The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification
Open accessAbstract
We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslational modification. The unique structure and genomic localization of histone Kcr suggest that it is mechanistically and functionally different from histone lysine acetylation (Kac). Specifically, in both human somatic and mouse male germ cell genomes, histone Kcr marks either active promoters or potential enhancers. In male germinal cells immediately following meiosis, Kcr is enriched on sex chromosomes and specifically marks testis-specific genes, including a significant proportion of X-linked genes that escape sex chromosome inactivation in haploid cells. These results therefore dramatically extend the repertoire of histone PTM sites and designate Kcr as a specific mark of active sex chromosome-linked genes in postmeiotic male germ cells.
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.
Integrity signals
Registry
Cites
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Histone crotonylation was previously shown to occur at the promoters or enhancers of gens that are actively transcribed, and play a role in spermatogenesis.111,179”
From Epigenetic regulation in major depression and other stress-related disorders: molecular mechanisms, clinical relevance and therapeutic potential (2023) · cites this paper as [179]
Experimental — accuracy not yet measuredIn the citing paper
“A number of functional studies have concentrated on histone lysine-crotonylation (Lys-cr) which is associated with active chromatin and overlaps with known sites of lysine-acetylation (Lys-ac)3,9.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [3]
In the citing paper
“Previous studies failed to detect significant decrotonylase activity for HDAC1/23,18 and this may be because they were using recombinant enzymes generated in isolation.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [3]
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
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398 · cited 1×
“As a control, we compared the Kcr distribution with previously obtained ChIP-seq results for H3K4me3 (marking gene promoters) and H3K4me1 (marking enhancers) distribution (Heintzman et al., 2007).”
ResultSelf-citationHistological and Histopathological Evaluation of the Testis
Russell, L. D., Ettlin, R. A., Hikim, A. P. S., & Clegg, E. D. (1993) · International Journal of Andrology · doi:10.1111/j.1365-2605.1993.tb01156.x · Cited by 2,249
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487
Self-citationHistones and histone modifications
Peterson, C. L., & Laniel, M.-A. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.007 · Cited by 1,313
A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
Wysocka, J., Swigut, T., Xiao, H., Milne, T. A., Kwon, S. Y., Landry, J., Kauer, M., Tackett, A. J., Chait, B. T., Badenhorst, P. W., et al. (2006) · Nature · doi:10.1038/nature04815 · Cited by 1,226
Self-citationExtraction, purification and analysis of histones
Shechter, D., Dormann, H. L., Allis, C. D., & Hake, S. B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.202 · Cited by 1,054
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,039
McGhee, J. D., & Felsenfeld, G. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.005343 · Cited by 976
Cited by
Sorted by citations
Metabolic regulation of gene expression by histone lactylation
Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371
Self-citationCancer epigenetics: from mechanism to therapy
Dawson, M. A., & Kouzarides, T. (2012) · Cell · doi:10.1016/j.cell.2012.06.013 · Cited by 3,203
MSFragger: ultrafast and comprehensive peptide identification in mass spectrometry–based proteomics
Kong, A. T., Leprevost, F. D. V., Avtonomov, D. M., Mellacheruvu, D., & Nesvizhskii, A. I. (2017) · Nature Methods · doi:10.1038/nmeth.4256 · Cited by 2,406
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Erasers of Histone Acetylation: The Histone Deacetylase EnzymesPreprint
Seto, E., & Yoshida, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018713 · Cited by 2,105
Modification of Enhancer Chromatin: What, How, and Why?
Calo, E., & Wysocka, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.038 · Cited by 1,457
Self-citationThe hallmarks of cancer metabolism: still emerging
Pavlova, N. N., Zhu, J., & Thompson, C. B. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.01.007 · Cited by 1,418
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Metabolic regulation of gene expression through histone acylations
Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,168
Self-citationHistone post-translational modifications - cause and consequence of genome function
Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00468-7 · Cited by 1,116
Histone Modifications and CancerPreprint
Audia, J. E., & Campbell, R. M. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019521 · Cited by 1,060
Histone core modifications regulating nucleosome structure and dynamics
Tessarz, P., & Kouzarides, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3890 · Cited by 1,018
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
Self-citationRegulation of nucleosome dynamics by histone modifications
Zentner, G. E., & Henikoff, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2470 · Cited by 923
Interplay between the Cancer Genome and Epigenome
Shen, H., & Laird, P. W. (2013) · Cell · doi:10.1016/j.cell.2013.03.008 · Cited by 949
Lateral Thinking: How Histone Modifications Regulate Gene Expression
Lawrence, M., Daujat, S., & Schneider, R. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.10.007 · Cited by 967
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844
“Our previous studies identified new lysine acylation modifications on histones (Chen et al., 2007; Tan et al., 2011; Xie et al., 2012), including lysine crotonylation and succinylation, revealing potential crosstalk between cellular physiology and gene transcription.”
BackgroundSelf-citationMolecular mechanisms and potential functions of histone demethylases
Kooistra, S. M., & Helin, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3327 · Cited by 913
Pal, S., & Tyler, J. K. (2016) · Science Advances · doi:10.1126/sciadv.1600584 · Cited by 860
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 774
New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?
Luger, K., Dechassa, M. L., & Tremethick, D. J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3382 · Cited by 738
Metabolic Regulation of Gene Expression by Histone Lysine β-Hydroxybutyrylation
Xie, Z., Zhang, D., Chung, D., Tang, Z., Huang, H., Dai, L., Qi, S., Li, J., Colak, G., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.036 · Cited by 744
Self-citationInterpreting the language of histone and DNA modifications
Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 792
Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation
Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659
Self-citationFeldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637
“Crotonyllysine was identified as a histone modification in several eukaryotic cells types and is associated with active promoters or enhancers (11).”
BackgroundChromatin modifiers and remodellers: regulators of cellular differentiation
Chen, T., & Dent, S. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3607 · Cited by 636
Status of Large-scale Analysis of Post-translational Modifications by Mass Spectrometry
Olsen, J. V., & Mann, M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.034181 · Cited by 607
Functions of bromodomain-containing proteins and their roles in homeostasis and cancer
Fujisawa, T., & Filippakopoulos, P. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.143 · Cited by 607
Fellows, R., Denizot, J., Stellato, C., Cuomo, A., Jain, P., Stoyanova, E., Balázsi, S., Hajnády, Z., Liebert, A., Kazakevych, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02651-5 · Cited by 568
Chromatin modifications as determinants of muscle stem cell quiescence and chronological aging
Liu, L., Cheung, T. H., Charville, G. W., Hurgo, B. M. C., Leavitt, T., Shih, J., Brunet, A., & Rando, T. A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.05.043 · Cited by 544
Epigenetic modifications of histones in cancer
Zhao, Z., & Shilatifard, A. (2019) · Genome biology · doi:10.1186/s13059-019-1870-5 · Cited by 591
Rivera, C. M., & Ren, B. (2013) · Cell · doi:10.1016/j.cell.2013.09.011 · Cited by 550
Self-citationChromatin dynamics during spermiogenesis
Rathke, C., Baarends, W. M., Awe, S., & Renkawitz‐Pohl, R. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.08.004 · Cited by 548
The impact of cellular metabolism on chromatin dynamics and epigenetics
Reid, M. A., Dai, Z., & Locasale, J. W. (2017) · Nature Cell Biology · doi:10.1038/ncb3629 · Cited by 515
Absence of a simple code: how transcription factors read the genome
Slattery, M., Zhou, T., Yang, L., Dantas Machado, A. C., Gordân, R., & Rohs, R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.07.002 · Cited by 537
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 521
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
Quantitative ChIP-Seq normalization reveals global modulation of the epigenome
Orlando, D. A., Chen, M. W., Brown, V. E., Solanki, S., Choi, Y. J., Olson, E. R., Fritz, C. C., Bradner, J. E., & Guenther, M. G. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.018 · Cited by 503
Regulation of chromatin and gene expression by metabolic enzymes and metabolites
Li, X., Egervári, G., Wang, Y., Berger, S. L., & Lu, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0029-7 · Cited by 501
Self-citationHistone lysine methyltransferases in biology and disease
Husmann, D., & Gozani, O. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0298-7 · Cited by 495
Comprehensive Catalog of Currently Documented Histone ModificationsPreprint
Zhao, Y., & Garcia, B. A. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a025064 · Cited by 484
Self-citationLysine 2-hydroxyisobutyrylation is a widely distributed active histone mark
Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1497 · Cited by 479
Self-citationEpigenetic mechanisms in neurological disease
Jakovcevski, M., & Akbarian, S. (2012) · Nature Medicine · doi:10.1038/nm.2828 · Cited by 450
CRISPR technologies for precise epigenome editing
Nakamura, M., Gao, Y., Dominguez, A. A., & Qi, L. S. (2021) · Nature Cell Biology · doi:10.1038/s41556-020-00620-7 · Cited by 456
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
SnapShot: histone modifications
Huang, H., Sabari, B. R., Garcia, B. A., Allis, C. D., & Zhao, Y. (2014) · Cell · doi:10.1016/j.cell.2014.09.037 · Cited by 439
Self-citationGenetic recombination is directed away from functional genomic elements in mice
Brick, K., Smagulova, F., Khil, P., Camerini-Otero, R. D., & Petukhova, G. V. (2012) · Nature · doi:10.1038/nature11089 · Cited by 414
Epigenetics and cardiovascular disease
Ordovás, J. M., & Smith, C. E. (2010) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2010.104 · Cited by 413
Noncoding Transcription at Enhancers: General Principles and Functional Models
Natoli, G., & Andrau, J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155459 · Cited by 418
Targeting Epigenetic Readers in Cancer
Dawson, M. A., Kouzarides, T., & Huntly, B. J. P. (2012) · New England Journal of Medicine · doi:10.1056/nejmra1112635 · Cited by 405
Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., et al. (2016) · Nature Communications · doi:10.1038/ncomms12235 · Cited by 400
Self-citationThe epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
Sadhukhan, S., Liu, X., Ryu, D., Nelson, O. D., Stupinski, J. A., Li, Z., Chen, W., Zhang, S., Weiss, R. S., Locasale, J. W., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519858113 · Cited by 376
The bromodomain interaction module
Filippakopoulos, P., & Knapp, S. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.045 · Cited by 404
Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation
Rothbart, S. B., Krajewski, K., Nady, N., Tempel, W., Xue, S., Badeaux, A. I., Baršytė-Lovejoy, D., Martínez-Márquez, J. Y., Bedford, M. T., Fuchs, S. M., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2391 · Cited by 403
Tang, X., Yang, T., Yu, D., Xiong, H., & Zhang, S. (2024) · Environment International · doi:10.1016/j.envint.2024.108535 · Cited by 407
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 383
Self-citationMolecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain
Li, Y., Sabari, B. R., Panchenko, T., Wen, H., Zhao, D., Guan, H., Wan, L., Huang, H., Tang, Z., Zhao, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.028 · Cited by 384
Self-citationLysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 375
Driver and Passenger Mutations in Cancer
Pon, J. R., & Marra, M. A. (2014) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040312 · Cited by 381
The emerging field of epigenetics in neurodegeneration and neuroprotection
Hwang, J.-Y., Aromolaran, K. A., & Zukin, R. S. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.46 · Cited by 353
Metabolic Regulation of Histone Post-Translational Modifications
Fan, J., Krautkramer, K. A., Feldman, J. L., & Denu, J. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500846u · Cited by 339
Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation
Fuhrmann, J., Clancy, K. W., & Thompson, P. R. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00003 · Cited by 325
Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324
Epigenetic regulation by gut microbiota
Woo, V., & Alenghat, T. (2022) · Gut Microbes · doi:10.1080/19490976.2021.2022407 · Cited by 338
Mechanisms and Dynamics of Protein Acetylation in Mitochondria
Baeza, J., Smallegan, M. J., & Denu, J. M. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.006 · Cited by 318
The role of histone modifications: from neurodevelopment to neurodiseases
Park, J., Lee, K., Kim, K., & Yi, S.-J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01078-9 · Cited by 333
Epigenetic mechanisms in tumorigenesis, tumor cell heterogeneity and drug resistance
Wilting, R. H., & Dannenberg, J. (2012) · Drug Resistance Updates · doi:10.1016/j.drup.2012.01.008 · Cited by 309
Epigenetic changes during aging and their reprogramming potential
Kane, A. E., & Sinclair, D. A. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1570075 · Cited by 283
Wei, W., Liu, X., Chen, J., Gao, S., Lu, L., Zhang, H., Ding, G., Wang, Z., Chen, Z., Shi, T., et al. (2017) · Cell Research · doi:10.1038/cr.2017.68 · Cited by 304
SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense
Zhou, L., Wang, F., Sun, R., Chen, X., Zhang, M., Xu, Q., Wang, Y., Wang, S., Xiong, Y., Guan, K., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541643 · Cited by 298
Signaling pathways in cancer metabolism: mechanisms and therapeutic targets
You, M., Xie, Z., Zhang, N., Zhang, Y., Xiao, D., Liu, S., Zhuang, W., Li, L., & Tao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01442-3 · Cited by 317
From profiles to function in epigenomics
Stricker, S. H., Köferle, A., & Beck, S. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.138 · Cited by 300
Identification of modified peptides using localization-aware open search
Yu, F., Teo, G. C., Kong, A. T., Haynes, S. E., Avtonomov, D. M., Geiszler, D., & Nesvizhskii, A. I. (2020) · Nature Communications · doi:10.1038/s41467-020-17921-y · Cited by 289
Chen, Z., Zhao, P., Li, C., Li, F., Xiang, D., Chen, Y., Akutsu, T., Daly, R. J., Webb, G. I., Zhao, Q., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab122 · Cited by 283
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Wu, X., Xu, M., Geng, M., Chen, S., Little, P. J., Xu, S., & Weng, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01439-y · Cited by 295
The functional diversity of protein lysine methylation
Lanouette, S., Mongeon, V., Figeys, D., & Couture, J. (2014) · Molecular Systems Biology · doi:10.1002/msb.134974 · Cited by 285
Epigenetic regulation of the histone-to-protamine transition during spermiogenesis
Bao, J., & Bedford, M. T. (2016) · Reproduction · doi:10.1530/rep-15-0562 · Cited by 299
Fatty acylation of proteins: The long and the short of it
Resh, M. D. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.05.002 · Cited by 286
Sirtuins in Epigenetic Regulation
Jing, H., & Lin, H. (2015) · Chemical Reviews · doi:10.1021/cr500457h · Cited by 276
Tropberger, P., Pott, S., Keller, C., Kamieniarz-Gdula, K., Caron, M. J., Richter, F. M., Li, G., Mittler, G., Liu, E. T., Bühler, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.032 · Cited by 290
Liu, R., Wu, J., Guo, H., Yao, W., Li, S., Lu, Y., Jia, Y., Liang, X., Tang, J., & Zhang, H. (2023) · MedComm · doi:10.1002/mco2.292 · Cited by 315
Combinatorial complexity in chromatin structure and function: revisiting the histone code
Rando, O. J. (2012) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.02.013 · Cited by 285
The Androgen Receptor in Health and Disease
Μatsumoto, T., Sakari, M., Okada, M., Yokoyama, A., Takahashi, S., Kouzmenko, A., & Kato, S. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183656 · Cited by 275
Wei, L., Yang, X., Wang, J., Wang, Z., Wang, Q., Ding, Y., & Yu, A. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02879-7 · Cited by 286
Compartmentalised acyl-CoA metabolism and roles in chromatin regulation
Trefely, S., Lovell, C. D., Snyder, N. W., & Wellen, K. E. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.005 · Cited by 272
Goudarzi, A., Zhang, D., Huang, H., Barral, S., Kwon, O. K., Qi, S., Tang, Z., Buchou, T., Vitte, A.-L., Tie-ming, H., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.014 · Cited by 281
Self-citationLiu, S., Yu, H., Liu, Y., Liu, X., Zhang, Y., Bu, C., Yuan, S., Chen, Z., Xie, G., Li, W., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.011 · Cited by 258
Self-citationModeling gene expression using chromatin features in various cellular contexts
Dong, X., Greven, M. C., Kundaje, A. B., Djebali, S., Brown, J., Cheng, C., Gingeras, T., Gerstein, M., Guigó, R., Birney, E., et al. (2012) · Genome biology · doi:10.1186/gb-2012-13-9-r53 · Cited by 263
Bromodomain‐dependent stage‐specific male genome programming by Brdt
Gaucher, J., Boussouar, F., Montellier, E., Curtet, S., Buchou, T., Bertrand, S. C., Héry, P., Jounier, S., Depaux, A., Vitte, A.-L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.233 · Cited by 283
Self-citationSirtuin catalysis and regulation
Feldman, J. L., Dittenhafer-Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.378877 · Cited by 248
Bromodomain biology and drug discovery
Zaware, N., & Zhou, M. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0309-8 · Cited by 264
The Substrate Specificity of Sirtuins
Bheda, P., Jing, H., Wolberger, C., & Lin, H. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014537 · Cited by 251
Histones: At the Crossroads of Peptide and Protein Chemistry
Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247
50+ years of eukaryotic transcription: an expanding universe of factors and mechanisms
Roeder, R. G. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0287-x · Cited by 246
Serine is a new target residue for endogenous ADP-ribosylation on histones
Leidecker, O., Bonfiglio, J. J., Colby, T., Zhang, Q., Atanassov, I., Žaja, R., Palazzo, L., Stockum, A., Ahel, I., & Matić, I. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2180 · Cited by 246
Protein acylation: mechanisms, biological functions and therapeutic targets
Shang, S., Liu, J., & Hua, F. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01245-y · Cited by 261
Lysine catabolism reprograms tumour immunity through histone crotonylation
Yuan, H., Wu, X., Wu, Q., Chatoff, A. G., Megill, E., Gao, J., Huang, T., Duan, T., Yang, K., Jin, C., et al. (2023) · Nature · doi:10.1038/s41586-023-06061-0 · Cited by 250
Self-citationThe Taf14 YEATS domain is a reader of histone crotonylation
Andrews, F. H., Shinsky, S. A., Shanle, E. K., Bridgers, J. B., Gest, A. M. M., Tsun, I. K., Krajewski, K., Shi, X., Strahl, B. D., & Kutateladze, T. G. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2065 · Cited by 248
Metadata
- Authors
- Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., Lu, Z., Ye, Z., Zhu, Q., Wysocka, J., Ye, Y., Khochbin, S., Ren, B., & Zhao, Y.
- Affiliations
- University of Chicago (US)
- University of California San Diego (US)
- Inserm (FR)
- Chinese Academy of Sciences (CN)
- Stanford Medicine (US)
- Corresponding author
- Zhao, Yingming
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 146
- Issue
- 6
- Pages
- 1016-1028
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3176443
- OpenAlex
- W2115862579
- Cited by
- 1,902
- References
- 61
- Citations by year
- 2026: 114 · 2025: 144 · 2024: 144 · 2023: 140 · 2022: 127 · 2021: 143 · 2020: 119 · 2019: 108 · 2018: 121 · 2017: 111 · 2016: 138 · 2015: 133 · 2014: 136 · 2013: 110 · 2012: 104
- FWCI
- 46.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- Agence Nationale de la Recherche
- Institut National Du Cancer
- National Institutes of Health
- Direction de l’hospitalisation et de l’offre de Soins
- National Cancer Institute (R01CA126832)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK082664)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- histone modifications, lysine acetylation, male germ cells, sex chromosome inactivation, X-linked genes, testis-specific genes, enhancers, promoter, meiosis, sex chromosomes
- MeSH terms
- Animals, Gene Expression Regulation, HeLa Cells, Histones, Humans, Lysine, Male, Meiosis, Protein Processing, Post-Translational, Testis, Histone Code, Mice
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
