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1. Full Text GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
by Freibaum, Brian D and Lu, Yubing and Lopez-Gonzalez, Rodrigo and Kim, Nam Chul and Almeida, Sandra and Lee, Kyung-Ha and Badders, Nisha and Valentine, Marc and Miller, Bruce L and Wong, Philip C and Petrucelli, Leonard and Kim, Hong Joo and Gao, Fen-Biao and Taylor, J. Paul
Nature, ISSN 0028-0836, 09/2015, Volume 525, Issue 7567, pp. 129 - 133
The GGGGCC (G(4)C(2)) repeat expansion in a noncoding region of C9orf72 is the most common cause of sporadic and familial forms of amyotrophic lateral... 
C9FTD/ALS | MULTIDISCIPLINARY SCIENCES | NUCLEAR-PORE COMPLEX | FRONTOTEMPORAL DEMENTIA | DISEASE | MESSENGER-RNA EXPORT | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | PROTEINS | HEXANUCLEOTIDE REPEAT | STEM-CELL MODELS | Protein Biosynthesis | Salivary Glands - pathology | DNA Repeat Expansion - genetics | Humans | Male | Neurons - cytology | Drosophila melanogaster - genetics | Salivary Glands - cytology | RNA - genetics | Drosophila melanogaster - metabolism | RNA Transport - genetics | Female | C9orf72 Protein | Neurons - metabolism | Induced Pluripotent Stem Cells - cytology | Muscles - metabolism | Active Transport, Cell Nucleus - genetics | Frontotemporal Dementia - pathology | Induced Pluripotent Stem Cells - metabolism | RNA - metabolism | Eye - metabolism | Frontotemporal Dementia - genetics | Animals, Genetically Modified | Amyotrophic Lateral Sclerosis - genetics | Nuclear Pore - pathology | Drosophila melanogaster - cytology | Nuclear Pore - genetics | Nuclear Pore - metabolism | Open Reading Frames - genetics | Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | Phenotype | Animals | HeLa Cells | Salivary Glands - metabolism | Muscles - cytology | Trinucleotide repeats | Genetic research | Genetic aspects | Research | Biological transport | Cytoplasm | Proteins | Insects | Toxicity | Pathogenesis | Amyotrophic lateral sclerosis | Chromosomes | Dementia | RAN translation | genetic screen | repeat expansion | Drosophila | DPR | FTD | ALS | C9ORF72 | nuclear pore
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2. Full Text The Nuclear Pore Complex as a Flexible and Dynamic Gate
by Knockenhauer, Kevin E and Schwartz, Thomas U
Cell, ISSN 0092-8674, 03/2016, Volume 164, Issue 6, pp. 1162 - 1171
Nuclear pore complexes (NPCs) perforate the nuclear envelope and serve as the primary transport gates for molecular exchange between nucleus and cytoplasm.... 
Nuclear Pore Complex Proteins - genetics | Animals | Humans | Nuclear Pore Complex Proteins - chemistry | Models, Molecular | Nuclear Pore - genetics | Nuclear Pore - chemistry | Evolution, Molecular
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3. Full Text TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
by Chou, Ching-Chieh and Zhang, Yi and Umoh, Mfon E and Vaughan, Spencer W and Lorenzini, Ileana and Liu, Feilin and Sayegh, Melissa and Donlin-Asp, Paul G and Chen, Yu Han and Duong, Duc M and Seyfried, Nicholas T and Powers, Maureen A and Kukar, Thomas and Hales, Chadwick M and Gearing, Marla and Cairns, Nigel J and Boylan, Kevin B and Dickson, Dennis W and Rademakers, Rosa and Zhang, Yong-Jie and Petrucelli, Leonard and Sattler, Rita and Zarnescu, Daniela C and Glass, Jonathan D and Rossoll, Wilfried
Nature Neuroscience, ISSN 1097-6256, 02/2018, Volume 21, Issue 2, pp. 228 - 239
The cytoplasmic mislocalization and aggregation of TAR DNA-binding protein-43 (TDP-43) is a common histopathological hallmark of the amyotrophic lateral... 
A315T MUTATION | REPEAT EXPANSION | MESSENGER-RNA | DROSOPHILA MODEL | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | FRONTOTEMPORAL LOBAR DEGENERATION | EXPRESSION | NEUROSCIENCES | RNA-BINDING PROTEIN | C9orf72 Protein - genetics | Active Transport, Cell Nucleus - physiology | Humans | Nuclear Envelope - ultrastructure | Male | Drosophila Proteins - metabolism | Cerebral Cortex - cytology | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Protein Aggregation, Pathological - pathology | Female | C9orf72 Protein - metabolism | Active Transport, Cell Nucleus - genetics | Neuroblastoma - pathology | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Animals, Genetically Modified | Amyotrophic Lateral Sclerosis - genetics | Drosophila | Mice, Inbred C57BL | Cells, Cultured | Nuclear Pore - genetics | DNA-Binding Proteins - genetics | Nuclear Pore - metabolism | DNA-Binding Proteins - ultrastructure | Amyotrophic Lateral Sclerosis - pathology | Animals | Larva | Amyotrophic Lateral Sclerosis - metabolism | C9orf72 Protein - ultrastructure | Embryo, Nonmammalian | Mice | Drosophila Proteins - genetics | Nuclear Envelope - pathology | Protein Aggregation, Pathological - metabolism | Fibroblasts | Amyotrophic lateral sclerosis | Research | Protein binding | Brain | Neurons | Cortex | Biotin | Ribonucleic acid--RNA | Pathology | DNA-binding protein | Nucleoporins | RNA transport | Aggregates | Stem cells | Dementia disorders | Mutation | Transport | Protein transport | Frontotemporal dementia | Pluripotency | Deoxyribonucleic acid--DNA
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4. Full Text Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells
by Mor, Amir and Suliman, Shimrit and Ben-Yishay, Rakefet and Yunger, Sharon and Brody, Yehuda and Shav-Tal, Yaron
Nature Cell Biology, ISSN 1465-7392, 06/2010, Volume 12, Issue 6, pp. 543 - 552
The flow of genetic information in eukaryotic cells occurs through the nucleocytoplasmic translocation of mRNAs. Knowledge of in vivo messenger RNA export... 
TRANSLOCATION | LOCALIZATION | COMPLEX | PROTEIN | PARTICLE | DYSTROPHIN | TRANSCRIPTION | KINETIC-ANALYSIS | MAMMALIAN-CELLS | MESSENGER-RNA TRANSPORT | CELL BIOLOGY | Mammals - genetics | Mammals - metabolism | Introns | RNA, Messenger - genetics | Nuclear Pore - genetics | Ribonucleoproteins - metabolism | Nuclear Pore - metabolism | RNA, Messenger - metabolism | Protein Transport - genetics | Animals | Cell Nucleus - metabolism | Cell Nucleus - genetics | Cells - metabolism | Chromosomes - metabolism | Biological Transport - genetics | Active Transport, Cell Nucleus - genetics | Physiological aspects | Genetic aspects | Messenger RNA | Research | Biological transport | Ribonucleoproteins
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5. Full Text The human TREX-2 complex is stably associated with the nuclear pore basket
by Umlauf, David and Bonnet, Jacques and Waharte, François and Fournier, Marjorie and Stierle, Matthieu and Fischer, Benoit and Brino, Laurent and Devys, Didier and Tora, László
Journal of Cell Science, ISSN 0021-9533, 06/2013, Volume 126, Issue 12, pp. 2656 - 2667
In eukaryotes, mRNA export involves many evolutionarily conserved factors that carry the nascent transcript to the nuclear pore complex (NPC). The THO/TREX... 
AMEX | mRNA export | NXF1 | Transcription | Nuclear pore complex | THO/TREX | TREX-2 | MESSENGER-RNA EXPORT | BINDING PROTEIN | PHOTORECEPTOR CELLS | SAGA | CELL BIOLOGY | STRUCTURAL BASIS | FUNCTIONAL COMPONENT | PROTEOMIC ANALYSIS | INTERACTION PLATFORM | LIVING CELLS | RNA-Binding Proteins - genetics | Acetyltransferases - metabolism | Humans | Intracellular Signaling Peptides and Proteins - metabolism | Phosphoproteins - metabolism | RNA, Messenger - metabolism | Acetyltransferases - genetics | Nuclear Pore Complex Proteins - genetics | Cell Nucleus - metabolism | Exodeoxyribonucleases - genetics | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Proto-Oncogene Proteins - metabolism | RNA Transport | Nuclear Pore Complex Proteins - metabolism | RNA, Messenger - genetics | Nuclear Pore - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Phosphoproteins - genetics | Transcription Factors - genetics | Nuclear Pore - metabolism | Nucleocytoplasmic Transport Proteins - genetics | Transcription Factors - metabolism | Transcription, Genetic - physiology | Nucleocytoplasmic Transport Proteins - metabolism | Cell Nucleus - genetics | Exodeoxyribonucleases - metabolism | Cell Line, Tumor | HeLa Cells | Transcription, Genetic - genetics | RNA-Binding Proteins - metabolism
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6. Full Text Nuclear pore association confers optimal expression levels for an inducible yeast gene
by Gasser, Susan M and Taddei, Angela and Hediger, Florence and Kalck, Veronique and Schober, Heiko and Cubizolles, Fabien and Van Houwe, Griet
Nature, ISSN 0028-0836, 06/2006, Volume 441, Issue 7094, pp. 774 - 778
The organization of the nucleus into subcompartments creates microenvironments that are thought to facilitate distinct nuclear functions. In budding yeast,... 
ORGANIZATION | LOCALIZATION | RECRUITMENT | CHROMOSOME DYNAMICS | REPRESSION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTIONAL ACTIVATOR | MACHINERY | PROTEINS | SACCHAROMYCES-CEREVISIAE | TELOMERES | Transcription, Genetic - drug effects | Galactose - metabolism | Galactose - pharmacology | Isoenzymes - genetics | Saccharomyces cerevisiae - genetics | RNA, Fungal - biosynthesis | 3' Untranslated Regions - genetics | Nuclear Pore - genetics | Saccharomyces cerevisiae - drug effects | Nuclear Pore - metabolism | RNA, Fungal - metabolism | Saccharomyces cerevisiae - cytology | Gene Expression Regulation, Fungal - drug effects | Saccharomyces cerevisiae - enzymology | Gene Expression Regulation, Fungal - genetics | RNA, Fungal - genetics | Transcription, Genetic - genetics | Hexokinase - genetics | Genes, Fungal - genetics | Chromatin | Gene expression | Molecular biology | Ribonucleic acid--RNA | Ribonucleic acid
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7. Full Text Channel Nucleoporins Recruit PLK-1 to Nuclear Pore Complexes to Direct Nuclear Envelope Breakdown in C. elegans
by Martino, Lisa and Morchoisne-Bolhy, Stéphanie and Cheerambathur, Dhanya K and Van Hove, Lucie and Dumont, Julien and Joly, Nicolas and Desai, Arshad and Doye, Valérie and Pintard, Lionel
Developmental Cell, ISSN 1534-5807, 10/2017, Volume 43, Issue 2, pp. 157 - 171.e7
In animal cells, nuclear envelope breakdown (NEBD) is required for proper chromosome segregation. Whereas mitotic kinases have been implicated in NEBD, how... 
development | Caenorhabditis elegans embryo | nucleoporin | cell division | Polo-like kinase | nuclear envelope breakdown | mitosis | phosphorylation | SPAT-1/BORA | CELL-DIVISION | ACTIVATION | CAENORHABDITIS-ELEGANS | PHOSPHORYLATION | FUNCTIONAL-ANALYSIS | ARCHITECTURE | DEVELOPMENTAL BIOLOGY | POLO-LIKE KINASE | REVEALS | CYCLE | CELL BIOLOGY | Embryo, Nonmammalian - cytology | Phosphorylation | Humans | Embryo, Nonmammalian - metabolism | Caenorhabditis elegans Proteins - metabolism | Nuclear Pore Complex Proteins - genetics | Cell Nucleus - metabolism | Cell Cycle Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Proto-Oncogene Proteins - metabolism | Caenorhabditis elegans - metabolism | Nuclear Envelope - genetics | Caenorhabditis elegans - growth & development | Caenorhabditis elegans - genetics | Nuclear Pore Complex Proteins - metabolism | Cell Cycle Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Nuclear Pore - genetics | Proto-Oncogene Proteins - genetics | Nuclear Pore - metabolism | Nuclear Envelope - metabolism | Animals | Cell Nucleus - genetics | Mitosis - physiology | HeLa Cells | Caenorhabditis elegans Proteins - genetics | Cells | Life Sciences | Development Biology | Cellular Biology | Biochemistry, Molecular Biology
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8. Full Text Interaction of a DNA Zip Code with the Nuclear Pore Complex Promotes H2A.Z Incorporation and INO1 Transcriptional Memory
by Light, William H and Brickner, Donna G and Brickner, Jason H and Brand, Veronica R
Molecular Cell, ISSN 1097-2765, 10/2010, Volume 40, Issue 1, pp. 112 - 125
DNA “zip codes” in the promoters of yeast genes confer interaction with the NPC and localization at the nuclear periphery upon activation. Some of these genes... 
ORGANIZATION | GAL GENES | CHROMATIN | HISTONE H2A.Z | BUDDING YEAST | PERIPHERY | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-EXPRESSION | MESSENGER-RNA EXPORT | VARIANT | GENOME | CELL BIOLOGY | Gene Expression Regulation, Fungal | Promoter Regions, Genetic | Inositol - metabolism | Nuclear Pore Complex Proteins - metabolism | Saccharomyces cerevisiae - genetics | Chromatin Assembly and Disassembly | Nuclear Pore - genetics | Myo-Inositol-1-Phosphate Synthase - genetics | DNA, Fungal - chemistry | Saccharomyces cerevisiae Proteins - genetics | Protein Transport | Nuclear Pore Complex Proteins - genetics | Histones - genetics | Time Factors | DNA, Fungal - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Transcription, Genetic | Myo-Inositol-1-Phosphate Synthase - metabolism | Histones - metabolism | Mutation | Nucleic Acid Conformation | Nuclear Pore - enzymology | Chromatin | DNA | Genetic aspects
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9. Full Text Nuclear architecture dictates HIV-1 integration site selection
by Marini, Bruna and Kertesz-Farkas, Attila and Ali, Hashim and Lucic, Bojana and Lisek, Kamil and Manganaro, Lara and Pongor, Sandor and Luzzati, Roberto and Recchia, Alessandra and Mavilio, Fulvio and Giacca, Mauro and Lusic, Marina
Nature, ISSN 0028-0836, 05/2015, Volume 521, Issue 7551, pp. 227 - 231
Long-standing evidence indicates that human immunodeficiency virus type 1 (HIV-1) preferentially integrates into a subset of transcriptionally active genes of... 
CELLS | DOMAIN | HUMAN GENOME | REPLICATION | LENTIVIRUS VECTOR | MULTIDISCIPLINARY SCIENCES | GENES | IMMUNODEFICIENCY-VIRUS TYPE-1 | INFECTION | LATENCY | EXPRESSION | Chromatin - metabolism | Virus Integration - genetics | Transcriptional Activation - genetics | Chromosome Positioning - genetics | Nuclear Pore Complex Proteins - metabolism | CD4-Positive T-Lymphocytes - cytology | Humans | CD4-Positive T-Lymphocytes - metabolism | Cells, Cultured | Genetic Loci - genetics | Half-Life | Nuclear Pore - genetics | HIV Integrase - metabolism | HIV-1 - genetics | Nuclear Pore - metabolism | Transcription Factors - metabolism | Cell Nucleus - metabolism | HIV-1 - physiology | Cell Nucleus - genetics | Adaptor Proteins, Signal Transducing - metabolism | Chromatin - genetics | Genetic aspects | Cell nuclei | Structure | HIV (Viruses) | Infections | Mutation | Gene expression | Lymphocytes | Human immunodeficiency virus--HIV | Deoxyribonucleic acid--DNA
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10. Full Text Congenital Heart Disease Genetics Uncovers Context-Dependent Organization and Function of Nucleoporins at Cilia
by del Viso, Florencia and Huang, Fang and Myers, Jordan and Chalfant, Madeleine and Zhang, Yongdeng and Reza, Nooreen and Bewersdorf, Joerg and Lusk, C. Patrick and Khokha, Mustafa K
Developmental Cell, ISSN 1534-5807, 09/2016, Volume 38, Issue 5, pp. 478 - 492
Human genomics is identifying candidate genes for congenital heart disease (CHD), but discovering the underlying mechanisms remains challenging. In a patient... 
3D nanoscopy | left-right patterning | super-resolution | heterotaxy | nucleoporin | congenital heart disease | nuclear pore complex | Xenopus tropicalis | MODEL SYSTEM | NUCLEAR-PORE COMPLEX | PERICENTRIOLAR MATERIAL | STRUCTURAL-ANALYSIS | LEFT-RIGHT AXIS | NUP107-160 COMPLEX | DEVELOPMENTAL BIOLOGY | LEFT-RIGHT ASYMMETRY | COPY NUMBER VARIANTS | CELL-DIFFERENTIATION | PERMEABILITY BARRIER | CELL BIOLOGY | Cilia - pathology | Heterotaxy Syndrome - genetics | Xenopus Proteins - genetics | Nuclear Pore Complex Proteins - metabolism | Xenopus - genetics | Humans | Heart Defects, Congenital - pathology | Nuclear Pore Complex Proteins - chemistry | Nuclear Pore - genetics | Nuclear Pore - metabolism | Protein Transport - genetics | Cilia - genetics | Gene Knockdown Techniques | Xenopus Proteins - chemistry | Nuclear Pore Complex Proteins - genetics | Heart Defects, Congenital - genetics | Animals | Protein Interaction Maps - genetics | Protein Conformation | Xenopus Proteins - metabolism | Heart Defects, Congenital - metabolism | Genome, Human | Heterotaxy Syndrome - pathology | Medical colleges | Embryonic development | Genetic disorders | Developmental biology | Genomics | Congenital heart disease | Heart diseases | Cells | Biomedical engineering | super resolution
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