Ask about this productRelated genes to: NUTF2 antibody
- Gene:
- NUTF2 NIH gene
- Name:
- nuclear transport factor 2
- Previous symbol:
- -
- Synonyms:
- NTF2, PP15
- Chromosome:
- 16q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-30
- Date modifiied:
- 2014-11-19
Related products to: NUTF2 antibody
Related articles to: NUTF2 antibody
- Oral squamous cell carcinoma (OSCC) is associated with a poor prognosis. Nuclear transport factor 2 (NUTF2) participates in nucleoprotein transport. However, the mechanism of NUTF2 in OSCC remains unclear. - Source: PubMed
Publication date: 2025/06/22
Chen ZhihongZhao ZhenyuanXu TengZou FengYang YuemeiLu PengChen YirenZhu ZaiouHe YaoWu YunongDing XuSong Xiaomeng - Urine samples are non-invasive approaches to study potential circulating biomarkers from the host organism. Specific proteins cross the bloodstream through the intestinal barrier and may also derive from gut microbiota. In this study, we aimed to evaluate the predictive role of the host and bacterial urine extracellular vesicle (EV) proteomes in patients with non-small cell lung cancer (NSCLC) treated with anti-PD1 immunotherapy. - Source: PubMed
Publication date: 2025/04/14
Dora DavidRevisnyei PeterPasic AlijaGalffy GabriellaDulka EditMihucz AnnaRoskó BrigittaSzincsak SaraIliuk AntonWeiss Glen JLohinai Zoltan - Oligomerization of proteoforms produces functional protein complexes. Characterization of these assemblies within cells is critical to understanding the molecular mechanisms involved in disease and to designing effective drugs. Here we present a native top-down proteomics (nTDP) strategy to identify protein assemblies (≤70 kDa) in breast cancer cells and in cells that overexpress epidermal growth factor receptor (EGFR), which serves as a resistance model of estrogen receptor-alpha (ER)-targeted therapies. This nTDP approach identified ~104 complexoforms from 17 protein complexes, which revealed several molecular features of the breast cancer proteome, including EGFR-induced dissociation of nuclear transport factor 2 (NUTF2) assemblies that modulate ER activity. We found that the K4 and K55 post-translational modification sites discovered with nTDP differentially impact the effects of NUTF2 on the inhibition of the ER signaling pathway. The characterization of endogenous proteoform-proteoform/ligand interactions revealed the molecular diversity of complexoforms and their role in breast cancer growth. - Source: PubMed
Publication date: 2025/04/04
Gomes Fabio PDurbin Kenneth RSchauer KevinNwachukwu Jerome CR Kobylski RobinNjeri Jacqline WSeath Ciaran PSaviola Anthony JMcClatchy Daniel BDiedrich Jolene KGarrett Patrick TPapa Alexandra BCiolacu IanisKelleher Neil LNettles Kendall WYates John R - Assisted reproduction technologies (ARTs) are generally considered safe; however, emerging evidence highlights the need to evaluate potential risks in adulthood to improve safety further. ART procedures like rederivation of embryos by vitrification differ from natural conditions, causing significant disparities between in vitro and in vivo embryos, affecting foetal physiology and postnatal life. This study aims to investigate whether hepatic transcriptome and metabolome changes observed postnatally are already present in foetal livers at the end of gestation. This study compared fresh and vitrified rabbit embryos, finding differences between foetuses obtained by the transfer of fresh and vitrified embryos at 24 days of gestation. Rederived embryos had reduced foetal and liver weights and crown-rump length. However, the offspring of vitrified embryos tended to be born with higher weight, showing compensatory growth in the final week of gestation (59.2 vs. 49.8 g). RNA-Seq analysis revealed 43 differentially expressed genes (DEGs) in the foetal liver of vitrified embryos compared to the fresh group. Notably, downregulated genes included BRAT1, CYP4A7, CYP2B4, RPL23, RPL22L1, PPILAL1, A1BG, IFGGC1, LRRC57, DIPP2, UGT2B14, IRGM1, NUTF2, MPST, and PPP1R1B, while upregulated genes included ACOT8, ERICH3, UBXN2A, METTL9, ALDH3A2, DERPC-like, NR5A2-like, AP-1, COG8, INHBE, and PLA2G4C. Overall, a functional annotation of these DEGs indicated an involvement in lipid metabolism and the stress and inflammatory process or immune response. Thus, our results suggest that vitrification and embryo transfer manipulation induce an adaptive response that can be observed in the liver during the last week of gestation. - Source: PubMed
Publication date: 2024/08/01
Vicente José SalvadorValdés-Hernández JesúsMarco-Jiménez Francisco - Oligomerization of proteins and their modified forms (proteoforms) produces functional protein complexes . Complexoforms are complexes that consist of the same set of proteins with different proteoforms . The ability to characterize these assemblies within cells is critical to understanding the molecular mechanisms involved in disease and to designing effective drugs. An outstanding biological question is how proteoforms drive function and oligomerization of complexoforms. However, tools to define endogenous proteoform-proteoform/ligand interactions are scarce . Here, we present a native top-down proteomics (nTDP) strategy that combines size-exclusion chromatography, nano liquid-chromatography in direct infusion mode, field asymmetric ion mobility spectrometry, and multistage mass spectrometry to identify protein assemblies (≤70 kDa) in breast cancer cells and in cells that overexpress EGFR, a resistance model of estrogen receptor-α (ER-α) targeted therapies. By identifying ~104 complexoforms from 17 protein complexes, our nTDP approach revealed several molecular features of the breast cancer proteome, including EGFR-induced dissociation of nuclear transport factor 2 (NUTF2) assemblies that modulate ER activity. Our findings show that the K4 and K55 posttranslational modification sites discovered with nTDP differentially impact the effects of NUTF2 on the inhibition of the ER signaling pathway. By characterizing endogenous proteoform-proteoform/ligand interactions, we reveal the molecular diversity of complexoforms, which allows us to propose a model for ER drug discovery in the context of designing effective inhibitors to selectively bind and disrupt the actions of targeted ER complexoforms. - Source: PubMed
Publication date: 2023/07/24
Yates JohnGomes FabioDurbin KennethSchauer KevinNwachukwu JeromeRusso RobinNjeri JacqlineSaviola AnthonyMcClatchy DanielDiedrich JoleneGarrett PatrickPapa AlexandraCiolacu IanisKelleher NeilNettles Kendall