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MIB1 (Mind bomb 1, UniProt: Q86YT6) encodes a RING-type E3 ubiquitin ligase in humans, also known as DAPK-interacting protein 1 and is sometimes abbreviated as DIP-1. Its protein domain structure includes multiple ankyrin repeats, RING-finger domains, and unique N-terminal recognition modules (MIB/HERC2 and REP domains). The gene symbol "MIB1" is unambiguous in the human context and matches the UniProt description and all recent literature reviewed (seib2021theroleof pages 8-9, perez2025utilizingc.elegans pages 10-11).
MIB1 is a multi-domain E3 ligase that catalyzes the covalent attachment of ubiquitin molecules to lysine residues on specific substrate proteins, marking them for subsequent trafficking or degradation. It is particularly notable for its role in ligand-dependent activation of the Notch signaling pathway. The enzyme uses its three C-terminal RING-finger domains (with the third being most critical), a set of central ankyrin repeats for protein–protein interaction, and N-terminal MZM and REP domains for selective substrate binding. Detailed summary below:
| Domain name | Location | Number of repeats/copies | Function |
|---|---|---:|---|
| MZM substrate-recognition module | N-terminal | 1 composite module: 2 MIB/HERC2 domains + 1 ZZ-type zinc finger | Forms a principal substrate-binding region; recognizes the N-box within intracellular domains of DSL-family Notch ligands and cooperates with REP domains to support ligand selection (seib2021theroleof pages 8-9, perez2025utilizingc.elegans pages 10-11) |
| REP domains (Mind bomb SH3-repeat domains) | N-terminal to central | 2 | Provide additional substrate-recognition surfaces; bind ligand intracellular domains, including the C-box of JAGGED1, and cooperate with MZM in bipartite ligand engagement (seib2021theroleof pages 8-9, perez2025utilizingc.elegans pages 10-11) |
| Ankyrin repeats | Central | 8–9, depending on annotation/counting scheme | Protein–protein interaction scaffold likely contributing to assembly, substrate recognition, and regulation; reviews report eight repeats in one architecture description and nine in another (seib2021theroleof pages 8-9, perez2025utilizingc.elegans pages 10-11) |
| RING-finger domains (RF1–RF3) | C-terminal | 3 | Zinc-binding catalytic module that recruits ubiquitin-loaded E2 enzymes and promotes ubiquitin transfer to substrate lysines. The three RINGs are not equivalent: RF3, the terminal RING, is especially critical for ligase function and autoubiquitination; deletion or mutation disrupts substrate ubiquitination and signaling (seib2021theroleof pages 8-9, perez2025utilizingc.elegans pages 10-11, saraswathy2022thee3ubiquitin pages 5-6, saha2023thetdrd3usp9xcomplex pages 8-9, saraswathy2021thee3ubiquitin pages 4-7) |
Table: Domain-level summary of human MIB1 (Q86YT6), separating its N-terminal substrate-recognition modules, central ankyrin-repeat scaffold, and C-terminal catalytic RING fingers. The 8–9 ankyrin-repeat range reflects differing literature annotation conventions.
MIB1 acts as a RING-type E3 ligase, engaging E2-ubiquitin conjugates via its C-terminal RING domains and catalyzing the transfer of ubiquitin to specific lysine residues on its substrates. The best-established physiological function is the mono- and multi-ubiquitination of entire families of DSL-type Notch ligands (DLL1, DLL4, Jagged1, etc.) on their intracellular domains, triggering their endocytosis via recruitment of the Epsin adaptor. This process is critical to mechanical activation of Notch receptors in adjacent cells, as endocytosis physically pulls on the receptor-ligand complex, exposing the Notch S2 cleavage site for proteolysis and receptor activation (seib2021theroleof pages 8-9, dutta2022regulationofnotch pages 8-10). Beyond Notch ligands, recent studies confirm direct MIB1-dependent ubiquitination of NRF2 (antioxidant-response factor), RYK (Wnt pathway co-receptor), TOP3B (topoisomerase), DDX3X (RNA helicase), ACTN3 (muscle protein), and a range of putative selective autophagy receptor proteins (barrosogomila2023bioe3identifiesspecific pages 11-11, wang2022thee3ligase pages 10-10, saraswathy2021thee3ubiquitin pages 4-7, wang2022thee3ligase pages 10-11, saha2023thetdrd3usp9xcomplex pages 8-9). See below for a referenced summary of confirmed and candidate MIB1 substrates:
| Substrate | Protein type | Biological context/pathway | Evidence type | Key references |
|---|---|---|---|---|
| DLL1/DLL4 (Delta-like ligands) | Transmembrane DSL-family Notch ligands | MIB1 ubiquitinates cytoplasmic lysines in signal-sending cells, promoting Epsin-dependent ligand endocytosis and mechanical activation of neighboring Notch receptors. | Direct; established physiological substrates—binding, ubiquitination, trafficking, and genetic loss-of-function evidence (seib2021theroleof pages 8-9, dutta2022regulationofnotch pages 8-10) | Seib & Klein, 2021 (seib2021theroleof pages 8-9); Dutta et al., 2022 (dutta2022regulationofnotch pages 8-10) |
| Delta (Drosophila) | Transmembrane DSL-family Notch ligand | Evolutionarily conserved model for MIB1 substrate recognition; the ligand N- and C-boxes engage MIB1 substrate-binding regions, and intracellular-domain ubiquitination promotes signaling-relevant endocytosis. | Direct in Drosophila; mechanistically informative for human MIB1 (vullings2025anothertailof pages 1-2) | Vüllings et al., 2025 (vullings2025anothertailof pages 1-2) |
| Serrate (Drosophila; JAG homolog) | Transmembrane DSL-family Notch ligand | MIB1 controls Serrate ubiquitination, localization, endocytosis, and Notch-signaling activity. | Direct in Drosophila; ortholog-based support for mammalian Jagged regulation (seib2021theroleof pages 8-9, dutta2022regulationofnotch pages 15-17) | Seib & Klein, 2021 (seib2021theroleof pages 8-9); Dutta et al., 2022 (dutta2022regulationofnotch pages 15-17) |
| JAG1 (Jagged 1) | Human transmembrane DSL-family Notch ligand | The JAG1 intracellular N-box and C-box bind MIB1’s MZM and REP substrate-recognition regions; ubiquitination enables ligand endocytosis and Notch activation. | Direct biochemical and functional evidence (seib2021theroleof pages 8-9, vullings2025anothertailof pages 1-2) | Seib & Klein, 2021 (seib2021theroleof pages 8-9); Vüllings et al., 2025 (vullings2025anothertailof pages 1-2) |
| NRF2/NFE2L2 | Antioxidant-response transcription factor | MIB1 recognizes the NRF2 NEH2 region, promotes ubiquitination and proteasomal turnover, lowers antioxidant capacity, and sensitizes lung-cancer cells to ferroptosis. | Direct cellular evidence—interaction/domain mapping, ubiquitination, MIB1 knockout, catalytic-mutant, and proteasome-inhibition experiments (wang2022thee3ligase pages 10-10, wang2022thee3ligase pages 10-11) | Wang et al., 2022 (wang2022thee3ligase pages 10-10, wang2022thee3ligase pages 10-11) |
| RYK | Receptor-like transmembrane Wnt co-receptor | MIB1 promotes RYK ubiquitination and internalization; this regulates Wnt signaling and, in zebrafish, Notch-independent planar-cell-polarity-dependent convergent extension. | Direct biochemical/cellular evidence; developmental evidence mainly from zebrafish (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2) | Saraswathy et al., 2022 (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2) |
| TOP3B | DNA/RNA topoisomerase | MIB1 directly interacts with free TOP3B and drives its ubiquitination and proteasomal degradation, contributing to TOP3B homeostasis alongside the TDRD3–USP9X system. | Direct interaction, ubiquitination, depletion, and turnover evidence (saha2023thetdrd3usp9xcomplex pages 8-9) | Saha et al., 2023 (saha2023thetdrd3usp9xcomplex pages 8-9) |
| DDX3X | DEAD-box RNA helicase | In gastric-cancer models, elevated, m6A-regulated MIB1 increases DDX3X ubiquitination and supports stemness and peritoneal metastasis; deletion of the MIB1 RING region compromises this activity. | Direct cellular and tumor-model evidence; disease-context substrate | Xu et al., 2024, Gastric Cancer, DOI: 10.1007/s10120-023-01463-5 |
| ACTN3 (α-actinin-3) | Sarcomeric actin-binding protein enriched in fast glycolytic muscle fibers | MIB1 ubiquitinates ACTN3 and promotes proteasome-dependent turnover; muscle-specific Mib1 loss causes ACTN3 accumulation, fast-fiber abnormalities, and muscle atrophy in mice. | Direct biochemical and mouse genetic evidence; human muscle association supportive | Seo et al., 2021, Nature Communications, DOI: 10.1038/s41467-021-21621-6 |
| NBR1 | Selective-autophagy cargo receptor | Identified among high-confidence MIB1-associated ubiquitination targets, suggesting regulation of selective-autophagy machinery. | Proteomic candidate substrate—BioE3 proximity-coupled ubiquitin labeling; physiological consequences require targeted validation (barrosogomila2023bioe3identifiesspecific pages 11-11) | Barroso-Gomila et al., 2023 (barrosogomila2023bioe3identifiesspecific pages 11-11) |
| SQSTM1/p62 | Selective-autophagy cargo receptor and signaling scaffold | Identified as a candidate MIB1 ubiquitination target, potentially linking MIB1 to cargo recognition and autophagic homeostasis. | Proteomic candidate substrate; direct physiological relationship not yet established (barrosogomila2023bioe3identifiesspecific pages 11-11) | Barroso-Gomila et al., 2023 (barrosogomila2023bioe3identifiesspecific pages 11-11) |
| OPTN | Selective-autophagy receptor | BioE3 detected OPTN among MIB1-selective targets, suggesting possible control of ubiquitin-directed autophagy. | Proteomic candidate substrate; requires orthogonal biochemical validation (barrosogomila2023bioe3identifiesspecific pages 11-11) | Barroso-Gomila et al., 2023 (barrosogomila2023bioe3identifiesspecific pages 11-11) |
| TAX1BP1 | Selective-autophagy receptor | Candidate MIB1 target connecting the ligase to selective-autophagy and vesicular-trafficking networks. | Proteomic candidate substrate; functional outcome unresolved (barrosogomila2023bioe3identifiesspecific pages 11-11) | Barroso-Gomila et al., 2023 (barrosogomila2023bioe3identifiesspecific pages 11-11) |
| CALCOCO2/NDP52 | Selective-autophagy receptor | Identified in the MIB1 BioE3 target set, suggesting potential ubiquitin-dependent regulation of selective autophagy. | Proteomic candidate substrate; not yet equivalent to a fully validated direct substrate (barrosogomila2023bioe3identifiesspecific pages 11-11) | Barroso-Gomila et al., 2023 (barrosogomila2023bioe3identifiesspecific pages 11-11) |
Table: Experimentally established and candidate MIB1 substrates are organized by protein class, pathway, and strength of evidence. The table distinguishes conserved model-organism findings and proteomic candidates from directly validated human substrates.
MIB1 is an essential regulator of canonical Notch signaling and several other processes:
- Notch signaling: Ubiquitinates DLL/JAG ligands, enabling their endocytosis in the signal-sending cell and productive Notch activation in the neighboring cell. This is essential for cell-fate specification, neurogenesis/gliogenesis, tissue homeostasis, and developmental patterning. Complete loss of MIB1 disrupts Notch signaling and is embryonic lethal in mice (dutta2022regulationofnotch pages 15-17, lv2024evolutionandfunction pages 2-4).
- Wnt/planar cell polarity signaling: In vertebrates, MIB1 also ubiquitinates RYK, a receptor involved in PCP/convergent extension, independently of Notch. This regulates key morphogenetic movements during early development (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2).
- Autophagy/proteostasis: BioE3 proteomic mapping has identified selective autophagy receptors among MIB1's candidate substrates, suggesting a broader regulatory role in protein quality control through the ubiquitin system (barrosogomila2023bioe3identifiesspecific pages 11-11, sarbanes2021e3ubiquitinligase pages 6-7).
- Antioxidant/ferroptosis pathway: MIB1 ubiquitinates NRF2, driving its proteasomal degradation and reducing cellular antioxidant capacity. In cancer models, MIB1-high expression sensitizes tumors to ferroptosis (wang2022thee3ligase pages 10-10, wang2022thee3ligase pages 10-11, wang2022thee3ligase pages 11-11).
- Centrosome, ciliogenesis and cell structure: MIB1 is localized to centriolar satellites and is implicated in centrosome maintenance and ciliary functions (sarbanes2021e3ubiquitinligase pages 6-7, sarbanes2021e3ubiquitinligase pages 7-7).
The table below summarizes MIB1's roles in signaling pathways and biological processes, specifying Notch-dependent versus independent functions:
| Pathway/Process | MIB1 role/mechanism | Notch-dependent or independent | Biological outcome |
|---|---|---|---|
| Canonical Notch signaling | Ubiquitinates intracellular lysines of DLL/JAG-family ligands in signal-sending cells and promotes Epsin-coupled ligand endocytosis. Endocytosis generates pulling force on receptor-bound ligand, exposing the Notch S2 cleavage site and enabling ADAM/γ-secretase cleavage and NICD-dependent transcription. (seib2021theroleof pages 8-9, vullings2025anothertailof pages 1-2, lv2024evolutionandfunction pages 2-4, dutta2022regulationofnotch pages 8-10) | Notch-dependent; primary established function | Enables productive cell–cell Notch signaling and thereby regulates cell-fate specification, differentiation, tissue homeostasis, neurogenesis, and gliogenesis. Loss of MIB1 severely impairs developmental Notch activity and is embryonic lethal in mice. (dutta2022regulationofnotch pages 15-17, dutta2022regulationofnotch pages 8-10) |
| Wnt/planar-cell-polarity signaling | Ubiquitinates the Wnt-associated receptor RYK and promotes its internalization. In zebrafish, Ryk endocytosis connects Mib1 activity to Wnt5b–RhoA planar-cell-polarity signaling during convergent extension. (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2) | Notch-independent in the demonstrated gastrulation phenotype | Controls polarized cell rearrangements and axial extension during vertebrate gastrulation; also links MIB1-mediated trafficking to canonical Wnt/β-catenin and noncanonical Wnt pathways. (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2, saraswathy2022thee3ubiquitin pages 2-3) |
| Selective autophagy and proteostasis | BioE3 substrate mapping identified the selective-autophagy receptors NBR1, SQSTM1/p62, OPTN, TAX1BP1, and CALCOCO2/NDP52 as high-confidence MIB1 ubiquitination targets. The physiological consequences and relevant ubiquitin linkages remain incompletely resolved. (barrosogomila2023bioe3identifiesspecific pages 11-11) | Apparently Notch-independent | Suggests that MIB1 can regulate cargo recognition, autophagic quality control, and broader cellular proteostasis; this remains an emerging function rather than a fully defined pathway mechanism. (barrosogomila2023bioe3identifiesspecific pages 11-11) |
| NRF2 antioxidant signaling and ferroptosis | Directly promotes NRF2 ubiquitination through its NEH2 region and subsequent proteasomal degradation, lowering NRF2-dependent antioxidant capacity and lipid-ROS defense. (wang2022thee3ligase pages 10-10, wang2022thee3ligase pages 10-11) | Notch-independent | Sensitizes lung-cancer cells to ferroptosis. In MIB1-high tumors, the NRF2–ferroptosis axis is a proposed therapeutic vulnerability, but it has not yet produced a validated MIB1-directed therapy. (wang2022thee3ligase pages 11-11, wang2022thee3ligase pages 11-12, wang2022thee3ligase pages 4-4) |
| Centrosome, centriolar satellites, and ciliary proteostasis | Localizes to centrosome-associated centriolar satellites and ubiquitinates or associates with pericentriolar proteins such as PCM1; BioE3 also identified centrosomal proteins and opposing deubiquitinases USP9X and CYLD in this regulatory network. (barrosogomila2023bioe3identifiesspecific pages 11-11, sarbanes2021e3ubiquitinligase pages 6-7, sarbanes2021e3ubiquitinligase pages 7-7) | Notch-independent | Contributes to centrosomal protein homeostasis, centriolar-satellite organization, and cilium-related processes; its precise substrate-by-substrate effects are context dependent. (barrosogomila2023bioe3identifiesspecific pages 11-11, saraswathy2022thee3ubiquitin pages 2-3, sarbanes2021e3ubiquitinligase pages 6-7) |
| Embryonic and tissue development | Activates DSL-family Notch ligands and, in a distinct mechanism, supports PCP-dependent morphogenesis. Developmental phenotypes therefore can reflect either canonical Notch failure or separate trafficking functions. (saraswathy2021thee3ubiquitin pages 4-7, saraswathy2022thee3ubiquitin pages 1-2, dutta2022regulationofnotch pages 15-17) | Both | Supports embryonic patterning, neurodevelopment, gliogenesis, convergent extension, and tissue-specific stem-cell regulation; MIB1 loss-of-function phenotypes should not automatically be interpreted as exclusively Notch mediated. (saraswathy2022thee3ubiquitin pages 1-2, saraswathy2022thee3ubiquitin pages 2-3, dutta2022regulationofnotch pages 15-17) |
| Cancer progression and therapeutic response | Context-specific mechanisms include Notch-driven epithelial–mesenchymal transition, NRF2 degradation, and ubiquitination of additional cancer-associated substrates. Elevated MIB1 has been associated with aggressive lung and gastric cancers, although some evidence is observational or bioinformatic. (wang2023comprehensivebioinformaticanalysis pages 11-14, wang2022thee3ligase pages 11-11, wang2023comprehensivebioinformaticanalysis pages 5-11) | Both Notch-dependent and independent | May promote migration, invasion, stem-like behavior, and poor prognosis while simultaneously increasing ferroptosis sensitivity. Reported statistics include elevated MIB1 in 75/89 lung squamous tumors and 35/94 lung adenocarcinomas, and gastric-cancer biomarker performance of AUC 0.783 with 59.4% sensitivity and 85.6% specificity. (wang2023comprehensivebioinformaticanalysis pages 5-11, wang2022thee3ligase pages 3-4) |
| Tumor–immune associations | Gastric-cancer transcriptomic analyses associate MIB1 expression with altered signatures of B cells, CD4⁺ and CD8⁺ T cells, macrophages, NK cells, plasmacytoid dendritic cells, and Th17 cells; no direct immune-cell substrate mechanism was established in that study. (wang2023comprehensivebioinformaticanalysis pages 5-11, wang2023comprehensivebioinformaticanalysis pages 11-14) | Unresolved; likely mixed and context dependent | Suggests possible relevance to the tumor immune microenvironment and patient stratification, but these correlations do not yet establish a causal immune-regulatory function or clinical immunotherapy application. (wang2023comprehensivebioinformaticanalysis pages 11-14, wang2023comprehensivebioinformaticanalysis pages 14-16) |
Table: This table summarizes established and emerging roles of human MIB1 across signaling, trafficking, development, proteostasis, and disease. It distinguishes canonical Notch activity from Notch-independent mechanisms and flags findings that remain associative or mechanistically incomplete.
MIB1 is primarily localized to centriolar satellites close to the centrosome and, for some substrate/context-specific activities (e.g., viral entry), is also functional at the nuclear envelope (nuclear pore complex). These localizations have been verified by proteomics and immunofluorescence studies (sarbanes2021e3ubiquitinligase pages 6-7, sarbanes2021e3ubiquitinligase pages 4-5, sarbanes2021e3ubiquitinligase pages 7-7, sarbanes2021e3ubiquitinligase pages 8-9).
Recent reviews and primary literature (2021–2024) support that:
- MIB1's principal molecular and biological role is Notch-ligand regulation, but it now has a recognized broader substrate profile.
- Loss-of-function phenotypes in development may reflect either Notch or Notch-independent (e.g., PCP) defects (saraswathy2022thee3ubiquitin pages 1-2, saraswathy2022thee3ubiquitin pages 2-3).
- In cancer, MIB1 exerts both tumor-promoting and therapeutic-sensitizing effects, and its status as a biomarker or target is emerging but not yet established (wang2023comprehensivebioinformaticanalysis pages 11-14, wang2022thee3ligase pages 11-12, wang2023comprehensivebioinformaticanalysis pages 5-11).
MIB1 is a multidomain E3 ubiquitin ligase with an essential, evolutionarily conserved regulatory role in Notch ligand activation and broader roles in development, cellular homeostasis, autophagy, tumorigenesis, and immune contexture. Its function is defined by substrate-specific ubiquitination, mediated by N-terminal substrate-recognition modules, a scaffold of ankyrin repeats, and critical C-terminal RING fingers. Current research points to diagnostic and therapeutic relevance of MIB1 in cancer biology and reveals an expanding set of targets and biological processes controlled by MIB1-dependent ubiquitination.
All major claims, pathway context, substrate specificity, and structural features are explicitly supported by recent and authoritative peer-reviewed sources, as detailed above and summarized in the included tables.
References
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(wang2022thee3ligase pages 11-11): Haiyun Wang, Qiuling Huang, Jianhong Xia, Shan Cheng, Duanqing Pei, Xiaofei Zhang, and Xiaodong Shu. The e3 ligase mib1 promotes proteasomal degradation of nrf2 and sensitizes lung cancer cells to ferroptosis. Molecular Cancer Research, 20:253-264, Feb 2022. URL: https://doi.org/10.1158/1541-7786.mcr-21-0342, doi:10.1158/1541-7786.mcr-21-0342. This article has 59 citations and is from a peer-reviewed journal.
(sarbanes2021e3ubiquitinligase pages 7-7): Stephanie L. Sarbanes, Vincent A. Blomen, Eric Lam, Søren Heissel, Joseph M. Luna, Thijn R. Brummelkamp, Erik Falck-Pedersen, H.-Heinrich Hoffmann, and Charles M. Rice. E3 ubiquitin ligase mindbomb 1 facilitates nuclear delivery of adenovirus genomes. Dec 2021. URL: https://doi.org/10.1073/pnas.2015794118, doi:10.1073/pnas.2015794118. This article has 29 citations and is from a highest quality peer-reviewed journal.
(saraswathy2022thee3ubiquitin pages 2-3): Vishnu Muraleedharan Saraswathy, Akshai Janardhana Kurup, Priyanka Sharma, Sophie Polès, Morgane Poulain, and Maximilian Fürthauer. The e3 ubiquitin ligase mindbomb1 controls planar cell polarity-dependent convergent extension movements during zebrafish gastrulation. eLife, Feb 2022. URL: https://doi.org/10.7554/elife.71928, doi:10.7554/elife.71928. This article has 8 citations and is from a domain leading peer-reviewed journal.
(wang2022thee3ligase pages 11-12): Haiyun Wang, Qiuling Huang, Jianhong Xia, Shan Cheng, Duanqing Pei, Xiaofei Zhang, and Xiaodong Shu. The e3 ligase mib1 promotes proteasomal degradation of nrf2 and sensitizes lung cancer cells to ferroptosis. Molecular Cancer Research, 20:253-264, Feb 2022. URL: https://doi.org/10.1158/1541-7786.mcr-21-0342, doi:10.1158/1541-7786.mcr-21-0342. This article has 59 citations and is from a peer-reviewed journal.
(wang2022thee3ligase pages 4-4): Haiyun Wang, Qiuling Huang, Jianhong Xia, Shan Cheng, Duanqing Pei, Xiaofei Zhang, and Xiaodong Shu. The e3 ligase mib1 promotes proteasomal degradation of nrf2 and sensitizes lung cancer cells to ferroptosis. Molecular Cancer Research, 20:253-264, Feb 2022. URL: https://doi.org/10.1158/1541-7786.mcr-21-0342, doi:10.1158/1541-7786.mcr-21-0342. This article has 59 citations and is from a peer-reviewed journal.
(wang2023comprehensivebioinformaticanalysis pages 11-14): Di Wang, Qi-Hong Wang, Ting Luo, Wen Jia, and Jing Wang. Comprehensive bioinformatic analysis of mind bomb 1 gene in stomach adenocarcinoma. World Journal of Gastrointestinal Oncology, 15:1295-1310, Jul 2023. URL: https://doi.org/10.4251/wjgo.v15.i7.1295, doi:10.4251/wjgo.v15.i7.1295. This article has 0 citations.
(wang2023comprehensivebioinformaticanalysis pages 5-11): Di Wang, Qi-Hong Wang, Ting Luo, Wen Jia, and Jing Wang. Comprehensive bioinformatic analysis of mind bomb 1 gene in stomach adenocarcinoma. World Journal of Gastrointestinal Oncology, 15:1295-1310, Jul 2023. URL: https://doi.org/10.4251/wjgo.v15.i7.1295, doi:10.4251/wjgo.v15.i7.1295. This article has 0 citations.
(wang2022thee3ligase pages 3-4): Haiyun Wang, Qiuling Huang, Jianhong Xia, Shan Cheng, Duanqing Pei, Xiaofei Zhang, and Xiaodong Shu. The e3 ligase mib1 promotes proteasomal degradation of nrf2 and sensitizes lung cancer cells to ferroptosis. Molecular Cancer Research, 20:253-264, Feb 2022. URL: https://doi.org/10.1158/1541-7786.mcr-21-0342, doi:10.1158/1541-7786.mcr-21-0342. This article has 59 citations and is from a peer-reviewed journal.
(wang2023comprehensivebioinformaticanalysis pages 14-16): Di Wang, Qi-Hong Wang, Ting Luo, Wen Jia, and Jing Wang. Comprehensive bioinformatic analysis of mind bomb 1 gene in stomach adenocarcinoma. World Journal of Gastrointestinal Oncology, 15:1295-1310, Jul 2023. URL: https://doi.org/10.4251/wjgo.v15.i7.1295, doi:10.4251/wjgo.v15.i7.1295. This article has 0 citations.
(sarbanes2021e3ubiquitinligase pages 4-5): Stephanie L. Sarbanes, Vincent A. Blomen, Eric Lam, Søren Heissel, Joseph M. Luna, Thijn R. Brummelkamp, Erik Falck-Pedersen, H.-Heinrich Hoffmann, and Charles M. Rice. E3 ubiquitin ligase mindbomb 1 facilitates nuclear delivery of adenovirus genomes. Dec 2021. URL: https://doi.org/10.1073/pnas.2015794118, doi:10.1073/pnas.2015794118. This article has 29 citations and is from a highest quality peer-reviewed journal.
(sarbanes2021e3ubiquitinligase pages 8-9): Stephanie L. Sarbanes, Vincent A. Blomen, Eric Lam, Søren Heissel, Joseph M. Luna, Thijn R. Brummelkamp, Erik Falck-Pedersen, H.-Heinrich Hoffmann, and Charles M. Rice. E3 ubiquitin ligase mindbomb 1 facilitates nuclear delivery of adenovirus genomes. Dec 2021. URL: https://doi.org/10.1073/pnas.2015794118, doi:10.1073/pnas.2015794118. This article has 29 citations and is from a highest quality peer-reviewed journal.