Affinage

NUP188

Nucleoporin NUP188 · UniProt Q5SRE5

Length
1749 aa
Mass
196.0 kDa
Annotated
2026-06-10
36 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/6 claims corpus-supported (83%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP188 encodes a large scaffold nucleoporin that is a core structural element of the inner ring of the nuclear pore complex (NPC), where it functions as a question mark-shaped keystone of a hetero-octameric inner ring complex and engages the linker nucleoporins Nic96, Nup145N, and Nup53 through defined surface pockets (PMID:35679425). It was first identified in yeast as a major NPC constituent that interacts with the pore membrane protein Pom152p and the nucleoporin Nic96p and is required for normal nuclear envelope and NPC morphology (PMID:8682855, PMID:8682854, PMID:9988776). Although Nup188 is individually non-essential, it operates within a functionally redundant inner-ring substructure: loss is synthetically lethal with POM152 or NUP170 and genetically intertwined with the GLFG transport domains of Nup145p and Nup116 needed for late NPC assembly (PMID:8522578, PMID:29033133, PMID:9305650). Functionally, Nup188 helps set the resting diameter of the central transport channel, as its deletion increases passive nuclear envelope permeability (PMID:10831607), and structural work shows it binds FG-repeats and can itself translocate through NPCs by facilitated diffusion, indicating an evolutionary kinship between scaffold and soluble transport machinery (PMID:23795296). Beyond the pore, Nup188 has independent, spatially distinct roles: a centrosomal pool localizes to the pericentriolar material where it binds Cep152 and is required for centriole duplication upstream of Sas6 loading (PMID:32211895); during mitosis it localizes to spindle poles, directly interacts with NuMA, and promotes K-fiber formation and chromosome alignment (PMID:23551833); and as part of the Nup93/Nup188/Nup205 sub-complex it tethers the HOXA cluster to the nuclear periphery to repress its expression (PMID:27980680). Additional roles include facilitating importin-β-mediated nuclear import of OCT4 and stabilizing SOX2 to drive liver cancer stem cell stemness (PMID:42119810) and supporting left-right body patterning in vertebrate development (PMID:21282601).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 High

    Established that Nup188 is a non-essential NPC component embedded within a functionally redundant inner-ring substructure, framing it as a scaffold buffer rather than a single critical pore subunit.

    Evidence Synthetic lethal genetic screen with pairwise NUP188/POM152/NUP170 deletions in yeast

    PMID:8522578

    Open questions at the time
    • Does not define the physical architecture of the redundant substructure
    • Mechanism of redundancy at the molecular level unresolved
  2. 1996 High

    Identified Nup188 as a major NPC constituent and placed it in direct contact with Pom152p and Nic96p, defining its first physical partners within the pore scaffold.

    Evidence Biochemical NPC fractionation, immunoEM, allele-specific genetics, and ProtA-Nup188p affinity purification in yeast

    PMID:8682854 PMID:8682855

    Open questions at the time
    • No atomic-resolution interface for the Nic96 or Pom152 contacts
    • Stoichiometry within the NPC not determined
  3. 1997 Medium

    Linked Nup188 function to the FG/GLFG transport domains by showing the free N-Nup145p domain becomes essential in a nup188 mutant background.

    Evidence Genetic synthetic lethality and in vivo cleavage domain dissection in yeast

    PMID:9305650

    Open questions at the time
    • Direct physical interaction between Nup188 and N-Nup145p not shown here
    • Functional consequence on transport not directly measured
  4. 1999 Medium

    Refined the Pom152p interaction to its lumenal C-terminal domain and connected NUP188 genetically to the Hsp70-dependent NLS import pathway.

    Evidence Domain truncation complementation in synthetic lethal strains and SSA1/SSB1 overexpression suppression of nup188-Δ import defects

    PMID:10347213 PMID:9988776

    Open questions at the time
    • Direct biochemical Pom152 lumenal-domain binding not demonstrated
    • Hsp70 link is genetic, not a physical interaction
  5. 2000 High

    Demonstrated that Nup188 contributes to setting the functional diameter of the NPC central transport channel and is part of a conserved vertebrate Nup93–Nup188–Nup205 complex.

    Evidence Passive permeability assays with sized NLS/NES-GFP reporters in nup188-Δ yeast; WGA-affinity chromatography and annulate lamellae assembly in Xenopus extracts

    PMID:10831607 PMID:11029043

    Open questions at the time
    • Structural basis for channel-diameter control unknown
    • How the sub-complex assembles into the ring not resolved
  6. 2013 High

    Provided the first crystal structure of Nup188 and showed it binds FG-repeats and translocates through NPCs, suggesting an evolutionary relationship between scaffold and soluble transport receptors.

    Evidence X-ray crystallography, FG-repeat binding, and facilitated diffusion assays

    PMID:23795296

    Open questions at the time
    • Physiological significance of facilitated diffusion in vivo unclear
    • Full-length architecture in the assembled NPC not resolved at this stage
  7. 2013 Medium

    Revealed a moonlighting mitotic role: human Nup188 localizes to spindle poles, binds NuMA, and is required for K-fiber formation and chromosome alignment.

    Evidence siRNA depletion, immunofluorescence, co-IP, and live-cell imaging in human cells

    PMID:23551833

    Open questions at the time
    • Mechanism of spindle-pole targeting not defined
    • NuMA interaction not validated by orthogonal structural or reciprocal methods
  8. 2016 Medium

    Connected the Nup93/Nup188/Nup205 sub-complex to gene regulation by showing it tethers and represses the HOXA cluster at the nuclear periphery.

    Evidence ChIP, siRNA knockdown, 3D-FISH, and histone-mark profiling in human cells

    PMID:27980680

    Open questions at the time
    • Nup188-specific contribution inferred from sub-complex depletion
    • Direct DNA or chromatin contact by Nup188 not shown
  9. 2017 High

    Showed Nup116 GLFG repeats act redundantly with Nup188 to stabilize scaffold interactions during late NPC assembly, with direct in vitro binding.

    Evidence In vitro FG-repeat binding, genetic redundancy analysis, and NPC assembly assay in yeast

    PMID:29033133

    Open questions at the time
    • Precise assembly step Nup188 stabilizes not pinpointed
    • Quantitative kinetics of assembly contribution unknown
  10. 2018 Medium

    Extended Nup188's assembly role by identifying Brl1 as an NPC-biogenesis partner and demonstrating compositional plasticity through the Nup188/Nup192 paralog pair.

    Evidence Brl1 co-IP and split-YFP; quantitative fluorescence microscopy (NuRIM) with genetic manipulation of Nup expression in yeast

    PMID:29439116 PMID:29632211

    Open questions at the time
    • Brl1 link rests on a single co-IP supported by split-YFP
    • Functional consequence of paralog substitution for transport unknown
  11. 2018 Medium

    Linked Nup188 to bidirectional nucleocytoplasmic transport via a cold-sensitive allele affecting both protein import and mRNA export.

    Evidence Cold-sensitive nup188-brr7 mutant with poly-A RNA in situ export and NLS-GFP import assays in yeast

    PMID:30021831

    Open questions at the time
    • Whether transport defects are direct or secondary to scaffold disruption unclear
    • Cargo selectivity not fully mapped
  12. 2019 Medium

    Placed NUP188 downstream of TDP-43, showing its mRNA splicing is TDP-43-dependent and its mis-splicing causes nuclear envelope defects.

    Evidence TDP-43 knockout human cells with transcriptomic and morphological phenotyping

    PMID:31527135

    Open questions at the time
    • Disease relevance of NUP188 mis-splicing not established
    • Functional NUP188 isoform consequences not characterized
  13. 2020 High

    Defined an NPC-independent centrosomal pool of Nup188 that binds Cep152 and is required for centriole duplication, establishing a distinct moonlighting function.

    Evidence Pulse-chase labeling, super-resolution microscopy, BioID, proteasome inhibition, co-IP, and siRNA centriole-duplication readout in human cells

    PMID:32211895

    Open questions at the time
    • How centrosomal versus NPC targeting is partitioned mechanistically unknown
    • Structural basis of Cep152 binding undefined
  14. 2022 High

    Delivered the near-atomic architecture of Nup188 as a question mark-shaped inner-ring keystone engaging linker nucleoporins through defined surface pockets, validated functionally.

    Evidence X-ray crystallography, cryo-EM, cryo-ET docking, reconstitution, and structure-guided mutagenesis of human and yeast NPCs

    PMID:35679425

    Open questions at the time
    • Dynamics of linker-scaffold engagement during assembly not captured
    • Does not address moonlighting localizations outside the NPC
  15. 2022 Medium

    Identified NUP188 as a Nesprin-2 (LINC complex) partner positioning the NPC for SV40 viral nuclear translocation.

    Evidence Co-IP, siRNA depletion, and viral infection assays in human cells

    PMID:36067270

    Open questions at the time
    • Single-lab co-IP without reciprocal structural validation
    • Generality beyond SV40 entry unknown
  16. 2025 Low

    Implicated Nup188 in DNA repair by placing it after DNA synthesis in break-induced replication, downstream of Nup84.

    Evidence Genome-wide deletion screen for BIR defects with epistasis ordering in yeast

    PMID:41398407

    Open questions at the time
    • Genome-wide screen with limited Nup188-specific mechanistic follow-up
    • Direct role versus indirect transport/scaffold effect not distinguished
  17. 2026 Medium

    Defined a pro-stemness role in liver cancer through importin-β-mediated OCT4 import and lysosome-protective SOX2 stabilization, with a targeting peptide showing therapeutic potential.

    Evidence siRNA/KO assays, co-IP, lysosome inhibition rescue, tumor sphere and in vivo tumor assays, and a NUP188-targeting peptide

    PMID:42119810

    Open questions at the time
    • Whether OCT4/SOX2 effects depend on NPC-resident or moonlighting Nup188 unclear
    • Mechanism of SOX2 protection from lysosomal degradation not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single scaffold nucleoporin is partitioned among its NPC, centrosomal, spindle-pole, and chromatin-tethering roles, and how these moonlighting activities are regulated, remains unresolved.
  • No unifying mechanism for targeting Nup188 to distinct compartments
  • Structural basis for non-NPC partner interactions (NuMA, Cep152, Nesprin-2) undefined
  • Regulation switching between pore and moonlighting pools unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005635 nuclear envelope 2 GO:0005815 microtubule organizing center 2 GO:0005634 nucleus 1
Pathway
R-HSA-1640170 Cell Cycle 2 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-9609507 Protein localization 2
Partners
CEP152NESPRIN-2NIC96/NUP93NUMA1NUP145NNUP205NUP53POM152
Complex memberships
NPC inner ring complexNup93-Nup188-Nup205 sub-complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 Yeast Nup188p is a major constituent of the nuclear pore complex (NPC) that localizes to both the cytoplasmic and nucleoplasmic faces of the NPC core, physically interacts with the pore membrane protein Pom152p and nucleoporin Nic96p, and is required for normal nuclear envelope and NPC morphology; null mutants appear normal but certain alleles cause dominant NPC-associated nuclear envelope herniations. Biochemical fractionation of NPCs, immunofluorescence, immunoelectron microscopy, genetic deletion and allelic analysis The Journal of cell biology High 8682855
1996 The C-terminal domain of Nic96p functionally and physically interacts with Nup188p in an allele-specific fashion; affinity purification of Nup188p co-purifies a fraction of Nic96p, placing Nup188p in a direct protein–protein interaction with Nic96p within the NPC scaffold. Allele-specific genetic interaction, affinity purification (ProtA-Nup188p pull-down), co-fractionation The Journal of cell biology High 8682854
1995 Genetic epistasis in yeast shows that deletion of NUP188 is not lethal alone, but pairwise deletion with POM152 or NUP170 is synthetically lethal, placing Nup188p in a functionally redundant inner-ring scaffold substructure of the NPC together with Pom152p and Nup170p. Synthetic lethal genetic screen, pairwise deletion analysis The Journal of cell biology High 8522578
2000 Deletion of NUP188 (nup188-Δ) in yeast increases passive nuclear envelope permeability: passive export rates of NLS-GFP reporters are significantly faster and the equilibrium sieving limit of the diffusion channel is greater than wild-type, indicating that Nup188p contributes to establishing the functional resting diameter of the NPC central transport channel. In vivo passive permeability assay using NLS-GFP and NES-GFP reporters of defined molecular weights in nup188-Δ cells The Journal of cell biology High 10831607
2000 Vertebrate (Xenopus) Nup188 exists in a complex with Nup93 (xNup93) and Nup205 (xNup205) at the nuclear pore; the Nup93-Nup188-Nup205 complex does not bind WGA directly but associates indirectly via N-acetylglucosamine-modified nucleoporins, and Nup188 assembles into annulate lamellae pore structures. WGA-affinity chromatography of Xenopus egg extracts, organelle trap (annulate lamellae assembly) assay, identification of human NUP188 gene Molecular biology of the cell High 11029043
2013 The structure of Nup188 was determined: it folds into an extended stack of helices where an N-terminal ~130 kDa segment forms an intricate closed ring and the C-terminal region is a superhelical structure with distant similarity to flexible S-shaped nuclear transport receptors (NTRs). Both Nup188 and Nup192 specifically bind FG-repeats and can translocate through NPCs by facilitated diffusion, suggesting an evolutionary relationship between NPC scaffold and soluble transport machinery. X-ray crystallography (structure determination), FG-repeat binding assay, facilitated diffusion assay through NPCs eLife High 23795296
2013 Human Nup188 localizes to spindle poles during mitosis via its C-terminal region; depletion of Nup188 causes failure of chromosome alignment at the metaphase plate, impairs robust K-fiber (kinetochore microtubule bundle) formation, and perturbs NuMA localization to spindle poles. Nup188 directly interacts with NuMA. siRNA depletion, immunofluorescence, co-immunoprecipitation (Nup188–NuMA interaction), live-cell imaging Cancer science Medium 23551833
2016 Nup188 (as part of the Nup93 sub-complex) associates with the HOXA gene cluster promoters and is required for tethering the HOXA locus to the nuclear periphery and repressing HOXA gene expression; depletion of the Nup93/Nup188/Nup205 sub-complex upregulates HOXA genes, increases active histone marks (H3K9ac), and decreases repressive marks (H3K27me3) at the HOXA1 promoter. ChIP, siRNA knockdown, 3D-FISH, histone mark analysis by ChIP Epigenetics & chromatin Medium 27980680
2017 GLFG repeats of Nup116 function redundantly with Nup188, a non-essential scaffold nucleoporin, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly; GLFG repeats directly bind multiple scaffold Nups including Nup188 in vitro. In vitro FG-repeat binding assay, genetic redundancy analysis (nup116Δ/nup188 synthetic interactions), NPC assembly assay Cell High 29033133
2018 The integral membrane protein Brl1 physically interacts with Nup188 (by immunoprecipitation) at NPC assembly sites, indicating a direct role for Brl1 in NPC biogenesis through contact with this inner-ring scaffold component. Immunoprecipitation (Brl1–Nup188 co-IP), split-YFP analysis The Journal of cell biology Medium 29439116
2018 Quantitative fluorescence microscopy in intact yeast NPCs reveals that Nup188 and its paralog Nup192 form a paralog pair whose altered expression leads to significant changes in NPC stoichiometry, inducing voids in NPC structure or substitution of one paralog by the other, demonstrating compositional plasticity of the NPC. Quantitative fluorescence microscopy (NuRIM pipeline), genetic manipulation of Nup expression Proceedings of the National Academy of Sciences of the United States of America Medium 29632211
2019 TDP-43 controls mRNA splicing of NUP188; complete loss of TDP-43 in human cells results in aberrant NUP188 splicing and nuclear envelope morphological defects. TDP-43 knockout human cells, transcriptomic analysis, cell biological phenotyping Life science alliance Medium 31527135
2020 Nup188 localizes to the pericentriolar material (PCM) of centrosomes independently of NPCs: pulse-chase labeling shows centrosomal Nup188 is newly synthesized and does not exchange with NPC-resident Nup188 even after mitotic NPC breakdown. The centrosomal pool is subject to proteasomal degradation (unlike the NPC pool). Nup188 directly binds Cep152 (by co-IP/proximity labeling), and depletion of Nup188 impairs centriole duplication at or upstream of Sas6 loading. Pulse-chase fluorescent labeling, super-resolution microscopy, proximity labeling (BioID), proteasome inhibition, co-immunoprecipitation (Nup188–Cep152), siRNA depletion with centriole duplication readout The Journal of cell biology High 32211895
2022 Near-atomic composite structures of the human and S. cerevisiae NPC were determined by combining crystal structures and cryo-EM structures of Nup188 and Nup192 scaffold hubs bound to Nic96, Nup145N, and Nup53 linker nucleoporin binding regions, revealing that Nup188 forms a question mark-shaped keystone of a hetero-octameric inner ring complex. Linkers bind scaffold surface pockets of Nup188 through short defined motifs. Structure-guided mutagenesis in yeast confirmed the physiological relevance of linker-scaffold interactions. Nup188 is positioned exclusively in the inner ring (not the outer rings) in the intact NPC. X-ray crystallography, single-particle cryo-EM, cryo-ET docking, biochemical reconstitution, structure-guided mutagenesis in S. cerevisiae Science (New York, N.Y.) High 35679425
2022 NUP188 was identified as a new binding partner of Nesprin-2 (LINC complex component) at the nuclear envelope; this interaction positions the NPC to capture SV40 virus upon its release from Nesprin-2, enabling NPC-mediated nuclear translocation of the virus. Co-immunoprecipitation (NUP188–Nesprin-2 interaction), siRNA depletion, viral infection assays PLoS pathogens Medium 36067270
2011 Morpholino knockdown of NUP188 in Xenopus strongly disrupts morphological left-right development and expression of pitx2, a molecular marker of left-right patterning, placing NUP188 as a functional gene required for left-right organizer activity. Morpholino knockdown in Xenopus, in situ hybridization for pitx2, morphological scoring of LR defects Proceedings of the National Academy of Sciences of the United States of America Medium 21282601
1997 The N-terminal GLFG domain of Nup145p (N-Nup145p), generated by in vivo cleavage, becomes essential in a nup188 mutant background, and generation of a free N-domain is a prerequisite for complementation of this synthetic lethal interaction, placing Nup188p in a functional relationship with the GLFG-containing transport domain of Nup145p. Genetic synthetic lethality analysis, in vivo cleavage domain dissection The EMBO journal Medium 9305650
1999 Full-length Pom152p (including its lumenal C-terminal domain) is uniquely required to rescue nup188 mutations, whereas N-terminal or transmembrane segments alone are insufficient, indicating that the lumenal structures of Pom152p play an important role in functional interactions with Nup188p on the pore-side of the NPC. Domain deletion/truncation complementation assay in synthetic lethal nup188 strains The Journal of biological chemistry Medium 9988776
1999 Elevated levels of SSA1 (but not SSB1) suppress NLS-GFP nuclear localization defects in nup188-Δ cells; NES-less Ssb1p also stimulates nuclear transport in nup188-Δ cells, demonstrating a genetic interaction between NUP188 and Hsp70 chaperones in the NLS-directed import pathway. Genetic suppression assay, GFP reporter localization in nup188-Δ cells, Ssa1p/Ssb1p overexpression The Journal of biological chemistry Medium 10347213
2018 A cold-sensitive nup188-brr7 allele causes defects in both select protein import pathways and mRNA export in S. cerevisiae, linking Nup188p (as part of the Nic96 nucleoporin complex) to bidirectional nucleocytoplasmic transport. Cold-sensitive mutant screen, dT50 in situ hybridization assay (poly-A RNA export), NLS-GFP import assay G3 (Bethesda, Md.) Medium 30021831
2025 In a genome-wide screen for yeast genes involved in break-induced replication (BIR), Nup188 was identified as functioning after DNA synthesis to support BIR repair completion, acting sequentially after Nup84 (which acts before DNA synthesis). Genome-wide deletion screen for BIR defects, epistasis ordering of Nup84 vs. Nup188 in BIR Nature communications Low 41398407
2026 NUP188 promotes liver cancer stem cell (LCSC) stemness through two mechanisms: (1) facilitating importin-β-mediated nuclear import of OCT4 (POU5F1), and (2) stabilizing SOX2 by preventing its lysosome-dependent degradation. A NUP188-targeting peptide suppressed tumor sphere formation and inhibited tumor growth in vivo. siRNA/KO functional assays, co-immunoprecipitation (NUP188–importin-β), lysosome inhibition rescue, in vitro and in vivo tumor assays, NUP188-targeting peptide The American journal of pathology Medium 42119810

Source papers

Stage 0 corpus · 36 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Rare copy number variations in congenital heart disease patients identify unique genes in left-right patterning. Proceedings of the National Academy of Sciences of the United States of America 205 21282601
1995 Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. The Journal of cell biology 163 8522578
2022 Architecture of the linker-scaffold in the nuclear pore. Science (New York, N.Y.) 97 35679425
2000 Yeast nucleoporins involved in passive nuclear envelope permeability. The Journal of cell biology 94 10831607
1996 Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. The Journal of cell biology 92 8682854
1997 Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins. The EMBO journal 87 9305650
2017 Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex. Cell 85 29033133
1996 The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. The Journal of cell biology 78 8682855
2018 Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy. Proceedings of the National Academy of Sciences of the United States of America 61 29632211
2013 Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. eLife 59 23795296
1999 A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. The Journal of biological chemistry 53 10347213
2013 Nucleoporin Nup188 is required for chromosome alignment in mitosis. Cancer science 46 23551833
2000 Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay. Molecular biology of the cell 46 11029043
2019 Pleiotropic requirements for human TDP-43 in the regulation of cell and organelle homeostasis. Life science alliance 45 31527135
2016 HOXA repression is mediated by nucleoporin Nup93 assisted by its interactors Nup188 and Nup205. Epigenetics & chromatin 44 27980680
2011 Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM. Nucleus (Austin, Tex.) 41 21738830
2017 Whole Exome Sequencing Identifies Truncating Variants in Nuclear Envelope Genes in Patients With Cardiovascular Disease. Circulation. Cardiovascular genetics 36 28611029
2018 Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis. The Journal of cell biology 35 29439116
1999 Topology and functional domains of the yeast pore membrane protein Pom152p. The Journal of biological chemistry 32 9988776
2008 Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction. PloS one 29 18197258
2019 NUP188 Biallelic Loss of Function May Underlie a New Syndrome: Nucleoporin 188 Insufficiency Syndrome? Molecular syndromology 17 32021605
2020 Biallelic loss of function NEK3 mutations deacetylate α-tubulin and downregulate NUP205 that predispose individuals to cilia-related abnormal cardiac left-right patterning. Cell death & disease 16 33230144
2021 Proteomic Response of Rat Pituitary Under Chronic Mild Stress Reveals Insights Into Vulnerability and Resistance to Anxiety or Depression. Frontiers in genetics 15 34603401
2020 Differential turnover of Nup188 controls its levels at centrosomes and role in centriole duplication. The Journal of cell biology 15 32211895
2010 Recurrent deletion of 9q34 in adult normal karyotype precursor B-cell acute lymphoblastic leukemia. Cancer genetics and cytogenetics 12 20417863
2023 Non-classical functions of nuclear pore proteins in ciliopathy. Frontiers in molecular biosciences 7 37908226
2022 Components of the LINC and NPC complexes coordinately target and translocate a virus into the nucleus to promote infection. PLoS pathogens 6 36067270
2022 A Boy with Sandestig-Stefanova Syndrome and Genital Abnormalities. Molecular syndromology 6 36158057
2018 Identification of the Novel Nup188-brr7 Allele in a Screen for Cold-Sensitive mRNA Export Mutants in Saccharomyces cerevisiae. G3 (Bethesda, Md.) 5 30021831
2025 Genome-wide screen reveals dependence of break induced replication on several distinct checkpoints. Nature communications 4 41398407
2010 Small-interfering RNA-mediated silencing of the MAPK p42 gene induces dual effects in HeLa cells. Oncology letters 4 22966358
2022 Gene network profiling in muscle-invasive bladder cancer: A systematic review and meta-analysis. Urologic oncology 3 35039218
2025 Serum Proteomics Analysis of Patients with Ascending Aortic Dilation. Cardiovascular toxicology 2 40169515
2024 A Novel Truncating Variant in Sandestig-Stefanova Syndrome with Hydrocephalus. Molecular syndromology 1 39911172
2026 The Nucleoporin NUP188 Enhances Liver Cancer Stemness via POU Class 5 Homeobox 1 Import and SRY-Box Transcription Factor 2 Stabilization. The American journal of pathology 0 42119810
2025 A Novel Homozygous Splice Variant in the NUP188 Gene Causing Sandestig-Stefanova Syndrome in a Saudi Patient. American journal of medical genetics. Part A 0 40859750

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