Library Subscription: Guest
Critical Reviews™ in Eukaryotic Gene Expression

Published 6 issues per year

ISSN Print: 1045-4403

ISSN Online: 2162-6502

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.6 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.2 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.3 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00058 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.33 SJR: 0.345 SNIP: 0.46 CiteScore™:: 2.5 H-Index: 67

Indexed in

Histone H1 and Chromatin Higher-Order Structure

Volume 7, Issue 3, 1997, pp. 215-230
DOI: 10.1615/CritRevEukarGeneExpr.v7.i3.20
Get accessGet access

ABSTRACT

The linker histone H1, or its variants such as H5, have long thought to be involved in promoting the organization of chromatin into a higher-order structure, the 30 nm filament. However, the location of H1 in the filament, its role in filament formation and the structure of the 30 nm filament itself have all been controversial. This article reviews recent results that address these questions.

CITED BY
  1. Tsai Chih-Cheng, Fondell Joseph D, Nuclear Receptor Recruitment of Histone-Modifying Enzymes to Target Gene Promoters, in Nuclear Receptor Coregulators, 68, 2004. Crossref

  2. Leuba S.H., Zlatanova J., Karymov M.A., Bash R., Liu Y.-Z., Lohr D., Harrington R.E., Lindsay S.M., The Mechanical Properties of Single Chromatin Fibers Under Tension, Single Molecules, 1, 2, 2000. Crossref

  3. Brown David T, Izard Tina, Misteli Tom, Mapping the interaction surface of linker histone H10 with the nucleosome of native chromatin in vivo, Nature Structural & Molecular Biology, 13, 3, 2006. Crossref

  4. Vujatovic Olivera, Zaragoza Katrin, Vaquero Alejandro, Reina Oscar, Bernués Jordi, Azorín Fernando, Drosophila melanogaster linker histone dH1 is required for transposon silencing and to preserve genome integrity, Nucleic Acids Research, 40, 12, 2012. Crossref

  5. Nakano Toshiaki, Goto Shigeru, Lai Chia-Yun, Hsu Li-Wen, Kao Ying-Hsien, Lin Yu-Chun, Kawamoto Seiji, Chiang Kuei-Chen, Ohmori Naoya, Goto Takeshi, Sato Shuji, Jawan Bruno, Cheng Yu-Fan, Ono Kazuhisa, Chen Chao-Long, Experimental and Clinical Significance of Antinuclear Antibodies in Liver Transplantation, Transplantation, 83, 8, 2007. Crossref

  6. Rabbani Azra, Finn Ron M., Ausió Juan, The anthracycline antibiotics: antitumor drugs that alter chromatin structure, BioEssays, 27, 1, 2005. Crossref

  7. Kaur Jaspreet, Kaur Jyotdeep, Epigenomics, in OMICS, 2013. Crossref

  8. Jerzmanowski A, The linker histones, in Chromatin Structure and Dynamics: State-of-the-Art, 39, 2004. Crossref

  9. Prusov Andrey N., Kireev Igor I., Polyakov Vladimir Yu., Visible Light Irradiation of Ethidium Bromide–stained Interphase Nuclei Causes DNA–Protein Linking and Structural Stabilization of Nucleoprotein Complexes¶, Photochemistry and Photobiology, 78, 6, 2003. Crossref

  10. Hamilton Charlotte, Hayward Richard L., Gilbert Nick, Global chromatin fibre compaction in response to DNA damage, Biochemical and Biophysical Research Communications, 414, 4, 2011. Crossref

  11. Ausió Juan, Abbott D.Wade, The role of histone variability in chromatin stability and folding, in Chromatin Structure and Dynamics: State-of-the-Art, 39, 2004. Crossref

  12. Gilbert Nick, Gilchrist Susan, Bickmore Wendy A., , 242, 2004. Crossref

  13. Zlatanova Jordanka, van Holde Kensal, Linker histones versus HMG1/2: a struggle for dominance?, BioEssays, 20, 7, 1998. Crossref

  14. Staynov D. Z., Proykova Y. G., Topological constraints on the possible structures of the 30 nm chromatin fibre, Chromosoma, 117, 1, 2008. Crossref

  15. Drobná E., Bialková A., Šubík J., Transcriptional regulators of seven yeast species: Comparative genome analysis — Review, Folia Microbiologica, 53, 4, 2008. Crossref

  16. Kundu Sharmistha, Peterson Craig L., Role of chromatin states in transcriptional memory, Biochimica et Biophysica Acta (BBA) - General Subjects, 1790, 6, 2009. Crossref

  17. Thomas Jean, Chromatin, in Encyclopedia of Molecular Biology, 2002. Crossref

  18. Pedersen Anders Gorm, Baldi Pierre, Chauvin Yves, Brunak Søren, The biology of eukaryotic promoter prediction—a review, Computers & Chemistry, 23, 3-4, 1999. Crossref

  19. Thomas Jean, Histones, in Encyclopedia of Molecular Biology, 2002. Crossref

  20. Kepper Nick, Foethke Dietrich, Stehr Rene, Wedemann Gero, Rippe Karsten, Nucleosome Geometry and Internucleosomal Interactions Control the Chromatin Fiber Conformation, Biophysical Journal, 95, 8, 2008. Crossref

  21. Prusov Andrey N., Kireev Igor I., Polyakov Vladimir Yu., Visible Light Irradiation of Ethidium Bromide-stained Interphase Nuclei Causes DNA-Protein Linking and Structural Stabilization of Nucleoprotein Complexes¶, Photochemistry and Photobiology, 78, 6, 2007. Crossref

  22. Nakano Toshiaki, Goto Shigeru, Lai Chia-Yun, Hsu Li-Wen, Takaoka Yuki, Kawamoto Seiji, Chiang Kuei-Chen, Shimada Yayoi, Ohmori Naoya, Goto Takeshi, Sato Shuji, Ono Kazuhisa, Cheng Yu-Fan, Chen Chao-Long, Immunological aspects and therapeutic significance of an autoantibody against histone H1 in a rat model of concanavalin A-induced hepatitis, Immunology, 129, 4, 2010. Crossref

  23. Thomas J., Linker DNA, in Encyclopedia of Molecular Biology, 2002. Crossref

  24. Staynov Dontcho Z., The controversial 30 nm chromatin fibre, BioEssays, 30, 10, 2008. Crossref

  25. Kornberg Roger D, Eukaryotic transcriptional control, Trends in Genetics, 15, 12, 1999. Crossref

  26. Chadwick Brian P, Willard Huntington F, Barring gene expression after XIST: maintaining facultative heterochromatin on the inactive X, Seminars in Cell & Developmental Biology, 14, 6, 2003. Crossref

  27. Gencheva Marieta, Boa Simon, Fraser Ross, Simmen Martin W., A. Whitelaw C. Bruce, Allan James, In Vitro and in Vivo Nucleosome Positioning on the Ovine β-Lactoglobulin Gene Are Related, Journal of Molecular Biology, 361, 2, 2006. Crossref

  28. Khochbin Saadi, Histone H1 diversity: bridging regulatory signals to linker histone function, Gene, 271, 1, 2001. Crossref

  29. Staynov D.Z., DNase I footprinting of the nucleosome in whole nuclei, Biochemical and Biophysical Research Communications, 372, 1, 2008. Crossref

  30. Thomas Jean O, Histone H1: location and role, Current Opinion in Cell Biology, 11, 3, 1999. Crossref

  31. Kepert Jochen Felix, Tóth Katalin Fejes, Caudron Maïwen, Mücke Norbert, Langowski Jörg, Rippe Karsten, Conformation of Reconstituted Mononucleosomes and Effect of Linker Histone H1 Binding Studied by Scanning Force Microscopy, Biophysical Journal, 85, 6, 2003. Crossref

  32. Ashrafi M., Bathaie S.Z., Taghikhani M., Moosavi-Movahedi A.A., The effect of carotenoids obtained from saffron on histone H1 structure and H1–DNA interaction, International Journal of Biological Macromolecules, 36, 4, 2005. Crossref

  33. Grigoryev Sergei A, Higher-order folding of heterochromatin: Protein bridges span the nucleosome arrays, Biochemistry and Cell Biology, 79, 3, 2001. Crossref

  34. Dou Yali, Gorovsky Martin A., Phosphorylation of Linker Histone H1 Regulates Gene Expression In Vivo by Creating a Charge Patch, Molecular Cell, 6, 2, 2000. Crossref

  35. Bhattacharjee Rabindra N., Archer Trevor K., Transcriptional silencing of the mouse mammary tumor virus promoter through chromatin remodeling is concomitant with histone H1 phosphorylation and histone H3 hyperphosphorylation at M phase, Virology, 346, 1, 2006. Crossref

  36. Kornberg Roger D, Eukaryotic transcriptional control, Trends in Cell Biology, 9, 12, 1999. Crossref

  37. Bonet-Costa Carles, Vilaseca Marta, Diema Claudio, Vujatovic Olivera, Vaquero Alejandro, Omeñaca Núria, Castejón Lucía, Bernués Jordi, Giralt Ernest, Azorín Fernando, Combined bottom-up and top-down mass spectrometry analyses of the pattern of post-translational modifications of Drosophila melanogaster linker histone H1, Journal of Proteomics, 75, 13, 2012. Crossref

  38. Ng Marlee K., Cheung Peter, A brief histone in time: understanding the combinatorial functions of histone PTMs in the nucleosome context, Biochemistry and Cell Biology, 94, 1, 2016. Crossref

  39. Butler P.Jonathan G, Thomas Jean O, Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA, Journal of Molecular Biology, 281, 3, 1998. Crossref

  40. Flanagan Thomas W., Brown David T., Molecular dynamics of histone H1, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 1859, 3, 2016. Crossref

  41. Shahhoseini Maryam, Favaedi Raha, Baharvand Hossein, Sharma Vikram, Stunnenberg Hendrik G, Evidence for a dynamic role of the linker histone variant H1x during retinoic acid-induced differentiation of NT2 cells, FEBS Letters, 584, 22, 2010. Crossref

  42. Staynov Dontcho Z., Proykova Yana G., The sequentiallity of nucleosomes in the 30 nm chromatin fibre, FEBS Journal, 275, 15, 2008. Crossref

  43. Woodcock Christopher L, Dimitrov Stefan, Higher-order structure of chromatin and chromosomes, Current Opinion in Genetics & Development, 11, 2, 2001. Crossref

  44. De Lucia Filomena, Alilat Mohamed, Sivolob Andrei, Prunell Ariel, Nucleosome Dynamics. III. Histone Tail-dependent Fluctuation of Nucleosomes Between Open and Closed DNA Conformations. Implications for Chromatin Dynamics and the Linking Number Paradox. A Relaxation Study of Mononucleosomes on DNA Minicircles, Journal of Molecular Biology, 285, 3, 1999. Crossref

  45. Kornberg Roger D, Lorch Yahli, Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome, Cell, 98, 3, 1999. Crossref

  46. Ausió Juan, Analytical ultracentrifugation and the characterization of chromatin structure, Biophysical Chemistry, 86, 2-3, 2000. Crossref

  47. Kornberg Roger D, Eukaryotic transcriptional control, Trends in Biochemical Sciences, 24, 12, 1999. Crossref

  48. Beato Miguel, Vicent Guillermo P., Impact of chromatin structure and dynamics on PR signaling. The initial steps in hormonal gene regulation, Molecular and Cellular Endocrinology, 357, 1-2, 2012. Crossref

  49. Nakano Toshiaki, Goto Shigeru, Lai Chia-Yun, Hsu Li-Wen, Ono Kazuhisa, Kawamoto Seiji, Lin Yu-Chun, Kao Ying-Hsien, Chiang Kuei-Chen, Ohmori Naoya, Goto Takeshi, Sato Shuji, Tu Chieh-Hsien, Jawan Bruno, Cheng Yu-Fan, Chen Chao-Long, Impact of vaccine therapy using nuclear histone H1 on allograft survival in experimental organ transplantation, Transplant Immunology, 17, 3, 2007. Crossref

  50. Xu Na, Lu Xingwu, Kavi Harsh, Emelyanov Alexander V., Bernardo Travis J., Vershilova Elena, Skoultchi Arthur I., Fyodorov Dmitry V., BEN domain protein Elba2 can functionally substitute for linker histone H1 in Drosophila in vivo, Scientific Reports, 6, 1, 2016. Crossref

  51. von Walden Ferdinand, Liu Chang, Aurigemma Nicole, Nader Gustavo A., mTOR signaling regulates myotube hypertrophy by modulating protein synthesis, rDNA transcription, and chromatin remodeling, American Journal of Physiology-Cell Physiology, 311, 4, 2016. Crossref

  52. Brown David T, Histone H1 and the dynamic regulation of chromatin function, Biochemistry and Cell Biology, 81, 3, 2003. Crossref

  53. Lu Xu, Hansen Jeffrey C, Revisiting the structure and functions of the linker histone C-terminal tail domain, Biochemistry and Cell Biology, 81, 3, 2003. Crossref

  54. Carruthers Lenny M., Hansen Jeffrey C., The Core Histone N Termini Function Independently of Linker Histones during Chromatin Condensation, Journal of Biological Chemistry, 275, 47, 2000. Crossref

  55. Kinyamu H.K., Mackey L.C., Crusselle-Davis V.J., Archer T.K., Epigenetics and Chromatin Remodeling, in Comprehensive Toxicology, 2018. Crossref

  56. Raghuram Nikhil, Carrero Gustavo, Th’ng John, Hendzel Michael J., Molecular dynamics of histone H1This paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process., Biochemistry and Cell Biology, 87, 1, 2009. Crossref

  57. Misteli Tom, Gunjan Akash, Hock Robert, Bustin Michael, Brown David T., Dynamic binding of histone H1 to chromatin in living cells, Nature, 408, 6814, 2000. Crossref

  58. Zlatanova Jordanka, Caiafa Paola, Van Holde Kensal, Linker histone binding and displacement: versatile mechanism for transcriptional regulation, The FASEB Journal, 14, 12, 2000. Crossref

  59. Thompson J. M. T., Sivolob Andrei, Prunell Ariel, Nucleosome conformational flexibility and implications for chromatin dynamics, Philosophical Transactions of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences, 362, 1820, 2004. Crossref

  60. KASINSKY HAROLD E., LEWIS JOHN D., DACKS JOEL B., AUSLÓ JUAN, Origin of H1 linker histones, The FASEB Journal, 15, 1, 2001. Crossref

  61. Happel Nicole, Schulze Ekkehard, Doenecke Detlef, Characterisation of human histone H1x, Biological Chemistry, 386, 6, 2005. Crossref

  62. Kaur Jaspreet, Mukesh Manishi, Anand Akshay, Gene Expression, in Manufacturing of Gene Therapeutics, 2002. Crossref

  63. Kavi Harsh, Lu Xingwu, Xu Na, Bartholdy Boris A, Vershilova Elena, Skoultchi Arthur I, Fyodorov Dmitry V, A Genetic Screen and Transcript Profiling Reveal a Shared Regulatory Program for Drosophila Linker Histone H1 and Chromatin Remodeler CHD1, G3 Genes|Genomes|Genetics, 5, 4, 2015. Crossref

  64. Li Pingxin, Hu Jing, Wang Yanming, Methods for Analyzing Histone Citrullination in Chromatin Structure and Gene Regulation, in Transcriptional Regulation, 809, 2012. Crossref

  65. Sivolob Andrei, Lavelle Christophe, Prunell Ariel, Flexibility Of Nucleosomes On Topologically Constrained DNA, in Mathematics of DNA Structure, Function and Interactions, 150, 2009. Crossref

  66. Klemm Sandy L., Shipony Zohar, Greenleaf William J., Chromatin accessibility and the regulatory epigenome, Nature Reviews Genetics, 20, 4, 2019. Crossref

  67. George Eric M., Izard Tina, Anderson Stephen D., Brown David T., Nucleosome Interaction Surface of Linker Histone H1c Is Distinct from That of H10, Journal of Biological Chemistry, 285, 27, 2010. Crossref

  68. Hill David A., Imbalzano Anthony N., Human SWI/SNF Nucleosome Remodeling Activity Is Partially Inhibited by Linker Histone H1, Biochemistry, 39, 38, 2000. Crossref

  69. Raghuram Nikhil, Carrero Gustavo, Stasevich Timothy J., McNally James G., Th’ng John, Hendzel Michael J., Core Histone Hyperacetylation Impacts Cooperative Behavior and High-Affinity Binding of Histone H1 to Chromatin, Biochemistry, 49, 21, 2010. Crossref

  70. Widom J., STRUCTURE, DYNAMICS, AND FUNCTION OF CHROMATIN IN VITRO, Annual Review of Biophysics and Biomolecular Structure, 27, 1, 1998. Crossref

  71. Jedrusik Monika A., Vogt Stefan, Claus Peter, Schulze Ekkehard, A novel linker histone-like protein is associated with cytoplasmic filaments inCaenorhabditis elegans, Journal of Cell Science, 115, 14, 2002. Crossref

  72. Snijders Ambrosius P. L., Pongdam Sayampong, Lambert Stan J., Wood Christopher M., Baldwin John P., Dickman Mark J., Characterization of Post-Translational Modifications of the Linker Histones H1 and H5 from Chicken Erythrocytes Using Mass Spectrometry, Journal of Proteome Research, 7, 10, 2008. Crossref

  73. Pérez-Montero Salvador, Carbonell Albert, Morán Tomás, Vaquero Alejandro, Azorín Fernando, The Embryonic Linker Histone H1 Variant of Drosophila, dBigH1, Regulates Zygotic Genome Activation, Developmental Cell, 26, 6, 2013. Crossref

  74. Kamakaka Rohinton T., Biggins Sue, Histone variants: deviants?, Genes & Development, 19, 3, 2005. Crossref

  75. Xu Na, Emelyanov Alexander V, Fyodorov Dmitry V, Skoultchi Arthur I, Drosophila linker histone H1 coordinates STAT-dependent organization of heterochromatin and suppresses tumorigenesis caused by hyperactive JAK-STAT signaling, Epigenetics & Chromatin, 7, 1, 2014. Crossref

  76. Widlak Piotr, Kalinowska Magdalena, Parseghian Missag H., Lu Xu, Hansen Jeffrey C., Garrard William T., The Histone H1 C-Terminal Domain Binds to the Apoptotic Nuclease, DNA Fragmentation Factor (DFF40/CAD) and Stimulates DNA Cleavage, Biochemistry, 44, 21, 2005. Crossref

  77. Hansen Jeffrey C., Conformational Dynamics of the Chromatin Fiber in Solution: Determinants, Mechanisms, and Functions, Annual Review of Biophysics and Biomolecular Structure, 31, 1, 2002. Crossref

  78. Reale Anna, Malanga Maria, Zardo Giuseppe, Strom Roberto, Scovassi A. Ivana, Farina Benedetta, Caiafa Paola, In Vitro Induction of H1−H1 Histone Cross-Linking by Adenosine Diphosphate−Ribose Polymers, Biochemistry, 39, 34, 2000. Crossref

  79. Garcia Benjamin A., Busby Scott A., Barber Cynthia M., Shabanowitz Jeffrey, Allis C. David, Hunt Donald F., Characterization of Phosphorylation Sites on Histone H1 Isoforms by Tandem Mass Spectrometry, Journal of Proteome Research, 3, 6, 2004. Crossref

  80. Gilbert Nick, Allan James, Distinctive higher-order chromatin structure at mammalian centromeres, Proceedings of the National Academy of Sciences, 98, 21, 2001. Crossref

  81. Graziano Vito, Luo Guobin, Blainey Paul C., Pérez-Berná Ana J., McGrath William J., Flint S. Jane, San Martín Carmen, Xie X. Sunney, Mangel Walter F., Regulation of a Viral Proteinase by a Peptide and DNA in One-dimensional Space, Journal of Biological Chemistry, 288, 3, 2013. Crossref

  82. Gunjan Akash, Sittman Donald B., Brown David T., Core Histone Acetylation Is Regulated by Linker Histone Stoichiometry in Vivo , Journal of Biological Chemistry, 276, 5, 2001. Crossref

  83. Banks Geoffrey C., Deterding Leesa J., Tomer Kenneth B., Archer Trevor K., Hormone-mediated Dephosphorylation of Specific Histone H1 Isoforms, Journal of Biological Chemistry, 276, 39, 2001. Crossref

  84. Fan Yuhong, Nikitina Tatiana, Morin-Kensicki Elizabeth M., Zhao Jie, Magnuson Terry R., Woodcock Christopher L., Skoultchi Arthur I., H1 Linker Histones Are Essential for Mouse Development and Affect Nucleosome Spacing In Vivo, Molecular and Cellular Biology, 23, 13, 2003. Crossref

  85. Folco H. Diego, Freitag Michael, Ramón Ana, Temporini Esteban D., Alvarez María E., García Irene, Scazzocchio Claudio, Selker Eric U., Rosa Alberto L., Histone H1 Is Required for Proper Regulation of Pyruvate Decarboxylase Gene Expression in Neurospora crassa , Eukaryotic Cell, 2, 2, 2003. Crossref

  86. Song Xiaoyuan, Gorovsky Martin A., Unphosphorylated H1 Is Enriched in a Specific Region of the Promoter when CDC2 Is Down-Regulated during Starvation , Molecular and Cellular Biology, 27, 5, 2007. Crossref

  87. Horn Peter J., Peterson Craig L., Chromatin Higher Order Folding--Wrapping up Transcription, Science, 297, 5588, 2002. Crossref

  88. MacLean James A., Bettegowda Anilkumar, Kim Byung Ju, Lou Chih-Hong, Yang Seung-Min, Bhardwaj Anjana, Shanker Sreenath, Hu Zhiying, Fan Yuhong, Eckardt Sigrid, McLaughlin K. John, Skoultchi Arthur I., Wilkinson Miles F., The Rhox Homeobox Gene Cluster Is Imprinted and Selectively Targeted for Regulation by Histone H1 and DNA Methylation , Molecular and Cellular Biology, 31, 6, 2011. Crossref

  89. Ner Sarbjit S, Harrington Michael J, Grigliatti Thomas A, A Role for the Drosophila SU(VAR)3-9 Protein in Chromatin Organization at the Histone Gene Cluster and in Suppression of Position-Effect Variegation, Genetics, 162, 4, 2002. Crossref

  90. de Oca Rocío Montes, Lee Kenneth K., Wilson Katherine L., Binding of Barrier to Autointegration Factor (BAF) to Histone H3 and Selected Linker Histones Including H1.1, Journal of Biological Chemistry, 280, 51, 2005. Crossref

  91. Rippe Karsten, The Folding of the Nucleosome Chain, in Genome Organization and Function in the Cell Nucleus, 2011. Crossref

  92. König Peter, Braunfeld Michael B., Sedat John W., Agard David A., The three-dimensional structure of in vitro reconstituted Xenopus laevis chromosomes by EM tomography, Chromosoma, 116, 4, 2007. Crossref

Forthcoming Articles

PRMT6 promotes the immune evasion of gastric cancer via upregulating ANXA1 Liang Xu, Fenger Zhang, Binqi Yu, Shengnan Jia, Sunfu Fan PURPL promotes M2 macrophage polarization in lung cancer via regulating RBM4/xCT signaling Jipeng Guo, Chongwen Gong, Hao Wang SIAH1 promotes the pyroptosis of cardiomyocytes in diabetic cardiomyopathy via regulating IκB-α/NF-κB signaling Jinbin Wu, Yaoming Yan SLC7A2-mediated lysine catabolism inhibits immunosuppression in triple negative breast cancer Yuanyuan Sun, Yaqing Li, Chengying Jiang, Chenying Liu, Yuanming Song SIAH2-mediated degradation of ACSL4 inhibits the anti-tumor activity of CD8+ T cells in hepatocellular carcinoma Fangzheng Shu, Yuhua Shi, Xiangxiang Shan, Wenzhang Zha, Rengen Fan, Wanjiang Xue RBM15-mediated N6-methyl adenosine (m6A) modification of EZH2 drives the epithelial-mesenchymal transition of cervical cancer Ruixue Wang, Wenhua Tan Evidence-Based Storytelling and A Strategic Roadmap to Promote Cancer Prevention Via Adolescent HPV Vaccination in Northern New England Matthew Dugan, Gary Stein, Jan Carney, Sheila Clifford-Bova KDM4A-AS1 promotes cell proliferation, migration and invasion via the miR-4306/STX6 axis in hepatocellular carcinoma Wei Cao, Yuhan Ren, Ying Liu, Guoshu Cao, Zhen Chen, Fan Wang HDAC1-mediated downregulation of NEU1 exacerbates the aggressiveness of cervical cancer Nanzi Xie, Sisi Mei, Changlan Dai, Wei Chen Effect of miR-26b-5p on progression of acute myeloid leukemia by regulating USP48-mediated Wnt/β-catenin pathway Yu Xie, Lin Tan, Kun Wu, Deyun Li, Chengping Li
Begell Digital Portal Begell Digital Library eBooks Journals References & Proceedings Research Collections Prices and Subscription Policies Begell House Contact Us Language English 中文 Русский Português German French Spain