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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 correct target is fruit-fly Fbxo42/CG6758 (FlyBase FBgn0034704; UniProt Q9W281), not mammalian FBXO42 or an FBXO6 protein from another organism. Gene-specific genetic mapping identifies Drosophila CG6758 as a 667-amino-acid F-box protein on chromosome 2R, interval 58C1–58D1, with an N-terminal F-box at approximately residues 21–70. This agrees with the supplied UniProt identity and domain annotation. The alias “FBXO6” is particularly hazardous because it commonly denotes a different vertebrate F-box protein; no such literature was used here. (santosUnknownyeartheroleofa pages 127-132)
The most defensible primary annotation is: Fbxo42 is a substrate-recognition/adaptor component of an SCF-type Cullin–RING E3 ubiquitin-ligase system that promotes ubiquitination and proteasomal turnover of Ataxin-2 during the unfolded-protein response (UPR), thereby regulating Xbp1 mRNA utilization and production of spliced Xbp1 protein. Fbxo42 is not shown to be an autonomous catalytic enzyme; ubiquitin transfer is performed by the assembled E2–SCF machinery. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofb pages 243-248, dui2012asystematicphenotypic pages 1-2)
The literature is unusually sparse. Searches found no 2023–2024 peer-reviewed primary article specifically devoted to Drosophila CG6758. The strongest recent gene-specific evidence is a dissertation based on research conducted during 2016–2025; its detailed findings should therefore be regarded as recent but not equivalent to independently replicated peer-reviewed evidence. (santosUnknownyeartheroleofa pages 11-17, santosUnknownyeartheroleofd pages 11-17)
Fbxo42 belongs functionally to the F-box class of substrate receptors. F-box proteins bind the Skp component of SCF complexes and help recruit selected proteins to a Cullin-1–Rbx catalytic core for ubiquitination. A 2012 systematic survey recognized CG6758 among 45 Drosophila F-box-domain genes; RNAi reagents were available for 44 genes in the survey. The retrieved results do not, however, resolve a CG6758-specific phenotype from that screen. The article was published in August 2012 and is available at https://doi.org/10.1016/j.jgg.2012.05.009. (dui2012asystematicphenotypic pages 2-4, dui2012asystematicphenotypic pages 1-2)
The supplied InterPro/Pfam annotations—F-box domain, F-box-like superfamily, F-box-only substrate-receptor family, Kelch-type β-propeller, and Beta-prop_FBX42—are structurally coherent with an SCF substrate receptor: the N-terminal F-box is expected to connect to Skp, whereas the β-propeller-like region is a plausible substrate-binding platform. These latter assignments are computational/domain-family annotations; an experimentally determined Q9W281 structure or purified receptor–substrate complex was not found.
Proteomic work recovered Skp-1, Cullin-1, and Rbx-1 with Fbxo42, providing direct support for association with the canonical SCF core. Nevertheless, full SCF–Fbxo42 ubiquitination has not been reconstituted with purified components, so the precise complex composition, E2 enzyme, recognition motif, and kinetic specificity remain incompletely defined. (santosUnknownyeartheroleofb pages 243-248)
Ataxin-2 is the best-supported substrate. In triplicate adult fly-head bioUb experiments, streptavidin-enriched ubiquitinated proteins were analyzed by mass spectrometry. Ataxin-2 was enriched with full-length Fbxo42 relative to the control F-box protein Fbxl7 and was identified by two unique peptides. The analysis used a two-sided Student’s t test, p < 0.05, with a twofold difference corresponding to an absolute log2 LFQ ratio of at least 1. Tagged overexpression and the small peptide count limit discovery-stage confidence, but subsequent orthogonal assays substantially strengthen the assignment. (santosUnknownyeartheroleofd pages 150-156)
Endogenous and overexpressed proteins co-immunoprecipitated. In fly eyes and S2 cells, Ataxin-2 formed slower-migrating ubiquitin conjugates; these conjugates were markedly reduced by the reducing agent DTT and abolished by Fbxo42 RNAi. Thus, Fbxo42 is required for the observed Ataxin-2 ubiquitination, and at least one conjugate appears to involve a reducible cysteine linkage. (santosUnknownyeartheroleofc pages 243-248, santosUnknownyeartheroleofd pages 156-161)
Ataxin-2 Cys244 is the leading acceptor-site candidate. A C244A mutant was more stable and lacked the DTT-sensitive conjugate, while AlphaFold modeling placed C244 near ubiquitin and the candidate E2 in a predicted complex. This is strong mutational support but not definitive chemical site identification; direct site-specific or intact-mass spectrometry was not reported. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofc pages 243-248)
Cycloheximide-chase experiments showed accelerated Ataxin-2 loss when Fbxo42 was overexpressed and protection when Fbxo42 was depleted. MG132 stabilized Ataxin-2, connecting the effect to the proteasome. Numerical half-lives and effect sizes were unavailable in the retrieved material. Collectively, these experiments support a sequence of substrate recognition, Fbxo42-dependent ubiquitination, and proteasomal turnover. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofd pages 243-248)
Proteomics also returned CCT3/CCT4 candidates, and PP1-87B was considered from phenotypic observations, but these candidates were not validated to the standard achieved for Ataxin-2. They should not currently be treated as established physiological substrates. (santosUnknownyeartheroleofb pages 243-248, santosUnknownyeartheroleofd pages 150-156)
The relevant pathway is the Ire1–Xbp1 branch of the UPR. ER stress activates Ire1-dependent processing of Xbp1 mRNA to produce Xbp1s, a transcription factor that drives protein-folding, ER quality-control, and ER-associated degradation programs. (santosUnknownyeartheroleof pages 95-101)
Under DTT-induced ER stress, Ataxin-2 forms cytoplasmic granules containing Xbp1 mRNA. Sequential immunofluorescence/smFISH and iCLIP showed Ataxin-2 association with the transcript, particularly its 3′ UTR. Actinomycin-D experiments indicated that Ataxin-2 stabilizes the mRNA, while Ataxin-2 depletion reduced Xbp1s protein. Similar accumulation of Xbp1 mRNA in Ataxin-2 granules was observed in HeLa cells, suggesting—but not proving—evolutionary conservation of the RNA-handling mechanism. (santosUnknownyeartheroleofa pages 248-254, santosUnknownyeartheroleofa pages 207-212)
Fbxo42 foci appear near Ataxin-2 granules after ER-stress induction. The working model is temporally ordered:
Several links are directly supported: Fbxo42 depletion or mutant clones reduce Xbp1s protein, and Ataxin-2 RNAi abolishes the suppression produced by an Fbxo42 mutant in the Xbp1s eye assay. The entire temporal-release model has not, however, been demonstrated in one causal live-cell experiment. In particular, the proposal that activated Ire1 phosphorylates Ataxin-2 to recruit Fbxo42 remains unverified; no kinase assay, phosphosite mapping, phosphomutant test, or phosphorylation-dependent binding assay was reported. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofa pages 207-212, santosUnknownyeartheroleofd pages 156-161)
A forward EMS screen sought suppressors of retinal degeneration caused by GMR-driven Xbp1s. Six suppressor alleles—Su209, Su212, Su217, Su218, Su226, and Su359—mapped to Fbxo42, with most producing premature termination codons. Tagged Fbxo42 and a genomic Pacman construct restored the phenotype, establishing locus-level causality. UAS-DsRed remained expressed in mutant cells, excluding general failure of GAL4/UAS transcription. (santosUnknownyeartheroleofa pages 127-132)
Loss of Fbxo42 also suppressed the rough-eye phenotype caused by Rh1 overexpression, another sensitized model associated with ER stress and UPR activation. These findings connect Fbxo42 to proteostasis and Xbp1-dependent retinal-cell outcomes, but eye overexpression models do not by themselves define the gene’s normal organism-wide physiological role. (santosUnknownyeartheroleofa pages 127-132)
The 2012 systematic F-box RNAi study used tub-Gal4 for ubiquitous depletion and ey-Gal4, en-/nub-Gal4, and pnr-Gal4 for eye, wing, and notum screens. Although CG6758 was included in the gene catalog, available text does not identify its specific viability, fertility, or tissue phenotype. The report that 14 F-box-gene knockdowns were lethal cannot be assigned to CG6758 without the missing gene-level table. (dui2012asystematicphenotypic pages 2-4, dui2012asystematicphenotypic pages 1-2)
An anti-Fbxo42 antibody detected protein in larval brain, ring gland, and eye imaginal disc, and in adult brain, testis, and ovary. This supports expression in neural, endocrine, visual-developmental, and germline/reproductive tissues, although quantitative abundance, comprehensive cell-type resolution, and all antibody-specificity controls were unavailable. (santosUnknownyeartheroleof pages 95-101, santosUnknownyeartheroleofd pages 11-17)
At the intracellular level, the strongest observation is stress-associated Fbxo42 foci close to Ataxin-2 granules. The evidence supports spatial proximity and possible recruitment but does not show that Fbxo42 is a stable granule constituent. No reliable basal assignment to nucleus, cytosol, ER membrane, or another organelle can presently be made. Endogenous fluorescent tagging, organelle-marker colocalization, biochemical fractionation, and live imaging would be needed for a definitive localization annotation. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofd pages 243-248)
| Annotation or claim | Specific evidence and assay | Evidence level | Confidence and limitations |
|---|---|---|---|
| Identity and architecture: Drosophila melanogaster Fbxo42 is CG6758, a 667-aa protein encoded on chromosome 2R in interval 58C1–58D1; its N-terminal F-box spans approximately residues 21–70. | Deficiency mapping and sequencing identified CG6758; the gene-specific study reports the protein length and F-box coordinates. These agree with the supplied UniProt Q9W281 and FlyBase FBgn0034704 identity. (santosUnknownyeartheroleofa pages 127-132) | Direct experimental for locus identity; supportive/inferred for domain boundaries | High. Exact identifier matching prevents confusion with vertebrate FBXO42 or proteins called FBXO6. The Kelch-type beta-propeller and PF13415 annotations are computational domain assignments rather than experimentally determined structures. |
| Primary molecular role: Fbxo42 is best classified as a substrate-recognition receptor or adaptor associated with an SCF-type Cullin–RING E3 ubiquitin ligase, not as the enzyme that directly transfers ubiquitin. | F-box proteins generally recruit substrates to SkpA or Skp-1–Cullin-1–Rbx-containing SCF ligases. Fbxo42 proteomics recovered Skp-1, Cullin-1 and Rbx-1, supporting association with the canonical SCF core. (santosUnknownyeartheroleofb pages 243-248, dui2012asystematicphenotypic pages 1-2) | Direct experimental for association with SCF components; supportive/inferred for precise receptor architecture | Moderate–high. SCF association and F-box architecture are compelling, but a complete Drosophila SCF–Fbxo42 complex was not purified and functionally reconstituted. |
| Ataxin-2 is an experimentally supported Fbxo42 substrate. | In triplicate adult fly-head bioUb and streptavidin-pulldown proteomics, Ataxin-2 was enriched with full-length Fbxo42 relative to Fbxl7 and identified by two unique peptides. Significance was defined as p less than 0.05, and a twofold difference corresponded to an absolute log2 LFQ ratio of at least 1. Endogenous and overexpression co-immunoprecipitation supported physical association. (santosUnknownyeartheroleofc pages 243-248, santosUnknownyeartheroleofd pages 150-156) | Direct experimental | Moderate–high. Multiple orthogonal assays support the relationship, but discovery proteomics used tagged proteins and eye-specific overexpression, and Ataxin-2 was identified by only two unique peptides. |
| Fbxo42-dependent, cysteine-linked Ataxin-2 ubiquitylation. | Fly-eye and S2-cell pulldowns detected slower-migrating Ataxin-2–ubiquitin conjugates. DTT markedly reduced a conjugate, consistent with a reducible cysteine linkage, and Fbxo42 RNAi abolished conjugate formation in S2 cells. (santosUnknownyeartheroleofd pages 150-156, santosUnknownyeartheroleofd pages 156-161) | Direct experimental | High for Fbxo42 dependence; moderate for linkage chemistry. DTT sensitivity supports but does not independently prove a thioester or other cysteine-linked conjugate. |
| Ataxin-2 Cys244 is the proposed ubiquitin-acceptor residue. | Ataxin-2 C244A was more stable and lacked the DTT-sensitive conjugates observed with wild-type Ataxin-2. AlphaFold modeling placed C244 near ubiquitin and the E2 enzyme in a predicted complex. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofc pages 243-248) | Direct experimental for the mutant phenotype; supportive/inferred for structural placement | Moderate–high. The mutation strongly implicates C244, but direct site assignment by intact-mass or site-specific mass spectrometry was not reported. |
| Fbxo42 promotes proteasomal turnover of Ataxin-2. | Cycloheximide-chase assays showed faster Ataxin-2 loss after Fbxo42 overexpression and protection after Fbxo42 knockdown; MG132 stabilized Ataxin-2. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofd pages 243-248) | Direct experimental | High for a role in proteasome-dependent turnover. Numerical half-lives and effect sizes were unavailable in the retrieved evidence, and overexpression may exaggerate turnover kinetics. |
| Role in the Ire1–Xbp1 unfolded-protein response: Fbxo42 facilitates production of spliced Xbp1 protein through regulation of Ataxin-2 turnover and release of stabilized Xbp1 mRNA for translation. | During ER stress, Ataxin-2 bound the Xbp1 mRNA 3-prime UTR, stabilized the transcript and promoted Xbp1s protein expression. Fbxo42 depletion or mutant clones reduced Xbp1s protein; Ataxin-2 RNAi abolished Fbxo42-mutant suppression of the Xbp1s-induced glossy-eye phenotype. (santosUnknownyeartheroleofa pages 248-254, santosUnknownyeartheroleofa pages 207-212, santosUnknownyeartheroleofd pages 156-161) | Direct experimental for genetic dependence and Xbp1s effects; supportive/inferred for the complete temporal-release model | Moderate–high. Genetics, imaging, RNA-binding and protein assays support the pathway, but the entire sequence from granule storage through Fbxo42 recruitment and mRNA release was not demonstrated in one causal experiment. |
| Biological-process phenotype: loss of Fbxo42 suppresses Xbp1s- and Rh1-overexpression eye phenotypes associated with ER stress. | A forward EMS suppressor screen recovered six Fbxo42 alleles: Su209, Su212, Su217, Su218, Su226 and Su359. Most encoded premature stops. Tagged Fbxo42 and a genomic Pacman construct restored the phenotype, while a UAS-DsRed control excluded general failure of GAL4/UAS transcription. Fbxo42 loss also suppressed the rough eye caused by Rh1 overexpression. (santosUnknownyeartheroleofa pages 127-132) | Direct experimental | High for causality at the Fbxo42 locus. Eye-overexpression models are sensitized systems and do not alone establish the protein's normal organism-wide physiological role. |
| Tissue expression: Fbxo42 protein occurs in larval brain, ring gland and eye imaginal disc, and in adult brain, testis and ovary. | A generated anti-Fbxo42 antibody detected protein in these larval and adult tissues. (santosUnknownyeartheroleof pages 95-101, santosUnknownyeartheroleofd pages 11-17) | Direct experimental | Moderate. Tissue detection is supported, but quantitative abundance, cell-type resolution and complete antibody-validation results were not available. |
| Stress-associated intracellular localization: Fbxo42 forms foci near stress-induced Ataxin-2 granules. | Following DTT-induced ER stress, Ataxin-2 granules appeared near Fbxo42 foci by immunofluorescence. The interpretation was recruitment near granules rather than Fbxo42 being an integral granule constituent. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofd pages 243-248) | Direct experimental for spatial proximity; supportive/inferred for recruitment | Moderate. Proximity does not prove direct binding at granules; precise organelle association, membrane contact and granule residence time remain undetermined. |
| 2012 systematic RNAi-screen inclusion: CG6758 was recognized as a Drosophila F-box gene and included in the survey framework. | The peer-reviewed screen catalogued 45 F-box-domain genes, obtained RNAi lines for 44, listed CG6758 in Table 1 and used ubiquitous, eye-, wing- and notum-specific drivers. (dui2012asystematicphenotypic pages 2-4, dui2012asystematicphenotypic pages 1-2) | Direct experimental for inclusion in the screen | Low for gene-specific conclusions. The retrieved material did not report CG6758-specific viability, fertility or tissue phenotypes; lethality observed for 14 knockdowns cannot be assigned to CG6758. |
| Direct catalytic reaction of Fbxo42. | No purified biochemical assay showed Fbxo42 independently transferring ubiquitin or catalyzing another chemical reaction. Its supported role is substrate recognition or adaptation within an E2–SCF ubiquitination system. (santosUnknownyeartheroleofb pages 243-248, dui2012asystematicphenotypic pages 1-2) | Unverified | Fbxo42 should not be annotated as an autonomous ubiquitin-transfer enzyme or assigned a standalone catalytic reaction without biochemical reconstitution. |
| Precise basal subcellular localization. | Available evidence establishes tissue expression and stress-associated foci near Ataxin-2 granules but does not define steady-state localization to the cytosol, nucleus, ER membrane or another organelle. (santosUnknownyeartheroleof pages 95-101, santosUnknownyeartheroleof pages 243-248) | Unverified | A basal localization assignment requires endogenous tagging, compartment markers and preferably live-cell imaging or biochemical fractionation. |
| Ire1 directly recruits Fbxo42 by phosphorylating Ataxin-2. | The gene-specific work proposes that activated Ire1 phosphorylates Ataxin-2 and thereby recruits Fbxo42 during ER stress, but explicitly identifies this mechanism as requiring validation. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofa pages 243-248) | Unverified | No direct Ire1–Ataxin-2 kinase assay, phosphosite mapping, phosphomutant test or phosphorylation-dependent Fbxo42-binding experiment was reported. |
Table: Evidence-ranked functional annotations for Drosophila Fbxo42/CG6758, separating direct experimental findings from structural inference and unresolved mechanisms.
No clinical, agricultural, diagnostic, or commercial implementation specifically targeting fly Fbxo42 was found. Its current application is as a research tool and mechanistic node in models of ER stress, proteostasis, RNA granules, Xbp1 signaling, and retinal degeneration. The Drosophila Xbp1s and Rh1 eye systems provide genetically tractable in-vivo assays for testing substrate-receptor biology and UPR modulation. Translation to mammals remains speculative because a human FBXO42–Ataxin-2 substrate relationship was not established in the retrieved evidence. (santosUnknownyeartheroleofa pages 248-254, santosUnknownyeartheroleofa pages 127-132)
Recommended primary molecular-function description: “Substrate-recognition component of an SCF-type E3 ubiquitin ligase; promotes Fbxo42-dependent ubiquitination and proteasomal degradation of Ataxin-2.”
Recommended biological-process description: “Regulates the Ire1–Xbp1 unfolded-protein-response branch by controlling Ataxin-2-containing RNA granules and the translation/output of spliced Xbp1 mRNA during ER stress.”
Recommended cellular-component wording: “SCF ubiquitin-ligase-associated; detected in stress-induced cytoplasmic foci near Ataxin-2 granules.” A stronger organelle assignment is not justified.
Substrate specificity: Ataxin-2 is currently the only well-supported substrate, with Cys244 implicated as an unusual ubiquitin-acceptor residue. CCT3, CCT4, PP1-87B, and other proteomic candidates remain provisional. (santosUnknownyeartheroleof pages 243-248, santosUnknownyeartheroleofb pages 243-248, santosUnknownyeartheroleofd pages 150-156)
Confidence: Moderate overall—high for gene identity, SCF association, the genetic eye phenotype, and Fbxo42-dependent Ataxin-2 turnover; moderate for Cys244 chemistry and the complete Xbp1 translational-release model; low for precise basal localization and broader physiological substrate range.
In summary, Q9W281 is securely identified as Drosophila Fbxo42/CG6758. Its clearest current function is not a standalone catalytic reaction but substrate selection within an SCF ubiquitin-ligase system, with Ataxin-2 turnover linking Fbxo42 to RNA-granule dynamics and Xbp1-mediated ER-stress signaling.
References
(santosUnknownyeartheroleofa pages 127-132): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleof pages 243-248): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofb pages 243-248): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(dui2012asystematicphenotypic pages 1-2): Wen Dui, Wei Lu, Jun Ma, and Renjie Jiao. A systematic phenotypic screen of f-box genes through a tissue-specific rnai-based approach in drosophila. Journal of genetics and genomics = Yi chuan xue bao, 39 8:397-413, Aug 2012. URL: https://doi.org/10.1016/j.jgg.2012.05.009, doi:10.1016/j.jgg.2012.05.009. This article has 27 citations.
(santosUnknownyeartheroleofa pages 11-17): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofd pages 11-17): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(dui2012asystematicphenotypic pages 2-4): Wen Dui, Wei Lu, Jun Ma, and Renjie Jiao. A systematic phenotypic screen of f-box genes through a tissue-specific rnai-based approach in drosophila. Journal of genetics and genomics = Yi chuan xue bao, 39 8:397-413, Aug 2012. URL: https://doi.org/10.1016/j.jgg.2012.05.009, doi:10.1016/j.jgg.2012.05.009. This article has 27 citations.
(santosUnknownyeartheroleofd pages 150-156): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofc pages 243-248): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofd pages 156-161): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofd pages 243-248): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleof pages 95-101): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofa pages 248-254): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofa pages 207-212): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(santosUnknownyeartheroleofa pages 243-248): CC Santos. The role of fbxo42 in ataxin-2-mediated regulation of xbp1 signalling. Unknown journal, Unknown year.
(stanyon2004adrosophilaproteininteraction pages 2-3): Clement A Stanyon, Guozhen Liu, Bernardo A Mangiola, Nishi Patel, Loic Giot, Bing Kuang, Huamei Zhang, Jinhui Zhong, and Russell L Finley. A drosophila protein-interaction map centered on cell-cycle regulators. Genome Biology, 5:R96-R96, Nov 2004. URL: https://doi.org/10.1186/gb-2004-5-12-r96, doi:10.1186/gb-2004-5-12-r96. This article has 249 citations and is from a highest quality peer-reviewed journal.
(stanyon2004adrosophilaproteininteraction pages 9-10): Clement A Stanyon, Guozhen Liu, Bernardo A Mangiola, Nishi Patel, Loic Giot, Bing Kuang, Huamei Zhang, Jinhui Zhong, and Russell L Finley. A drosophila protein-interaction map centered on cell-cycle regulators. Genome Biology, 5:R96-R96, Nov 2004. URL: https://doi.org/10.1186/gb-2004-5-12-r96, doi:10.1186/gb-2004-5-12-r96. This article has 249 citations and is from a highest quality peer-reviewed journal.