Affinage

NUP58

Nucleoporin p58/p45 · UniProt Q9BVL2

Round 2 corrected
Length
599 aa
Mass
60.9 kDa
Annotated
2026-04-29
63 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP58 is a central channel nucleoporin that, together with Nup54 and Nup62, forms the dynamic core of the nuclear pore complex transport channel and participates in mitotic regulation and gene control. The Nup62–Nup54–NUP58 heterotrimer assembles via coiled-coil interactions with Nup54 as the central scaffold, and multivalent binding of the transport factor Kapβ1 to NUP58's disordered FG-repeat domains allosterically shifts the structured domain between homo- and hetero-oligomeric ring states, providing a mechanism for transport-responsive dilation and constriction of the NPC channel (PMID:26046439, PMID:24574455, PMID:26025361). During mitosis, NUP58 redistributes from the nuclear envelope to centrosomes, spindles, and midbodies—regulated in part by TIP60-mediated acetylation of Nup62 that dissolves the heterotrimer—where it recruits PLK-1 to promote nuclear envelope breakdown and accurate chromosome segregation (PMID:29065307, PMID:31388347, PMID:36190325). Beyond nucleocytoplasmic transport, NUP58 contributes to homologous recombination repair, tissue-specific piRNA-mediated transposon silencing, and serves as a docking site for HIV-1 Vpr at the nuclear envelope (PMID:29986057, PMID:33856346, PMID:12228227).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1995 High

    Establishing that NUP58 is a soluble nucleoporin whose integration into nuclear pore complexes requires a GTP-dependent step resolved the basic question of how central channel components are assembled into membranes.

    Evidence Biochemical reconstitution of annulate lamellae in Xenopus egg extracts with GTPγS inhibition, EM, and flotation assays

    PMID:7790348

    Open questions at the time
    • Identity of the GTPase required for NUP58 pore incorporation was not determined
    • Whether NUP58 assembly is co-translational or post-translational was not resolved
  2. 2001 High

    Demonstrating that the Nup62 complex (containing NUP58) binds importin β at intermediate affinity between cytoplasmic and nuclear FG-nucleoporins established the affinity gradient model for directional transport through the central channel.

    Evidence Quantitative solid-phase binding assays and antibody inhibition of nuclear import in permeabilized cells

    PMID:11266456

    Open questions at the time
    • Individual contribution of NUP58 versus Nup62 and Nup54 FG domains to importin β binding not dissected
    • In vivo validation of the affinity gradient not performed
  3. 2002 High

    Identification of NUP58 as a direct binding partner of HIV-1 Vpr through its N-terminal (non-FG) domain revealed the NPC central channel as a viral docking platform distinct from canonical FG-mediated transport.

    Evidence Yeast two-hybrid, in vitro pulldown, co-immunoprecipitation, and digitonin-permeabilized cell nuclear import assays

    PMID:12228227

    Open questions at the time
    • Structural basis of the Vpr–NUP58 interaction not resolved
    • Functional consequence for viral replication not fully demonstrated in this study
  4. 2013 High

    Integrated structural mapping of the human NPC placed the Nup62 subcomplex (including NUP58) within the central transport channel relative to the scaffold rings, answering where NUP58 sits in the intact pore architecture.

    Evidence Cryo-electron tomography, single-particle EM, and crosslinking mass spectrometry of human NPCs

    PMID:24315095

    Open questions at the time
    • Atomic-resolution structure of NUP58 within the intact NPC not achieved
    • Conformational dynamics of NUP58 in situ not captured
  5. 2014 High

    Quantitative demonstration that Nup62, Nup54, and NUP58 form a 1:1:1 heterotrimer with Nup54 as the central scaffold resolved the subunit stoichiometry and architecture of the channel nucleoporin complex.

    Evidence Analytical ultracentrifugation and gel filtration of recombinant complex; evolutionary conservation validated with yeast Nsp1 complex

    PMID:24574455

    Open questions at the time
    • Whether the 1:1:1 trimer is the only relevant stoichiometry in the assembled NPC was debated
  6. 2015 High

    Crystal structures and binding equilibria revealed that NUP58 segments can switch between homo-oligomeric and NUP58–Nup54 hetero-oligomeric ring conformations, and that Kapβ1 binding to NUP58's FG domains allosterically drives this switch—providing the first mechanistic model for how transport factor occupancy modulates central channel diameter.

    Evidence X-ray crystallography, analytical ultracentrifugation, and quantitative equilibrium binding analyses

    PMID:26025361 PMID:26046439

    Open questions at the time
    • In vivo validation that the homo-to-hetero switch occurs during active transport not directly demonstrated
    • Contribution of post-translational modifications to the conformational equilibrium unknown
  7. 2017 High

    Discovery that NUP58 and other channel nucleoporins recruit PLK-1 via Polo-box domain docking sites primed by Cdk1 established a mitotic signaling function for NUP58 at the nuclear envelope, required for efficient NEBD and chromosome segregation.

    Evidence C. elegans RNAi epistasis, live imaging, co-immunoprecipitation, phosphorylation site mapping; confirmed in human cells

    PMID:29065307

    Open questions at the time
    • Which specific phosphosites on human NUP58 are essential for PLK-1 recruitment not fully mapped
    • Whether NUP58's mitotic role is independent of its transport function not resolved
  8. 2018 Medium

    A radiosensitivity siRNA screen implicated the Nup54–NUP58 complex in homologous recombination repair, linking central channel nucleoporins to DNA damage response for the first time.

    Evidence High-throughput siRNA screen, HR reporter assay, Rad51 foci quantification, and epistasis analysis with Rad51

    PMID:29986057

    Open questions at the time
    • NUP58 was identified as co-depleted partner of Nup54; individual NUP58 knockdown phenotype in HR not separately validated
    • Mechanism by which channel nucleoporins promote HR (e.g. mRNA export of repair factors versus direct nuclear role) not determined
  9. 2019 Medium

    Super-resolution imaging demonstrated that NUP58 redistributes from the nuclear rim to centrosomes, spindle poles, and midbodies during mitosis, and its depletion causes centrosomal defects and delayed abscission, broadening its mitotic role beyond NEBD to cytokinesis.

    Evidence STED nanoscopy, confocal and live-cell imaging, siRNA depletion with phenotypic scoring

    PMID:31388347

    Open questions at the time
    • Molecular partners of NUP58 at centrosomes and midbodies not identified
    • Whether NUP58's cytokinetic function depends on the Nup62 complex or is independent unknown
  10. 2020 Medium

    In vivo conformational sensors confirmed that NUP58, Nup54, and Nup62 are the flexible, transport-responsive elements of the NPC, validating the earlier in vitro allosteric dilation model in living cells.

    Evidence Live-cell imaging with orientation-sensitive mEGFP sensors under transport perturbation

    PMID:33346731

    Open questions at the time
    • Sensor reports on orientation, not directly on ring diameter or stoichiometry changes
    • Magnitude of conformational change and its relationship to cargo flux not quantified
  11. 2021 Medium

    Three parallel studies expanded NUP58's biology: (1) hypomorphic alleles showed NUP58 is essential and its impairment drives ordered adaptive evolution via focal gene amplification; (2) Drosophila genetics revealed a tissue-specific role in piRNA-mediated transposon silencing; (3) in vitro studies showed NUP58 can form amyloid aggregates, suggesting intrinsic phase-separation capacity.

    Evidence CRISPR hypomorphic alleles with RNA-seq and copy-number analysis; Drosophila RNAi with small-RNA sequencing; in vitro amyloid assays with Congo red/ThT and EM

    PMID:33856346 PMID:34528284 PMID:34680573

    Open questions at the time
    • Whether amyloid formation is physiologically relevant or an artifact of overexpression unknown
    • How NUP58 selectively regulates the flamenco piRNA locus versus other loci not mechanistically explained
    • Whether the adaptive amplification mechanism operates in tumors in vivo not tested
  12. 2022 Medium

    Identification of TIP60-mediated acetylation of Nup62-K432 as the signal that dissolves the Nup62–NUP58–Nup54 complex during mitotic entry provided a PTM-based mechanism coupling interphase NPC disassembly to spindle orientation and chromosome segregation.

    Evidence Mass spectrometry, site-directed mutagenesis of K432, co-immunoprecipitation of complex dissolution, and mitotic phenotyping after TIP60 or Nup62 perturbation

    PMID:36190325

    Open questions at the time
    • Whether NUP58 itself is acetylated during mitosis not examined
    • Temporal coordination between K432 acetylation and PLK-1 recruitment to NUP58 not resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: (1) the atomic-resolution structure of NUP58 within an intact NPC; (2) how NUP58 mechanistically contributes to homologous recombination independently of its transport role; (3) the physiological relevance of NUP58 amyloid formation; and (4) whether NUP58 cleavage by viral proteases disrupts transport in infected cells.
  • No high-resolution in situ structure of NUP58 in the intact human NPC
  • Mechanism linking NUP58 to HR repair pathway not established
  • In vivo relevance of NUP58 amyloid aggregation unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005635 nuclear envelope 5 GO:0005634 nucleus 2 GO:0005815 microtubule organizing center 2 GO:0005856 cytoskeleton 2
Pathway
R-HSA-9609507 Protein localization 4 R-HSA-1640170 Cell Cycle 3 R-HSA-73894 DNA Repair 1
Partners
KAT5KPNB1NUP54NUP62PLK1
Complex memberships
Nup62 complex (Nup62–Nup54–NUP58)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 NUP58 (nup58) is a soluble nucleoporin that assembles into nuclear pore complexes (annulate lamellae) in a time- and temperature-dependent manner in a Xenopus egg extract reconstitution system. Assembly of nup58 into membranes was inhibited by GTPγS, indicating a GTP-dependent step in nuclear pore assembly. Biochemical reconstitution of annulate lamellae in Xenopus egg extracts; immunoblotting of membrane fractions; electron microscopy; flotation assay The Journal of cell biology High 7790348
2001 The Nup62 complex (containing NUP58) resides in the central channel of the NPC and binds importin β with intermediate affinity, between the lower-affinity cytoplasmic Nup358 and the higher-affinity nuclear Nup153, establishing a gradient of increasing affinity along the import pathway. Quantitative solid-phase binding analysis; antibody inhibition of nuclear import in permeabilized cells The Journal of cell biology High 11266456
2002 HIV-1 Vpr interacts with the nucleoporin hCG1 (NUP58) via the N-terminal region of hCG1 (not the FG repeat domain), and this interaction mediates docking of Vpr at the nuclear envelope, as demonstrated by yeast two-hybrid, in vitro binding, co-immunoprecipitation in transfected cells, and nuclear import assays. Yeast two-hybrid; in vitro pulldown; co-immunoprecipitation; FRAP in living cells; digitonin-permeabilized cell nuclear import assay The Journal of biological chemistry High 12228227
2013 Integrated cryo-electron tomography, single-particle EM, and crosslinking mass spectrometry placed the Nup62 subcomplex (including NUP58) within the central channel of the human NPC scaffold, revealing its position relative to the Nup107 subcomplex rings. Electron tomography; single-particle EM; crosslinking mass spectrometry Cell High 24315095
2014 The Nup62 complex (Nup62, Nup54, NUP58) forms a 1:1:1 stoichiometric heterotrimer in solution, with Nup54 as the central scaffold that directly binds both Nup62 and NUP58 via coiled-coil segments. The same 1:1:1 stoichiometry is conserved in the yeast Nsp1 complex. At high concentration the complex forms larger assemblies while maintaining this ratio. Analytical ultracentrifugation; gel filtration; in vitro reconstitution Molecular biology of the cell High 24574455
2015 Crystallographic and solution analyses demonstrated that NUP58 and Nup54 cognate segments can form either homo-oligomers or hetero-oligomers, enabling inter-convertible 'mid-plane' ring structures that model dilation and constriction of the NPC central transport channel. The full ordered regions of Nup62, Nup54, and NUP58 form a dynamic triple complex in solution consistent with a 4:2:1 (Nup62:Nup54:NUP58) copy-number stoichiometry. X-ray crystallography; size exclusion chromatography; analytical ultracentrifugation; solution binding analysis The Journal of biological chemistry High 26025361
2015 A structured domain of NUP58 is allosterically coupled to its neighboring disordered FG domain: multivalent binding of the transport factor Kapβ1 to disordered domains of NUP58 stabilizes the adjacent structured domain associated with Nup54, shifting conformational equilibria from NUP58 homo-oligomers to Nup54–NUP58 hetero-oligomers. This allosteric mechanism provides a quantitative framework for constriction and dilation of the NPC central channel as a function of transport factor occupancy. Analysis of multiple binding equilibria; crystallography-based structural framework; in vitro binding assays Cell High 26046439
2017 The channel nucleoporins NPP-1/Nup58, NPP-4/Nup54, and NPP-11/Nup62 in C. elegans recruit Polo-like kinase 1 (PLK-1) to the nuclear pore complex via the PLK-1 Polo-box domain (PBD) just prior to nuclear envelope breakdown (NEBD). Cdk1 and PLK-1 itself prime multiple Polo-docking sites on these nucleoporins, and this NE-localized PLK-1 pool is required for efficient NEBD and proper chromosome segregation. Genetic epistasis (C. elegans); RNAi knockdown; live imaging; co-immunoprecipitation; phosphorylation site mapping; PLK-1 localization assays in human cells Developmental cell High 29065307
2018 NUP58 (as part of the Nup54–Nup62–NUP58 central channel complex) was identified by siRNA screen as a novel factor in radiosensitivity. Nup54 (and concomitantly NUP58) depletion impaired homologous recombination (HR) repair, decreased Rad51 focus formation, reduced sister chromatid exchanges, and caused mitotic catastrophe after ionizing radiation. Nup54 is epistatic with the HR factor Rad51. High-throughput siRNA screen; clonogenic survival assay; HR repair reporter assay; immunofluorescence for DNA damage foci; epistasis analysis Nucleic acids research Medium 29986057
2019 NUP58 localizes to the nuclear rim during interphase and redistributes to mitotic spindles, centrosomes, and midbodies during mitosis. Depletion of NUP58 causes centrosomal abnormalities and delayed abscission, establishing a role for NUP58 in centrosome homeostasis and cytokinetic abscission. Confocal microscopy; live-cell imaging; STED (stimulated emission depletion) nanoscopy; siRNA depletion with phenotypic readout Cell division Medium 31388347
2019 NUP58 knockdown in lung adenocarcinoma cell lines (A549, H1299) inhibited metastasis and invasion in vitro and in vivo. Silencing NUP58 altered expression of EMT markers and suppressed GSK-3β/Snail pathway activity, indicating NUP58 promotes EMT-driven metastasis through the GSK-3β/Snail signaling axis. Lentiviral shRNA knockdown; invasion/migration assays; in vivo xenograft; Western blotting for EMT markers and pathway components American journal of translational research Low 30787996
2020 In vivo conformational sensors (mEGFP rigidly conjugated to NPC proteins) showed that NUP58 and its inner-ring neighbors Nup54 and Nup62 undergo conformational changes when nucleocytoplasmic transport is perturbed, while Nups elsewhere in the NPC do not, demonstrating that the central channel nucleoporins are the flexible, transport-responsive elements of the NPC. Live-cell imaging with orientation-sensitive fluorescent sensors; transport perturbation assays eLife Medium 33346731
2021 Hypomorphic alleles of NUP58 in human cells trigger early transcriptome rewiring (upregulation of NPC-interacting genes) as a non-genetic adaptation, followed by focal genomic amplification of the NUP58 locus to restore protein expression as a long-term genetic adaptation, establishing NUP58 as an essential NPC gene whose impairment drives ordered adaptive evolution. Generation of hypomorphic alleles by CRISPR; RNA-seq; genomic copy number analysis; clonal fitness assays The EMBO journal Medium 34528284
2021 Drosophila Nup54 and Nup58 (channel nucleoporins) are essential for piRNA-mediated transposon silencing in ovarian follicle cells, specifically from the flamenco locus, while knockdown of other NPC subunits has broader consequences. This demonstrates tissue-specific, locus-specific gene regulatory roles for NUP58 beyond its canonical transport function. Drosophila RNAi knockdown in ovarian follicle cells; small RNA sequencing; transposon derepression assays eLife Medium 33856346
2021 Human NUP58 can form amyloid aggregates both in vitro and in vivo (in bacterial and yeast systems), existing as both oligomers and polymers stabilized by disulfide bonds. Bioinformatic analysis identified conserved amyloidogenic regions across all known NUP58 orthologs, suggesting an intrinsic aggregation propensity of NUP58 related to its phase-separation capacity. In vitro amyloid formation assays; Congo red/ThT fluorescence; electron microscopy of fibrils; in vivo expression in bacteria and yeast; bioinformatic amyloid prediction Biomedicines Medium 34680573
2022 TIP60 acetyltransferase acetylates Nup62 at Lys432, which dissolves the Nup62–NUP58–Nup54 complex during mitotic entry, promoting redistribution of Nup62 to the mitotic spindle for correct spindle orientation and accurate chromosome segregation. Mass spectrometry identification of acetylation; mutagenesis of acetylation site; co-immunoprecipitation; immunofluorescence; siRNA knockdown with mitotic phenotype readout Journal of molecular cell biology Medium 36190325
2024 NUP58 is a host substrate of coronavirus 3C-like protease (3CLpro): in vitro cleavage experiments and mutational analysis validated NUP58 as a high-scoring cleavage target of Gammacoronavirus/Deltacoronavirus 3CLpro, suggesting 3CLpro may modulate nucleo-cytoplasmic transport by cleaving NUP58. PSSM-based computational prediction; in vitro cleavage assay; mutational analysis of cleavage site Biochimica et biophysica acta. Proteins and proteomics Low 39454742
2025 NUP58 acts as a binding enhancer for HIV capsid core within the NPC central channel: biochemical and biophysical analyses showed that FG/FxFG motifs of NUP58 bind HIV capsid (CA) with enhanced affinity compared to canonical FxFG motifs, contributing to an avidity gradient along the cytoplasmic-nuclear axis that promotes unidirectional HIV capsid translocation into the nucleus. Biochemical binding assays; biophysical affinity measurements; structural analyses (AlphaFold-guided); mutational analysis of FG motifs bioRxivpreprint Low 41256404

Source papers

Stage 0 corpus · 63 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2020 A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 3411 32353859
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2014 A proteome-scale map of the human interactome network. Cell 977 25416956
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2020 Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science (New York, N.Y.) 564 33060197
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2014 Probing nuclear pore complex architecture with proximity-dependent biotinylation. Proceedings of the National Academy of Sciences of the United States of America 436 24927568
2015 A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. Cell 433 26638075
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
1996 Normalization and subtraction: two approaches to facilitate gene discovery. Genome research 401 8889548
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2007 Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS genetics 325 17500595
2013 Integrated structural analysis of the human nuclear pore complex scaffold. Cell 284 24315095
2011 A directed protein interaction network for investigating intracellular signal transduction. Science signaling 258 21900206
2010 Identification and characterization of nuclear pore complex components in Arabidopsis thaliana. The Plant cell 239 21189294
2001 Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. The Journal of cell biology 238 11266456
2011 Next-generation sequencing to generate interactome datasets. Nature methods 200 21516116
2010 A human MAP kinase interactome. Nature methods 165 20936779
2020 Comparative Application of BioID and TurboID for Protein-Proximity Biotinylation. Cells 146 32344865
2020 Persistent Polyfunctional Chimeric Antigen Receptor T Cells That Target Glypican 3 Eliminate Orthotopic Hepatocellular Carcinomas in Mice. Gastroenterology 141 32060001
1999 Nuclear import of hepatic glucokinase depends upon glucokinase regulatory protein, whereas export is due to a nuclear export signal sequence in glucokinase. The Journal of biological chemistry 115 10601273
2018 Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei. Molecular & cellular proteomics : MCP 101 30021884
2002 Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1. The Journal of biological chemistry 95 12228227
2016 Pooled-matrix protein interaction screens using Barcode Fusion Genetics. Molecular systems biology 89 27107012
2014 Meta-analysis of human methylation data for evidence of sex-specific autosomal patterns. BMC genomics 81 25406947
1995 Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation. The Journal of cell biology 72 7790348
2017 Channel Nucleoporins Recruit PLK-1 to Nuclear Pore Complexes to Direct Nuclear Envelope Breakdown in C. elegans. Developmental cell 70 29065307
2013 Genetic amplification of the NOTCH modulator LNX2 upregulates the WNT/β-catenin pathway in colorectal cancer. Cancer research 70 23319804
2015 Allosteric Regulation in Gating the Central Channel of the Nuclear Pore Complex. Cell 37 26046439
2013 Cancer driver-passenger distinction via sporadic human and dog cancer comparison: a proof-of-principle study with colorectal cancer. Oncogene 34 23416983
2014 Cancer driver candidate genes AVL9, DENND5A and NUPL1 contribute to MDCK cystogenesis. Oncoscience 31 25621300
2020 Investigating the Transition of Pre-Symptomatic to Symptomatic Huntington's Disease Status Based on Omics Data. International journal of molecular sciences 26 33049985
2014 The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution. Molecular biology of the cell 22 24574455
2021 Channel nuclear pore complex subunits are required for transposon silencing in Drosophila. eLife 20 33856346
2018 Nucleoporin 54 contributes to homologous recombination repair and post-replicative DNA integrity. Nucleic acids research 17 29986057
2020 Conformation of the nuclear pore in living cells is modulated by transport state. eLife 15 33346731
2015 Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution. The Journal of biological chemistry 15 26025361
2019 Nucleoporin Nup58 localizes to centrosomes and mid-bodies during mitosis. Cell division 11 31388347
2017 The Nup62 Coiled-Coil Motif Provides Plasticity for Triple-Helix Bundle Formation. Biochemistry 11 28406021
2022 Acetylation of Nup62 by TIP60 ensures accurate chromosome segregation in mitosis. Journal of molecular cell biology 10 36190325
2022 A Nucleoporin NUP58 modulates responses to drought and salt stress in maize (Zea mays L.). Plant science : an international journal of experimental plant biology 9 35643613
2019 NUP58 facilitates metastasis and epithelial-mesenchymal transition of lung adenocarcinoma via the GSK-3β/Snail signaling pathway. American journal of translational research 9 30787996
2023 Regulation of FLC nuclear import by coordinated action of the NUP62-subcomplex and importin β SAD2. Journal of integrative plant biology 8 37278318
2023 Single-cell transcriptomics uncover hub genes and cell-cell crosstalk in patients with hypertensive nephropathy. International immunopharmacology 8 37897949
2021 The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo. Biomedicines 6 34680573
2023 Identification of New FG-Repeat Nucleoporins with Amyloid Properties. International journal of molecular sciences 5 37239918
2021 Non-genetic and genetic rewiring underlie adaptation to hypomorphic alleles of an essential gene. The EMBO journal 5 34528284
2018 Involvement in surface antigen expression by a moonlighting FG-repeat nucleoporin in trypanosomes. Molecular biology of the cell 5 29496964
2023 Indel driven rapid evolution of core nuclear pore protein gene promoters. Scientific reports 4 37198214
2025 Histone Deacetylase Inhibitors orchestrate epigenetic signalling and alter the nucleoporins and nuclear envelope in cervical cancer. Translational oncology 0 40865161
2025 Morphological and Transcriptomic Analyses of the Adrenal Gland in Acomys cahirinus: A Novel Model for Murine Adrenal Physiology. Cells 0 41002397
2025 Translocation of HIV capsid core through the Nuclear Pore Complex by affinity gradient. bioRxiv : the preprint server for biology 0 41256404
2025 Light-exclusion bagging modulates phenylpropanoid metabolism to balance preharvest quality and postharvest granulation in 'Sanhongmiyou' pomelo. Food chemistry 0 41443065
2024 Preliminary study of identified novel susceptibility loci for HAPE risk in a Chinese male Han population. Personalized medicine 0 38940394
2024 Deciphering the cleavage sites of 3C-like protease in Gammacoronaviruses and Deltacoronaviruses. Biochimica et biophysica acta. Proteins and proteomics 0 39454742