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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

Lamins and Lamin-Binding Proteins in Functional Chromatin Organization

卷 9, 册 3-4, 1999, pp. 257-265
DOI: 10.1615/CritRevEukarGeneExpr.v9.i3-4.100
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摘要

Lamins are the major components of the nuclear lamina, a two-dimensional filamentous network at the periphery of the nucleus in higher eukaryotes, directly underlying the inner nuclear membrane. Several integral proteins of the inner nuclear membrane bind to lamins and may link the nuclear membrane to the core lamina network. The lamins and the lamin-binding proteins lamina-associated polypeptide (LAP)2β and lamin B receptor (LBR) have been described to bind to DNA or to interact with chromatin via histones, BAF-1, and HP1 chromodomain proteins, respectively, and may provide anchorage sites for chromatin fibers at the nuclear periphery. In addition, lamin A structures on intranuclear filaments, or lamin B in replication foci have been described in the nuclear interior, but their specific roles remain unclear. An isoform of the LAP2 protein family, LAP2α, has been found to colocalize with A-type lamins in the nucleoplasm and might be involved in intranuclear structure organization. In the course of cell-cycle-dependent dynamics of the nucleus in higher eukaryotes, lamins as well as lamin-binding proteins seem to possess important functions during various steps of post-mitotic nuclear reassembly, including cross-linking of chromatides, nuclear membrane targeting, nuclear lamina assembly, and the formation of a replication-competent nucleus.

对本文的引用
  1. Platts Adrian, Quayle Amelia, Krawetz Stephen, In-silico prediction and observations of nuclear matrix attachment, Cellular and Molecular Biology Letters, 11, 2, 2006. Crossref

  2. Bao Xiaomin, Girton Jack, Johansen Jørgen, Johansen Kristen M., The lamin Dm0 allele Ari3 acts as an enhancer of position effect variegation of the w m4 allele in Drosophila, Genetica, 129, 3, 2007. Crossref

  3. Brandizzi Federica, Irons Sarah L., Evans David E., The plant nuclear envelope: new prospects for a poorly understood structure, New Phytologist, 163, 2, 2004. Crossref

  4. Maraldi Nadir M., Lattanzi Giovanna, Capanni Cristina, Columbaro Marta, Mattioli Elisabetta, Sabatelli Patrizia, Squarzoni Stefano, Manzoli Francesco A., Laminopathies: A chromatin affair, Advances in Enzyme Regulation, 46, 1, 2006. Crossref

  5. Durzan D. J., Salmine and the homeotic integrity of early embryos of Norway spruce, Cytology and Genetics, 44, 2, 2010. Crossref

  6. Bowen Adam J., Corcoran Anne E., How chromatin remodelling allows shuffling of immunoglobulin heavy chain genes, Molecular BioSystems, 4, 8, 2008. Crossref

  7. Li Guohong, Tolstonog Genrich V., Traub Peter, InteractionIn Vitroof Type III Intermediate Filament Proteins with Z-DNA and B-Z-DNA Junctions, DNA and Cell Biology, 22, 3, 2003. Crossref

  8. Weber Peter J.A., Thymopoietin, in Wiley Encyclopedia of Molecular Medicine, 2002. Crossref

  9. Schöfer Christian, Weipoltshammer Klara, Gene dynamics and nuclear architecture during differentiation, Differentiation, 76, 1, 2008. Crossref

  10. Lyons David B., Lomvardas Stavros, Repressive histone methylation: A case study in deterministic versus stochastic gene regulation, Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 1839, 12, 2014. Crossref

  11. Puga Alvaro, Maier Andrew, Medvedovic Mario, The transcriptional signature of dioxin in human hepatoma HepG2 cells, Biochemical Pharmacology, 60, 8, 2000. Crossref

  12. Tolstonog Genrich V., Sabasch Michael, Traub Peter, Cytoplasmic Intermediate Filaments Are Stably Associated with Nuclear Matrices and Potentially Modulate Their DNA-Binding Function, DNA and Cell Biology, 21, 3, 2002. Crossref

  13. Verstraeten Valerie L. R. M., Lammerding Jan, Experimental techniques for study of chromatin mechanics in intact nuclei and living cells, Chromosome Research, 16, 3, 2008. Crossref

  14. Dahl K.N., Ribeiro A.J.S., 7.9 Biophysics of Nuclear Organization and Dynamics, in Comprehensive Biophysics, 2012. Crossref

  15. Cohen Merav, Gruenbaum Yosef, Lee Kenneth K, Wilson Katherine L, Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina, Trends in Biochemical Sciences, 26, 1, 2001. Crossref

  16. Gotzmann Josef, Gerner Christopher, Meissner Michael, Holzmann Klaus, Grimm Rudolf, Mikulits Wolfgang, Sauermann Georg, hNMP 200: A Novel Human Common Nuclear Matrix Protein Combining Structural and Regulatory Functions, Experimental Cell Research, 261, 1, 2000. Crossref

  17. Hobbs Cheryl A, Paul Barry A, Gilmour Susan K, Elevated levels of polyamines alter chromatin in murine skin and tumors without global changes in nucleosome acetylation1Abbreviations used: HAT, histone acetyltransferase; HDAC, histone deacetylase; ODC, ornithine decarboxylase; DFMO, α-difluoromethylornithine; SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis., Experimental Cell Research, 290, 2, 2003. Crossref

  18. References, in Molecular and Cellular Biomechanics, 2015. Crossref

  19. Krimm Isabelle, Östlund Cecilia, Gilquin Bernard, Couprie Joël, Hossenlopp Paul, Mornon Jean-Paul, Bonne Gisèle, Courvalin Jean-Claude, Worman Howard J, Zinn-Justin Sophie, The Ig-like Structure of the C-Terminal Domain of Lamin A/C, Mutated in Muscular Dystrophies, Cardiomyopathy, and Partial Lipodystrophy, Structure, 10, 6, 2002. Crossref

  20. Kalverda Bernike, Röling Michael D., Fornerod Maarten, Chromatin organization in relation to the nuclear periphery, FEBS Letters, 582, 14, 2008. Crossref

  21. Bala Shashi, Kumar Ajay, Soni Shivani, Sinha Sudha, Hanspal Manjit, Emp is a component of the nuclear matrix of mammalian cells and undergoes dynamic rearrangements during cell division, Biochemical and Biophysical Research Communications, 342, 4, 2006. Crossref

  22. Gruenbaum Yosef, Wilson Katherine L., Harel Amnon, Goldberg Michal, Cohen Merav, Review: Nuclear Lamins—Structural Proteins with Fundamental Functions, Journal of Structural Biology, 129, 2-3, 2000. Crossref

  23. Dechat Thomas, Vlcek Sylvia, Foisner Roland, Review: Lamina-Associated Polypeptide 2 Isoforms and Related Proteins in Cell Cycle-Dependent Nuclear Structure Dynamics, Journal of Structural Biology, 129, 2-3, 2000. Crossref

  24. Isaji Mamiko, Iwata Hisataka, Harayama Hiroshi, Miyake Masashi, The localization of LAP2β during pronuclear formation in bovine oocytes after fertilization or activation, Zygote, 14, 2, 2006. Crossref

  25. Yam Hin-Fai, Lam Dennis Shun-Chiu, Pang Chi-Pui, Changes of Nuclear Matrix in Long-Term Culture of Limbal Epithelial Cells, Cornea, 21, 2, 2002. Crossref

  26. Paramio Jesus M., Jorcano Jos� L., Beyond structure: do intermediate filaments modulate cell signalling?, BioEssays, 24, 9, 2002. Crossref

  27. Maxwell Christopher A, Hendzel Michael J, The integration of tissue structure and nuclear function, Biochemistry and Cell Biology, 79, 3, 2001. Crossref

  28. Smith Elizabeth R., George Sophia H., Kobetz Erin, Xu Xiang‐Xi, New biological research and understanding ofPapanicolaou's test, Diagnostic Cytopathology, 46, 6, 2018. Crossref

  29. Hofemeister Helmut, Weber Klaus, Stick Reimer, Gall Joseph, Association of Prenylated Proteins with the Plasma Membrane and the Inner Nuclear Membrane Is Mediated by the Same Membrane-targeting Motifs, Molecular Biology of the Cell, 11, 9, 2000. Crossref

  30. Lee Kenneth K., Gruenbaum Yosef, Spann Perah, Liu Jun, Wilson Katherine L., Gall Joseph, C. elegansNuclear Envelope Proteins Emerin, MAN1, Lamin, and Nucleoporins Reveal Unique Timing of Nuclear Envelope Breakdown during Mitosis, Molecular Biology of the Cell, 11, 9, 2000. Crossref

  31. Smith Elizabeth R., Capo-chichi Callinice D., Xu Xiang-Xi, Defective Nuclear Lamina in Aneuploidy and Carcinogenesis, Frontiers in Oncology, 8, 2018. Crossref

  32. Singh Namrata, Johnstone Duncan B., Martin Kayla A., Tempera Italo, Kaplan Mariana J., Denny Michael F., Alterations in nuclear structure promote lupus autoimmunity in a mouse model, Disease Models & Mechanisms, 2016. Crossref

  33. Foisner Roland, Dynamic Connections of Nuclear Envelope Proteins to Chromatin and the Nuclear Matrix, in Nuclear Envelope Dynamics in Embryos and Somatic Cells, 2002. Crossref

  34. Suzuki Yuka, Bilir Şükriye, Hatano Yu, Fukuda Tatsuhito, Mashiko Daisuke, Kobayashi Shouhei, Hiraoka Yasushi, Haraguchi Tokuko, Yamagata Kazuo, Nuclear formation induced by DNA-conjugated beads in living fertilised mouse egg, Scientific Reports, 9, 1, 2019. Crossref

  35. Ralle Thorsten, Grund Christine, Franke Werner W., Stick Reimer, Intranuclear membrane structure formations by CaaX-containing nuclear proteins, Journal of Cell Science, 117, 25, 2004. Crossref

  36. Bao Xiaomin, Zhang Weiguo, Krencik Robert, Deng Huai, Wang Yanming, Girton Jack, Johansen Jørgen, Johansen Kristen M., The JIL-1 kinase interacts with lamin Dm0 and regulates nuclear lamina morphology ofDrosophilanurse cells, Journal of Cell Science, 118, 21, 2005. Crossref

  37. Vlcek Sylvia, Korbei Barbara, Foisner Roland, Distinct Functions of the Unique C Terminus of LAP2α in Cell Proliferation and Nuclear Assembly, Journal of Biological Chemistry, 277, 21, 2002. Crossref

  38. Dechat T., Korbei B., Vaughan O.A., Vlcek S., Hutchison C.J., Foisner R., Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins, Journal of Cell Science, 113, 19, 2000. Crossref

  39. Foisner Roland, Intermediate Filaments, in eLS, 2001. Crossref

  40. Kiseleva Elena, Rutherford Sandra, Cotter Laura M., Allen Terence D., Goldberg Martin W., Steps of nuclear pore complex disassembly and reassembly during mitosis in earlyDrosophilaembryos, Journal of Cell Science, 114, 20, 2001. Crossref

  41. Gotzmann J., Vlcek S., Foisner R., Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2 alpha, Journal of Cell Science, 113, 21, 2000. Crossref

  42. Wong Xianrong, Cutler Jevon A, Hoskins Victoria E, Gordon Molly, Madugundu Anil K, Pandey Akhilesh, Reddy Karen L, Mapping the micro-proteome of the nuclear lamina and lamina-associated domains, Life Science Alliance, 4, 5, 2021. Crossref

  43. Kosak Steven T., Groudine Mark, Form follows function: the genomic organization of cellular differentiation, Genes & Development, 18, 12, 2004. Crossref

  44. Ahn Jinsook, Lee Jinwook, Jeong Soyeon, Kang So-mi, Park Bum-Joon, Ha Nam-Chul, Beta-strand-mediated dimeric formation of the Ig-like domains of human lamin A/C and B1, Biochemical and Biophysical Research Communications, 550, 2021. Crossref

  45. Haque Farhana, Lloyd David J., Smallwood Dawn T., Dent Carolyn L., Shanahan Catherine M., Fry Andrew M., Trembath Richard C., Shackleton Sue, SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton, Molecular and Cellular Biology, 26, 10, 2006. Crossref

  46. Benvenuti Silvia, Cramer Rainer, Bruce Jim, Waterfield Michael D, Jat Parmjit S, Identification of novel candidates for replicative senescence by functional proteomics, Oncogene, 21, 28, 2002. Crossref

  47. Kosak Steven T., Skok Jane A., Medina Kay L., Riblet Roy, Le Beau Michelle M., Fisher Amanda G., Singh Harinder, Subnuclear Compartmentalization of Immunoglobulin Loci During Lymphocyte Development, Science, 296, 5565, 2002. Crossref

  48. Sans-Fons M. Gloria, Sole Sonia, Sanfeliu Coral, Planas Anna M., Matrix Metalloproteinase-9 and Cell Division in Neuroblastoma Cells and Bone Marrow Macrophages, The American Journal of Pathology, 177, 6, 2010. Crossref

  49. Natesan Ramakrishnan, Gowrishankar Kripa, Kuttippurathu Lakshmi, Kumar P. B. Sunil, Rao Madan, Active Remodeling of Chromatin and Implications for In Vivo Folding, The Journal of Physical Chemistry B, 126, 1, 2022. Crossref

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