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1996 1
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2001 2
2003 5
2004 2
2006 1
2007 3
2008 3
2009 2
2010 3
2011 3
2013 2
2015 7
2016 2
2017 4
2018 1
2019 1
2020 0
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43 results
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Page 1
An improved smaller biotin ligase for BioID proximity labeling
Kim DI, et al. Mol Biol Cell 2016. PMID 26912792 Free PMC article.
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins in living cells. ...Thus BioID2 improves the efficiency of screening for protein-protein associations. We also demonstrate that the biotinylation range of BioID2 can be considerably modulated using flexible linkers, thus enabling application-specific adjustment of the biotin-labeling radius....
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins in livi …
The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions.
Zuccolo M, et al. EMBO J 2007. PMID 17363900 Free PMC article.
We previously demonstrated that a fraction of the human Nup107-160 nuclear pore subcomplex is recruited to kinetochores at the onset of mitosis. ...Together, our data thus provide the first molecular clues underlying the function of the human Nup107-160 complex at kinetochores....
We previously demonstrated that a fraction of the human Nup107-160 nuclear pore subcomplex is recruited to kinetochores at the …
Homozygous mutation in NUP107 leads to microcephaly with steroid-resistant nephrotic condition similar to Galloway-Mowat syndrome.
Rosti RO, et al. J Med Genet 2017. PMID 28280135
The founder mutation was associated with concomitant reduction in NUP107 protein and in the obligate binding partner NUP133 protein, as well as density of nuclear pores in patient cells. CONCLUSION: Recently, NUP107 was suggested as a candidate in a family with nephrotic syndrome and developmental delay. Other NUP107-reported cases had isolated renal phenotypes. ...
The founder mutation was associated with concomitant reduction in NUP107 protein and in the obligate binding partner NUP133 …
Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death
Gasset-Rosa F, et al. Neuron 2019. PMID 30853299 Free PMC article.
Cytoplasmic TDP-43 droplets slowly recruit importin-α and Nup62 and induce mislocalization of RanGap1, Ran, and Nup107, thereby provoking inhibition of nucleocytoplasmic transport, clearance of nuclear TDP-43, and cell death. ...
Cytoplasmic TDP-43 droplets slowly recruit importin-α and Nup62 and induce mislocalization of RanGap1, Ran, and Nup107, thereby provo …
Biallelic Mutations in Nuclear Pore Complex Subunit NUP107 Cause Early-Childhood-Onset Steroid-Resistant Nephrotic Syndrome.
Miyake N, et al. Am J Hum Genet 2015. PMID 26411495 Free PMC article.
The nuclear pore complex (NPC) is a huge protein complex embedded in the nuclear envelope. It has central functions in nucleocytoplasmic transport, nuclear framework, and gene regulation. Nucleoporin 107 kDa (NUP107) is a component of the NPC central scaffold and is an essential protein in all eukaryotic cells. ...
The nuclear pore complex (NPC) is a huge protein complex embedded in the nuclear envelope. It has central functions in nucleocytoplas …
Functional study of a novel missense single-nucleotide variant of NUP107 in two daughters of Mexican origin with premature ovarian insufficiency.
Ren Y, et al. Mol Genet Genomic Med 2018. PMID 29363275 Free PMC article.
Nucleoporin 107 (NUP107), a protein involved in transport between cytoplasm and nucleus with putative roles in meiosis/mitosis progression, was recently implicated as a cause of HH. We identified a NUP107 genetic variant in a nonconsanguineous family with two sisters affected with primary amenorrhea and HH, and generated a mouse model that carried the human variant. ...
Nucleoporin 107 (NUP107), a protein involved in transport between cytoplasm and nucleus with putative roles in meiosis/mitosis …
NUP107 mutations in children with steroid-resistant nephrotic syndrome.
Park E, et al. Nephrol Dial Transplant 2017. PMID 27190346
CONCLUSIONS: An unexpectedly high incidence of NUP107 mutations was observed in Korean children with SR-FSGS. Initial genetic screening of children with SR-FSGS should include the NUP107 gene, at least in Korea. Further studies are necessary to determine the incidences of NUP107 mutations in other countries....
CONCLUSIONS: An unexpectedly high incidence of NUP107 mutations was observed in Korean children with SR-FSGS. Initial genetic screeni …
The Nup107-160 complex and gamma-TuRC regulate microtubule polymerization at kinetochores.
Mishra RK, et al. Nat Cell Biol 2010. PMID 20081840 Free PMC article.
Our data indicate that Nup107-160 and gamma-TuRC act cooperatively to promote spindle assembly through microtubule nucleation at kinetochores: HeLa cells lacking Nup107-160 or gamma-TuRC were profoundly deficient in kinetochore-associated microtubule nucleation. Moreover, co-precipitated Nup107-160- gamma-TuRC complexes nucleated microtubule formation in assays using purified tubulin. ...
Our data indicate that Nup107-160 and gamma-TuRC act cooperatively to promote spindle assembly through microtubule nucleation at kine …
The Nup107-160 nucleoporin complex is required for correct bipolar spindle assembly.
Orjalo AV, et al. Mol Biol Cell 2006. PMID 16807356 Free PMC article.
To examine Nup107-160 complex recruitment to kinetochores, we stained human cells with antisera to four complex components. Each antibody stained not only kinetochores but also prometaphase spindle poles and proximal spindle fibers, mirroring the dual prometaphase localization of the spindle checkpoint proteins Mad1, Mad2, Bub3, and Cdc20. ...In mitotic Xenopus egg extracts, the Nup107-160 complex localized throughout reconstituted spindles. When the Nup107-160 complex was depleted from extracts, the spindle checkpoint remained intact, but spindle assembly was rendered strikingly defective. ...
To examine Nup107-160 complex recruitment to kinetochores, we stained human cells with antisera to four complex components. Ea …
A mutation in the nucleoporin-107 gene causes XX gonadal dysgenesis
Weinberg-Shukron A, et al. J Clin Invest 2015. PMID 26485283 Free PMC article.
NUP107 is a component of the nuclear pore complex, and the NUP107-associated protein SEH1 is required for oogenesis in Drosophila. In Drosophila, Nup107 knockdown in somatic gonadal cells resulted in female sterility, whereas males were fully fertile. Transgenic rescue of Drosophila females bearing the Nup107D364N mutation, which corresponds to the human NUP107 (p.D447N), resulted in almost complete sterility, with a marked reduction in progeny, morphologically aberrant eggshells, and disintegrating egg chambers, indicating defective oogenesis. ...
NUP107 is a component of the nuclear pore complex, and the NUP107-associated protein SEH1 is required for oogenesis in
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