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Literatura académica sobre el tema "Nucleoporins (Nups)"
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Artículos de revistas sobre el tema "Nucleoporins (Nups)"
Xu, Songli y Maureen A. Powers. "In vivo analysis of human nucleoporin repeat domain interactions". Molecular Biology of the Cell 24, n.º 8 (15 de abril de 2013): 1222–31. http://dx.doi.org/10.1091/mbc.e12-08-0585.
Texto completoHeinß, Nike, Mikhail Sushkin, Miao Yu y Edward A. Lemke. "Multifunctionality of F-rich nucleoporins". Biochemical Society Transactions 48, n.º 6 (18 de diciembre de 2020): 2603–14. http://dx.doi.org/10.1042/bst20200357.
Texto completoMakio, Tadashi, Leslie H. Stanton, Cheng-Chao Lin, David S. Goldfarb, Karsten Weis y Richard W. Wozniak. "The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly". Journal of Cell Biology 185, n.º 3 (4 de mayo de 2009): 459–73. http://dx.doi.org/10.1083/jcb.200810029.
Texto completoFlemming, Dirk, Phillip Sarges, Philipp Stelter, Andrea Hellwig, Bettina Böttcher y Ed Hurt. "Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores". Journal of Cell Biology 185, n.º 3 (4 de mayo de 2009): 387–95. http://dx.doi.org/10.1083/jcb.200810016.
Texto completoHuang, Kai y Igal Szleifer. "Modeling the nucleoporins that form the hairy pores". Biochemical Society Transactions 48, n.º 4 (14 de agosto de 2020): 1447–61. http://dx.doi.org/10.1042/bst20190941.
Texto completoColussi, Claudia y Claudio Grassi. "Epigenetic Regulation of Neural Stem Cells: The Emerging Role of Nucleoporins". Stem Cells 39, n.º 12 (25 de agosto de 2021): 1601–14. http://dx.doi.org/10.1002/stem.3444.
Texto completoHolden, Jennifer M., Ludek Koreny, Samson Obado, Alexander V. Ratushny, Wei-Ming Chen, Jean-Mathieu Bart, Miguel Navarro et al. "Involvement in surface antigen expression by a moonlighting FG-repeat nucleoporin in trypanosomes". Molecular Biology of the Cell 29, n.º 9 (mayo de 2018): 1100–1110. http://dx.doi.org/10.1091/mbc.e17-06-0430.
Texto completoPulupa, Joan, Manas Rachh, Michael D. Tomasini, Joshua S. Mincer y Sanford M. Simon. "A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics". Journal of General Physiology 149, n.º 10 (8 de septiembre de 2017): 951–66. http://dx.doi.org/10.1085/jgp.201711769.
Texto completoTerry, Laura J. y Susan R. Wente. "Flexible Gates: Dynamic Topologies and Functions for FG Nucleoporins in Nucleocytoplasmic Transport". Eukaryotic Cell 8, n.º 12 (2 de octubre de 2009): 1814–27. http://dx.doi.org/10.1128/ec.00225-09.
Texto completoSachdev, Ruchika, Cornelia Sieverding, Matthias Flötenmeyer y Wolfram Antonin. "The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes". Molecular Biology of the Cell 23, n.º 4 (15 de febrero de 2012): 740–49. http://dx.doi.org/10.1091/mbc.e11-09-0761.
Texto completoTesis sobre el tema "Nucleoporins (Nups)"
Lin, Junyan. "Assembly and function of cytosolic nuclear pore complexes". Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAJ037.
Texto completoNuclear pore complexes (NPCs), huge protein assemblies built into the nuclear envelope (NE), serve as pivotal structures for bidirectional transport, maintaining the equilibrium between the nucleus and cytoplasm. Beyond their residence within the NE, NPCs are also found in stacked cytoplasmic membranes known as annulate lamellae (AL). However, the function and pathways governing the biogenesis of AL remain enigmatic. Our investigation in mammalian cells unveils a mechanism wherein AL formation arises through the fusion of pre-assembled cytosolic NPCs. The movement of cytosolic NPCs is intricately linked to the dynamics of the endoplasmic reticulum (ER), as they migrate towards and integrate into NE during early interphase under normal growth conditions, a process mediated by microtubules. RanBP2 (Nup358), a constituent of the NPC cytoplasmic filaments, emerges as necessary and sufficient for AL formation in the cytoplasm. Mechanistically, the FG repeats in the N-terminus of RanBP2 play a pivotal role by orchestrating the oligomerization state of the NPC outer ring units, known as Y-complexes. Our study elucidates an assembly process crucial for NE nourishment, ensuring the functionality of nuclear pores and underscoring the significance of cytosolic NPCs in mammalian cellular homeostasis
Markossian, Sarine W. "Nup2 and a Newly Discovered Nuclear Pore Complex Protein, NupA, Function at Mitotic Chromatin Controlled by the NIMA Kinase". The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1306851345.
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