Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb
Open accessAbstract
The histone gene cluster on mouse chromosome 13 has been isolated and characterized. Using overlapping YAC clones containing histone genes from chromosome 13, a contig of approximately 2 Mb has been defined. It contains 45 histone genes, organized in three patches containing tightly clustered genes. An 80-kb patch (patch III) containing 12 histone genes is near one end of the contig, and a similar-sized patch (patch I) containing 15 histone genes is near the other end of the contig, located at least 500 kb from the central patch (patch II) of histone genes. The entire cluster contains six histone H1 genes, including the testis-specific histone H1t gene that maps to the middle of the cluster. All nine histone H3 genes in this cluster have been sequenced, and their level of expression determined. Each histone H3 gene is distinct, with five genes encoding the H3.2 protein subtype and four genes encoding the H3.1 protein. They are all expressed, with each histone H3 gene accounting for a small proportion of the total histone H3 mRNA.
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
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Separation of yeast chromosome-sized DNAs by pulsed field gradient gel electrophoresis
Schwartz, D. C., & Cantor, C. R. (1984) · Cell · doi:10.1016/0092-8674(84)90301-5 · Cited by 2,859 · see citing works
Transcription termination and 3′ processing: the end is in site!
Birnstiel, M. L., Busslinger, M., & Strub, K. (1985) · Cell · doi:10.1016/s0092-8674(85)80007-6 · Cited by 1,477 · see citing works
Kornberg, R. D. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004435 · Cited by 1,304 · see citing works
Riley, J. W., Butler, R., Ogilvie, D., Finniear, R. S., Jenner, D. C., Powell, S., Anand, R., Smith, J. C., & MARKHAM, A. F. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.10.2887 · Cited by 644 · see citing works
Heintz, N., Sive, H. L., & Roeder, R. G. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.4.539 · Cited by 457 · see citing works
Separation of basal histone synthesis from S-phase histone synthesis in dividing cells
Wu, R. S., & Bonner, W. M. (1981) · Cell · doi:10.1016/0092-8674(81)90415-3 · Cited by 360 · see citing works
Histone mRNA concentrations are regulated at the level of transcription and mRNA degradation.
Sittman, D. B., Graves, R. A., & Marzluff, W. F. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.7.1849 · Cited by 298 · see citing works
Frey, M. R., & Matera, A. G. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.5915 · Cited by 246 · see citing works
Mowry, K. L., & STEITZ, J. A. (1987) · Science · doi:10.1126/science.2825355 · Cited by 224 · see citing works
Arris, M. E. H., Böhni, R., Schneiderman, M. H., Ramamurthy, L., Schümperli, D., & Marzluff, W. F. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2416-2424.1991 · Cited by 218 · see citing works
Wells, D. E., & Kedes, L. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.2834 · Cited by 175 · see citing works
Mannironi, C., Bonner, W. M., & Hatch, C. L. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.22.9113 · Cited by 159 · see citing works
The structure of the human histone genes: Clustered but not tandemly repeated
Heintz, N., Zernik, M., & Roeder, R. G. (1981) · Cell · doi:10.1016/0092-8674(81)90092-1 · Cited by 152 · see citing works
Gick, O., Krämer, A., Keller, W., & Birnstiel, M. L. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04362.x · Cited by 139 · see citing works
Organization of human histone genes.
Sierra, F., Lichtler, A., Marashi, F., Rickles, R. J., Dyke, T. V., Clark, S. J., Wells, J. R. E., Stein, G., & Stein, J. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.1795 · Cited by 138 · see citing works
Histone 3' ends: essential and regulatory functions.
Marzluff, W. F. (1992) · PubMed · Cited by 119 · see citing works
A rapid procedure for colony screening using nylon filters
Buluwela, L., Forster, A. M., Boehm, T. L. J., & Rabbitts, T. H. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.1.452 · Cited by 117 · see citing works
Replacement Variant Histone Genes Contain Intervening Sequences
Brush, D., Dodgson, J. B., Choi, O.-R., Stevens, P. W., & Engel, J. D. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.6.1307-1317.1985 · Cited by 116 · see citing works
Inhibition of Protein Synthesis Stabilizes Histone mRNA
Stimac, E., Groppi, V. E., & Coffino, P. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.10.2082 · Cited by 113 · see citing works
Olson, M. V., Loughney, K., & Hall, B. D. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90267-5 · Cited by 101 · see citing works
Isolation of two clusters of mouse histone genes.
Sittman, D. B., Chiu, I., Pan, C. J., Cohn, R. H., Kedes, L., & Marzluff, W. F. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4078 · Cited by 86 · see citing works
Organization and expression of H1 histone and H1 replacement histone genes
Doenecke, D., Albig, W., Bouterfa, H., & Drabent, B. (1994) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240540409 · Cited by 86 · see citing works
Human histone genes map to multiple chromosomes.
Tripputi, P., Emanuel, B. S., Croce, C. M., Green, L., Stein, G. S., & Stein, J. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.10.3185 · Cited by 81 · see citing works
Soldati‐Favre, D., & Schümperli, D. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.4.1518 · Cited by 78 · see citing works
Differential expression of two clusters of mouse histone genes
Graves, R. A., Wellman, S. E., Chiu, I.-M., & Marzluff, W. F. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90211-6 · Cited by 77 · see citing works
Structure of a cluster of mouse histone genes
Sittman, D. B., Graves, R. A., & Marzluff, W. F. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.19.6679 · Cited by 76 · see citing works
A rat histone H4 gene closely associated with the testis-specific H1t gene
Grimes, S. R., Weisz-Carrington, P., Daum, H. A., Smith, J. M., Green, L., Wright, K. L., Stein, G. S., & Stein, J. L. (1987) · Experimental Cell Research · doi:10.1016/0014-4827(87)90293-x · Cited by 74 · see citing works
Two Chemically and Metabolically Distinct Forms of Calf Thymus Histone F3
Marzluff, W. F., Sanders, L. A., Miller, D. M., & McCarty, K. S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45485-9 · Cited by 73 · see citing works
A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences
Parseghian, M. H., Henschen, A., KRIEGLSTEIN, K. G., & Hamkalo, B. A. (1994) · Protein Science · doi:10.1002/pro.5560030406 · Cited by 70 · see citing works
Structure and expression of the mouse testicular H1 histone gene (H1t)
Drabent, B., Bode, C., & Doenecke, D. (1993) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(93)90162-7 · Cited by 57 · see citing works
Sequences of four mouse histone H3 genes: Implications for evolution of mouse histone genes
Taylor, J. D., Wellman, S. E., & Marzluff, W. F. (1986) · Journal of Molecular Evolution · doi:10.1007/bf02115580 · Cited by 54 · see citing works
Selection on silent sites in the rodent H3 histone gene family.
DeBry, R. W., & Marzluff, W. F. (1994) · Genetics · doi:10.1093/genetics/138.1.191 · Cited by 53 · see citing works
Histone-Gene Reiteration in the Genome of Mouse
Jacob, E. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10415.x · Cited by 50 · see citing works
Yang, Y. S., Brown, D. T., Wellman, S. E., & Sittman, D. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45499-3 · Cited by 46 · see citing works
Characterization of the 55-kb mouse histone gene cluster on chromosome 3.Preprint
Wang, Z. F., Tisovec, R., DeBry, R. W., Frey, M. R., Matera, A. G., & Marzluff, W. F. (1996) · Genome Research · doi:10.1101/gr.6.8.702 · Cited by 43 · see citing works
Liu, T.-J., Liu, L., & Marzluff, W. F. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.7.3023 · Cited by 40 · see citing works
Nucleotide sequence of two mouse histone H4 genes
Meier, V. S., Böhni, R., & Schümperli, D. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.2.795 · Cited by 39 · see citing works
The Efficiency of 3′-End Formation Contributes to the Relative Levels of Different Histone mRNAs
Liu, T. J., Levine, B. J., Skoultchi, A. I., & Marzluff, W. F. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.8.3499 · Cited by 38 · see citing works
Fluorescence in situ hybridization using digital imaging microscopy.
Ballard, S. G., & Ward, D. C. (1993) · Journal of Histochemistry & Cytochemistry · doi:10.1177/41.12.8245423 · Cited by 37 · see citing works
Structure and organization of the chicken H2B histone gene family
Grandy, D. K., & Dodgson, J. B. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.3.1063 · Cited by 35 · see citing works
Polyadenylated and 3′ processed mRNAs are transcribed from the mouse histone H2A.X gene
Nagata, T., Kato, T., Morita, T., Nozaki, M., KUBOTA, H. Y., Yagi, H., & Matsushiro, A. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.9.2441 · Cited by 34 · see citing works
Hurt, M. M., Bowman, T. L., & Marzluff, W. F. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.2929 · Cited by 31 · see citing works
Histone III. VI. Two forms of calf thymus histone III.
Patthy, L., & Smith, E. L. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41782-1 · Cited by 30 · see citing works
Isolation and characterization of two replication-dependent mouse H1 histone genes
Dong, Y., Sirotkin, A., Yang, Y.-S., Brown, D. T., Sittman, D. B., & Skoultchi, A. I. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.8.1421 · Cited by 28 · see citing works
Chodchoy, N., Levine, B. J., Sprecher, C. A., Skoultchi, A. I., & Marzluff, W. F. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.3.1039 · Cited by 27 · see citing works
A region in the coding sequence is required for high-level expression of murine histone H3 gene.
Hurt, M. M., Pandey, N. B., & Marzluff, W. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.12.4450 · Cited by 25 · see citing works
Single-copy flanking sequences in human histone gene clusters map to chromosomes 1 and 6
Allen, B. S., Stein, J. L., Stein, G. S., & D, H. O. M. (1991) · Genomics · doi:10.1016/0888-7543(91)90337-e · Cited by 25 · see citing works
Structure of a mouse histone-encoding gene cluster
Gruber, A., Streit, A., Reist, M., Benninger, P., Böhni, R., & Schümperli, D. (1990) · Gene · doi:10.1016/0378-1119(90)90377-4 · Cited by 24 · see citing works
Histone gene number and organisation inXenopus: Xenopus borealishas a homogeneous major cluster
Turner, P., & Woodland, H. R. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.4.971 · Cited by 23 · see citing works
Ivanova, V., Zimonjic, D. B., Popescu, N. C., & Bonner, W. M. (1994) · Human Genetics · doi:10.1007/bf00208289 · Cited by 19 · see citing works
Association of Histone H4 Genes with the Mammalian Testis-Specific H1t Histone Gene
Drabent, B., Kardalinou, E., Bode, C., & Doenecke, D. (1995) · DNA and Cell Biology · doi:10.1089/dna.1995.14.591 · Cited by 16 · see citing works
Fecker, L. F., Ekblom, P., Kurkinen, M. T., & Ekblom, M. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.6.2848-2854.1990 · Cited by 15 · see citing works
Organization of Xenopus histone gene variants within clusters and their transcriptional expression
Destrée, O., Bendig, M. M., de Laaf, R. T. M., & Koster, J. G. (1984) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(84)90016-2 · Cited by 14 · see citing works
The chicken histone gene family
Nakayama, T., Takechi, S., & Takami, Y. (1993) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(93)90189-c · Cited by 11 · see citing works
Nucleotide sequences of mouse histone genes H2A and H3.1
Kosciessa, U., & Doenecke, D. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.21.8861 · Cited by 10 · see citing works
Structure of a cluster of mouse histone genes
Brown, V. D., Wang, Z.-F., Williams, A. S., & Marzluff, W. F. (1996) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(96)00013-9 · Cited by 9 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Lennox, R.W. and L.H. Cohen. 1984. The H1 subtypes of mammals: Metabolic characteristics and tissue distribution. In Histone genes: Structure, organization and regulation (ed. G.S. Stein, J.L. Stein, and W.F. Marzluff), pp. 373-396.
- Zweidler A. 1984. Core histone variants of the mouse: Primary structure and expression. In Histone genes: Structure, organization and regulation (ed. G. Stein, W. Stein, and W. Marzluff), pp. 373-395.
Cited by
Sorted by citations
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 · see citing works
The Human and Mouse Replication-Dependent Histone Genes
Marzluff, W. F., Gongidi, P., Woods, K., Jin, J., & Maltais, L. J. (2002) · Genomics · doi:10.1006/geno.2002.6850 · Cited by 461 · see citing works
Histone H1 and its isoforms: Contribution to chromatin structure and function
Happel, N., & Doenecke, D. (2008) · Gene · doi:10.1016/j.gene.2008.11.003 · Cited by 424 · see citing works
H1 Linker Histones Are Essential for Mouse Development and Affect Nucleosome Spacing In Vivo
Fan, Y., Tv, N., Morin‐Kensicki, E., Zhao, J., Magnuson, T., Woodcock, C. L. F., & Skoultchi, A. I. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4559-4572.2003 · Cited by 325 · see citing works
Marzluff, W. F., & Duronio, R. J. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00387-3 · Cited by 265 · see citing works
Formation of the 3′ end of histone mRNA
Domiński, Z., & Marzluff, W. F. (1999) · Gene · doi:10.1016/s0378-1119(99)00367-4 · Cited by 225 · see citing works
Histone editing elucidates the functional roles of H3K27 methylation and acetylation in mammals
Sankar, A., Mohammad, F., Sundaramurthy, A. K., Wang, H., Lerdrup, M., Tatar, T., & Helin, K. (2022) · Nature Genetics · doi:10.1038/s41588-022-01091-2 · Cited by 152 · see citing works
Chromatin Organization in the Mammalian Nucleus
Gilbert, N., Gilchrist, S., & Bickmore, W. A. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)42007-5 · Cited by 151 · see citing works
Gene conversion drives GC content evolution in mammalian histones
Galtier, N. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(02)00002-1 · Cited by 145 · see citing works
Sànchez, R., & Marzluff, W. F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7093-7104.2002 · Cited by 138 · see citing works
Sullivan, E., Santiago, C., Parker, E. D., Dominski, Z., Yang, X., Lanzotti, D. J., Ingledue, T. C., Marzluff, W. F., & Duronio, R. J. (2001) · Genes & Development · doi:10.17615/dbcb-5f65 · Cited by 134 · see citing works
Normal Spermatogenesis in Mice Lacking the Testis-Specific Linker Histone H1t
Lin, Q., Sirotkin, A., & Skoultchi, A. I. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2122-2128.2000 · Cited by 132 · see citing works
Domiński, Z., Zheng, L.-X., Sànchez, R., & Marzluff, W. F. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3561 · Cited by 131 · see citing works
Dileep, V., Boix, C. A., Mathys, H., Marco, A., Welch, G. M., Meharena, H. S., Loon, A., Jeloka, R., Peng, Z., Bennett, D. A., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.038 · Cited by 130 · see citing works
Histones: genetic diversity and tissue-specific gene expression
Doenecke, D., Albig, W., Bode, C., Drabent, B., Franke, K., Gavénis, K., & Witt, O. (1997) · Histochemistry and Cell Biology · doi:10.1007/s004180050083 · Cited by 113 · see citing works
Human Histone Gene Organization: Nonregular Arrangement within a Large Cluster
Albig, W., Kioschis, P., Poustka, A., Meergans, K., & Doenecke, D. (1997) · Genomics · doi:10.1006/geno.1996.4592 · Cited by 105 · see citing works
Purifying Selection and Birth-and-death Evolution in the Histone H4 Gene Family
Piontkivska, H., Rooney, A. P., & Nei, M. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004127 · Cited by 102 · see citing works
Lanzotti, D. J., Kaygun, H., Yang, X., Duronio, R. J., & Marzluff, W. F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.2267-2282.2002 · Cited by 97 · see citing works
H2B Tyr37 phosphorylation suppresses expression of replication-dependent core histone genes
Mahajan, K. N., Fang, B., Koomen, J. M., & Mahajan, N. P. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2356 · Cited by 96 · see citing works
Molecular Evolution of the Nontandemly Repeated Genes of the Histone 3 Multigene Family
Rooney, A. P., Piontkivska, H., & Nei, M. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a003983 · Cited by 88 · see citing works
The mouse histone H1 genes: gene organization and differential regulation
Wang, Z.-F., Sirotkin, A., Buchold, G. M., Skoultchi, A. I., & Marzluff, W. F. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1166 · Cited by 87 · see citing works
Role of H1 linker histones in mammalian development and stem cell differentiation
Pan, C., & Fan, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.12.002 · Cited by 80 · see citing works
Male germline-specific histones in mouse and man
Churikov, D., Zalenskaya, I. A., & Zalensky, A. O. (2004) · Cytogenetic and Genome Research · doi:10.1159/000078190 · Cited by 79 · see citing works
Shopland, L. S., Byron, M., Stein, J. L., Lian, J. B., Stein, G. S., & Lawrence, J. B. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.3.565 · Cited by 79 · see citing works
Shah, P. C., Bertolino, E., & Singh, H. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.7105 · Cited by 61 · see citing works
Tissue-specific expression of histone H3 variants diversified after species separation
Maehara, K., Harada, A., Sato, Y., Matsumoto, M., Nakayama, K. I., Kimurâ, H., & Ohkawa, Y. (2015) · Epigenetics & Chromatin · doi:10.1186/s13072-015-0027-3 · Cited by 58 · see citing works
Doynova, M., Markworth, J. F., Cameron‐Smith, D., Vickers, M. H., & O'Sullivan, J. M. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0122-1 · Cited by 55 · see citing works
The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism
Müller, B., & Schümperli, D. (1997) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1997.0182 · Cited by 55 · see citing works
Lin, Q., Inselman, A. L., Han, X., Xu, H., Zhang, W., Handel, M. A., & Skoultchi, A. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400925200 · Cited by 54 · see citing works
Domiński, Z., Yang, X.-C., Raska, C. S., Santiago, C., Borchers, C. H., Duronio, R. J., & Marzluff, W. F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6648-6660.2002 · Cited by 52 · see citing works
Testis-specific transcriptional control
Grimes, S. R. (2004) · Gene · doi:10.1016/j.gene.2004.08.021 · Cited by 44 · see citing works
Characterization of the 55-kb mouse histone gene cluster on chromosome 3.Preprint
Wang, Z. F., Tisovec, R., DeBry, R. W., Frey, M. R., Matera, A. G., & Marzluff, W. F. (1996) · Genome Research · doi:10.1101/gr.6.8.702 · Cited by 43 · see citing works
Gene factories, microfunctionalization and the evolution of gene families
Hancock, J. M. (2005) · Trends in Genetics · doi:10.1016/j.tig.2005.08.008 · Cited by 41 · see citing works
The Human H2A and H2B Histone Gene Complement
Albig, W., Trappe, R. U., Kardalinou, E., Eick, S., & Doenecke, D. (1999) · Biological Chemistry · doi:10.1515/bc.1999.002 · Cited by 39 · see citing works
Expression of murine H1 histone genes during postnatal development
Franke, K., Drabent, B., & Doenecke, D. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00062-1 · Cited by 35 · see citing works
Visualization of individual cell division history in complex tissues using iCOUNT
Denoth‐Lippuner, A., Jaeger, B. N., Liang, T., Royall, L. N., Chie, S. E., Buthey, K., Machado, D., Korobeynyk, V. I., Kruse, M., Munz, C. M., et al. (2021) · Cell stem cell · doi:10.1016/j.stem.2021.08.012 · Cited by 29 · see citing works
Linker histone H1 FOO regulates the chromatin structure in mouse zygotes
Funaya, S., Ooga, M., Suzuki, M. G., & Aoki, F. (2018) · FEBS Letters · doi:10.1002/1873-3468.13175 · Cited by 27 · see citing works
Histone Gene Expression and Chromatin Structure during Spermatogenesis
Doenecke, D., Drabent, B., Bode, C., Bramlage, B., Franke, K., Gavénis, K., Kosciessa, U., & Witt, O. (1997) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-5913-9_4 · Cited by 26 · see citing works
van der Meijden, C. M. J., Vaughan, P. S., Staal, A., Albig, W., Doenecke, D., Stein, J. L., Stein, G. S., & van Wijnen, A. J. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00147-x · Cited by 25 · see citing works
Male Mice Lacking Three Germ Cell Expressed Genes Are Fertile1
Nayernia, K., Drabent, B., Adham, I. M., Möschner, M., Wolf, S., Meinhardt, A., & Engel, W. (2003) · Biology of Reproduction · doi:10.1095/biolreprod.103.018564 · Cited by 24 · see citing works
Scienski, K., Fay, J. C., & Conant, G. C. (2015) · Genome Biology and Evolution · doi:10.1093/gbe/evv216 · Cited by 24 · see citing works
Genetic Analysis of H1 Linker Histone Subtypes and Their Functions in Mice
Fan, Y., & Skoultchi, A. I. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)77005-0 · Cited by 22 · see citing works
Drosophila Octamer Elements and Pdm-1 Dictate the Coordinated Transcription of Core Histone Genes
Lee, M., Toh, L.-L., Yaw, L. P., & Luo, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.075358 · Cited by 19 · see citing works
Gupta, S., Marcel, N., Talwar, S., Garg, M., Indulaxmi, R., Perumalsamy, L. R., Sarin, A., & Shivashankar, G. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043718 · Cited by 19 · see citing works
Takami, Y., & Nakayama, T. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(97)00077-8 · Cited by 18 · see citing works
Dual role for the RNA-binding domain of Xenopus laevis SLBP1 in histone pre-mRNA processing
Ingledue, T. C., Domiński, Z., SÁNCHEZ, R., Erkmann, J. A., & MARZLUFF, W. F. (2000) · RNA · doi:10.1017/s1355838200000819 · Cited by 15 · see citing works
Genes for Polymorphic H1 Histones Are Linked in the Japanese Quail Genome
Pałyga, J. (1998) · Biochemical Genetics · doi:10.1023/a:1018756320718 · Cited by 14 · see citing works
Histone variants in skeletal myogenesis
Karthik, N., & Taneja, R. (2020) · Epigenetics · doi:10.1080/15592294.2020.1795606 · Cited by 12 · see citing works
Gleason, R. J., Guo, Y., Semancik, C. S., Ow, C., Lakshminarayanan, G., & Chen, X. (2023) · Science Advances · doi:10.1126/sciadv.adh0411 · Cited by 10 · see citing works
The Expression and Nuclear Deposition of Histone H3.1 in Murine Oocytes and Preimplantation Embryos
Kawamura, M., Akiyama, T., Tsukamoto, S., Suzuki, M. G., & Aoki, F. (2012) · Journal of Reproduction and Development · doi:10.1262/jrd.2012-074 · Cited by 10 · see citing works
Identification of the Protein That Interacts with the 3′ End of Histone mRNA
Marzluff, W. F., Domiński, Z., Whitfield, M. L., & Wang, Z.-F. (1997) · Elsevier eBooks · doi:10.1016/b978-012587545-5/50011-2 · Cited by 10 · see citing works
Physical Mapping of the Mouse Genome
Herman, G. E. (1998) · Methods · doi:10.1006/meth.1997.0573 · Cited by 9 · see citing works
The HIST1 Locus Escapes Reprogramming in Cloned Bovine Embryos
Min, B., Cho, S., Park, J. S., Jeon, K., & Kang, Y. (2016) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.026666 · Cited by 8 · see citing works
Cruz‐Cosme, R., Martinez, F. W. P., Perez, K. J., & Tang, Q. (2011) · Journal of General Virology · doi:10.1099/vir.0.033225-0 · Cited by 7 · see citing works
Shalhoub, V., Aslam, F., Breen, E. C., van Wijnen, A. J., Bortell, R., Stein, G. S., Stein, J. L., & Lian, J. B. (1998) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19980501)69:2 · Cited by 36 · see citing works
Asymmetrical deposition and modification of histone H3 variants are essential for zygote development
Kawamura, M., Funaya, S., Sugie, K., Suzuki, M. G., & Aoki, F. (2021) · Life Science Alliance · doi:10.26508/lsa.202101102 · Cited by 6 · see citing works
Comparative Analysis of Evolution in a Rodent Histone H2a Pseudogene
DeBry, R. W. (1998) · Journal of Molecular Evolution · doi:10.1007/pl00006312 · Cited by 6 · see citing works
Localization of the Human H3F3A Histone Gene to 1q41, outside of the Normal Histone Gene Clusters
Lin, X., & Wells, D. E. (1997) · Genomics · doi:10.1006/geno.1997.5037 · Cited by 5 · see citing works
The Genornic and Sequence Analysis of Rat Histone H2B Genes
Choi, Y., & Chae, C.-W. (1998) · DNA sequence · doi:10.3109/10425179809008476 · Cited by 2 · see citing works
Zimmerer, E. J., Carneal, J., Robertson, J. B., Ozturk, M., Cardiff, S., & Luo, M. (2000) · Biochemical Genetics · doi:10.1023/a:1002075821782 · Cited by 2 · see citing works
Spatially resolved mapping of histones reveals selective neuronal response in Rett syndrome
Schäfer, F., Rocco, G. D., Völker-Albert, M. C., Forné, I., Landsberger, N., Imhof, A., & Lahiri, S. (2026) · FEBS Journal · doi:10.1111/febs.70534 · Cited by 1 · see citing works
A vector system encoding histone H3 mutants facilitates manipulations of the neuronal epigenome
Warren, S., Xiong, S., Robles-Magallanes, D., & Baizabal, J. (2024) · Scientific Reports · doi:10.1038/s41598-024-74270-2 · Cited by 1 · see citing works
Oocyte-Specific Linker Histone in Mammalian Species
Tanaka, M., Teranishi, T., Miyakoshi, K., Jiaxue, W., Ueno, K., Matsumoto, T., Hattori, Y., & Yoshimura, Y. (2002) · Journal of Mammalian Ova Research · doi:10.1274/jmor.19.61 · Cited by 1 · see citing works
Putative Histone H2A Genes from a Red Alga, Griffithsia japonica
Lee, Y., & Lee, H. K. (2003) · ALGAE · doi:10.4490/algae.2003.18.3.191 · Cited by 1 · see citing works
Luong, M. X. (2003) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/10ah-dx47
Checkpoint Kinase Mediated Regulation of Histone Gene Expression in Response to Genotoxic Stress
Gajjalaiahvari, U. R. (2012)
Gleason, R. J., Semancik, C. S., Lakshminarayanan, G., & Chen, X. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.01.482564
3′ Processing of Animal Replication‐Dependent Histone mRNAs
Marzluff, W. F. (2026) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70035
Falcone, S., Raman, P., Marzluff, W. F., & Rieder, L. E. (2026) · Molecular Biology of the Cell · doi:10.1091/mbc.e26-04-0191
- Authors
- Wang, Z. F., Krasikov, T., Frey, M. R., Wang, J., Matera, A. G., & Marzluff, W. F.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- ORCID
- Venue
- Genome Research
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1996-08
- Volume
- 6
- Issue
- 8
- Pages
- 688-701
- ISSN
- 1088-9051 (ISSN-L)
- OpenAlex
- W2114053397
- Cited by
- 70
- References
- 56
- Citations by year
- 2026: 3 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 3 · 2013: 2 · 2012: 4
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genome Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- National Institutes of Health (5r01gm053034-18)
- National Institute of General Medical Sciences (GM 29832, R01GM029832, GM-53034)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Chromosomal and Genetic Variations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- histone gene clusters, mouse chromosome 13, histone H3 gene, histone H3.1, histone H3.2, gene expression levels, gene clusters, YAC contig, gene structure
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Chromosome Mapping, Multigene Family, Histones, Molecular Sequence Data, Sequence Alignment, Chromosomes, Artificial, Yeast, 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