Ask about this productRelated genes to: NUP155 antibody
- Gene:
- NUP155 NIH gene
- Name:
- nucleoporin 155
- Previous symbol:
- -
- Synonyms:
- KIAA0791, N155
- Chromosome:
- 5p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-21
- Date modifiied:
- 2016-10-05
Related products to: NUP155 antibody
Related articles to: NUP155 antibody
- Sepsis-induced coagulopathy (SIC) is a life-threatening complication characterized by high heterogeneity and mortality. Current prognostic models relying solely on clinical indices often fail to capture complex molecular pathophysiology, limiting precise risk stratification. This study aimed to unveil the molecular landscape of SIC via multi-omics integration and develop a robust machine learning (ML) predictive model. - Source: PubMed
Publication date: 2026/02/12
Qian SongzanZheng RuiShi YiyiLai MishaHu JunhaoXu MingyuePang DanxiaoGe HeweiWang DingyuanPan Jingye - The nucleus is enclosed by the nuclear envelope, which contains nuclear pore complexes (NPCs). While NPCs have been well studied in vertebrates, yeast and algae, in situ structural data for higher plants is lacking. Here we show that individual nucleoporins of Arabidopsis thaliana and humans exhibit high structural similarity. We report an in situ NPC structure of higher plants, derived from A. thaliana root protoplasts using cryo-electron tomography, subtomogram averaging and homology-based integrative modelling. We present the AtNPC model based on predictions of A. thaliana nucleoporins (NUPs), supported by mass spectrometry. Here the AtNPC scaffold contains one Y-complex ring at the cytosolic and two at the nuclear ring. The AtNPC contains prominent NUP155 connector elements that are conserved in human NPCs but not in Chlamydomonas reinhardtii NPCs. Our model suggests that the ELYS homologue HOS1 plays an important role in the head-to-tail connection of Y-complexes in AtNPCs. - Source: PubMed
Publication date: 2025/10/31
Sanchez Carrillo Ingrid BereniceHoffmann Patrick CObarska-Kosinska AgnieszkaFourcassié VictorBeck MartinGermain Hugo - MALAT1 is one of the most well-studied lncRNAs in various diseases. This work attempted to investigate whether long non-coding RNA MALAT1 participate in the development of allergic rhinitis (AR). In this work, nasal mucosal tissues were obtained from AR patients. The mouse AR model was established by sensitization and challenge with ovalbumin. MALAT1, GATA3 and NUP155 were up-regulated, miR-422a was down-regulated in AR patients and mice. The sneezing number, rubbing number and rhinorrhea were increased in AR mice as compared with normal mice. The levels of IL-4, IL-5, IL-9 and IL-13 were elevated in nasal lavage fluid of AR mice. MALAT1 deficiency repressed the secretion of Th2 cytokines in ILC2 cells, which was abrogated by NUP155 overexpression. NUP155 knockdown reversed the promotion of MALAT1 overexpression on the secretion of Th2 cytokines. Moreover, MALAT1 elevated NUP155 expression by sponging miR-422a. In vivo, MALAT1 silencing reduced the sneezing number, rubbing number and rhinorrhea, ameliorated damage of nasal mucosal tissues in AR mice. Similarly, NUP155 knockdown also significantly alleviated AR clinical symptoms, improved nasal mucosal pathology, and suppressed the secretion of Th2 cytokines in vivo. In conclusion, this work demonstrated that MALAT1 elevated the secretion of Th2 cytokines in ILC2 cells by regulating miR-422a/NUP155 axis, which contributed to AR progression. Thus, MALAT1 may be a potential target for AR treatment. - Source: PubMed
Publication date: 2025/08/28
Zhang XuYang RuiBai DaomingLiu MengyuanHuang XinyuWan WeiYang Chunping - Lung adenocarcinoma (LUAD) is a common histopathological variant of non-small cell lung cancer. Individuals with type 2 diabetes (T2DM) face an elevated risk of developing LUAD. We examined the common genomic characteristics between LUAD and T2DM through bioinformatics analysis. - Source: PubMed
Publication date: 2025/03/25
Nueraihemaiti NuerbiyeDilimulati DilihumaBaishan AlharHailati SendaerMaihemuti NulibiyaAikebaier AlifeiyePaerhati YipaerguliZhou Wenting - Despite the exciting progress of bifunctional degrader molecules, also known as proteolysis-targeting chimeras (PROTACs), the rapidly expanding field is still significantly hampered by the lack of available E3 ligase ligands. Our research bridges this gap by uncovering a series of small-molecule ligands to the E3 ligase TRIM21 through DNA-Encoded Library (DEL) technology. We confirmed their interaction with TRIM21 using crystallography and demonstrated their antiproliferative effects across various cancer cell types. Furthermore, proteomic studies identified that the mRNA Export Factor GLE1 and the Nuclear Pore Complex Protein NUP155 were significantly downregulated on TRIM21 ligand treatment. This degradation required TRIM21 and was ubiquitin-proteasome-dependent. More specifically, NUP155 was the primary target for the TRIM21 ligands, while GLE1 was considered a passenger target on initial degradation of NUP155. Using immunofluorescence techniques, we further demonstrated that the degradation of GLE1 and NUP155 proteins impaired the integrity of the nuclear envelope, leading to cell death. Highlighted by this research, a novel mode of action has been discovered for the TRIM21 E3 ligase ligand, acting as a monovalent degrader that triggers de novo interaction with functional complex proteins and induces their degradation. - Source: PubMed
Publication date: 2025/04/18
Li XiaomeiWang QingyangGuo AnpingQiu YapingChen QiuxiaLi YouZhang LanjunGuo YaxinMeng XiaoyunLi ShiqianLiu GuizhiZhang LiyunLiu JianLi XianyangCai LongyingCheng XueminLiu ChuanWang XiaotaoWood AndrewMurray JamesLiu GuansaiLi JinHuang XiaodongDou Dengfeng