Ask about this productRelated genes to: PDCD8 antibody
- Gene:
- AIFM1 NIH gene
- Name:
- apoptosis inducing factor mitochondria associated 1
- Previous symbol:
- PDCD8, NAMSD
- Synonyms:
- AIF, CMTX4
- Chromosome:
- Xq26.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-28
- Date modifiied:
- 2017-01-12
Related products to: PDCD8 antibody
Related articles to: PDCD8 antibody
- CRISPR gene editing technologies have transformed functional genomics and biotechnology. Despite these advances, challenges such as limited delivery capacity and off-target activity continue to hinder their therapeutic translation. We developed a chimeric gene editing platform by fusing the compact, catalytically inactive Cas12m guiding module (GoCas12m) with the FokI nuclease domain. GoCas12m-FokI system integrates the programmable DNA-binding capability of Cas12m with the dimerization-dependent cleavage mechanism of FokI, enabling precise genome editing. Our engineered XTEN-fused GoCas12m-FokI editor exhibits robust activity on both surrogate reporters and endogenous human loci, achieving high-efficiency editing at clinically relevant targets-including CLTA1, HBB, AIFM1, and ABL with no detectable off-target activity at in silico-predicted sites, as confirmed by targeted deep sequencing. Notably, GoCas12m-FokI is nearly half the size of conventional Cas9- or Cas12a-based editors, facilitating delivery via adeno-associated virus and other cargo-limited vectors. This dual-guided editor showed comparable editing efficiency to previously reported FokI-dCas9 systems on endogenous loci, while possessing a different PAM requirement and domain orientation. By combining compact architecture, high specificity, and modular programmability, the GoCas12m-FokI editor offers a powerful alternative for therapeutic genome editing and a promising tool for in vivo gene therapy applications. - Source: PubMed
Marsic TinGundra Sivakrishna RaoAouida MustaphaMasood MaazallahSalibi AlexanderSchmidt FabianAlquwayzani ReemMahfouz Magdy M - Type II NADH: Quinone oxidoreductase (NDH2) represents a critical metabolic target in Plasmodium parasites. Although NDH2 lacks a direct human isoenzyme, it shares significant structural homology with human Apoptosis-Inducing Factor Mitochondrion-associated 1 (AIF-M1), presenting a substantial challenge for selective drug design. To address this selectivity hurdle, the first comparative computational study was conducted across five human-infecting Plasmodium species (P. falciparum, P. knowlesi, P. malariae, P. ovale, and P. vivax) using a natural compound library. - Source: PubMed
Publication date: 2026/04/16
Baye Bertha CinthiaMoses VuyaniUgbaja Samuel ChimaLobb Kevin Alan - - Source: PubMed
Publication date: 2026/04/09
Ferrer MiguelPedrón MaríaSoriano OlgaMartínez-Julvez MartaMarín-Baquero MikelGarcía-Villanueva RutVelázquez-Campoy AdriánMarco-Brualla JoaquínRipollés-Yuba CristinaFernández-Silva PatricioMedina MilagrosMiramar María DoloresBestué MaríaMoreno-Loshuertos RaquelFerreira Patricia - Oxeiptosis is a reactive oxygen species (ROS)-dependent form of programmed cell death that plays a key role in cellular homeostasis and holds promise as a cancer therapy. This review explores its molecular mechanisms, emphasizing the KEAP1-PGAM5-AIFM1 signalling pathway and its reliance on ROS accumulation. Compared to other cell death pathways, oxeiptosis offers a distinct approach, especially for targeting cancer cells resistant to conventional therapies. The review evaluates emerging inducers, both synthetic and natural, that selectively trigger oxeiptosis in cancer cells. It also examines the potential synergy between oxeiptosis and ROS-generating chemotherapies, particularly in the oxidative tumour microenvironment. However, challenges remain, including identifying tumour-specific inducers, overcoming cancer cell resistance to oxidative stress and reducing off-target effects. The review concludes by highlighting the need for targeted delivery strategies and rigorous preclinical studies to translate oxeiptosis into effective cancer treatments. Overall, it underscores oxeiptosis as a promising avenue to address drug resistance and improve therapeutic outcomes in oncology. - Source: PubMed
Publication date: 2026/03/27
Kciuk MateuszWanke KatarzynaKałuzińska-Kołat ŻanetaKontek Renata - Mitochondrial proteases regulate dynamic properties of organelle morphology and ensure functional plasticity at the cellular level. The metalloprotease OMA1 mediates constitutive and stress-inducible processing of its mitochondrial substrates, although only a few of its direct functional targets have been characterized. Using in vitro and in vivo multiproteomic and biochemical approaches, we here demonstrate that the membrane-anchored intermembrane space (IMS) protein AIFM1 serves as a mitochondrial stress-responsive OMA1 substrate. Under stress conditions, OMA1 cleaves AIFM1 in the IMS with slower kinetics than its conventional substrate, the dynamin-like GTPase OPA1. OMA1-mediated dislocation of cleaved AIFM1 from the mitochondrial inner membrane reduces its interaction with oxidative phosphorylation subunits, thereby decreasing respiratory activity and impairing cell growth. Furthermore, we reveal that under steady-state conditions AIFM1 broadly safeguards the mitochondrial proteome by mediating the import of proteins, particularly respiratory complex I subunits, via the TIM23 complex. Similar changes to the mitochondrial proteome occur in the lungs of virally infected mice, accompanied by stress-inducible AIFM1 processing. These findings identify OMA1 as a key integrator of mitochondrial stress and cellular energetics through AIFM1 remodeling. - Source: PubMed
Publication date: 2026/03/24
Nishigori MitsuhiroHirata SerinaKosako HidetakaIchinohe TakeshiNolte HendrikRiemer JanLanger ThomasKoshiba Takumi