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The gene tub (also known as tube) in Drosophila melanogaster encodes the Tube protein (UniProt accession P22812), a well-characterized death domain-containing adaptor protein in the Toll signaling pathway. This protein is distinct from other proteins or anatomical structures that might share similar names. The protein contains the characteristic DEATH-like domain superfamily (IPR011029), Death domain (IPR000488), Tube-specific Death domain (IPR029397), and Death_2 domain (PF14786) as indicated in UniProt, which match the experimentally established Toll pathway component (rashidi2022insilicocharacterization pages 8-11, rashidi2022insilicocharacterization pages 6-8).
Tube functions as a non-enzymatic adaptor and scaffolding protein in the Toll signaling pathway. Unlike kinases or enzymes with specific substrates, Tube does not catalyze biochemical reactions. Instead, its primary molecular role is to mediate protein-protein interactions through its death domain, organizing the signaling complex required for Toll pathway activation (rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2).
Tube contains an N-terminal death domain that serves as its principal functional module. Structural studies have revealed that this domain adopts a characteristic fold with eight α-helices and four β-sheets (rashidi2022insilicocharacterization pages 11-14). The death domain mediates homotypic protein-protein interactions with two critical binding partners:
MyD88 (Myeloid differentiation primary response 88): The adaptor protein recruited to the activated Toll receptor through TIR domain interactions (cammaratamouchtouris2022dynamicregulationof pages 4-6, rashidi2022insilicocharacterization pages 16-18)
Pelle: A serine/threonine kinase that is homologous to mammalian IRAK (Interleukin-1 receptor-associated kinase) proteins (rashidi2022insilicocharacterization pages 8-11, rashidi2022insilicocharacterization pages 6-8)
Tube serves as a critical bridge between MyD88 and Pelle, as these proteins do not directly interact with each other. By connecting MyD88 to Pelle through its death domain, Tube assembles the functional MyD88-Tube-Pelle signaling complex (rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2, cammaratamouchtouris2022dynamicregulationof pages 4-6, yokoi2022pelleandtube pages 1-2).
Structurally, Tube shares evolutionary relationships with mammalian MyD88 pathway components, particularly IRAK proteins. However, in Drosophila melanogaster, Tube itself lacks catalytic kinase activity—this function is instead performed by Pelle (rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2). While some insect species show kinase-related domain annotations in their Tube orthologs, the D. melanogaster Tube is characterized primarily by its death domain adaptor function rather than enzymatic activity (rashidi2022insilicocharacterization pages 8-11, rashidi2022insilicocharacterization pages 6-8).
Tube is a cytoplasmic protein that becomes membrane-associated upon pathway activation. Following ligand binding to the Toll receptor, Tube is recruited to the plasma membrane as part of the receptor-proximal signaling complex (stein2014maternalcontrolof pages 12-14).
Membrane localization is functionally essential: experimental studies have shown that artificially targeting Tube to the plasma membrane through myristylation or fusion to a transmembrane domain is sufficient to activate ventralizing Toll signaling, even in the absence of upstream signals (stein2014maternalcontrolof pages 12-14). Tube is neither secreted nor does it possess a transmembrane domain—it functions exclusively on the cytoplasmic face of the plasma membrane when recruited to the activated receptor complex.
Tube functions as a core component of the canonical Toll signaling pathway, which follows this sequence:
Spätzle → Toll → MyD88 → Tube → Pelle → Cactus → NF-κB (Dorsal/Dif)
The pathway is initiated when the processed form of the cytokine-like ligand Spätzle (Spz) binds to the extracellular domain of the Toll receptor (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, rashidi2022insilicocharacterization pages 16-18, yu2022drosophilainnateimmunity pages 5-7). This activation triggers receptor dimerization and recruitment of intracellular signaling components.
Upon Toll activation, the following molecular events occur:
The intracellular TIR (Toll/Interleukin-1 receptor) domain of Toll recruits MyD88 through TIR-TIR interactions (cammaratamouchtouris2022dynamicregulationof pages 4-6, rashidi2022insilicocharacterization pages 16-18)
MyD88 recruits Tube through death domain-death domain interactions, and Tube in turn recruits the kinase Pelle, forming the membrane-associated heterotrimeric MyD88-Tube-Pelle complex (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, yokoi2022pelleandtube pages 1-2)
This complex positioning enables Pelle to become activated and phosphorylate Cactus, the Drosophila homolog of mammalian IκB (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2)
Phosphorylated Cactus is targeted for proteasomal degradation, removing the inhibitory constraint on the NF-κB-like transcription factors Dorsal and Dif (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2)
Released Dorsal and Dif translocate to the nucleus, where they activate transcription of target genes (carboniUnknownyearfunctionalcharacterizationof pages 19-23, cammaratamouchtouris2022dynamicregulationof pages 4-6, rashidi2022insilicocharacterization pages 16-18)
Importantly, Tube does not directly phosphorylate Cactus—this is the function of Pelle kinase. Rather, Tube's role is to assemble and position Pelle within the signaling complex to enable its activation (rashidi2022insilicocharacterization pages 16-18).
Tube participates in two major biological processes in Drosophila: innate immunity and embryonic development.
The Toll pathway, including Tube, is activated primarily in response to:
Fungal infections: Recognition of β-1,3-glucans on fungal cell walls by pattern recognition receptors such as GNBP3 (rashidi2022insilicocharacterization pages 16-18, yokoi2022pelleandtube pages 1-2, carboniUnknownyearfunctionalcharacterizationof pages 19-23, yu2022drosophilainnateimmunity pages 5-7)
Gram-positive bacterial infections: Detection of lysine-type peptidoglycans (Lys-PGN) by receptors including GNBP1 and PGRP-SA (rashidi2022insilicocharacterization pages 16-18, yokoi2022pelleandtube pages 1-2, yu2022drosophilainnateimmunity pages 5-7, cammaratamouchtouris2022dynamicregulationof pages 2-4)
Viral infections: The Toll pathway also contributes to antiviral defense, particularly against orally acquired viruses, though this is less extensively characterized than antibacterial and antifungal responses (rashidi2022insilicocharacterization pages 16-18, rashidi2022insilicocharacterization pages 23-24)
These pattern recognition events trigger an extracellular serine protease cascade involving proteases such as ModSP, Grass, Hayan, Persephone, and SPE, which process the inactive Spätzle precursor into its active form (carboniUnknownyearfunctionalcharacterizationof pages 19-23). Processed Spätzle then activates Toll, initiating the Tube-containing signaling cascade.
Tube-mediated Toll signaling induces expression of antimicrobial peptides and other immune effectors, particularly in the fat body, the functional equivalent of the mammalian liver (rashidi2022insilicocharacterization pages 16-18, carboniUnknownyearfunctionalcharacterizationof pages 19-23). The most well-characterized antimicrobial effector is:
Additional antimicrobial peptides regulated by the Toll pathway include Defensin, Metchnikowin, and immune-induced molecule 1 (IM1), as well as newer classes such as Bomanins, Daishos, and Baramycins (rashidi2022insilicocharacterization pages 16-18, wang2026transcriptomicanalysisreveals pages 5-6, carboniUnknownyearfunctionalcharacterizationof pages 23-26). These effectors are secreted into the hemolymph where they combat invading pathogens.
Tube is an essential maternal-effect gene belonging to the "dorsal group" of genes required for establishing the dorsoventral (DV) body axis of the Drosophila embryo (stein2014maternalcontrolof pages 3-4, stein2014maternalcontrolof pages 6-7, stein2014maternalcontrolof pages 4-6). The protein is supplied maternally and deposited in the egg during oogenesis.
During embryonic development, the Toll pathway establishes a ventral-to-dorsal gradient of nuclear Dorsal transcription factor, which patterns the embryo into distinct dorsal, lateral, and ventral cell fates. Tube is essential for transmitting the spatially restricted Toll activation signal on the ventral side of the embryo into the downstream signaling cascade (stein2014maternalcontrolof pages 3-4, stein2014maternalcontrolof pages 6-7, stein2014maternalcontrolof pages 4-6).
Embryos from mothers lacking functional tube fail to establish normal dorsoventral polarity and exhibit a characteristic dorsalized phenotype (stein2014maternalcontrolof pages 3-4). These embryos:
Genetic epistasis experiments have shown that tube functions downstream of the extracellular protease cascade and Spätzle/Toll activation, but upstream of Pelle, Cactus, and Dorsal in the developmental pathway (stein2014maternalcontrolof pages 6-7, stein2014maternalcontrolof pages 4-6). Constitutively active forms of upstream proteases can bypass many early pathway components but cannot rescue tube mutant embryos, confirming Tube's essential intracellular role (stein2014maternalcontrolof pages 6-7).
Experimental evidence indicates several structural requirements for Tube function:
Death domain integrity: The conserved death domain is essential for binding both MyD88 and Pelle through homotypic death domain interactions (rashidi2022insilicocharacterization pages 8-11, lima2021evolutionoftoll pages 1-2)
Membrane localization: Recruitment to the plasma membrane is functionally critical. Forced membrane targeting is sufficient to activate the pathway, demonstrating that membrane-proximal positioning is a key structural requirement (stein2014maternalcontrolof pages 12-14)
Complex assembly: Tube must form a stable higher-order signaling complex with MyD88 and Pelle. The structural models show that Tube positions Pelle molecules within the receptor-associated complex, enabling Pelle kinase activation through proximity-dependent mechanisms (stein2014maternalcontrolof pages 12-14, rashidi2022insilicocharacterization pages 8-11)
Recent research (2020-2025) has continued to elucidate the roles of Toll signaling in Drosophila:
Tissue-specific immune responses: Studies have revealed that Toll pathway activation, including Tube-mediated signaling, varies across different tissues beyond the fat body, including the brain, Malpighian tubules, and epithelial barriers (yu2022drosophilainnateimmunity pages 5-7)
Dynamic regulation: Work published in 2022-2024 has emphasized the sophisticated regulatory mechanisms controlling Toll pathway dynamics, including feedback loops, post-translational modifications, and tissue-specific modulators (cammaratamouchtouris2022dynamicregulationof pages 4-6)
Comparative immunity: Systematic comparative studies have assessed the relative contributions of different immune modules, confirming the importance of Toll signaling (involving Tube) against specific pathogen classes while revealing synergistic effects with other immune pathways (ryckebusch2025layersofimmunity pages 22-23, ryckebusch2025layersofimmunity pages 19-20)
Conservation and evolution: Phylogenetic analyses published in 2021 have examined the evolution of Toll pathway components including Tube across insect orders, revealing both conserved features and lineage-specific adaptations (lima2021evolutionoftoll pages 1-2)
The following table provides a comprehensive summary of Tube protein features and functions:
| Feature | Functional annotation for Drosophila melanogaster Tube (tub; UniProt P22812) | Evidence |
|---|---|---|
| Protein identity | Tube is the D. melanogaster tub/tube gene product and a core intracellular component of canonical Toll signaling; this identity is distinct from unrelated genes or anatomical “tubes.” | The accession and death-domain annotation match the experimentally established Toll-pathway adaptor Tube (rashidi2022insilicocharacterization pages 8-11, rashidi2022insilicocharacterization pages 6-8). |
| Domains | Contains an N-terminal death domain (InterPro IPR000488) within the death-like domain superfamily (IPR011029); related annotations include Tube-specific death-domain families. These are protein-interaction modules, not catalytic domains. | Comparative domain analysis identifies the conserved death/death-like domain and the structurally characterized Pelle–Tube death-domain interface (rashidi2022insilicocharacterization pages 8-11, rashidi2022insilicocharacterization pages 11-14). |
| Primary molecular function | Non-enzymatic adaptor/scaffold protein. Tube assembles the receptor-proximal signaling machinery and bridges Toll-associated MyD88 to the kinase Pelle; no catalytic reaction or substrate specificity is established for D. melanogaster Tube. | Tube is characterized as the scaffold connecting MyD88 and Pelle through death-domain interactions (rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2). |
| Direct/complex partners | MyD88 and Pelle are the principal partners in the MyD88–Tube–Pelle complex. The Tube–Pelle association is directly supported structurally by their death-domain complex; MyD88 recruits Tube through corresponding death-domain interactions. | Structural modeling and pathway studies support Tube–Pelle binding and MyD88–Tube–Pelle assembly (rashidi2022insilicocharacterization pages 8-11, cammaratamouchtouris2022dynamicregulationof pages 4-6). |
| Subcellular localization | Functions on the cytoplasmic face of the plasma membrane after recruitment to ligand-activated Toll. Forced membrane targeting of Tube can activate ventralizing Toll output, demonstrating that membrane-proximal localization is functionally important. It is not secreted or transmembrane. | Membrane-associated complex formation and membrane-targeting experiments are summarized in the developmental Toll literature (stein2014maternalcontrolof pages 12-14). |
| Core signaling pathway | Acts in the canonical Spätzle–Toll–MyD88–Tube–Pelle–Cactus–NF-κB pathway. Tube is not assigned a primary role in the distinct Imd pathway. | Multiple pathway syntheses place Tube specifically in the Toll signaling module (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, yu2022drosophilainnateimmunity pages 5-7). |
| Proximal pathway mechanism | Processed Spätzle activates Toll; Toll recruits MyD88, which recruits Tube and Pelle. Tube-mediated assembly positions Pelle for signaling, leading to phosphorylation-dependent loss of Cactus and activation of NF-κB-family transcription factors. | The receptor-to-NF-κB sequence and Tube’s bridging role are described in recent pathway reviews and comparative work (cammaratamouchtouris2022dynamicregulationof pages 4-6, rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2). |
| Downstream regulator: Cactus | Cactus, the fly IκB-like inhibitor, is the proximal inhibitory target downstream of the Tube-containing complex. Pelle-dependent phosphorylation promotes Cactus degradation, although Tube itself is not the kinase. | Cactus phosphorylation/degradation is linked to assembly of the MyD88–Tube–Pelle complex (cammaratamouchtouris2022dynamicregulationof pages 4-6, kietz2023drosophilacaspasesas pages 3-4, yokoi2022pelleandtube pages 1-2). |
| Downstream transcription factors | Cactus removal releases Dorsal and Dif, permitting their nuclear translocation. Dorsal is especially central to embryonic patterning, whereas Dif is prominent in systemic immune transcription; both can participate in immune Toll output. | Nuclear activation of Dorsal/Dif downstream of Tube-containing signaling is consistently reported (carboniUnknownyearfunctionalcharacterizationof pages 19-23, cammaratamouchtouris2022dynamicregulationof pages 4-6, rashidi2022insilicocharacterization pages 16-18). |
| Biological process: innate immunity | Required for Toll-dependent defense, principally against fungi/yeasts and Gram-positive bacteria recognized through fungal β-glucans or lysine-type peptidoglycan; antiviral Toll functions have also been reported, but they are less directly attributable to Tube-specific experiments. | Pathogen recognition and downstream Tube signaling are supported by recent immunity reviews (yokoi2022pelleandtube pages 1-2, carboniUnknownyearfunctionalcharacterizationof pages 19-23, yu2022drosophilainnateimmunity pages 5-7). |
| Immune tissues and output location | The intracellular Tube complex functions within Toll-responsive cells, notably fat-body cells during systemic immunity. The resulting antimicrobial products—not Tube—are secreted into the hemolymph. | Tube-containing signaling induces immune genes in the fat body following infection (rashidi2022insilicocharacterization pages 16-18, carboniUnknownyearfunctionalcharacterizationof pages 19-23). |
| Antimicrobial effectors | Drosomycin is the best-established Toll-responsive antifungal readout downstream of Tube-associated signaling. Defensin has been listed among Toll-associated fly antimicrobial peptides in comparative summaries, but its regulation is less specific than that of Drosomycin and should not be treated as a uniquely Tube-dependent output. | Drosomycin is repeatedly identified as a canonical output (rashidi2022insilicocharacterization pages 16-18, yokoi2022pelleandtube pages 1-2, lima2021evolutionoftoll pages 1-2); Defensin appears in a comparative Toll-associated effector table (wang2026transcriptomicanalysisreveals pages 5-6). |
| Biological process: embryonic dorsoventral patterning | Tube is a maternally supplied dorsal-group gene product required to convert spatially restricted ventral Toll activation into the ventral-to-dorsal nuclear Dorsal gradient that specifies embryonic cell fates. | Genetic epistasis places maternal Tube downstream of active Spätzle/Toll and upstream of Pelle, Cactus, and Dorsal (stein2014maternalcontrolof pages 3-4, stein2014maternalcontrolof pages 6-7, stein2014maternalcontrolof pages 4-6). |
| Loss-of-function phenotype | Embryos from mothers lacking functional tube fail to establish normal dorsoventral polarity and become strongly dorsalized, with dorsal characteristics around the circumference and loss of normal ventral and lateral structures. | Classical maternal-effect phenotypes of the dorsal group, including tube, are summarized in developmental reviews (stein2014maternalcontrolof pages 3-4). |
| Evolutionary interpretation | The death-domain-mediated MyD88–Tube–Pelle assembly is organizationally analogous to mammalian MyD88–IRAK complexes. Tube is the scaffold and Pelle is the principal kinase; therefore, Tube should not be annotated as an active IRAK-like enzyme solely from distant homology or kinase-like predictions in other insects. | Evolutionary and structural comparisons distinguish the adaptor role of D. melanogaster Tube from the kinase role of Pelle/IRAK proteins (rashidi2022insilicocharacterization pages 16-18, lima2021evolutionoftoll pages 1-2, rashidi2022insilicocharacterization pages 6-8). |
Table: Key molecular, cellular, developmental, and immune features of the death-domain adaptor Tube (tub; UniProt P22812). The table distinguishes well-supported functions from comparative or less-specific annotations.
The Drosophila melanogaster Tube protein (tub, UniProt P22812) is a highly conserved death domain-containing adaptor protein that plays essential roles in both innate immunity and embryonic development. Its primary molecular function is to serve as a non-enzymatic scaffold that assembles the MyD88-Tube-Pelle signaling complex downstream of activated Toll receptors. In immunity, Tube-mediated signaling controls antimicrobial peptide expression in response to fungal and bacterial infections. In development, maternal Tube is absolutely required for establishing the embryonic dorsoventral axis, with loss of function resulting in severe dorsalization. The protein functions at the cytoplasmic face of the plasma membrane and bridges MyD88 and Pelle through death domain interactions, enabling Pelle-dependent phosphorylation of the inhibitor Cactus and subsequent activation of NF-κB transcription factors (Dorsal and Dif). Recent research continues to reveal the sophisticated regulation and diverse contexts in which Tube-containing Toll signaling operates in the fruit fly.
References
(rashidi2022insilicocharacterization pages 8-11): Mahnaz Rashidi and Nabil Killiny. In silico characterization and gene expression analysis of toll signaling pathway-related genes in diaphorina citri. Insects, 13:783, Aug 2022. URL: https://doi.org/10.3390/insects13090783, doi:10.3390/insects13090783. This article has 4 citations.
(rashidi2022insilicocharacterization pages 6-8): Mahnaz Rashidi and Nabil Killiny. In silico characterization and gene expression analysis of toll signaling pathway-related genes in diaphorina citri. Insects, 13:783, Aug 2022. URL: https://doi.org/10.3390/insects13090783, doi:10.3390/insects13090783. This article has 4 citations.
(rashidi2022insilicocharacterization pages 16-18): Mahnaz Rashidi and Nabil Killiny. In silico characterization and gene expression analysis of toll signaling pathway-related genes in diaphorina citri. Insects, 13:783, Aug 2022. URL: https://doi.org/10.3390/insects13090783, doi:10.3390/insects13090783. This article has 4 citations.
(lima2021evolutionoftoll pages 1-2): Letícia Ferreira Lima, André Quintanilha Torres, Rodrigo Jardim, Rafael Dias Mesquita, and Renata Schama. Evolution of toll, spatzle and myd88 in insects: the problem of the diptera bias. BMC Genomics, Jul 2021. URL: https://doi.org/10.1186/s12864-021-07886-7, doi:10.1186/s12864-021-07886-7. This article has 39 citations and is from a peer-reviewed journal.
(rashidi2022insilicocharacterization pages 11-14): Mahnaz Rashidi and Nabil Killiny. In silico characterization and gene expression analysis of toll signaling pathway-related genes in diaphorina citri. Insects, 13:783, Aug 2022. URL: https://doi.org/10.3390/insects13090783, doi:10.3390/insects13090783. This article has 4 citations.
(cammaratamouchtouris2022dynamicregulationof pages 4-6): Alexandre Cammarata-Mouchtouris, Adrian Acker, Akira Goto, Di Chen, Nicolas Matt, and Vincent Leclerc. Dynamic regulation of nf-κb response in innate immunity: the case of the imd pathway in drosophila. Biomedicines, 10:2304, Sep 2022. URL: https://doi.org/10.3390/biomedicines10092304, doi:10.3390/biomedicines10092304. This article has 48 citations.
(yokoi2022pelleandtube pages 1-2): K Yokoi, D Kato, and K Miura. Pelle and tube contribute to the toll pathway-dependent antimicrobial peptide production in the red fl our beetle, tribolium castaneum (coleoptera …. Unknown journal, 2022.
(stein2014maternalcontrolof pages 12-14): David S. Stein and Leslie M. Stevens. Maternal control of the drosophila dorsal–ventral body axis. Wiley Interdisciplinary Reviews: Developmental Biology, 3:301-330, Sep 2014. URL: https://doi.org/10.1002/wdev.138, doi:10.1002/wdev.138. This article has 76 citations.
(kietz2023drosophilacaspasesas pages 3-4): Christa Kietz and Annika Meinander. Drosophila caspases as guardians of host-microbe interactions. Cell Death and Differentiation, 30:227-236, Jul 2023. URL: https://doi.org/10.1038/s41418-022-01038-4, doi:10.1038/s41418-022-01038-4. This article has 24 citations and is from a domain leading peer-reviewed journal.
(yu2022drosophilainnateimmunity pages 5-7): Shichao Yu, Fangzhou Luo, Yongyi Xu, Yan Zhang, and Li Hua Jin. Drosophila innate immunity involves multiple signaling pathways and coordinated communication between different tissues. Frontiers in Immunology, Jul 2022. URL: https://doi.org/10.3389/fimmu.2022.905370, doi:10.3389/fimmu.2022.905370. This article has 232 citations and is from a peer-reviewed journal.
(carboniUnknownyearfunctionalcharacterizationof pages 19-23): A Carboni, SK Boquete, and B Lemaitre. Functional characterization of immune-induced dnases in drosophila innate immunity. Unknown journal, Unknown year.
(cammaratamouchtouris2022dynamicregulationof pages 2-4): Alexandre Cammarata-Mouchtouris, Adrian Acker, Akira Goto, Di Chen, Nicolas Matt, and Vincent Leclerc. Dynamic regulation of nf-κb response in innate immunity: the case of the imd pathway in drosophila. Biomedicines, 10:2304, Sep 2022. URL: https://doi.org/10.3390/biomedicines10092304, doi:10.3390/biomedicines10092304. This article has 48 citations.
(rashidi2022insilicocharacterization pages 23-24): Mahnaz Rashidi and Nabil Killiny. In silico characterization and gene expression analysis of toll signaling pathway-related genes in diaphorina citri. Insects, 13:783, Aug 2022. URL: https://doi.org/10.3390/insects13090783, doi:10.3390/insects13090783. This article has 4 citations.
(wang2026transcriptomicanalysisreveals pages 5-6): Haiquan Wang, Yan Zhao, Zhongxian Yang, Feng Zhang, and Zhiyong Di. Transcriptomic analysis reveals members and expression characteristics of innate immunity genes in chinese scorpion mesobuthus martensii. Scientific Reports, Aug 2026. URL: https://doi.org/10.1038/s41598-025-30434-2, doi:10.1038/s41598-025-30434-2. This article has 0 citations and is from a peer-reviewed journal.
(carboniUnknownyearfunctionalcharacterizationof pages 23-26): A Carboni, SK Boquete, and B Lemaitre. Functional characterization of immune-induced dnases in drosophila innate immunity. Unknown journal, Unknown year.
(stein2014maternalcontrolof pages 3-4): David S. Stein and Leslie M. Stevens. Maternal control of the drosophila dorsal–ventral body axis. Wiley Interdisciplinary Reviews: Developmental Biology, 3:301-330, Sep 2014. URL: https://doi.org/10.1002/wdev.138, doi:10.1002/wdev.138. This article has 76 citations.
(stein2014maternalcontrolof pages 6-7): David S. Stein and Leslie M. Stevens. Maternal control of the drosophila dorsal–ventral body axis. Wiley Interdisciplinary Reviews: Developmental Biology, 3:301-330, Sep 2014. URL: https://doi.org/10.1002/wdev.138, doi:10.1002/wdev.138. This article has 76 citations.
(stein2014maternalcontrolof pages 4-6): David S. Stein and Leslie M. Stevens. Maternal control of the drosophila dorsal–ventral body axis. Wiley Interdisciplinary Reviews: Developmental Biology, 3:301-330, Sep 2014. URL: https://doi.org/10.1002/wdev.138, doi:10.1002/wdev.138. This article has 76 citations.
(ryckebusch2025layersofimmunity pages 22-23): Faustine Ryckebusch, Yao Tian, Mylene Rapin, Fanny Schüpfer, Mark A Hanson, and Bruno Lemaitre. Layers of immunity: deconstructing the drosophila effector response. Jun 2025. URL: https://doi.org/10.7554/elife.107030.1, doi:10.7554/elife.107030.1. This article has 15 citations.
(ryckebusch2025layersofimmunity pages 19-20): Faustine Ryckebusch, Yao Tian, Mylene Rapin, Fanny Schüpfer, Mark A Hanson, and Bruno Lemaitre. Layers of immunity: deconstructing the drosophila effector response. Jun 2025. URL: https://doi.org/10.7554/elife.107030.1, doi:10.7554/elife.107030.1. This article has 15 citations.