Elevated NSD3 histone methylation activity drives squamous cell lung cancer.

Animals Biocatalysis Carcinogenesis / genetics Carcinoma, Squamous Cell / genetics Female Histone-Lysine N-Methyltransferase / deficiency Histones / chemistry Humans Lung Neoplasms / genetics Male Methylation Mice Models, Molecular Mutation Nuclear Proteins / deficiency Receptor, Fibroblast Growth Factor, Type 1 / deficiency Xenograft Model Antitumor Assays

Journal

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

Informations de publication

Date de publication:
02 2021
Historique:
received: 30 04 2020
accepted: 23 12 2020
pubmed: 5 2 2021
medline: 20 3 2021
entrez: 4 2 2021
Statut: ppublish

Résumé

Amplification of chromosomal region 8p11-12 is a common genetic alteration that has been implicated in the aetiology of lung squamous cell carcinoma (LUSC)

Identifiants

DOI: 10.1038/s41586-020-03170-y PMID: 33536620 PMC: PMC7895461
pubmed: 33536620
doi: 10.1038/s41586-020-03170-y
pii: 10.1038/s41586-020-03170-y
pmc: PMC7895461
mid: NIHMS1657561
doi:

Substances chimiques

Histones 0
Nuclear Proteins 0
Histone-Lysine N-Methyltransferase EC 2.1.1.43
NSD3 protein, human EC 2.1.1.43
FGFR1 protein, human EC 2.7.10.1
Receptor, Fibroblast Growth Factor, Type 1 EC 2.7.10.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

504-508

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM139569
Pays : United States
Organisme : BLRD VA
ID : I01 BX000286
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM079641
Pays : United States
Organisme : NCI NIH HHS
ID : K99 CA255936
Pays : United States
Organisme : NCI NIH HHS
ID : P50 CA070907
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA236118
Pays : United States
Organisme : NCI NIH HHS
ID : R00 CA197816
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA236949
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG050997
Pays : United States
Organisme : NCI NIH HHS
ID : U54 CA224065
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : CommentIn
Type : CommentIn

Références

Balsara, B. R. et al. Comparative genomic hybridization analysis detects frequent, often high-level, overrepresentation of DNA sequences at 3q, 5p, 7p, and 8q in human non-small cell lung carcinomas. Cancer Res. 57, 2116–2120 (1997).
pubmed: 9187106
Tonon, G. et al. High-resolution genomic profiles of human lung cancer. Proc. Natl Acad. Sci. USA 102, 9625–9630 (2005).
doi: 10.1073/pnas.0504126102 pubmed: 15983384 pmcid: 1160520
Rooney, C. et al. Characterization of FGFR1 locus in sqNSCLC reveals a broad and heterogeneous amplicon. PLoS ONE 11, e0149628 (2016).
pubmed: 26905262 pmcid: 4764357 doi: 10.1371/journal.pone.0149628
Weiss, J. et al. Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer. Sci. Transl. Med. 2, 62ra93 (2010).
pubmed: 21160078 pmcid: 3990281 doi: 10.1126/scitranslmed.3001451
Lim, S. H. et al. Efficacy and safety of dovitinib in pretreated patients with advanced squamous non-small cell lung cancer with FGFR1 amplification: a single-arm, phase 2 study. Cancer 122, 3024–3031 (2016).
doi: 10.1002/cncr.30135 pubmed: 27315356
Yang, Z. Q., Liu, G., Bollig-Fischer, A., Giroux, C. N. & Ethier, S. P. Transforming properties of 8p11-12 amplified genes in human breast cancer. Cancer Res. 70, 8487–8497 (2010).
pubmed: 20940404 pmcid: 3089754 doi: 10.1158/0008-5472.CAN-10-1013
Turner-Ivey, B. et al. Development of mammary hyperplasia, dysplasia, and invasive ductal carcinoma in transgenic mice expressing the 8p11 amplicon oncogene NSD3. Breast Cancer Res. Treat. 164, 349–358 (2017).
pubmed: 28484924 pmcid: 5928774 doi: 10.1007/s10549-017-4258-9
Travis, W. D. Lung cancer pathology: current concepts. Clin. Chest Med. 41, 67–85 (2020).
doi: 10.1016/j.ccm.2019.11.001 pubmed: 32008630
Husmann, D. & Gozani, O. Histone lysine methyltransferases in biology and disease. Nat. Struct. Mol. Biol. 26, 880–889 (2019).
pubmed: 31582846 pmcid: 6951022 doi: 10.1038/s41594-019-0298-7
Landau, D. A. et al. Evolution and impact of subclonal mutations in chronic lymphocytic leukemia. Cell 152, 714–726 (2013).
pubmed: 23415222 pmcid: 3575604 doi: 10.1016/j.cell.2013.01.019
Qiao, Q. et al. The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation. J. Biol. Chem. 286, 8361–8368 (2011).
doi: 10.1074/jbc.M110.204115 pubmed: 21196496
Graham, S. E., Tweedy, S. E. & Carlson, H. A. Dynamic behavior of the post-SET loop region of NSD1: implications for histone binding and drug development. Protein Sci. 25, 1021–1029 (2016).
pubmed: 26940890 pmcid: 4838653 doi: 10.1002/pro.2912
Yang, S. et al. Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase. Genes Dev. 30, 1611–1616 (2016).
pubmed: 27474439 pmcid: 4973290 doi: 10.1101/gad.284323.116
Skene, P. J. & Henikoff, S. An efficient targeted nuclease strategy for high-resolution mapping of DNA binding sites. eLife 6, e21856 (2017).
pubmed: 28079019 pmcid: 5310842 doi: 10.7554/eLife.21856
Munoz, D. M. et al. CRISPR screens provide a comprehensive assessment of cancer vulnerabilities but generate false-positive hits for highly amplified genomic regions. Cancer Discov. 6, 900–913 (2016).
doi: 10.1158/2159-8290.CD-16-0178 pubmed: 27260157
Bass, A. J. et al. SOX2 is an amplified lineage-survival oncogene in lung and esophageal squamous cell carcinomas. Nat. Genet. 41, 1238–1242 (2009).
pubmed: 19801978 pmcid: 2783775 doi: 10.1038/ng.465
Zhang, Q. et al. Structural mechanism of transcriptional regulator NSD3 recognition by the ET domain of BRD4. Structure 24, 1201–1208 (2016).
pubmed: 27291650 pmcid: 4938737 doi: 10.1016/j.str.2016.04.019
Shen, C. et al. NSD3-short is an adaptor protein that couples BRD4 to the CHD8 chromatin remodeler. Mol. Cell 60, 847–859 (2015).
pubmed: 26626481 pmcid: 4688131 doi: 10.1016/j.molcel.2015.10.033
Bradbury, R. H. et al. Optimization of a series of bivalent triazolopyridazine based bromodomain and extraterminal inhibitors: the discovery of (3R)-4-[2-[4-[1-(3-methoxy-[1,2,4]triazolo[4,3-b]pyridazin-6-yl)-4-piperidyl]phenoxy]ethyl]-1,3-dimethyl-piperazin-2-one (AZD5153). J. Med. Chem. 59, 7801–7817 (2016).
doi: 10.1021/acs.jmedchem.6b00070 pubmed: 27528113
Siegel, R. L., Miller, K. D. & Jemal, A. Cancer statistics, 2019. CA Cancer J. Clin. 69, 7–34 (2019).
pubmed: 30620402 doi: 10.3322/caac.21551
Cochran, A. G., Conery, A. R. & Sims, R. J. III. Bromodomains: a new target class for drug development. Nat. Rev. Drug Discov. 18, 609–628 (2019).
pubmed: 31273347 doi: 10.1038/s41573-019-0030-7
Lin, K. H. et al. Using antagonistic pleiotropy to design a chemotherapy-induced evolutionary trap to target drug resistance in cancer. Nat. Genet. 52, 408–417 (2020).
pubmed: 32203462 pmcid: 7398704 doi: 10.1038/s41588-020-0590-9
Su, Y. et al. Novel NanoLuc substrates enable bright two-population bioluminescence imaging in animals. Nat. Methods 17, 852–860 (2020).
pubmed: 32661427 doi: 10.1038/s41592-020-0889-6
Kuo, A. J. et al. NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Mol. Cell 44, 609–620 (2011).
pubmed: 22099308 pmcid: 3222870 doi: 10.1016/j.molcel.2011.08.042
Lowary, P. T. & Widom, J. New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol. 276, 19–42 (1998).
pubmed: 9514715 doi: 10.1006/jmbi.1997.1494
Cheema, M. S. & Ausió, J. Analytical ultracentrifuge analysis of nucleosomes assembled from recombinant, acid-extracted, HPLC-purified histones. Methods Mol. Biol. 1528, 75–95 (2017).
pubmed: 27854017 doi: 10.1007/978-1-4939-6630-1_6
Luger, K., Rechsteiner, T. J. & Richmond, T. J. Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 119, 1–16 (1999).
pubmed: 10804500
Shi, X. et al. Modulation of p53 function by SET8-mediated methylation at lysine 382. Mol. Cell 27, 636–646 (2007).
pubmed: 17707234 pmcid: 2693209 doi: 10.1016/j.molcel.2007.07.012
Chen, S. et al. The PZP domain of AF10 senses unmodified H3K27 to regulate DOT1L-mediated methylation of H3K79. Mol. Cell 60, 319–327 (2015).
pubmed: 26439302 pmcid: 4609290 doi: 10.1016/j.molcel.2015.08.019
Mazur, P. K. et al. Combined inhibition of BET family proteins and histone deacetylases as a potential epigenetics-based therapy for pancreatic ductal adenocarcinoma. Nat. Med. 21, 1163–1171 (2015).
pubmed: 26390243 pmcid: 4959788 doi: 10.1038/nm.3952
Edelman, B. L. & Redente, E. F. Isolation and characterization of mouse fibroblasts. Methods Mol. Biol. 1809, 59–67 (2018).
doi: 10.1007/978-1-4939-8570-8_5 pubmed: 29987782
Liu, S. et al. METTL13 methylation of eEF1A increases translational output to promote tumorigenesis. Cell 176, 491–504.e21 (2019).
pubmed: 30612740 pmcid: 6499081 doi: 10.1016/j.cell.2018.11.038
Adams, J. R. et al. Cooperation between Pik3ca and p53 mutations in mouse mammary tumor formation. Cancer Res. 71, 2706–2717 (2011).
doi: 10.1158/0008-5472.CAN-10-0738 pubmed: 21324922
Ferone, G. et al. SOX2 is the determining oncogenic switch in promoting lung squamous cell carcinoma from different cells of origin. Cancer Cell 30, 519–532 (2016).
pubmed: 27728803 pmcid: 5065004 doi: 10.1016/j.ccell.2016.09.001
Krimpenfort, P. et al. p15Ink4b is a critical tumour suppressor in the absence of p16Ink4a. Nature 448, 943–946 (2007).
doi: 10.1038/nature06084 pubmed: 17713536
Hoch, R. V. & Soriano, P. Context-specific requirements for Fgfr1 signaling through Frs2 and Frs3 during mouse development. Development 133, 663–673 (2006).
doi: 10.1242/dev.02242 pubmed: 16421190
Skarnes, W. C. et al. A conditional knockout resource for the genome-wide study of mouse gene function. Nature 474, 337–342 (2011).
pubmed: 21677750 pmcid: 3572410 doi: 10.1038/nature10163
Raymond, C. S. & Soriano, P. High-efficiency FLP and PhiC31 site-specific recombination in mammalian cells. PLoS ONE 2, e162 (2007).
pubmed: 17225864 pmcid: 1764711 doi: 10.1371/journal.pone.0000162
Chu, V. T. et al. Efficient generation of Rosa26 knock-in mice using CRISPR/Cas9 in C57BL/6 zygotes. BMC Biotechnol. 16, 4 (2016).
pubmed: 26772810 pmcid: 4715285 doi: 10.1186/s12896-016-0234-4
Mazur, P. K. et al. SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer. Nature 510, 283–287 (2014).
pubmed: 24847881 pmcid: 4122675 doi: 10.1038/nature13320
Fraser, M. et al. Genomic hallmarks of localized, non-indolent prostate cancer. Nature 541, 359–364 (2017).
doi: 10.1038/nature20788 pubmed: 28068672
Shultz, L. D. et al. Subcapsular transplantation of tissue in the kidney. Cold Spring Harb. Protoc. 2014, 737–740 (2014).
pubmed: 24987138 pmcid: 4411958 doi: 10.1101/pdb.prot078089
Iwano, S. et al. Single-cell bioluminescence imaging of deep tissue in freely moving animals. Science 359, 935–939 (2018).
doi: 10.1126/science.aaq1067 pubmed: 29472486
Fushiki, H. et al. Quantification of mouse pulmonary cancer models by microcomputed tomography imaging. Cancer Sci. 100, 1544–1549 (2009).
doi: 10.1111/j.1349-7006.2009.01199.x pubmed: 19459854
Wang, Z. et al. SETD5-coordinated chromatin reprogramming regulates adaptive resistance to targeted pancreatic cancer therapy. Cancer Cell 37, 834–849.e13 (2020).
doi: 10.1016/j.ccell.2020.04.014 pubmed: 32442403 pmcid: 8187079
Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wüthrich, K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl Acad. Sci. USA 95, 13585–13590 (1998).
doi: 10.1073/pnas.95.23.13585 pubmed: 9811843 pmcid: 24862
Balwierz, W., Armata, J., Moryl-Bujakowska, A. & Pekacki, A. Is first salvage chemotherapy the last-line chemotherapy in children with Hodgkin’s disease? A tentative answer based on long observation of two patients. Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. 114, 789–796 (1987).
pubmed: 2453408
Li, Y. et al. Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor. Biomol. NMR Assign. 11, 225–229 (2017).
doi: 10.1007/s12104-017-9753-8 pubmed: 28808922
Shen, Y. & Bax, A. Protein structural information derived from NMR chemical shift with the neural network program TALOS-N. Methods Mol. Biol. 1260, 17–32 (2015).
pubmed: 25502373 pmcid: 4319698 doi: 10.1007/978-1-4939-2239-0_2
Lakomek, N. A., Ying, J. & Bax, A. Measurement of
pubmed: 22689066 pmcid: 3412688 doi: 10.1007/s10858-012-9626-5
Williamson, M. P. Using chemical shift perturbation to characterise ligand binding. Prog. Nucl. Magn. Reson. Spectrosc. 73, 1–16 (2013).
doi: 10.1016/j.pnmrs.2013.02.001 pubmed: 23962882
van Zundert, G. C. P. et al. The HADDOCK2.2 web server: user-friendly integrative modeling of biomolecular complexes. J. Mol. Biol. 428, 720–725 (2016).
doi: 10.1016/j.jmb.2015.09.014 pubmed: 26410586
Morrison, M. J. et al. Identification of a peptide inhibitor for the histone methyltransferase WHSC1. PLoS ONE 13, e0197082 (2018).
pubmed: 29742153 pmcid: 5942779 doi: 10.1371/journal.pone.0197082
Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 46 (W1), W296–W303 (2018).
pubmed: 29788355 pmcid: 6030848 doi: 10.1093/nar/gky427
Zhang, Y. et al. Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation. Sci. Rep. 7, 43906 (2017).
pubmed: 28256625 pmcid: 5335568 doi: 10.1038/srep43906
Tisi, D. et al. Structure of the epigenetic oncogene MMSET and inhibition by N-alkyl sinefungin derivatives. ACS Chem. Biol. 11, 3093–3105 (2016).
doi: 10.1021/acschembio.6b00308 pubmed: 27571355
Kim, D., Langmead, B. & Salzberg, S. L. HISAT: a fast spliced aligner with low memory requirements. Nat. Methods 12, 357–360 (2015).
pubmed: 25751142 pmcid: 4655817 doi: 10.1038/nmeth.3317
Frankish, A. et al. GENCODE reference annotation for the human and mouse genomes. Nucleic Acids Res. 47 (D1), D766–D773 (2019).
doi: 10.1093/nar/gky955 pubmed: 30357393
Liao, Y., Smyth, G. K. & Shi, W. featureCounts: an efficient general purpose program for assigning sequence reads to genomic features. Bioinformatics 30, 923–930 (2014).
doi: 10.1093/bioinformatics/btt656 pubmed: 24227677
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
Subramanian, A. et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc. Natl Acad. Sci. USA 102, 15545–15550 (2005).
pubmed: 16199517 pmcid: 1239896 doi: 10.1073/pnas.0506580102
Cancer Genome Atlas Research Network. Comprehensive genomic characterization of squamous cell lung cancers. Nature 489, 519–525 (2012).
doi: 10.1038/nature11404
Gao, J. et al. Integrative analysis of complex cancer genomics and clinical profiles using the cBioPortal. Sci. Signal. 6, pl1 (2013).
pubmed: 23550210 pmcid: 4160307 doi: 10.1126/scisignal.2004088
Cerami, E. et al. The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data. Cancer Discov. 2, 401–404 (2012).
doi: 10.1158/2159-8290.CD-12-0095 pubmed: 22588877
Hainer, S. J. & Fazzio, T. G. High-resolution chromatin profiling using CUT&RUN. Curr. Protoc. Mol. Biol. 126, e85 (2019).
pubmed: 30688406 pmcid: 6422702 doi: 10.1002/cpmb.85
Zhu, Q., Liu, N., Orkin, S. H. & Yuan, G. C. CUT&RUNTools: a flexible pipeline for CUT&RUN processing and footprint analysis. Genome Biol. 20, 192 (2019).
pubmed: 31500663 pmcid: 6734249 doi: 10.1186/s13059-019-1802-4
Bolger, A. M., Lohse, M. & Usadel, B. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30, 2114–2120 (2014).
pubmed: 24695404 pmcid: 4103590 doi: 10.1093/bioinformatics/btu170
Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357–359 (2012).
pubmed: 22388286 pmcid: 3322381 doi: 10.1038/nmeth.1923
Shen, L., Shao, N., Liu, X. & Nestler, E. ngs.plot: Quick mining and visualization of next-generation sequencing data by integrating genomic databases. BMC Genomics 15, 284 (2014).
pubmed: 24735413 pmcid: 4028082 doi: 10.1186/1471-2164-15-284
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

Auteurs

Gang Yuan (G)

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

Natasha M Flores (NM)

Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Simone Hausmann (S)

Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Shane M Lofgren (SM)

Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Vladlena Kharchenko (V)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.

Maria Angulo-Ibanez (M)

Department of Medicine, Stanford University School of Medicine, Stanford, CA, USA.
Geriatric Research, Education, and Clinical Center, Veterans Affairs Palo Alto Health Care System, Palo Alto, CA, USA.

Deepanwita Sengupta (D)

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

Xiaoyin Lu (X)

Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Iwona Czaban (I)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.
ORCID: 0000-0002-8038-1573

Dulat Azhibek (D)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.

Silvestre Vicent (S)

University of Navarra, Center for Applied Medical Research, Pamplona, Spain.

Wolfgang Fischle (W)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.

Mariusz Jaremko (M)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.

Bingliang Fang (B)

Department of Thoracic and Cardiovascular Surgery, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Ignacio I Wistuba (II)

Department of Translational Molecular Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Katrin F Chua (KF)

Department of Medicine, Stanford University School of Medicine, Stanford, CA, USA.
Geriatric Research, Education, and Clinical Center, Veterans Affairs Palo Alto Health Care System, Palo Alto, CA, USA.
ORCID: 0000-0003-3821-4226

Jack A Roth (JA)

Department of Thoracic and Cardiovascular Surgery, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
ORCID: 0000-0002-8955-1313

John D Minna (JD)

Hamon Center for Therapeutic Oncology Research, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA.

Ning-Yi Shao (NY)

Faculty of Health Sciences, University of Macau, Macau SAR, China. nshao@um.edu.mo.
ORCID: 0000-0003-4231-828X

Łukasz Jaremko (Ł)

Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia. lukasz.jaremko@kaust.edu.sa.
ORCID: 0000-0001-7684-9359

Pawel K Mazur (PK)

Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA. pkmazur@mdanderson.org.
ORCID: 0000-0002-5820-8344

Or Gozani (O)

Department of Biology, Stanford University, Stanford, CA, USA. ogozani@stanford.edu.
ORCID: 0000-0002-1365-4463

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Métabolisme › Biocatalyse › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Processus néoplasiques › Carcinogenèse › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Tumeurs › Tumeurs par type histologique › Tumeurs épithéliales épidermoïdes et glandulaires › Tumeurs épidermoïdes › Carcinome épidermoïde › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Protein Methyltransferases › Histone méthyltransférases › Histone-lysine N-methyltransferase › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Histone › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Maladies de l'appareil respiratoire › Tumeurs de l'appareil respiratoire › Tumeurs du poumon › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Métabolisme › Alkylation › Méthylation › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines nucléaires › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur facteur croissance › Récepteur facteur croissance fibroblaste › Récepteur FGFR1 › Elevated NSD3 histone methylation activity...
questionsmedicales.fr › Techniques d'investigation › Transplantation tumorale › Tests d'activité antitumorale sur modèle de xénogreffe › Elevated NSD3 histone methylation activity...