek B. Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. The Biochemical Journal. 378: 939-47. PMID 14640983 DOI: 10.1042/BJ20030662 |
0.423 |
|
| 2004 |
Liem AA, Appleyard MV, O'Neill MA, Hupp TR, Chamberlain MP, Thompson AM. Doxorubicin and vinorelbine act independently via p53 expression and p38 activation respectively in breast cancer cell lines. British Journal of Cancer. 88: 1281-4. PMID 12698197 DOI: 10.1038/sj.bjc.6600898 |
0.308 |
|
| 2003 |
Dornan D, Shimizu H, Burch L, Smith AJ, Hupp TR. The proline repeat domain of p53 binds directly to the transcriptional coactivator p300 and allosterically controls DNA-dependent acetylation of p53. Molecular and Cellular Biology. 23: 8846-61. PMID 14612423 |
0.392 |
|
| 2003 |
Craig A, Scott M, Burch L, Smith G, Ball K, Hupp T. Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain. Embo Reports. 4: 787-92. PMID 12897801 DOI: 10.1038/sj.embor.embor901 |
0.397 |
|
| 2003 |
Craig AL, Bray SE, Finlan LE, Kernohan NM, Hupp TR. Signaling to p53: the use of phospho-specific antibodies to probe for in vivo kinase activation. Methods in Molecular Biology (Clifton, N.J.). 234: 171-202. PMID 12824532 DOI: 10.1385/1-59259-408-5:171 |
0.344 |
|
| 2003 |
Achison M, Hupp TR. Hypoxia attenuates the p53 response to cellular damage. Oncogene. 22: 3431-40. PMID 12776195 DOI: 10.1038/sj.onc.1206434 |
0.358 |
|
| 2003 |
Lane DP, Hupp TR. Drug discovery and p53. Drug Discovery Today. 8: 347-55. PMID 12681938 DOI: 10.1016/S1359-6446(03)02669-2 |
0.506 |
|
| 2003 |
Dornan D, Shimizu H, Burch L, Smith AJ, Hupp TR. The Proline Repeat Domain of p53 Binds Directly to the Transcriptional Coactivator p300 and Allosterically Controls DNA-Dependent Acetylation of p53 Molecular and Cellular Biology. 23: 8846-8861. DOI: 10.1128/MCB.23.23.8846-8861.2003 |
0.392 |
|
| 2003 |
Dornan D, Shimizu H, Perkins ND, Hupp TR. DNA-dependent Acetylation of p53 by the Transcription Coactivator p300 Journal of Biological Chemistry. 278: 13431-13441. DOI: 10.1074/JBC.M211460200 |
0.326 |
|
| 2002 |
Dornan D, Shimizu H, Perkins ND, Hupp TR. DNA-dependent acetylation of p53 by the transcription coactivator p300. The Journal of Biological Chemistry. 278: 13431-41. PMID 12499368 DOI: 10.1074/jbc.M211460200 |
0.411 |
|
| 2002 |
Shimizu H, Burch LR, Smith AJ, Dornan D, Wallace M, Ball KL, Hupp TR. 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. The Journal of Biological Chemistry. 277: 28446-58. PMID 11925449 DOI: 10.1074/jbc.M202296200 |
0.368 |
|
| 2001 |
Dornan D, Hupp TR. Inhibition of p53-dependent transcription by BOX-I phospho-peptide mimetics that bind to p300. Embo Reports. 2: 139-44. PMID 11258706 DOI: 10.1093/embo-reports/kve025 |
0.403 |
|
| 2000 |
Blaydes JP, Luciani MG, Pospisilova S, Ball HM, Vojtesek B, Hupp TR. Stoichiometric phosphorylation of human p53 at Ser315 stimulates p53-dependent transcription. The Journal of Biological Chemistry. 276: 4699-708. PMID 11078726 DOI: 10.1074/jbc.M003485200 |
0.424 |
|
| 2000 |
Luciani MG, Hutchins JR, Zheleva D, Hupp TR. The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A. Journal of Molecular Biology. 300: 503-18. PMID 10884347 DOI: 10.1006/jmbi.2000.3830 |
0.39 |
|
| 2000 |
Webley K, Bond JA, Jones CJ, Blaydes JP, Craig A, Hupp T, Wynford-Thomas D. Posttranslational modifications of p53 in replicative senescence overlapping but distinct from those induced by DNA damage. Molecular and Cellular Biology. 20: 2803-8. PMID 10733583 DOI: 10.1128/Mcb.20.8.2803-2808.2000 |
0.467 |
|
| 2000 |
Craig AL, Blaydes JP, Burch LR, Thompson AM, Hupp TR. Dephosphorylation of p53 at Ser20 after cellular exposure to low levels of non-ionizing radiation. Oncogene. 18: 6305-12. PMID 10597229 DOI: 10.1038/sj.onc.1203085 |
0.302 |
|
| 2000 |
HUPP TR, LANE DP, BALL KL. Strategies for manipulating the p53 pathway in the treatment of human cancer Biochemical Journal. 352: 1-17. DOI: 10.1042/Bj3520001 |
0.507 |
|
| 1999 |
Cohen PA, Hupp TR, Lane DP, Daniels DA. Biochemical characterization of different conformational states of the Sf9 cell-purified p53His175 mutant protein. Febs Letters. 463: 179-84. PMID 10601663 DOI: 10.1016/S0014-5793(99)01603-8 |
0.546 |
|
| 1999 |
Blaydes JP, Sparks A, Hupp TR. Activation of p53 protein function in response to cellular irradiation Methods in Molecular Biology (Clifton, N.J.). 113: 591-598. PMID 10443454 DOI: 10.1385/1-59259-675-4:591 |
0.342 |
|
| 1999 |
Bond JA, Webley K, Wyllie FS, Jones CJ, Craig A, Hupp T, Wynford-Thomas D. p53-Dependent growth arrest and altered p53-immunoreactivity following metabolic labelling with 32P ortho-phosphate in human fibroblasts. Oncogene. 18: 3788-92. PMID 10391688 DOI: 10.1038/sj.onc.1202733 |
0.388 |
|
| 1999 |
Hupp TR. Regulation of p53 protein function through alterations in protein-folding pathways. Cellular and Molecular Life Sciences : Cmls. 55: 88-95. PMID 10065154 DOI: 10.1007/s000180050272 |
0.45 |
|
| 1999 |
CRAIG AL, BURCH L, VOJTESEK B, MIKUTOWSKA J, THOMPSON A, HUPP TR. Novel phosphorylation sites of human tumour suppressor protein p53 at Ser20 and Thr18 that disrupt the binding of mdm2 (mouse double minute 2) protein are modified in human cancers Biochemical Journal. 342: 133. DOI: 10.1042/0264-6021:3420133 |
0.368 |
|
| 1998 |
Blaydes JP, Hupp TR. DNA damage triggers DRB-resistant phosphorylation of human p53 at the CK2 site. Oncogene. 17: 1045-52. PMID 9747884 DOI: 10.1038/SJ.ONC.1202014 |
0.356 |
|
| 1997 |
Mundt M, Hupp T, Fritsche M, Merkle C, Hansen S, Lane D, Groner B. Protein interactions at the carboxyl terminus of p53 result in the induction of its in vitro transactivation potential Oncogene. 15: 237-244. PMID 9244359 DOI: 10.1038/Sj.Onc.1201174 |
0.572 |
|
| 1997 |
Fourie AM, Hupp TR, Lane DP, Sang BC, Barbosa MS, Sambrook JF, Gething MJ. HSP70 binding sites in the tumor suppressor protein p53. The Journal of Biological Chemistry. 272: 19471-9. PMID 9235949 DOI: 10.1074/jbc.272.31.19471 |
0.556 |
|
| 1996 |
Hansen S, Midgley CA, Lane DP, Freeman BC, Morimoto RI, Hupp TR. Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70. The Journal of Biological Chemistry. 271: 30922-8. PMID 8940078 DOI: 10.1074/Jbc.271.48.30922 |
0.578 |
|
| 1996 |
Marszalek J, Zhang W, Hupp TR, Margulies C, Carr KM, Cherry S, Kaguni JM. Domains of DnaA protein involved in interaction with DnaB protein, and in unwinding the Escherichia coli chromosomal origin. The Journal of Biological Chemistry. 271: 18535-42. PMID 8702501 DOI: 10.1074/Jbc.271.31.18535 |
0.347 |
|
| 1996 |
Hansen S, Hupp TR, Lane DP. Allosteric regulation of the thermostability and DNA binding activity of human p53 by specific interacting proteins. CRC Cell Transformation Group. The Journal of Biological Chemistry. 271: 3917-24. PMID 8632013 DOI: 10.1074/Jbc.271.7.3917 |
0.58 |
|
| 1996 |
Kernohan NM, Hupp TR, Lane DP. Modification of an N-terminal regulatory domain of T antigen restores p53-T antigen complex formation in the absence of an essential metal ion cofactor. The Journal of Biological Chemistry. 271: 4954-60. PMID 8617769 DOI: 10.1074/Jbc.271.9.4954 |
0.468 |
|
| 1996 |
Lane D, Hupp T, Warbrick E, Picksley S, Sparks A, Farheus R, Paramio J, Ball K, Lain S, Glover D, Hall P. Regulating and replacing suppressor gene function with small synthetic molecules; design of an active synthetic suppressor protein Biochemical Society Transactions. 24: 592S-592S. DOI: 10.1042/Bst024592Sa |
0.432 |
|
| 1995 |
Hupp TR, Lane DP. Allosteric activation of latent p53 tetramers. Current Biology : Cb. 4: 865-75. PMID 7850419 DOI: 10.1016/S0960-9822(00)00195-0 |
0.588 |
|
| 1995 |
Lane DP, Lu X, Hupp T, Hall PA. The role of the p53 protein in the apoptotic response. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 345: 277-80. PMID 7846126 DOI: 10.1098/Rstb.1994.0106 |
0.567 |
|
| 1995 |
Lane DP, Midgley CA, Hupp TR, Lu X, Vojtesek B, Picksley SM. On the regulation of the p53 tumour suppressor, and its role in the cellular response to DNA damage. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 347: 83-7. PMID 7746859 DOI: 10.1098/Rstb.1995.0013 |
0.537 |
|
| 1995 |
Hupp TR, Lane DP. Two distinct signaling pathways activate the latent DNA binding function of p53 in a casein kinase II-independent manner. The Journal of Biological Chemistry. 270: 18165-74. PMID 7629129 DOI: 10.1074/Jbc.270.30.18165 |
0.556 |
|
| 1995 |
Hupp TR, Lane DP. Regulation of the cryptic sequence-specific DNA-binding function of p53 by protein kinases. Cold Spring Harbor Symposia On Quantitative Biology. 59: 195-206. PMID 7587070 DOI: 10.1101/SQB.1994.059.01.024 |
0.592 |
|
| 1995 |
Hupp TR, Sparks A, Lane DP. Small peptides activate the latent sequence-specific DNA binding function of p53 Cell. 83: 237-245. PMID 7585941 DOI: 10.1016/0092-8674(95)90165-5 |
0.553 |
|
| 1995 |
Cox L, Hupp T, Midgley C, Lane D. A direct effect of activated human p53 on nuclear DNA replication. The Embo Journal. 14: 2099-2105. DOI: 10.1002/J.1460-2075.1995.Tb07201.X |
0.565 |
|
| 1994 |
Picksley SM, Hupp TR, Lu X, Midgley CA, Vojtesek B, Lane DP. Regulation of p53 protein expression in human cancer Cancer Genetics and Cytogenetics. 77: 153. DOI: 10.1016/0165-4608(94)90250-X |
0.497 |
|
| 1993 |
Lane DP, Midgley C, Hupp T. Tumour suppressor genes and molecular chaperones. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 339: 369-72; discussion 3. PMID 8493291 DOI: 10.1098/Rstb.1993.0036 |
0.537 |
|
| 1993 |
Hupp TR, Meek DW, Midgley CA, Lane DP. Activation of the cryptic DNA binding function of mutant forms of p53. Nucleic Acids Research. 21: 3167-74. PMID 8341590 DOI: 10.1093/Nar/21.14.3167 |
0.547 |
|
| 1992 |
Hupp TR, Meek DW, Midgley CA, Lane DP. Regulation of the specific DNA binding function of p53. Cell. 71: 875-86. PMID 1423635 DOI: 10.1016/0092-8674(92)90562-Q |
0.568 |
|
| Show low-probability matches. |