provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2026-01-30T08:21:33.399779'
end_time: '2026-01-30T08:28:53.116367'
duration_seconds: 439.72
template_file: templates/gene_research_go_focused.md
template_variables:
organism: ANOGA
gene_id: D7r2
gene_symbol: D7r2
uniprot_accession: Q9UB31
protein_description: 'RecName: Full=Short form salivary protein D7R2 {ECO:0000305};
AltName: Full=D7-related 2 protein {ECO:0000312|EMBL:CAB39728.1}; Flags: Precursor;'
gene_info: Name=D7r2 {ECO:0000303|PubMed:16301315}; ORFNames=AgaP_AGAP008282 {ECO:0000312|EMBL:EAA12290.2};
organism_full: Anopheles gambiae (African malaria mosquito).
protein_family: Belongs to the PBP/GOBP family. .
protein_domains: PBP/GOBP. (IPR006170); PBP_GOBP_sf. (IPR036728); PBP_GOBP (PF01395)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 33

Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9UB31
• Protein Description: RecName: Full=Short form salivary protein D7R2 {ECO:0000305}; AltName: Full=D7-related 2 protein {ECO:0000312|EMBL:CAB39728.1}; Flags: Precursor;
• Gene Information: Name=D7r2 {ECO:0000303|PubMed:16301315}; ORFNames=AgaP_AGAP008282 {ECO:0000312|EMBL:EAA12290.2};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the PBP/GOBP family. .
• Key Domains: PBP/GOBP. (IPR006170); PBP_GOBP_sf. (IPR036728); PBP_GOBP (PF01395)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "D7r2" matches the protein description above
2. Verify the organism is correct: Anopheles gambiae (African malaria mosquito).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'D7r2' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene D7r2 (gene ID: D7r2, UniProt: Q9UB31) in ANOGA.

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.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9UB31
• Protein Description: RecName: Full=Short form salivary protein D7R2 {ECO:0000305}; AltName: Full=D7-related 2 protein {ECO:0000312|EMBL:CAB39728.1}; Flags: Precursor;
• Gene Information: Name=D7r2 {ECO:0000303|PubMed:16301315}; ORFNames=AgaP_AGAP008282 {ECO:0000312|EMBL:EAA12290.2};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the PBP/GOBP family. .
• Key Domains: PBP/GOBP. (IPR006170); PBP_GOBP_sf. (IPR036728); PBP_GOBP (PF01395)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "D7r2" matches the protein description above
2. Verify the organism is correct: Anopheles gambiae (African malaria mosquito).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'D7r2' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene D7r2 (gene ID: D7r2, UniProt: Q9UB31) in ANOGA.

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.

Plan and verification
- Identity check: The target corresponds to the Anopheles gambiae short-form D7 family member D7r2 within the salivary D7 gene cluster. Population-genetic analysis explicitly maps D7-related 2 (D7r2) to AGAP008282, a salivary-gland–expressed gene in An. gambiae, consistent with the UniProt entry Q9UB31 and gene symbol provided (D7r2) (published Feb 2014; https://doi.org/10.1111/imb.12068) (arca2014positiveselectiondrives pages 2-4, arca2014positiveselectiondrives pages 4-5). The D7 proteins belong to the odorant-binding protein (OBP) superfamily/PBP-GOBP-related class (short forms ~17 kDa, single OBP-like domain; long forms ~31–35 kDa, two domains) (published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Feb 2017; https://doi.org/10.1186/s12864-017-3579-8) (calvo2006functionandevolution pages 1-1, arca2017anophelinesalivaryprotein pages 7-9, arca2017anophelinesalivaryprotein pages 9-10). The organism matches (An. gambiae), and the domain/family assignment aligns with literature.

1) Key concepts and definitions
- D7 family and kratagonism: D7 proteins are highly expressed mosquito salivary proteins derived from the OBP/PBP-GOBP fold. They act as “kratagonists,” neutralizing host hemostatic and inflammatory agonists by high-affinity binding rather than enzymatic degradation (published Feb 2017; https://doi.org/10.1186/s12864-017-3579-8) (arca2017anophelinesalivaryprotein pages 9-10, arca2017anophelinesalivaryprotein pages 7-9).
- Short vs long forms: Short-form D7s (including D7r2) are one-domain OBP-like proteins specialized for biogenic amine binding (serotonin, histamine, norepinephrine/epinephrine). Long forms contain two OBP-like domains; their N-terminal domain often binds eicosanoids (cysteinyl leukotrienes, TXA2) while the C-terminal domain can bind biogenic amines (published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Nov 2010; https://doi.org/10.1371/journal.pbio.1000547) (calvo2006functionandevolution pages 1-1, alvarenga2010thefunctionand pages 1-2, jablonka2019functionalandstructural pages 9-10).
- Gene cluster and nomenclature: In An. gambiae, eight D7 genes are clustered on chromosome arm 3R (~20 kb), comprising three long and five short (D7r1–D7r5). D7r2 forms a paralogous clade with D7r3, consistent with duplication and functional conservation in amine sequestration (published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Feb 2017; https://doi.org/10.1186/s12864-017-3579-8) (calvo2006functionandevolution pages 6-7, arca2017anophelinesalivaryprotein pages 7-9, arca2017anophelinesalivaryprotein pages 9-10).

2) Primary molecular function, ligands, structure, and localization
- Function and ligand specificity: Recombinant An. gambiae short-form D7 proteins bind biogenic amines. Across D7r paralogs, serotonin exhibits the highest affinity (low-nanomolar Kd), with stoichiometry near one binding site per protein; D7r2/D7r3 show optimized binding for catecholamines (norepinephrine/epinephrine) in addition to serotonin and histamine (published Jan 2006; https://doi.org/10.1074/jbc.M510359200) (calvo2006functionandevolution pages 2-3, calvo2006functionandevolution pages 6-7, calvo2006functionandevolution pages 5-6, mans2007thecrystalstructure pages 1-1).
- Quantitative/statistical data: Calorimetry and bioassay data indicate low-nanomolar Kd for serotonin binding and near 1:1 stoichiometry. D7 proteins account for an estimated 5–20% of total salivary protein, and salivary glands contain ~1–3 µg protein, with about half discharged during feeding (published Jan 2006; https://doi.org/10.1074/jbc.M510359200) (calvo2006functionandevolution pages 5-6, calvo2006functionandevolution pages 2-3, calvo2006functionandevolution pages 1-1).
- Structural insights: The D7 fold is all-helical and stabilized by disulfide bonds; the crystal structure of the related An. gambiae D7r4 reveals an eight-helix bundle with three disulfide bonds and a defined amine-binding pocket, supporting shared structural determinants across short D7s, including D7r2 (published Dec 2007; https://doi.org/10.1074/jbc.M706410200) (mans2007thecrystalstructure pages 1-1). Comparative studies further show that long-form D7s use the N-terminal pocket for eicosanoids and, in some species, TXA2, while the C-terminal pocket of mosquito long D7s is compatible with amine ligands (published Nov 2010; https://doi.org/10.1371/journal.pbio.1000547; published Mar 2019; https://doi.org/10.1038/s41598-019-41848-0) (alvarenga2010thefunctionand pages 1-2, jablonka2019functionalandstructural pages 9-10).
- Localization and site of action: D7r2 is salivary-gland–expressed and secreted in saliva; its action occurs at the bite site to sequester host agonists and facilitate blood feeding (published Feb 2014; https://doi.org/10.1111/imb.12068; published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Feb 2017; https://doi.org/10.1186/s12864-017-3579-8) (arca2014positiveselectiondrives pages 2-4, calvo2006functionandevolution pages 5-6, arca2017anophelinesalivaryprotein pages 7-9).

3) Biological pathways and roles in hemostasis/inflammation
- Hemostasis and inflammation modulation: By binding serotonin, histamine, and catecholamines, D7r2 counteracts vasoconstriction, increases in vascular permeability, platelet aggregation, and nociception at the feeding site, thereby promoting efficient blood intake. Functional assays with salivary D7s demonstrate antagonism of amine-induced smooth muscle contraction and prolongation effects on coagulation tests by certain paralogs, linking D7s to antihemostatic and anti-inflammatory roles (published Jan 2006; https://doi.org/10.1074/jbc.M510359200) (calvo2006functionandevolution pages 5-6, calvo2006functionandevolution pages 1-1, calvo2006functionandevolution pages 6-7, mans2007thecrystalstructure pages 1-1).
- Pathway complementarity with long D7s: Long-form D7s can sequester cysteinyl leukotrienes and TXA2, directly inhibiting platelet activation and vascular smooth muscle contraction, complementing the amine-focused kratagonism of short forms (published Nov 2010; https://doi.org/10.1371/journal.pbio.1000547; published Mar 2019; https://doi.org/10.1038/s41598-019-41848-0) (alvarenga2010thefunctionand pages 1-2, jablonka2019functionalandstructural pages 9-10).

4) Evolutionary and selection context
- Gene family evolution: D7r2/D7r3 form a conserved clade derived from duplication, with conserved amine-binding function, while D7r1/D7r4 diverged in specificity and additional activities. Short-form D7s align to the C-terminal domain of long forms and retain the OBP-like scaffold (published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Feb 2017; https://doi.org/10.1186/s12864-017-3579-8) (calvo2006functionandevolution pages 6-7, arca2017anophelinesalivaryprotein pages 7-9, arca2017anophelinesalivaryprotein pages 9-10).
- Selection metrics: Across An. gambiae populations, salivary genes show elevated nucleotide diversity relative to housekeeping genes. For D7r2 (AGAP008282), dN/dS ≈ 0.08 indicates strong purifying selection on the protein sequence despite higher non-coding diversity, consistent with functional constraint on ligand-binding residues (published Feb 2014; https://doi.org/10.1111/imb.12068) (arca2014positiveselectiondrives pages 4-5, arca2014positiveselectiondrives pages 2-4).

5) Recent developments (2023–2024) and applications
- Functional genetics in mosquitoes (long-form D7s): CRISPR/Cas9 knockouts of Aedes aegypti D7 long-form proteins (D7L1, D7L2) demonstrated prolonged probing times and reduced Plasmodium gallinaceum oocyst loads, confirming in vivo kratagonism and suggesting that reingested salivary D7s can modulate the midgut environment and pathogen infection dynamics (published Dec 2023; https://doi.org/10.1128/mbio.02289-23) (martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 7-9, martinmartin2023aedesaegyptid7 pages 16-17).
- Salivary-protein frameworks in transmission: Complementary 2024 work on other Anopheles salivary proteins (e.g., apyrase) underscores how abundant salivary factors regulate hemostasis and can modulate malaria transmission, reinforcing the conceptual framework in which D7r2 operates at the bite and potentially upon reingestion (published Sep 2024; https://doi.org/10.1038/s41467-024-52502-3) (arca2014positiveselectiondrives pages 2-4).
- Exposure biomarkers and vaccines: Reviews and pooled analyses have advanced salivary-protein serology as exposure biomarkers, with increasing attention to D7 antigens; 2023–2024 literature strengthened the case for D7-based exposure assessment and vector-targeted vaccine strategies, including D7-derived components (e.g., reports of D7L antigens for human exposure readouts and broader salivary-antigen vaccine overviews) (published Jan 2025 review referencing 2024 developments; https://doi.org/10.3390/biom15010082) (guo2025unravelingthemolecular pages 21-21). While these items are not Anopheles D7r2-specific, they are mechanistically consistent with the D7 family’s roles and support translational applications.

6) Current applications and real-world implementations
- Serology for exposure: Antibody responses to mosquito salivary proteins are being used to infer human exposure to bites. D7 family members are among the abundant antigens considered for such assays; recent syntheses list D7s among candidate markers as methods are standardized for surveillance (published Jan 2025; https://doi.org/10.3390/biom15010082) (guo2025unravelingthemolecular pages 21-21).
- Vector-targeted vaccine concepts: Vector-saliva–based vaccines are under exploration as adjuncts to pathogen vaccines. D7-like proteins, because of their abundant expression and defined pharmacology, are frequently proposed as candidates, though clinical validation for D7r2 per se is pending (published Jan 2025; https://doi.org/10.3390/biom15010082) (guo2025unravelingthemolecular pages 21-21).

7) Expert analysis and synthesis
- Mechanistic consensus: The weight of biochemical, structural, and evolutionary evidence supports D7r2 as a short-form salivary OBP-like protein that kratagonizes biogenic amines—especially serotonin and catecholamines—at the bite site, dampening vasoconstriction, platelet activation, and inflammation. The conserved purifying selection on D7r2 coding sequence suggests functional constraints on its binding pocket and structural core (published Jan 2006; https://doi.org/10.1074/jbc.M510359200; published Dec 2007; https://doi.org/10.1074/jbc.M706410200; published Feb 2014; https://doi.org/10.1111/imb.12068) (calvo2006functionandevolution pages 2-3, calvo2006functionandevolution pages 1-1, mans2007thecrystalstructure pages 1-1, arca2014positiveselectiondrives pages 4-5, arca2014positiveselectiondrives pages 2-4).
- Pathway relevance today: 2023 genetic knockouts in Aedes confirm that D7s materially affect feeding behavior and parasite biology in vivo, strengthening the long-standing model and suggesting analogous importance for Anopheles D7s, including short forms like D7r2, at the bite site and possibly after reingestion (published Dec 2023; https://doi.org/10.1128/mbio.02289-23) (martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 7-9, martinmartin2023aedesaegyptid7 pages 16-17).

8) Data highlights and key statistics
- Identity mapping: D7r2 = AGAP008282; salivary-gland gene under strong purifying selection (dN/dS ~0.08) (published Feb 2014; https://doi.org/10.1111/imb.12068) (arca2014positiveselectiondrives pages 2-4, arca2014positiveselectiondrives pages 4-5).
- Abundance: D7 proteins constitute ~5–20% of total salivary protein; salivary glands hold ~1–3 µg protein with ~50% delivered during blood feeding (published Jan 2006; https://doi.org/10.1074/jbc.M510359200) (calvo2006functionandevolution pages 5-6, calvo2006functionandevolution pages 1-1).
- Binding: Short-form D7s, including the D7r2/D7r3 clade, bind serotonin with low-nanomolar affinity and also bind norepinephrine/epinephrine and histamine, typically with ~1:1 stoichiometry (published Jan 2006; https://doi.org/10.1074/jbc.M510359200) (calvo2006functionandevolution pages 2-3, calvo2006functionandevolution pages 6-7, mans2007thecrystalstructure pages 1-1).
- Structure: Short-form D7 (exemplified by D7r4) adopts an eight-helix OBP-like fold stabilized by three disulfide bonds; binding-pocket residues govern amine specificity (published Dec 2007; https://doi.org/10.1074/jbc.M706410200) (mans2007thecrystalstructure pages 1-1).

Conclusions
Anopheles gambiae D7r2 (AGAP008282; UniProt Q9UB31) is a salivary-gland, short-form D7 protein belonging to the OBP/PBP-GOBP superfamily. It localizes to saliva and functions at the bite site as a high-affinity kratagonist of biogenic amines—particularly serotonin and catecholamines—thereby diminishing vasoconstriction, platelet aggregation, and inflammatory signaling to facilitate blood feeding. Structural and phylogenetic data support conserved OBP-like architecture and selective constraint on functional residues. Recent 2023 functional genetics in mosquitoes reinforce the central role of D7 proteins in feeding and pathogen interactions, while translational work highlights D7s as candidate exposure biomarkers and potential components of vector-targeted vaccines. URLs and dates are provided above for all cited sources (arca2014positiveselectiondrives pages 2-4, arca2014positiveselectiondrives pages 4-5, calvo2006functionandevolution pages 1-1, calvo2006functionandevolution pages 2-3, mans2007thecrystalstructure pages 1-1, arca2017anophelinesalivaryprotein pages 7-9, arca2017anophelinesalivaryprotein pages 9-10, alvarenga2010thefunctionand pages 1-2, jablonka2019functionalandstructural pages 9-10, martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 7-9, martinmartin2023aedesaegyptid7 pages 16-17, guo2025unravelingthemolecular pages 21-21).

References

1. (arca2014positiveselectiondrives pages 2-4): B. Arcà, C. J. Struchiner, V. Pham, Gabriella Sferra, F. Lombardo, Marco Pombi, and José M. C. Ribeiro. Positive selection drives accelerated evolution of mosquito salivary genes associated with blood‐feeding. Insect Molecular Biology, 23:122-131, Feb 2014. URL: https://doi.org/10.1111/imb.12068, doi:10.1111/imb.12068. This article has 33 citations and is from a peer-reviewed journal.

2. (arca2014positiveselectiondrives pages 4-5): B. Arcà, C. J. Struchiner, V. Pham, Gabriella Sferra, F. Lombardo, Marco Pombi, and José M. C. Ribeiro. Positive selection drives accelerated evolution of mosquito salivary genes associated with blood‐feeding. Insect Molecular Biology, 23:122-131, Feb 2014. URL: https://doi.org/10.1111/imb.12068, doi:10.1111/imb.12068. This article has 33 citations and is from a peer-reviewed journal.

3. (calvo2006functionandevolution pages 1-1): Eric Calvo, Ben J. Mans, John F. Andersen, and José M.C. Ribeiro. Function and evolution of a mosquito salivary protein family*. Journal of Biological Chemistry, 281:1935-1942, Jan 2006. URL: https://doi.org/10.1074/jbc.m510359200, doi:10.1074/jbc.m510359200. This article has 292 citations and is from a domain leading peer-reviewed journal.

4. (arca2017anophelinesalivaryprotein pages 7-9): Bruno Arcà, Fabrizio Lombardo, Claudio J. Struchiner, and José M. C. Ribeiro. Anopheline salivary protein genes and gene families: an evolutionary overview after the whole genome sequence of sixteen anopheles species. BMC Genomics, Feb 2017. URL: https://doi.org/10.1186/s12864-017-3579-8, doi:10.1186/s12864-017-3579-8. This article has 86 citations and is from a peer-reviewed journal.

5. (arca2017anophelinesalivaryprotein pages 9-10): Bruno Arcà, Fabrizio Lombardo, Claudio J. Struchiner, and José M. C. Ribeiro. Anopheline salivary protein genes and gene families: an evolutionary overview after the whole genome sequence of sixteen anopheles species. BMC Genomics, Feb 2017. URL: https://doi.org/10.1186/s12864-017-3579-8, doi:10.1186/s12864-017-3579-8. This article has 86 citations and is from a peer-reviewed journal.

6. (alvarenga2010thefunctionand pages 1-2): Patricia H. Alvarenga, Ivo M. B. Francischetti, Eric Calvo, Anderson Sá-Nunes, José M. C. Ribeiro, and John F. Andersen. The function and three-dimensional structure of a thromboxane a2/cysteinyl leukotriene-binding protein from the saliva of a mosquito vector of the malaria parasite. PLoS Biology, 8:e1000547, Nov 2010. URL: https://doi.org/10.1371/journal.pbio.1000547, doi:10.1371/journal.pbio.1000547. This article has 72 citations and is from a highest quality peer-reviewed journal.

7. (jablonka2019functionalandstructural pages 9-10): Willy Jablonka, Il Hwan Kim, Patricia H. Alvarenga, Jesus G. Valenzuela, Jose´ M. C. Ribeiro, and John F. Andersen. Functional and structural similarities of d7 proteins in the independently-evolved salivary secretions of sand flies and mosquitoes. Scientific Reports, Mar 2019. URL: https://doi.org/10.1038/s41598-019-41848-0, doi:10.1038/s41598-019-41848-0. This article has 22 citations and is from a peer-reviewed journal.

8. (calvo2006functionandevolution pages 6-7): Eric Calvo, Ben J. Mans, John F. Andersen, and José M.C. Ribeiro. Function and evolution of a mosquito salivary protein family*. Journal of Biological Chemistry, 281:1935-1942, Jan 2006. URL: https://doi.org/10.1074/jbc.m510359200, doi:10.1074/jbc.m510359200. This article has 292 citations and is from a domain leading peer-reviewed journal.

9. (calvo2006functionandevolution pages 2-3): Eric Calvo, Ben J. Mans, John F. Andersen, and José M.C. Ribeiro. Function and evolution of a mosquito salivary protein family*. Journal of Biological Chemistry, 281:1935-1942, Jan 2006. URL: https://doi.org/10.1074/jbc.m510359200, doi:10.1074/jbc.m510359200. This article has 292 citations and is from a domain leading peer-reviewed journal.

10. (calvo2006functionandevolution pages 5-6): Eric Calvo, Ben J. Mans, John F. Andersen, and José M.C. Ribeiro. Function and evolution of a mosquito salivary protein family*. Journal of Biological Chemistry, 281:1935-1942, Jan 2006. URL: https://doi.org/10.1074/jbc.m510359200, doi:10.1074/jbc.m510359200. This article has 292 citations and is from a domain leading peer-reviewed journal.

11. (mans2007thecrystalstructure pages 1-1): Ben J. Mans, Eric Calvo, José M.C. Ribeiro, and John F. Andersen. The crystal structure of d7r4, a salivary biogenic amine-binding protein from the malaria mosquito anopheles gambiae*. Journal of Biological Chemistry, 282:36626-36633, Dec 2007. URL: https://doi.org/10.1074/jbc.m706410200, doi:10.1074/jbc.m706410200. This article has 94 citations and is from a domain leading peer-reviewed journal.

12. (martinmartin2023aedesaegyptid7 pages 1-2): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

13. (martinmartin2023aedesaegyptid7 pages 7-9): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

14. (martinmartin2023aedesaegyptid7 pages 16-17): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

15. (guo2025unravelingthemolecular pages 21-21): Jiayin Guo, Xiaoe He, Jianli Tao, Hui Sun, and Jing Yang. Unraveling the molecular mechanisms of mosquito salivary proteins: new frontiers in disease transmission and control. Biomolecules, 15:82, Jan 2025. URL: https://doi.org/10.3390/biom15010082, doi:10.3390/biom15010082. This article has 5 citations and is from a poor quality or predatory journal.

Citations

1. mans2007thecrystalstructure pages 1-1
2. arca2014positiveselectiondrives pages 2-4
3. guo2025unravelingthemolecular pages 21-21
4. arca2014positiveselectiondrives pages 4-5
5. calvo2006functionandevolution pages 1-1
6. arca2017anophelinesalivaryprotein pages 7-9
7. arca2017anophelinesalivaryprotein pages 9-10
8. alvarenga2010thefunctionand pages 1-2
9. jablonka2019functionalandstructural pages 9-10
10. calvo2006functionandevolution pages 6-7
11. calvo2006functionandevolution pages 2-3
12. calvo2006functionandevolution pages 5-6
13. https://doi.org/10.1111/imb.12068
14. https://doi.org/10.1074/jbc.M510359200;
15. https://doi.org/10.1186/s12864-017-3579-8
16. https://doi.org/10.1371/journal.pbio.1000547
17. https://doi.org/10.1074/jbc.M510359200
18. https://doi.org/10.1074/jbc.M706410200
19. https://doi.org/10.1371/journal.pbio.1000547;
20. https://doi.org/10.1038/s41598-019-41848-0
21. https://doi.org/10.1111/imb.12068;
22. https://doi.org/10.1128/mbio.02289-23
23. https://doi.org/10.1038/s41467-024-52502-3
24. https://doi.org/10.3390/biom15010082
25. https://doi.org/10.1074/jbc.M706410200;
26. https://doi.org/10.1111/imb.12068,
27. https://doi.org/10.1074/jbc.m510359200,
28. https://doi.org/10.1186/s12864-017-3579-8,
29. https://doi.org/10.1371/journal.pbio.1000547,
30. https://doi.org/10.1038/s41598-019-41848-0,
31. https://doi.org/10.1074/jbc.m706410200,
32. https://doi.org/10.1128/mbio.02289-23,
33. https://doi.org/10.3390/biom15010082,