Rewiring cancer drivers to activate apoptosis.

Humans Apoptosis / drug effects Cell Cycle Proteins / metabolism Gene Expression Regulation, Neoplastic / drug effects Lymphoma, Large B-Cell, Diffuse / drug therapy Proto-Oncogene Proteins c-bcl-6 / genetics Transcription Factors / metabolism Epigenesis, Genetic / drug effects Promoter Regions, Genetic Carcinogenesis / drug effects

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
Aug 2023
Historique:
received: 15 08 2022
accepted: 20 06 2023
medline: 11 8 2023
pubmed: 27 7 2023
entrez: 26 7 2023
Statut: ppublish

Résumé

Genes that drive the proliferation, survival, invasion and metastasis of malignant cells have been identified for many human cancers

Identifiants

DOI: 10.1038/s41586-023-06348-2 PMID: 37495688
pubmed: 37495688
doi: 10.1038/s41586-023-06348-2
pii: 10.1038/s41586-023-06348-2
doi:

Substances chimiques

BRD4 protein, human 0
Cell Cycle Proteins 0
Proto-Oncogene Proteins c-bcl-6 0
Transcription Factors 0
BCL6 protein, human 0
TP53 protein, human 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

417-425

Subventions

Organisme : NCI NIH HHS
ID : R01 CA163915
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA276167
Pays : United States
Organisme : NINDS NIH HHS
ID : R37 NS046789
Pays : United States
Organisme : NIMH NIH HHS
ID : RF1 MH126720
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : ErratumIn

Informations de copyright

© 2023. The Author(s), under exclusive licence to Springer Nature Limited.

Références

Weinberg, R. A. The action of oncogenes in the cytoplasm and nucleus. Science 230, 770–776 (1985).
pubmed: 2997917 doi: 10.1126/science.2997917
Davoli, T. et al. Cumulative haploinsufficiency and triplosensitivity drive aneuploidy patterns and shape the cancer genome. Cell 155, 948–962 (2013).
pubmed: 24183448 pmcid: 3891052 doi: 10.1016/j.cell.2013.10.011
Sanchez-Vega, F. et al. Oncogenic signaling pathways in The Cancer Genome Atlas. Cell 173, 321–337.e10 (2018).
pubmed: 29625050 pmcid: 6070353 doi: 10.1016/j.cell.2018.03.035
Denny, S. K. et al. Nfib promotes metastasis through a widespread increase in chromatin accessibility. Cell 166, 328–342 (2016).
pubmed: 27374332 pmcid: 5004630 doi: 10.1016/j.cell.2016.05.052
Hengartner, M. O. & Horvitz, H. R. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell 76, 665–676 (1994).
pubmed: 7907274 doi: 10.1016/0092-8674(94)90506-1
Strasser, A., O’Connor, L. & Dixit, V. M. Apoptosis signaling. Annu. Rev. Biochem. 69, 217–245 (2000).
pubmed: 10966458 doi: 10.1146/annurev.biochem.69.1.217
Schmitz, R. et al. Genetics and pathogenesis of diffuse large B-cell lymphoma. N. Engl. J. Med. 378, 1396–1407 (2018).
pubmed: 29641966 pmcid: 6010183 doi: 10.1056/NEJMoa1801445
Phan, R. T. & Dalla-Favera, R. The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B cells. Nature 432, 635–639 (2004).
pubmed: 15577913 doi: 10.1038/nature03147
Spencer, D. M., Wandless, T. J., Schreiber, S. L. & Crabtree, G. R. Controlling signal transduction with synthetic ligands. Science 262, 1019–1024 (1993).
pubmed: 7694365 doi: 10.1126/science.7694365
Spencer, D. M., Graef, I., Austin, D. J., Schreiber, S. L. & Crabtree, G. R. A general strategy for producing conditional alleles of Src-like tyrosine kinases. Proc. Natl Acad. Sci. USA 92, 9805–9809 (1995).
pubmed: 7568222 pmcid: 40891 doi: 10.1073/pnas.92.21.9805
Graef, I. A., Holsinger, L. J., Diver, S., Schreiber, S. L. & Crabtree, G. R. Proximity and orientation underlie signaling by the non-receptor tyrosine kinase ZAP70. EMBO J. 16, 5618–5628 (1997).
pubmed: 9312021 pmcid: 1170194 doi: 10.1093/emboj/16.18.5618
Ho, S. N., Biggar, S. R., Spencer, D. M., Schreiber, S. L. & Crabtree, G. R. Dimeric ligands define a role for transcriptional activation domains in reinitiation. Nature 382, 822–826 (1996).
pubmed: 8752278 doi: 10.1038/382822a0
Erwin, G. S. et al. Synthetic transcription elongation factors license transcription across repressive chromatin. Science 358, 1617–1622 (2017).
pubmed: 29192133 pmcid: 6037176 doi: 10.1126/science.aan6414
Hathaway, N. A. et al. Dynamics and memory of heterochromatin in living cells. Cell 149, 1447–1460 (2012).
pubmed: 22704655 pmcid: 3422694 doi: 10.1016/j.cell.2012.03.052
Stanton, B. Z., Chory, E. J. & Crabtree, G. R. Chemically induced proximity in biology and medicine. Science https://doi.org/10.1126/science.aao5902 (2018).
Stanton, B. Z. et al. Smarca4 ATPase mutations disrupt direct eviction of PRC1 from chromatin. Nat. Genet. 49, 282–288 (2017).
pubmed: 27941795 doi: 10.1038/ng.3735
Burslem, G. M. & Crews, C. M. Proteolysis-targeting chimeras as therapeutics and tools for biological discovery. Cell 181, 102–114 (2020).
pubmed: 31955850 pmcid: 7319047 doi: 10.1016/j.cell.2019.11.031
Gestwicki, J. E., Crabtree, G. R. & Graef, I. A. Harnessing chaperones to generate small-molecule inhibitors of amyloid β aggregation. Science 306, 865–869 (2004).
pubmed: 15514157 doi: 10.1126/science.1101262
Freiberg, R. A. et al. Specific triggering of the Fas signal transduction pathway in normal human keratinocytes. J. Biol. Chem. 271, 31666–31669 (1996).
pubmed: 8940187 doi: 10.1074/jbc.271.49.31666
MacCorkle, R. A., Freeman, K. W. & Spencer, D. M. Synthetic activation of caspases: artificial death switches. Proc. Natl Acad. Sci. USA 95, 3655–3660 (1998).
pubmed: 9520421 pmcid: 19891 doi: 10.1073/pnas.95.7.3655
Yang, X., Chang, H. Y. & Baltimore, D. Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. Science 281, 1355–1357 (1998).
pubmed: 9721101 doi: 10.1126/science.281.5381.1355
Basso, K. et al. Integrated biochemical and computational approach identifies BCL6 direct target genes controlling multiple pathways in normal germinal center B cells. Blood 115, 975–984 (2010).
pubmed: 19965633 pmcid: 2817639 doi: 10.1182/blood-2009-06-227017
Kerres, N. et al. Chemically induced degradation of the oncogenic transcription factor BCL6. Cell Rep. 20, 2860–2875 (2017).
pubmed: 28930682 doi: 10.1016/j.celrep.2017.08.081
Filippakopoulos, P. et al. Selective inhibition of BET bromodomains. Nature 468, 1067–1073 (2010).
pubmed: 20871596 pmcid: 3010259 doi: 10.1038/nature09504
Loven, J. et al. Selective inhibition of tumor oncogenes by disruption of super-enhancers. Cell 153, 320–334 (2013).
pubmed: 23582323 pmcid: 3760967 doi: 10.1016/j.cell.2013.03.036
Nagel, S. et al. Amplification at 11q23 targets protein kinase SIK2 in diffuse large B-cell lymphoma. Leuk. Lymphoma 51, 881–891 (2010).
pubmed: 20367563 doi: 10.3109/10428191003699878
Dyer, M. J., Fischer, P., Nacheva, E., Labastide, W. & Karpas, A. A new human B-cell non-Hodgkin’s lymphoma cell line (Karpas 422) exhibiting both t (14;18) and t(4;11) chromosomal translocations. Blood 75, 709–714 (1990).
pubmed: 2297573 doi: 10.1182/blood.V75.3.709.709
Shu, S. et al. Response and resistance to BET bromodomain inhibitors in triple-negative breast cancer. Nature 529, 413–417 (2016).
pubmed: 26735014 pmcid: 4854653 doi: 10.1038/nature16508
Ghandi, M. et al. Next-generation characterization of the Cancer Cell Line Encyclopedia. Nature 569, 503–508 (2019).
pubmed: 31068700 pmcid: 6697103 doi: 10.1038/s41586-019-1186-3
Yu, C. et al. High-throughput identification of genotype-specific cancer vulnerabilities in mixtures of barcoded tumor cell lines. Nat. Biotechnol. 34, 419–423 (2016).
pubmed: 26928769 pmcid: 5508574 doi: 10.1038/nbt.3460
Winter, G. E. et al. Drug development. Phthalimide conjugation as a strategy for in vivo target protein degradation. Science 348, 1376–1381 (2015).
pubmed: 25999370 pmcid: 4937790 doi: 10.1126/science.aab1433
Slabicki, M. et al. Small-molecule-induced polymerization triggers degradation of BCL6. Nature 588, 164–168 (2020).
pubmed: 33208943 pmcid: 7816212 doi: 10.1038/s41586-020-2925-1
Nowak, R. P. et al. Plasticity in binding confers selectivity in ligand-induced protein degradation. Nat. Chem. Biol. 14, 706–714 (2018).
pubmed: 29892083 pmcid: 6202246 doi: 10.1038/s41589-018-0055-y
Schultz, L. W. & Clardy, J. Chemical inducers of dimerization: the atomic structure of FKBP12-FK1012A-FKBP12. Bioorg. Med. Chem. Lett. 8, 1–6 (1998).
pubmed: 9871618 doi: 10.1016/S0960-894X(97)10195-0
Schreiber, S. L. The rise of molecular glues. Cell 184, 3–9 (2021).
pubmed: 33417864 doi: 10.1016/j.cell.2020.12.020
Barish, G. D. et al. Bcl-6 and NF-κB cistromes mediate opposing regulation of the innate immune response. Genes Dev. 24, 2760–2765 (2010).
pubmed: 21106671 pmcid: 3003193 doi: 10.1101/gad.1998010
Perez-Rosado, A. et al. BCL6 represses NFκB activity in diffuse large B-cell lymphomas. J. Pathol. 214, 498–507 (2008).
pubmed: 18189332 doi: 10.1002/path.2279
Brunet, A. et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96, 857–868 (1999).
pubmed: 10102273 doi: 10.1016/S0092-8674(00)80595-4
Hatzi, K. et al. A hybrid mechanism of action for BCL6 in B cells defined by formation of functionally distinct complexes at enhancers and promoters. Cell Rep. 4, 578–588 (2013).
pubmed: 23911289 doi: 10.1016/j.celrep.2013.06.016
Renault, V. M. et al. The pro-longevity gene FoxO3 is a direct target of the p53 tumor suppressor. Oncogene 30, 3207–3221 (2011).
pubmed: 21423206 pmcid: 3136551 doi: 10.1038/onc.2011.35
Bradner, J. E., Hnisz, D. & Young, R. A. Transcriptional addiction in cancer. Cell 168, 629–643 (2017).
pubmed: 28187285 pmcid: 5308559 doi: 10.1016/j.cell.2016.12.013
Tsherniak, A. et al. Defining a cancer dependency map. Cell 170, 564–576.e16 (2017).
pubmed: 28753430 pmcid: 5667678 doi: 10.1016/j.cell.2017.06.010
Zou, Z., Ohta, T., Miura, F. & Oki, S. ChIP-Atlas 2021 update: a data-mining suite for exploring epigenomic landscapes by fully integrating ChIP-seq, ATAC-seq and Bisulfite-seq data. Nucleic Acids Res. https://doi.org/10.1093/nar/gkac199 (2022).
Hurtz, C. et al. Rationale for targeting BCL6 in MLL-rearranged acute lymphoblastic leukemia. Genes Dev. 33, 1265–1279 (2019).
pubmed: 31395741 pmcid: 6719625 doi: 10.1101/gad.327593.119
Winter, G. E. et al. BET bromodomain proteins function as master transcription elongation factors independent of CDK9 recruitment. Mol. Cell 67, 5–18.e19 (2017).
pubmed: 28673542 pmcid: 5663500 doi: 10.1016/j.molcel.2017.06.004
Adelman, K. & Lis, J. T. Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans. Nat. Rev. Genet. 13, 720–731 (2012).
pubmed: 22986266 pmcid: 3552498 doi: 10.1038/nrg3293
Creyghton, M. P. et al. Histone H3K27ac separates active from poised enhancers and predicts developmental state. Proc. Natl Acad. Sci. USA 107, 21931–21936 (2010).
pubmed: 21106759 pmcid: 3003124 doi: 10.1073/pnas.1016071107
Wang, Z. et al. Combinatorial patterns of histone acetylations and methylations in the human genome. Nat. Genet. 40, 897–903 (2008).
pubmed: 18552846 pmcid: 2769248 doi: 10.1038/ng.154
Whyte, W. A. et al. Master transcription factors and mediator establish super-enhancers at key cell identity genes. Cell 153, 307–319 (2013).
pubmed: 23582322 pmcid: 3653129 doi: 10.1016/j.cell.2013.03.035
Hnisz, D. et al. Super-enhancers in the control of cell identity and disease. Cell 155, 934–947 (2013).
pubmed: 24119843 doi: 10.1016/j.cell.2013.09.053
Huang, C., Hatzi, K. & Melnick, A. Lineage-specific functions of Bcl-6 in immunity and inflammation are mediated by distinct biochemical mechanisms. Nat. Immunol. 14, 380–388 (2013).
pubmed: 23455674 pmcid: 3604075 doi: 10.1038/ni.2543
Wang, X., Li, Z., Naganuma, A. & Ye, B. H. Negative autoregulation of BCL-6 is bypassed by genetic alterations in diffuse large B cell lymphomas. Proc. Natl Acad. Sci. USA 99, 15018–15023 (2002).
pubmed: 12407182 pmcid: 137537 doi: 10.1073/pnas.232581199
Pasqualucci, L. et al. Mutations of the BCL6 proto-oncogene disrupt its negative autoregulation in diffuse large B-cell lymphoma. Blood 101, 2914–2923 (2003).
pubmed: 12515714 doi: 10.1182/blood-2002-11-3387
Gearhart, M. D., Corcoran, C. M., Wamstad, J. A. & Bardwell, V. J. Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets. Mol. Cell. Biol. 26, 6880–6889 (2006).
pubmed: 16943429 pmcid: 1592854 doi: 10.1128/MCB.00630-06
Huang, C. et al. The BCL6 RD2 domain governs commitment of activated B cells to form germinal centers. Cell Rep. 8, 1497–1508 (2014).
pubmed: 25176650 pmcid: 4163070 doi: 10.1016/j.celrep.2014.07.059
Uhlen, M. et al. Proteomics. Tissue-based map of the human proteome. Science 347, 1260419 (2015).
pubmed: 25613900 doi: 10.1126/science.1260419
Davis, O. A. et al. Optimizing shape complementarity enables the discovery of potent tricyclic BCL6 inhibitors. J. Med. Chem. 65, 8169–8190 (2022).
pubmed: 35657291 pmcid: 9234963 doi: 10.1021/acs.jmedchem.1c02174
Bellenie, B. R. et al. Achieving in vivo target depletion through the discovery and optimization of benzimidazolone BCL6 degraders. J. Med. Chem. 63, 4047–4068 (2020).
pubmed: 32275432 pmcid: 7184563 doi: 10.1021/acs.jmedchem.9b02076
Ho, S. N., Boyer, S. H., Schreiber, S. L., Danishefsky, S. J. & Crabtree, G. R. Specific inhibition of formation of transcription complexes by a calicheamicin oligosaccharide: a paradigm for the development of transcriptional antagonists. Proc. Natl Acad. Sci. USA 91, 9203–9207 (1994).
pubmed: 7937742 pmcid: 44780 doi: 10.1073/pnas.91.20.9203
Corsello, S. M. et al. Discovering the anti-cancer potential of non-oncology drugs by systematic viability profiling. Nat. Cancer 1, 235–248 (2020).
pubmed: 32613204 pmcid: 7328899 doi: 10.1038/s43018-019-0018-6
McCoull, W. et al. Development of a novel B-cell lymphoma 6 (BCL6) PROTAC to provide insight into small molecule targeting of BCL6. ACS Chem. Biol. 13, 3131–3141 (2018).
pubmed: 30335946 doi: 10.1021/acschembio.8b00698
Stead, M. A. et al. Structure of the wild-type human BCL6 POZ domain. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 1101–1104 (2008).
pubmed: 19052359 pmcid: 2593701 doi: 10.1107/S1744309108036063
Martin, M. Cutadapt removes adapter sequences from high-throughput sequencing reads. EMBnet.journal 17, 10 (2011).
doi: 10.14806/ej.17.1.200
Bray, N. L., Pimentel, H., Melsted, P. & Pachter, L. Near-optimal probabilistic RNA-seq quantification. Nat. Biotechnol. 34, 525–527 (2016).
pubmed: 27043002 doi: 10.1038/nbt.3519
Love, M. I., Huber, W. & Anders, S. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol. 15, 550 (2014).
pubmed: 25516281 pmcid: 4302049 doi: 10.1186/s13059-014-0550-8
Zhu, A., Ibrahim, J. G. & Love, M. I. Heavy-tailed prior distributions for sequence count data: removing the noise and preserving large differences. Bioinformatics 35, 2084–2092 (2019).
pubmed: 30395178 doi: 10.1093/bioinformatics/bty895
Chen, E. Y. et al. Enrichr: interactive and collaborative HTML5 gene list enrichment analysis tool. BMC Bioinformatics 14, 128 (2013).
pubmed: 23586463 pmcid: 3637064 doi: 10.1186/1471-2105-14-128
Zhang, Y. et al. Model-based analysis of ChIP-seq (MACS). Genome Biol. 9, R137 (2008).
pubmed: 18798982 pmcid: 2592715 doi: 10.1186/gb-2008-9-9-r137
Li, H. et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics 25, 2078–2079 (2009).
pubmed: 19505943 pmcid: 2723002 doi: 10.1093/bioinformatics/btp352
Quinlan, A. R. & Hall, I. M. BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics 26, 841–842 (2010).
pubmed: 20110278 pmcid: 2832824 doi: 10.1093/bioinformatics/btq033
Ramírez, F. et al. deepTools2: a next generation web server for deep-sequencing data analysis. Nucleic Acids Res. 44, W160–W165 (2016).
pubmed: 27079975 pmcid: 4987876 doi: 10.1093/nar/gkw257
Amemiya, H. M., Kundaje, A. & Boyle, A. P. The ENCODE Blacklist: identification of problematic regions of the genome. Sci. Rep. https://doi.org/10.1038/s41598-019-45839-z (2019).
Bal, E. et al. Super-enhancer hypermutation alters oncogene expression in B cell lymphoma. Nature 607, 808–815 (2022).
pubmed: 35794478 pmcid: 9583699 doi: 10.1038/s41586-022-04906-8

Auteurs

Sai Gourisankar (S)

Department of Pathology, Stanford University, Stanford, CA, USA.
Department of Chemical Engineering, Stanford University, Stanford, CA, USA.

Andrey Krokhotin (A)

Department of Pathology, Stanford University, Stanford, CA, USA.

Wenzhi Ji (W)

Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, CA, USA.

Xiaofan Liu (X)

Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, CA, USA.

Chiung-Ying Chang (CY)

Department of Pathology, Stanford University, Stanford, CA, USA.

Samuel H Kim (SH)

Department of Pathology, Stanford University, Stanford, CA, USA.

Zhengnian Li (Z)

Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, CA, USA.

Wendy Wenderski (W)

Department of Pathology, Stanford University, Stanford, CA, USA.
Department of Developmental Biology, Stanford University, Stanford, CA, USA.

Juste M Simanauskaite (JM)

Department of Pathology, Stanford University, Stanford, CA, USA.

Haopeng Yang (H)

Department of Lymphoma & Myeloma, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Hannes Vogel (H)

Department of Pathology, Stanford University, Stanford, CA, USA.

Tinghu Zhang (T)

Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, CA, USA.

Michael R Green (MR)

Department of Lymphoma & Myeloma, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
ORCID: 0000-0001-6309-9472

Nathanael S Gray (NS)

Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, CA, USA. nsgray01@stanford.edu.
ORCID: 0000-0001-5354-7403

Gerald R Crabtree (GR)

Department of Pathology, Stanford University, Stanford, CA, USA. crabtree@stanford.edu.
Department of Developmental Biology, Stanford University, Stanford, CA, USA. crabtree@stanford.edu.
ORCID: 0000-0001-9685-7911

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Mort cellulaire › Mort cellulaire régulée › Apoptose › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cycle cellulaire › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes tumoraux › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Maladies du système immunitaire › Syndromes immunoprolifératifs › Syndromes lymphoprolifératifs › Lymphomes › Lymphome malin non hodgkinien › Lymphome B › Lymphome B diffus à grandes cellules › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Protéines proto-oncogènes c-bcl-6 › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Épigenèse génétique › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › Phénomènes génétiques › Structures génétiques › Génome › Composants de génome › Gènes › Composants de gène › Éléments de régulation transcriptionnelle › Régions promotrices (génétique) › Rewiring cancer drivers to activate apoptosis.
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Processus néoplasiques › Carcinogenèse › Rewiring cancer drivers to activate apoptosis.