@article{11116,
  abstract     = {The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly.},
  author       = {Franz, Cerstin and Walczak, Rudolf and Yavuz, Sevil and Santarella, Rachel and Gentzel, Marc and Askjaer, Peter and Galy, Vincent and HETZER, Martin W and Mattaj, Iain W and Antonin, Wolfram},
  issn         = {1469-3178},
  journal      = {EMBO reports},
  keywords     = {Genetics, Molecular Biology, Biochemistry},
  number       = {2},
  pages        = {165--172},
  publisher    = {EMBO},
  title        = {{MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly}},
  doi          = {10.1038/sj.embor.7400889},
  volume       = {8},
  year         = {2007},
}

@article{12201,
  abstract     = {The development of plant lateral organs is interesting because, although many of the same genes seem to be involved in the early growth of primordia, completely different gene combinations are required for the complete development of organs such as leaves and stamens. Thus, the genes common to the development of most organs, which generally form and polarize the primordial ‘envelope’, must at some stage interact with those that ‘install’ the functional content of the organ – in the case of the stamen, the four microsporangia. Although distinct genetic pathways of organ initiation, polarity establishment and setting up the reproductive cell line can readily be recognized, they do not occur sequentially. Rather, they are activated early and run in parallel. There is evidence for continuing crosstalk between these pathways.},
  author       = {Feng, Xiaoqi and Dickinson, Hugh G.},
  issn         = {0168-9525},
  journal      = {Trends in Genetics},
  keywords     = {Genetics},
  number       = {10},
  pages        = {503--510},
  publisher    = {Elsevier BV},
  title        = {{Packaging the male germline in plants}},
  doi          = {10.1016/j.tig.2007.08.005},
  volume       = {23},
  year         = {2007},
}

@article{12203,
  abstract     = {Geranylgeranyl diphosphate synthase (GGPPS, EC: 2.5.1.29) catalyzes the biosynthesis of geranylgeranyl diphosphate (GGPP), which is a key precursor for ginkgolide biosynthesis. Here we reported for the first time the cloning of a new full-length cDNA encoding GGPPS from the living fossil plant Ginkgo biloba. The full-length cDNA encoding G. biloba GGPPS (designated as GbGGPPS) was 1657bp long and contained a 1176bp open reading frame encoding a 391 amino acid protein. Comparative analysis showed that GbGGPPS possessed a 79 amino acid transit peptide at its N-terminal, which directed GbGGPPS to target to the plastids. Bioinformatic analysis revealed that GbGGPPS was a member of polyprenyltransferases with two highly conserved aspartate-rich motifs like other plant GGPPSs. Phylogenetic tree analysis indicated that plant GGPPSs could be classified into two groups, angiosperm and gymnosperm GGPPSs, while GbGGPPS had closer relationship with gymnosperm plant GGPPSs.},
  author       = {Liao, Zhihua and Chen, Min and Gong, Yifu and Guo, Liang and Tan, Qiumin and Feng, Xiaoqi and Sun, Xiaofen and Tan, Feng and Tang, Kexuan},
  issn         = {1042-5179},
  journal      = {DNA Sequence},
  keywords     = {Endocrinology, Genetics, Molecular Biology, Biochemistry},
  number       = {2},
  pages        = {153--158},
  publisher    = {Informa UK Limited},
  title        = {{A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides}},
  doi          = {10.1080/10425170410001667348},
  volume       = {15},
  year         = {2004},
}

@article{11122,
  abstract     = {Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex.},
  author       = {Walther, Tobias C. and Alves, Annabelle and Pickersgill, Helen and Loı̈odice, Isabelle and HETZER, Martin W and Galy, Vincent and Hülsmann, Bastian B. and Köcher, Thomas and Wilm, Matthias and Allen, Terry and Mattaj, Iain W. and Doye, Valérie},
  issn         = {0092-8674},
  journal      = {Cell},
  keywords     = {General Biochemistry, Genetics and Molecular Biology},
  number       = {2},
  pages        = {195--206},
  publisher    = {Elsevier},
  title        = {{The conserved Nup107-160 complex is critical for nuclear pore complex assembly}},
  doi          = {10.1016/s0092-8674(03)00235-6},
  volume       = {113},
  year         = {2003},
}

@article{11124,
  abstract     = {Ran GTPase plays important roles in nucleocytoplasmic transport in interphase [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes. We propose that the Ran binding capacity of chromatin contributes to localized spindle and NE assembly.},
  author       = {Bilbao-Cortés, Daniel and HETZER, Martin W and Längst, Gernot and Becker, Peter B. and Mattaj, Iain W.},
  issn         = {0960-9822},
  journal      = {Current Biology},
  keywords     = {General Agricultural and Biological Sciences, General Biochemistry, Genetics and Molecular Biology},
  number       = {13},
  pages        = {1151--1156},
  publisher    = {Elsevier BV},
  title        = {{Ran binds to chromatin by two distinct mechanisms}},
  doi          = {10.1016/s0960-9822(02)00927-2},
  volume       = {12},
  year         = {2002},
}