The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The supplied identity is internally consistent and matches the literature: M9NFK2 is the D. melanogaster ftz-f1 product, an NR5-family orphan nuclear receptor, not the similarly named Fushi tarazu (ftz) homeodomain protein and not an FTZ-F1 orthologue from another animal. The literature uses ftz-f1, FTZ-F1, Ftz-F1, and Ftz-Factor1; αFTZ-F1 and βFTZ-F1 are alternative-promoter isoforms with distinct amino termini. The reported zinc-finger DNA-binding and nuclear-receptor ligand-binding domains, including AF-2, agree with the UniProt/InterPro annotations supplied in the question. (lu2015evolutionofpairrule pages 40-45, schwartz2001ftz‐factor1andfushi pages 1-2, lu2015evolutionofpairrule pages 22-26)
Its primary biochemical function is sequence-specific transcriptional regulation in the nucleus. FTZ-F1 is neither an enzyme nor a transporter: it binds regulatory DNA principally as a monomer and recruits or interacts with transcriptional partners. Its best-resolved functions are (1) acting with the Fushi tarazu homeoprotein during embryonic segmentation, (2) conferring competence for temporally appropriate ecdysone responses during molting and metamorphosis, and (3) promoting lipid/sterol acquisition in steroidogenic tissues through transcriptional control of the scavenger receptor Snmp1. (lu2015evolutionofpairrule pages 40-45, schwartz2001ftz‐factor1andfushi pages 1-2, talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
| Annotation aspect | Best-supported conclusion | Evidence type | Confidence and limitations |
|---|---|---|---|
| Identity and isoforms | M9NFK2 corresponds to Drosophila melanogaster ftz-f1, an NR5A-family nuclear receptor. Alternative promoters produce αFTZ-F1 and βFTZ-F1 with distinct N-termini. Maternal αFTZ-F1 supports early segmentation, whereas βFTZ-F1 has later molting and metamorphic functions. | Gene-structure, expression, and mutant studies (lu2015evolutionofpairrule pages 40-45, schwartz2001ftz‐factor1andfushi pages 1-2) | High. Organism, aliases, isoforms, and family agree with the supplied UniProt record. |
| Domain architecture | FTZ-F1 has a canonical nuclear-receptor DNA-binding domain with two zinc fingers, a hinge region, and a ligand-binding domain containing a C-terminal AF-2 activation and interaction motif. | Sequence conservation, deletion constructs, biochemical binding, and rescue experiments (schwartz2001ftz‐factor1andfushi pages 4-5, lu2015evolutionofpairrule pages 22-26, schwartz2001ftz‐factor1andfushi pages 8-9) | High. Exact domain boundaries in M9NFK2 were not established from the retrieved papers. |
| Cellular localization | FTZ-F1 is constitutively nuclear in early embryonic somatic cells. It also performs transcriptional functions in steroidogenic prothoracic-gland and ovarian follicle cells. | Embryonic localization and tissue-specific genetic evidence (lu2015evolutionofpairrule pages 45-49, field2015theevolutionand pages 71-76, talamillo2015scavengerreceptorsmediate pages 1-2) | High for embryonic nuclear localization; moderate for later tissues, where localization is partly inferred from tissue-specific transcriptional activity. |
| Primary molecular function | FTZ-F1 is a sequence-specific, principally monomeric DNA-binding transcription factor and constitutive transcriptional activator, not an enzyme, transporter, or structural protein. Recognition sites contain an AAGG core, while cofactors and composite regulatory elements provide target specificity. | DNA-binding and transactivation assays, motif analysis, target expression, and genetics (lu2015evolutionofpairrule pages 40-45, field2015theevolutionand pages 76-80, field2015theevolutionand pages 71-76) | High. Motif representations vary among assays and computational models, so one rigid consensus should not be overinterpreted. |
| Fushi tarazu cofactor mechanism | During embryonic segmentation, FTZ-F1 binds the homeoprotein Fushi tarazu. The FTZ-F1 AF-2 surface recognizes an LXXLL-like motif in Ftz, and cooperative binding at composite elements restricts activation to Ftz-positive stripes despite broad FTZ-F1 expression. | In-vitro and in-vivo interaction assays, AF-2 deletion and substitution, cooperative DNA binding, and mutant rescue (schwartz2001ftz‐factor1andfushi pages 1-2, lu2015evolutionofpairrule pages 45-49, schwartz2001ftz‐factor1andfushi pages 4-5) | High. This is the best-resolved molecular mechanism for FTZ-F1. |
| Embryonic transcriptional outputs | The Ftz–FTZ-F1 complex activates segmentation genes including engrailed and candidate or direct targets such as ftz, apt, Sulf1, drm, noc, and 5-HT2. Maternal ftz-f1 mutants lose alternate segments and phenocopy ftz mutants. | Mutant phenotypes, enhancer mutagenesis, expression profiling, ChIP-informed analysis, and rescue (lu2015evolutionofpairrule pages 45-49, field2015theevolutionand pages 76-80, field2015theevolutionand pages 71-76) | High for segmentation and engrailed; moderate for the broader target set because some assignments come from integrative or candidate-enhancer analyses. |
| βFTZ-F1 and ecdysone competence | Temporally restricted βFTZ-F1 provides competence for stage-specific transcriptional and morphogenetic responses to later ecdysone pulses during molting and metamorphosis. | Temporal-expression and loss-of-function genetics summarized in Drosophila literature (lu2015evolutionofpairrule pages 40-45, talamillo2015scavengerreceptorsmediate pages 16-16) | High for the competence-factor model. Quantitative results from the foundational experiments were unavailable in the retrieved full-text evidence. |
| Steroidogenic lipid uptake | In the prothoracic gland, Ftz-f1 promotes expression of the SR-BI and CD36-family receptor Snmp1, supporting acquisition or mobilization of cholesterol-containing lipids required for ecdysone synthesis. Prothoracic-gland ftz-f1 RNAi causes larval arrest, and related lipid defects occur in ovarian follicle cells. | Tissue-specific RNAi, promoter activation, lipid staining, developmental phenotypes, and rescue experiments (talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2, talamillo2015scavengerreceptorsmediate pages 15-16) | High for pathway involvement; moderate for direct cholesterol specificity. FTZ-F1 regulates a lipid transporter but is not itself a transporter. |
| SUMO regulation | Ftz-f1 is SUMOylated in vitro and in vivo and participates in a SUMO–Ftz-f1–Snmp1 regulatory axis. The ratio of SUMOylated to unmodified receptor may tune Snmp1 transcription and steroidogenic lipid homeostasis. | Biochemical SUMOylation, tissue-specific knockdown, promoter assays, and genetic rescue (talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2) | High for SUMOylation and pathway involvement; moderate for the proposed activity-tuning mechanism. |
| Ligand status | FTZ-F1 is classified as an orphan nuclear receptor. Evidence supports a constitutively active ligand-binding-domain conformation, with activity controlled primarily by expression, post-translational modification, and cofactors rather than by a demonstrated activating ligand. | Domain analysis and functional interpretation of receptor conformation and cofactor dependence (lu2015evolutionofpairrule pages 45-49, schwartz2001ftz‐factor1andfushi pages 4-5) | Moderate to high. No endogenous activating ligand has been established, but this does not prove that the receptor cannot bind a ligand. |
| 2023–2024 evidence gap | No substantive 2023–2024 primary study retrieved in this search directly revised the molecular annotation of D. melanogaster ftz-f1. Recent publications mainly address broader insect nuclear-receptor biology and should not replace direct evidence about M9NFK2. | Targeted literature searches and organism-specific evidence screening | Moderate. This is a search-based conclusion, not proof that no relevant publication exists. |
Table: Compact functional annotation of Drosophila melanogaster ftz-f1 (UniProt M9NFK2), distinguishing strongly supported molecular functions from pathway-level inference and current evidence gaps.
The accession supplied is not necessarily the canonical database accession most frequently cited by older papers; nevertheless, its organism, gene aliases, description, and domain content all map to the same D. melanogaster ftz-f1 locus. This report annotates the gene product represented by M9NFK2, without assuming that every historical construct has an identical sequence to that specific UniProt entry.
FTZ-F1 binds DNA as a monomer and behaves as a strong, often constitutive transcriptional activator. Experimentally and computationally derived recognition motifs consistently contain an AAGG core, although reported extended consensuses vary with assay and model; examples in the retrieved evidence include BSAAGGHYRHH. Therefore, “NR5-type response element with an AAGG core” is more defensible than assigning M9NFK2 one rigid universal motif. (lu2015evolutionofpairrule pages 40-45, field2015theevolutionand pages 76-80, field2015theevolutionand pages 71-76)
The receptor is considered an orphan nuclear receptor: no endogenous activating ligand has been established. Structural-functional interpretation supports an active ligand-binding-domain conformation without a required agonist. Its output appears to be controlled mainly by developmental expression, DNA context, cofactors, and post-translational modifications rather than by a demonstrated small-molecule ligand. This should not be overinterpreted as proof that the ligand-binding pocket can never bind a metabolite. (lu2015evolutionofpairrule pages 45-49, schwartz2001ftz‐factor1andfushi pages 4-5)
The best-defined molecular mechanism is the FTZ–FTZ-F1 partnership. FTZ-F1’s AF-2 surface recognizes an LXXLL-like nuclear-receptor box in the Fushi tarazu protein—reported as LRALL in the retrieved synthesis. FTZ and FTZ-F1 interact directly in vitro and in vivo and bind composite regulatory elements cooperatively. Deleting FTZ-F1 AF-2 nearly abolishes detectable binding; replacing it with the corresponding human FTF or SF-1 AF-2 restores binding, whereas the more divergent DHR39 sequence restores it weakly. These results demonstrate a conserved receptor–coactivator interaction rather than mere genetic correlation. (schwartz2001ftz‐factor1andfushi pages 1-2, lu2015evolutionofpairrule pages 45-49, schwartz2001ftz‐factor1andfushi pages 4-5)
Although maternal FTZ-F1 is broadly present, Fushi tarazu is expressed in seven embryonic stripes. Partner availability therefore spatially gates FTZ-F1 activity: a widely distributed nuclear receptor generates stripe-specific transcription because productive complexes form predominantly in FTZ-positive cells. Importantly, ftz-f1 mutants retain normal ftz RNA and protein but lose downstream FTZ-dependent expression, establishing FTZ-F1 principally as an FTZ cofactor rather than simply an upstream inducer of ftz. (schwartz2001ftz‐factor1andfushi pages 1-2, lu2015evolutionofpairrule pages 45-49)
αFTZ-F1 is maternally supplied and broadly distributed in the early embryo. Loss of maternal ftz-f1 causes a pair-rule phenotype with loss of alternate, even-numbered parasegments, closely phenocopying ftz. One reported null maternal background produced pair-rule defects in most embryos, with approximately 10% viable-larval escapers. (lu2015evolutionofpairrule pages 40-45, schwartz2001ftz‐factor1andfushi pages 1-2, schwartz2001ftz‐factor1andfushi pages 4-5)
The FTZ–FTZ-F1 complex activates segmentation outputs including alternate engrailed stripes. Additional supported direct or candidate targets include ftz, apt, Sulf1, drm, noc, and 5-HT2. For drm, enhancer activity was lost in ftz or ftz-f1 mutants and abolished by mutating FTZ-F1 sites. A developmental microarray used three replicates at each of three embryonic stages for control and mutant conditions—18 arrays total—and identified nine high-priority shared candidate targets using an FDR-adjusted threshold of p<0.05. A motif survey found approximately 30,000 potential FTZ-F1 sites, versus more than 14 million candidate FTZ sites, illustrating how the more selective receptor motif and cooperative binding can constrain target choice. (lu2015evolutionofpairrule pages 45-49, field2015theevolutionand pages 76-80, field2015theevolutionand pages 71-76)
The broad target list should be interpreted with different confidence levels: segmentation, engrailed, and the requirement for the FTZ interaction are strongly established; some additional genes are candidate targets derived from expression profiling, binding data, or enhancer tests rather than equivalent genome-wide proof of direct regulation.
βFTZ-F1 is expressed at later developmental transitions and is classically designated a competence factor for stage-specific responses to ecdysone. In the insect endocrine cascade, successive ecdysone pulses can elicit different transcriptional and morphogenetic programs because the intervening regulatory state changes; βFTZ-F1 is a key component of that changing competence. Drosophila work links its temporally restricted expression to embryogenesis, molting, metamorphosis, and morphogenesis at the prepupal–pupal transition. (lu2015evolutionofpairrule pages 40-45, talamillo2015scavengerreceptorsmediate pages 16-16)
The mechanistic interpretation is that βFTZ-F1 does not catalyze ecdysone synthesis and is not the ecdysone receptor. Rather, as a nuclear transcription factor it prepares tissues to execute the appropriate transcriptional response to a later steroid pulse. The canonical ecdysone receptor is EcR/USP; FTZ-F1 sits in the temporal transcriptional network and also affects steroid availability through steroidogenic-tissue targets.
A second, experimentally precise role operates in the prothoracic gland, which synthesizes ecdysone from dietary cholesterol. Drosophila cannot synthesize sterol de novo, making lipid uptake and intracellular mobilization critical for steroid production. Prothoracic-gland ftz-f1 knockdown phenocopies disruption of the SUMO pathway, causing arrest before the larval–pupal transition. Ftz-f1 activates the promoter of Snmp1, one of 14 Drosophila CD36-family genes; Snmp1 encodes an SR-BI-family scavenger receptor implicated in steroidogenic lipid acquisition or mobilization. (talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
The evidence places FTZ-F1 upstream of the transporter rather than identifying FTZ-F1 itself as a transporter. Snmp1 or peste depletion in the prothoracic gland arrests animals during the third larval instar before pupariation. Snmp1 overexpression restores lipid-droplet levels in SUMO-depleted gland cells but does not restore the developmental transition, indicating that accumulating lipid is insufficient unless the sterol can also be mobilized and converted to enough ecdysone. (talamillo2015scavengerreceptorsmediate pages 12-13)
The same regulatory logic extends to ovarian follicle cells. Knockdown of smt3 (SUMO), ftz-f1, or scavenger-receptor components depletes follicle-cell lipid, while Snmp1 overexpression rescues lipid content. Targeted Snmp1 RNAi leaves droplets concentrated basally and depletes the apical side, supporting a role in transcellular lipid handling. Thus, the pathway is best summarized as SUMO/FTZ-F1 → scavenger-receptor transcription → sterol-containing lipid uptake or mobilization → steroidogenesis, in both the prothoracic gland and ovary. (talamillo2015scavengerreceptorsmediate pages 1-2, talamillo2015scavengerreceptorsmediate pages 15-16)
FTZ-F1 itself is SUMOylated in vitro and in vivo. Available data support a model in which the balance between SUMOylated and unmodified receptor tunes Snmp1 activation, although that ratio-dependent interpretation is less firmly established than the existence of SUMOylation and the genetic pathway. (talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
The most direct localization evidence places FTZ-F1 constitutively in nuclei of early embryonic somatic cells. This localization is fully consistent with its zinc-finger DNA-binding and transcriptional functions. In embryos, spatially restricted output is not achieved by restricting nuclear FTZ-F1 itself, but by the striped distribution of Fushi tarazu. (lu2015evolutionofpairrule pages 45-49, field2015theevolutionand pages 71-76)
Later tissue-specific genetics localizes physiologically important activity to:
Nuclear localization in the latter tissues is strongly expected from the receptor’s mechanism and tissue-specific promoter activity, but the retrieved evidence was more direct for embryonic nuclei than for subcellular imaging in every later tissue.
The evidence supports viewing FTZ-F1 as a developmental context integrator rather than a conventional ligand-driven switch. Its conserved NR5 receptor machinery supplies sequence-specific DNA recognition and an AF-2 protein-interaction surface; developmental timing, cofactors such as Fushi tarazu, and SUMO-dependent regulation determine when and where transcription occurs. This model explains how the same locus can support early segmentation, later steroid-response competence, and steroidogenic lipid homeostasis without invoking unrelated enzymatic activities. (schwartz2001ftz‐factor1andfushi pages 1-2, lu2015evolutionofpairrule pages 45-49, talamillo2015scavengerreceptorsmediate pages 12-13)
There is no clinical use, approved drug, or deployed biotechnology specifically targeting D. melanogaster ftz-f1. Its current real-world value is principally as:
The last application remains translationally indirect. FTZ-F1 functions in pest or vector species cannot be assigned from M9NFK2 without species-specific validation, because expression, paralogy, and endocrine wiring can differ.
Targeted searches prioritizing 2023–2024 did not retrieve a substantive primary paper that directly revises the molecular annotation of D. melanogaster ftz-f1. The strongest direct mechanistic studies remain older: Schwartz et al., published February 2001, established the AF-2/LXXLL interaction (DOI/URL: https://doi.org/10.1093/emboj/20.3.510), while Talamillo et al., published April 2013, established the SUMO–Ftz-f1–scavenger-receptor steroidogenesis axis (DOI/URL: https://doi.org/10.1371/journal.pgen.1003473). (schwartz2001ftz‐factor1andfushi pages 1-2, talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
This recency gap should not be mistaken for uncertainty in the core annotation. Rather, current papers tend to use the established FTZ-F1 framework or investigate related nuclear-receptor and endocrine mechanisms. The search-based conclusion is not proof that no 2023–2024 mention exists, only that no recent organism-specific study recovered here displaced the foundational model.
Molecular function: NR5-family orphan nuclear receptor; sequence-specific, principally monomeric DNA-binding transcriptional activator; binds NR5-type response elements containing an AAGG core; uses its AF-2 surface to engage LXXLL-like cofactors, especially Fushi tarazu. (lu2015evolutionofpairrule pages 40-45, schwartz2001ftz‐factor1andfushi pages 1-2, schwartz2001ftz‐factor1andfushi pages 4-5, field2015theevolutionand pages 71-76)
Biological processes: Fushi tarazu-dependent embryonic segmentation; stage-specific competence for ecdysone responses during molting and metamorphosis; regulation of steroidogenic lipid/sterol acquisition and mobilization in the prothoracic gland and ovary. (lu2015evolutionofpairrule pages 40-45, lu2015evolutionofpairrule pages 45-49, talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
Cellular component: nucleus, directly demonstrated in embryonic somatic cells and mechanistically supported in steroidogenic and ecdysone-responsive tissues. (lu2015evolutionofpairrule pages 45-49, field2015theevolutionand pages 71-76)
Catalysis/substrate statement: No catalytic reaction or transported substrate applies to FTZ-F1 itself. Its relevant molecular substrates are regulatory DNA elements and protein cofactors. In steroidogenesis, it transcriptionally controls Snmp1, whose downstream physiological cargo is sterol-containing lipid; FTZ-F1 does not transport cholesterol directly. (talamillo2015scavengerreceptorsmediate pages 12-13, talamillo2015scavengerreceptorsmediate pages 1-2)
Confidence: High for identity, NR5 domain architecture, nuclear transcription-factor function, Fushi tarazu interaction, segmentation role, and steroidogenic Snmp1 pathway. Moderate for a single exact DNA consensus, universal ligand independence, and subcellular localization in every post-embryonic tissue. Quantitative effect sizes remain limited because several foundational hormone-competence papers were identifiable only through citations rather than retrievable full text.
References
(lu2015evolutionofpairrule pages 40-45): Yong Lu. Evolution of pair-rule genes. ArXiv, Jan 2015. URL: https://doi.org/10.13016/m2ds56, doi:10.13016/m2ds56. This article has 1 citations.
(schwartz2001ftz‐factor1andfushi pages 1-2): Carol J.E. Schwartz, Heidi M. Sampson, Daniela Hlousek, A. Percival-Smith, J. Copeland, A. Simmonds, and H. Krause. Ftz‐factor1 and fushi tarazu interact via conserved nuclear receptor and coactivator motifs. The EMBO Journal, 20:510-519, Feb 2001. URL: https://doi.org/10.1093/emboj/20.3.510, doi:10.1093/emboj/20.3.510. This article has 86 citations.
(lu2015evolutionofpairrule pages 22-26): Yong Lu. Evolution of pair-rule genes. ArXiv, Jan 2015. URL: https://doi.org/10.13016/m2ds56, doi:10.13016/m2ds56. This article has 1 citations.
(talamillo2015scavengerreceptorsmediate pages 12-13): Ana Talamillo, Leire Herboso, Lucia Pirone, Coralia Pérez, Monika González, Jonatan Sánchez, Ugo Mayor, Fernando Lopitz-Otsoa, Manuel S. Rodriguez, James D. Sutherland, and Rosa Barrio. Scavenger receptors mediate the role of sumo and ftz-f1 in drosophila steroidogenesis. Apr 2013. URL: https://doi.org/10.1371/journal.pgen.1003473, doi:10.1371/journal.pgen.1003473. This article has 82 citations and is from a domain leading peer-reviewed journal.
(talamillo2015scavengerreceptorsmediate pages 1-2): Ana Talamillo, Leire Herboso, Lucia Pirone, Coralia Pérez, Monika González, Jonatan Sánchez, Ugo Mayor, Fernando Lopitz-Otsoa, Manuel S. Rodriguez, James D. Sutherland, and Rosa Barrio. Scavenger receptors mediate the role of sumo and ftz-f1 in drosophila steroidogenesis. Apr 2013. URL: https://doi.org/10.1371/journal.pgen.1003473, doi:10.1371/journal.pgen.1003473. This article has 82 citations and is from a domain leading peer-reviewed journal.
(schwartz2001ftz‐factor1andfushi pages 4-5): Carol J.E. Schwartz, Heidi M. Sampson, Daniela Hlousek, A. Percival-Smith, J. Copeland, A. Simmonds, and H. Krause. Ftz‐factor1 and fushi tarazu interact via conserved nuclear receptor and coactivator motifs. The EMBO Journal, 20:510-519, Feb 2001. URL: https://doi.org/10.1093/emboj/20.3.510, doi:10.1093/emboj/20.3.510. This article has 86 citations.
(schwartz2001ftz‐factor1andfushi pages 8-9): Carol J.E. Schwartz, Heidi M. Sampson, Daniela Hlousek, A. Percival-Smith, J. Copeland, A. Simmonds, and H. Krause. Ftz‐factor1 and fushi tarazu interact via conserved nuclear receptor and coactivator motifs. The EMBO Journal, 20:510-519, Feb 2001. URL: https://doi.org/10.1093/emboj/20.3.510, doi:10.1093/emboj/20.3.510. This article has 86 citations.
(lu2015evolutionofpairrule pages 45-49): Yong Lu. Evolution of pair-rule genes. ArXiv, Jan 2015. URL: https://doi.org/10.13016/m2ds56, doi:10.13016/m2ds56. This article has 1 citations.
(field2015theevolutionand pages 71-76): Amanda Field. The evolution and function of the pair-rule gene fushi tarazu (ftz). ArXiv, Jan 2015. URL: https://doi.org/10.13016/m25k9g, doi:10.13016/m25k9g. This article has 2 citations.
(field2015theevolutionand pages 76-80): Amanda Field. The evolution and function of the pair-rule gene fushi tarazu (ftz). ArXiv, Jan 2015. URL: https://doi.org/10.13016/m25k9g, doi:10.13016/m25k9g. This article has 2 citations.
(talamillo2015scavengerreceptorsmediate pages 16-16): Ana Talamillo, Leire Herboso, Lucia Pirone, Coralia Pérez, Monika González, Jonatan Sánchez, Ugo Mayor, Fernando Lopitz-Otsoa, Manuel S. Rodriguez, James D. Sutherland, and Rosa Barrio. Scavenger receptors mediate the role of sumo and ftz-f1 in drosophila steroidogenesis. Apr 2013. URL: https://doi.org/10.1371/journal.pgen.1003473, doi:10.1371/journal.pgen.1003473. This article has 82 citations and is from a domain leading peer-reviewed journal.
(talamillo2015scavengerreceptorsmediate pages 15-16): Ana Talamillo, Leire Herboso, Lucia Pirone, Coralia Pérez, Monika González, Jonatan Sánchez, Ugo Mayor, Fernando Lopitz-Otsoa, Manuel S. Rodriguez, James D. Sutherland, and Rosa Barrio. Scavenger receptors mediate the role of sumo and ftz-f1 in drosophila steroidogenesis. Apr 2013. URL: https://doi.org/10.1371/journal.pgen.1003473, doi:10.1371/journal.pgen.1003473. This article has 82 citations and is from a domain leading peer-reviewed journal.