Alberts, B. ら (中村桂子・松原謙一 監訳) (2010) 『細胞の分子生物学 (第5版) 』ニュートンプレス.
Clamp, M. et al. (2007) Distinguishing protein-coding and noncoding genes in the human genome. Proc. Natl. Acad. Sci. USA, 104 : 19428-19433.
Henking, H. (1891) Unlersuehungen ueber die ersten Entwicklungsvorgange in den Eiern der Insekten. II. Ueber Spermatogenese und deren Beziehung zur Entwickelung bei Pyrrhocoris apterus L. Zeitschrift fur wissenschaftliche Zoologie, 51 : 685-736.
Stevens, N. M. (1905) Studies in spermatogenesis with especial reference to the "accessory chromosome". Carnegie Institute Report 36. (Washington, D. C.)
Richardson, B. E., Lehmann, R. (2010) Mechanisms guiding primordial germ cell migration : strategies from different organisms. Nat. Rev. Mol. Cell Biol., 11 : 37-49.
Chou, P. Y., Fasman, G. D. (1974) Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry, 13 : 211-222.
Wilson, K. P. et al. (1996) Crystal structure of p38 mitogen-activated protein kinase. J. Biol. Chem., 271 : 27696-27700.
Lujan, S. A. et al. (2016) DNA polymerases divide the labor of genome replication. Trends Cell Biol., 26 : 640-654.
Johnson, R. E. et al. (2015) A major role of DNA polymerase δ in replication of both the leading and lagging DNA strands. Mol. Cell. Jul., 59 : 163-175.
Jin, Y. H. et al. (2001) The 3'→5' exonuclease of DNA polymerase delta can substitute for the 5' flap endonuclease Rad27/Fen1 in processing Okazaki fragments and preventing genome instability. Proc. Natl. Acad. Sci. USA, 98 : 5122-5127.
Chen, R., Wold, M. S. (2014) Replication protein A : single-stranded DNA's first responder : dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair. Bioessays, 36 : 1156-1161.
Kunkel, T., Erie, D. A. (2005) DNA mismatch repair. Annu. Rev. Biochem., 74 : 681-710.
Pluciennik, A. et al. (2010) PCNA function in the activation and strand direction of MutLα endonuclease in mismatch repair. Proc. Natl. Acad. Sci. USA, 107 : 16066-16071.
Weigel, C. et al. (1997) DnaA protein binding to individual DnaA boxes in the Escherichia coli replication origin, oriC. EMBO J., 16 : 6574-6583.
Messer, W. (2002) The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol. Rev., 26 : 355-374.
Nieduszynski, C.A. et al. (2006) Genome-wide identification of replication origins in yeast by comparative genomics. Genes Dev., 20 : 1874-1879.
Kawakami, H. et al. (2015) Specific binding of eukaryotic ORC to DNA replication origins depends on highly conserved basic residues. Sci. Rep., 5 : 14929.
Masumoto, H. et al. (2002) S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast. Nature, 415 : 651-655.
Tanaka, S. et al. (2007) CDK-dependent phosphorylation of Sld2 and Sld3 initiates DNA replication in budding yeast. Nature, 445 : 328-332.
DePamphilis, M.L. (2016) Genome duplication at the beginning of mammalian development. Curr. Top Dev. Biol., 120 : 55-102.
Leonard, A. C., Mechali, M. (2013) DNA replication origins. Cold Spring Harb. Perspect Biol., 5 : a010116.
Cook, J. G. et al. (2002) Analysis of Cdc6 function in the assembly of mammalian prereplication complexes. Proc. Natl. Acad. Sci. USA, 99 : 1347-1352.
Bell, S. P., Kaguni, J. M. (2013) Helicase loading at chromosomal origins of replication. Cold Spring Harb. Perspect. Biol., 5. pii : a010124.
Chistol, G., Walter, J. C. (2015) Single-molecule visualization of MCM2-7 DNA loading : Seeing is believing. Cell, 161 : 429-430.
Marzluff, W. F. (2005) Metazoan replication-dependent histone mRNAs : a distinct set of RNA polymerase II transcripts. Curr. Opi. Cell Biol., 17 : 274-280.
Mannironi, C. et al. (1989) H2A.X, a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals. Nucleic Acids Res., 17 : 9113-9126
Harley, C. B. et al. (1990) Telomeres shorten during ageing of human fibroblasts. Nature, 345 : 458-460.
Yu, G. L. et al. (1990) In vivo alteration of telomere sequences and senescence caused by mutated Tetrahymena telomerase RNAs. Nature, 344 : 126-132.
Siefert, J. C. et al. (2015) Cell cycle control in the early embryonic development of aquatic animal species. Comp. Biochem. Physiol. C Toxicol. Pharmacol., 178 : 8-15.
Elledge, S. J. (1996) Cell cycle checkpoints : preventing an identity crisis. Science, 274 : 1664-1672.
Gladden, A. B., Diehl, J. A. (2003) The cyclin D1-dependent kinase associates with the pre-replication complex and modulates RB. MCM7 binding. J. Biol. Chem., 278 : 9754-9860.
Lunn, C. L. et al. (2010) Activation of Cdk2/Cyclin E complexes is dependent on the origin of replication licensing factor Cdc6 in mammalian cells. Cell Cycle, 9 : 4533-4541.
Chu, I. M. et al. (2008) The Cdk inhibitor p27 in human cancer : prognostic potential and relevance to anticancer therapy. Nat. Rev. Cancer, 8 : 253-267.
Xie, C. M. et al. (2013) Role of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases in skin cancer. J. Genet. Genomics, 40 : 97-106.
Bendris, N. et al. (2011) Cyclin A2 mutagenesis analysis : a new insight into CDK activation and cellular localization requirements. PLoS One. 6 : e22879.
Lin, D. I. et al. (2006) Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF (FBX4-alphaB crystallin) complex. Mol. Cell, 24 : 355-366.
Lee, W. H. et al. (1987) The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNA binding activity. Nature, 329 : 642-645.
De Boer, L. et al. (2008) Cyclin A/cdk2 coordinates centrosomal and nuclear mitotic events. Oncogene, 27 : 4261-4268.
Brown, N. R. et al. (1999) The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol., 1 : 438-443.
Smith, L. D., Ecker, R. E. (1971) The interaction of steroids with Rana pipiens oocytes in the induction of maturation. Dev. Biol., 25 : 232-247.
Masui, Y., Markert, C. L. (1971) Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool., 177 : 129-145.
Izawa, D., Pines, J. (2011) How APC/C-Cdc20 changes its substrate specificity in mitosis. Nat. Cell Biol., 13 : 223-233.
Robbins, J. A., Cross, F. R. (2010) Regulated degradation of the APC coactivator Cdc20. Cell Div., 5 : 23.
Zhang, S. et al. (2016) Molecular mechanism of APC/C activation by mitotic phosphorylation. Nature, 533 : 260-264.
Thornton, B. R., Toczyski, D. P. (2003) Securin and B-cyclin/CDK are the only essential targets of the APC. Nat. Cell Biol., 5 : 1090-1094.
Santaguida, S., Amon, A. (2015) Short- and long-term effects of chromosome mis-segregation and aneuploidy. Nat. Rev. Mol. Cell Biol., 16 : 473-485.
Lara-Gonzalez, P. et al. (2011) BubR1 blocks substrate recruitment to the APC/C in a KEN-boxdependent manner. J. Cell Sci., Dec 15;124 (Pt 24) : 4332-4345. doi : 10.1242/jcs.094763. Epub 2011 Dec 22.
Izawa, D., Pines, J. (2015) The mitotic checkpoint complex binds a second CDC20 to inhibit active APC/C. Nature, 517 : 631-634.
Izawa, D., Pines, J. (2012) Mad2 and the APC/C compete for the same site on Cdc20 to ensure proper chromosome segregation. J. Cell Biol., 199 : 27-37.
Ray, A. et al. (2016) ATR- and ATM-mediated DNA damage response is dependent on excision repair assembly during G1 but not in S phase of cell cycle. PLoS One, 11 : e0159344.
Donzelli, M., Draetta, G. F. (2003) Regulating mammalian checkpoints through Cdc25 inactivation. EMBO Rep., 4 : 671-677.
Qie, S., Diehl, J. A. (2016) Cyclin D1, cancer progression, and opportunities in cancer treatment. J. Mol. Med (Berl)., 94 : 1313-1326.
Aiello, K. A., Alter, O. (2016) Platform-independent genome-wide pattern of DNA copy-number alterations predicting astrocytoma survival and response to treatment revealed by the GSVD Formulated as a Comparative Spectral Decomposition. PLoS One, 11 : e0164546.
Casimiro, M. C. et al. (2012) Cyclins and cell cycle control in cancer and disease. Genes Cancer, 3 : 649-657.
Sun, X. et al. (2017) Prognostic and clinicopathological significance of cyclin B expression in patients with breast cancer : A meta-analysis. Medicine (Baltimore), 96 : e6860.
Clevers, H., Nusse, R. (2012) Wnt/β-catenin signaling and disease. Cell, 149 : 1192-1205.
Aubrey, B. J. et al. (2018) How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression? Cell Death Differ., 25 : 104-113.
Pfleger, C. M., Kirschner, M. W. (2000) The KEN box : an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev., 14 : 655-665.
Willyard, C. (2018) New human gene tally reignites debate. Nature, 558 : 354-355.
Sydow, J. F., Cramer, P. (2009) RNA polymerase fidelity and transcriptional proofreading. Curr. Opin. Struct. Biol., 19 : 732-739.
Gupta, K. et al. (2016) Zooming in on transcription preinitiation. J. Mol. Biol., 428 : 2581-2591.
Usheva, A. et al. (1992) Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein. Cell, 69 : 871-881.
Schultz, P. et al. (2000) Molecular structure of human TFIIH. Cell, 102 : 599-607.
Vannini, A., Cramer, P. (2012) Conservation between the RNA polymerase I, II, and III transcription initiation machineries. Mol. Cell, 45 : 439-446.
Jantzen, H. M. et al. (1990) Nucleolar transcription factor hUBF contains a DNA-binding motif with homology to HMG proteins. Nature, 344 : 830-836.
Goodfellow, S. J., Zomerdijk, J. C. (2013) Basic mechanisms in RNA polymerase I transcription of the ribosomal RNA genes. Subcell Biochem., 61 : 211-236.
Vorlander, M. K. et al. (2018) Molecular mechanism of promoter opening by RNA polymerase III. Nature, 553 : 295-300.
Abascal-Palacios, G. et al. (2018) Structural basis of RNA polymerase III transcription initiation. Nature, 553 : 301-306.
Fan, X. et al. (2005) Distinct transcriptional responses of RNA polymerases I, II and III to aptamers that bind TBP. Nucleic Acids Res., 33 : 838-845.
Ringel, R. et al. (2011) Structure of human mitochondrial RNA polymerase. Nature, 478 : 269-273.
Stern, D. S. et al. (1997) Transcription and translation in chloroplasts. Trends Plant Sci., 2 : 308-315.
Veloso, A. et al. (2014) Rate of elongation by RNA polymerase II is associated with specific gene features and epigenetic modifications. Genome Res., 24 : 896-905.
Mitchell, P. et al. (1997) The exosome : a conserved eukaryotic RNA processing complex containing multiple 3' → 5' exoribonucleases. Cell, 91 : 457-466.
Woese, C. R. et al. (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev., 64 : 202-236.
Kozak, M. (1984) Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo. Nature, 308 : 241-246.
Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell, 44 : 283-292.
Kozak, M. (1987) An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res., 15 : 8125-8148.
Mamane, Y. et al. (2006) mTOR, translation initiation and cancer. Oncogene, 25 : 6416-6422.
Young, R., Bremer, H. (1976) Polypeptide-chain-elongation rate in Escherichia coli B/r as a function of growth rate. Biochem. J., 160 : 185-194.
Waldron, C. et al. (1974) The elongation rate of proteins of different molecular weight classes in yeast. FEBS Lett., 46 : 11-16.
Chang, Y. F. et al. (2007) The nonsense-mediated decay RNA surveillance pathway. Annu. Rev. Biochem., 76 : 51-74.
Englander, S. W., Mayne, L. (2014) The nature of protein folding pathways. Proc. Natl. Acad. Sci. USA, 111 : 15873-15880.
Stroud, R. M., Walter, P. (1999) Signal sequence recognition and protein targeting. Curr. Opin. Struct. Biol., 9 : 754-759.
Dev, I. K., Ray, P. H. (1990) Signal peptidases and signal peptide hydrolases. J. Bioenerg. Biomembr., 22 : 271-290.
Zimmermann, R. et al. (2011) Protein translocation across the ER membrane. Biochim. Biophys. Acta, 1808 : 912-924.
Rapoport, T. A. (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature, 450 : 663-669.
Johnson, N. et al. (2013) Post-translational translocation into the endoplasmic reticulum. Biochim. Biophys. Acta, 1833 : 2403-2409.
Dudek, J. (2015) Protein transport into the human endoplasmic reticulum. J. Mol. Biol., 427 (6 Pt A) : 1159-1175.
du Plessis, D.J. et al. (2011) The Sec translocase. Biochim. Biophys. Acta, 1808 : 851-865.
Endo, T., Yamano, K. (2010) Transport of proteins across or into the mitochondrial outer membrane. Biochim. Biophys. Acta, 1803 : 706-714.
Shiota, T. et al. (2011) In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work. Proc. Natl. Acad. Sci. USA., 108 : 15179-15183.
Kabachinski, G., Schwartz, T. U. (2015) The nuclear pore complex--structure and function at a glance. J. Cell Sci., 128 : 423-429.
Sagai, T. et al. (2005) Elimination of a long-range cis-regulatory module causes complete loss of limb-specific Shh expression and truncation of the mouse limb. Development, 132 : 797-803.
Wittkopp, P. J., Kalay, G. (2011) Cis-regulatory elements : molecular mechanisms and evolutionary processes underlying divergence. Nat. Rev. Genet., 13 : 59-69.
Malan, T. P. et al. (1984) Mechanism of CRP-cAMP activation of lac operon transcription initiation activation of the P1 promoter. J. Mol. Biol., 180 : 881-909.
Lewis, M. (2005) The lac repressor. C. R. Biol., 328 : 521-548.
Wolberger, C. et al. (1991) Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell, 67 : 517-528.
Lin, S., Riggs, A. D. (1975) The general affinity of lac repressor for E. coli DNA : implications for gene regulation in procaryotes and eucaryotes. Cell, 4 : 107-111.
Yin, J. W., Wang, G. (2014) The Mediator complex : a master coordinator of transcription and cell lineage development. Development, 141 : 977-987.
Cairns, B. R. et al. (1996) RSC, an essential, abundant chromatin-remodeling complex. Cell, 87 : 1249-1260.
Hammond, C. M. (2017) Histone chaperone networks shaping chromatin function. Nat. Rev. Mol. Cell Biol., 18 : 141-158.
Fry, C. J., Peterson, C. L. (2002) Transcription. Unlocking the gates to gene expression. Science, 295 : 1847-1848.
Biterge, B., Schneider, R. (2014) Histone variants : key players of chromatin. Cell Tissue Res., 356 : 457-466.
Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature, 389 : 349-352.
Rossetto, D. et al. (2012) Histone phosphorylation : a chromatin modification involved in diverse nuclear events. Epigenetics, 7 : 1098-1108.
Harr, J. C. et al. (2016) Histones and histone modifications in perinuclear chromatin anchoring : from yeast to man. EMBO Rep., 17 : 139-155.
de Napoles, M. et al. (2004) Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. Dev. Cell, 7 : 663-676.
Vire, E. et al. (2006) The Polycomb group protein EZH2 directly controls DNA methylation. Nature, 439 : 871-874.
West, A. G. et al. (2002) Insulators : many functions, many mechanisms. Genes Dev., 16 : 271-288.
Valenzuela, L., Kamakaka, R. T. (2006) Chromatin insulators. Annu. Rev. Genet., 40 : 107-138.
Doetsch, P. W. et al. (1986) Mechanism of action of a mammalian DNA repair endonuclease. Biochemistry, 25 : 2212-2220.
Morin, R. et al. (2008) Profiling the HeLa S3 transcriptome using randomly primed cDNA and massively parallel short-read sequencing. Biotechniques, 45 : 81-94.
Niwa, H. et al. (2005) Interaction between Oct3/4 and Cdx2 determines trophectoderm differentiation. Cell, 123 : 917-929.
Nichols, J. (1998) Formation of pluripotent stem cells in the mammalian embryo depends on the POU transcription factor Oct4. Cell, 95 : 379-391.
Avilion, A. A. (2003) Multipotent cell lineages in early mouse development depend on SOX2 function. Genes Dev., 17 : 126-140.
Hackett, J. A., Surani, M. A. (2014) Regulatory principles of pluripotency : from the ground state up. Cell Stem Cell, 15 : 416-430.
Yagi, M. et al. (2017) Derivation of ground-state female ES cells maintaining gamete-derived DNA methylation. Nature, 548 : 224-227.
Takahashi, K., Yamanaka, S. (2006) Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell, 126 : 663-676. Epub 2006 Aug 10.
Takahashi, K. et al. (2007) Induction of pluripotent stem cells from adult human fibroblasts by defined factors. Cell, 131 : 861-872.
Rowland, B. D. et al. (2005) The KLF4 tumour suppressor is a transcriptional repressor of p53 that acts as a context-dependent oncogene. Nat. Cell Biol., 7 : 1074-1082.
Wei, Z. et al. (2009) Klf4 interacts directly with Oct4 and Sox2 to promote reprogramming. Stem Cells, 27 : 2969-2978.
Fujimori, K. et al. (2018) Modeling sporadic ALS in iPSC-derived motor neurons identifies a potential therapeutic agent. Nat. Med., 24 : 1579-1589.
Nakagawa, M. et al. (2008) Generation of induced pluripotent stem cells without Myc from mouse and human fibroblasts. Nat. Biotechnol., 26 : 101-106.
Wernig, M. et al. (2008) c-Myc is dispensable for direct reprogramming of mouse fibroblasts. Cell Stem Cell, 2 : 10-12.
Nakagawa, M. et al. (2010) Promotion of direct reprogramming by transformation-deficient Myc. Proc. Natl. Acad. Sci. USA, 107 : 14152-14157.
Murakami, K. et al. (2016) NANOG alone induces germ cells in primed epiblast in vitro by activation of enhancers. Nature, 529 : 403-407.
Mikkelsen, T.S. et al. (2008) Dissecting direct reprogramming through integrative genomic analysis. Nature, 454 : 49-55.
Shimamoto, R. (2014) Generation and characterization of induced pluripotent stem cells from Aiddeficient mice. PLoS One, 9 : e94735.
Koche, R. P. et al. (2011) Reprogramming factor expression initiates widespread targeted chromatin remodeling. Cell Stem Cell, 8 : 96-105.