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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: A0A1S4HE90
• Protein Description: RecName: Full=Long form salivary protein D7L3 {ECO:0000305}; Short=AngaD7L3 {ECO:0000303|PubMed:35460690}; Flags: Precursor;
• Gene Information: Name=7DL3 {ECO:0000303|PubMed:35568118};
• 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 "7DL3" 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 '7DL3' 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 7DL3 (gene ID: 7DL3, UniProt: A0A1S4HE90) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: A0A1S4HE90
• Protein Description: RecName: Full=Long form salivary protein D7L3 {ECO:0000305}; Short=AngaD7L3 {ECO:0000303|PubMed:35460690}; Flags: Precursor;
• Gene Information: Name=7DL3 {ECO:0000303|PubMed:35568118};
• 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 "7DL3" 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 '7DL3' 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 7DL3 (gene ID: 7DL3, UniProt: A0A1S4HE90) 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
- Verified identity: 7DL3 (AngaD7L3) is one of three long-form D7 salivary proteins (D7L1, D7L2, D7L3) in Anopheles gambiae; these are abundant, female salivary proteins. The protein class is odorant-binding protein–like, typically placed within the broader PBP/GOBP-related OBP superfamily, though D7 domains show distinct features compared with canonical PBP/GOBP OBPs (see Domain/Family). (oseno2022characterizationofanopheles pages 1-2, arora2023malariainfluenceof pages 6-7, sharma2025olfactorygenedynamics pages 5-6, sharma2025olfactorygenedynamics pages 6-9)
- Collected recent evidence (2023–2024 prioritized where available) on D7 long-form function, localization, and translational use; where AngaD7L3-specific data are sparse, we infer carefully from closely related D7 long-forms in mosquitoes, stating the limitations.
- Synthesized a functional annotation with explicit citations and URLs.

Key concepts and definitions
- D7 salivary proteins: Highly abundant mosquito salivary proteins, expressed predominantly in adult female salivary glands, that act as kratagonists to bind and sequester host hemostatic and inflammatory agonists at the bite site. D7s occur as long forms (~27–30 kDa) with two ligand-binding domains and short forms (~15–20 kDa) with a single domain. In An. gambiae, the multigene D7 family comprises three long forms (D7L1, D7L2, D7L3) and five short forms (D7r1–D7r5). (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022; Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (oseno2022characterizationofanopheles pages 1-2, arora2023malariainfluenceof pages 6-7)
- Domain/family context: D7 proteins were initially characterized as odorant-binding protein (OBP)-like. Comparative analyses indicate D7 domains share alpha-helical architecture with OBPs but are structurally and sequence-divergent from canonical PBP/GOBP OBPs; they may have larger ligand cavities supporting broad ligand repertoires. Thus, AngaD7L3’s UniProt assignment to PBP/GOBP-related OBP superfamily is consistent at a high level, with recognition of D7’s distinct domain features. (Arora 2023; Sharma 2025, Sci Rep, https://doi.org/10.1038/s41598-025-21404-9, Oct 2025) (arora2023malariainfluenceof pages 6-7, sharma2025olfactorygenedynamics pages 5-6, sharma2025olfactorygenedynamics pages 6-9)

Recent developments and latest research (emphasis 2023–2024)
- Functional genetics in Aedes validates D7 long-form roles in vivo: CRISPR/Cas9 knockouts of D7L1 and D7L2 prolong probing time and reduce Plasmodium gallinaceum oocyst numbers, confirming D7 long forms counteract host inflammatory mediators and may influence parasite infection dynamics. While performed in Ae. aegypti, these data support conserved roles for D7 long forms across mosquitoes, including Anopheles. (Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 1-2)
- Contemporary reviews reinforce D7 abundance and anti-hemostatic functions in Anopheles saliva and their contribution to facilitating Plasmodium infection at the bite site, situating D7s within a broader pharmacological saliva toolkit. (Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (arora2023malariainfluenceof pages 6-7)

Current applications and real-world implementations
- Biomarkers of mosquito exposure: In Kenyan and Ugandan cohorts, anti-D7 IgG responses (assayed with An. gambiae D7 family antigens) tracked transmission intensity, were age-associated, and were reduced in users of insecticide-treated bed nets. D7L2 showed performance as an exposure biomarker; this supports the general concept that D7 long-form salivary proteins (including AngaD7L3) are immunogenic surveillance targets for human–vector contact. (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022) (oseno2022characterizationofanopheles pages 1-2)
- Vector control and transmission modulation (inference to Anopheles): The in vivo roles of D7 long forms in Aedes (probing and parasite infection) suggest that targeting homologous Anopheles D7 long-form proteins (including D7L3) could influence feeding success and potentially parasite establishment. This remains to be tested directly for AngaD7L3 but is plausible by homology. (Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 1-2)

Expert opinions and analysis from authoritative sources
- Trends in Immunology perspective (2023): D7 proteins are among the most abundant components of Anopheles saliva; they function as OBP-like kratagonists that scavenge biogenic amines and lipid mediators, shaping early host responses to facilitate Plasmodium transmission. This review frames D7s as central effectors of anti-hemostatic and anti-inflammatory activity at the bite site. (Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (arora2023malariainfluenceof pages 6-7)
- Structural/biochemical paradigm (Nature Communications 2020): Long-form D7s can exhibit diverse ligand-binding specificities, including classical biogenic amines and eicosanoids (CxD7L2) and, strikingly, adenine nucleotides/nucleosides (CxD7L1), expanding the mechanistic repertoire by which D7s inhibit platelet aggregation and hemostasis. While cross-species, this establishes the mechanistic landscape relevant for annotating D7L3. (Martin‑Martin 2020, Nat Commun, https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2)

Relevant statistics and data from recent studies
- Exposure biomarker performance in humans (An. gambiae D7 antigens): IgG responses to D7 antigens mirrored site-specific transmission intensity (highest in Kitgum, Uganda > Junju, Kenya > malaria-naïve Europeans), increased with age, and were lower among bed-net users, supporting utility for surveillance and intervention monitoring. Numerical effect sizes vary by cohort; the directionality and utility are consistently reported. (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022) (oseno2022characterizationofanopheles pages 1-2)
- Functional outcomes of D7L loss (Aedes model): D7 long-form knockouts increased probing time, and both D7L1/D7L2 KOs reduced oocyst burden, highlighting quantifiable impacts on feeding dynamics and parasite infection; these phenotypes are directly measured and statistically supported in the mBio study. (Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 1-2)
- Ligand-binding and structural data (Culex model): ITC quantification and crystal structure demonstrate high-affinity ADP/ATP binding by CxD7L1 and amine/eicosanoid binding by CxD7L2, with ex vivo/in vivo inhibition of platelet aggregation. (Martin‑Martin 2020, Nat Commun, https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2)

Functional annotation of Anopheles gambiae 7DL3 (AngaD7L3; UniProt A0A1S4HE90)
- Identity and nomenclature: AngaD7L3 is one of three D7 long-form genes (D7L1–D7L3) in Anopheles gambiae; D7 genes include five short forms (D7r1–D7r5). Family members are among the most abundant salivary proteins in adult females. An. gambiae D7 family mapping places these loci on chromosome arm 3R (~30B). (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022) (oseno2022characterizationofanopheles pages 1-2)
- Protein family/domains: D7 proteins are OBP-like; comparative analyses indicate D7 domains are related to OBPs yet diverge from canonical PBP/GOBP OBPs in sequence and some aspects of fold, often with larger ligand cavities. Thus, AngaD7L3’s OBP/PBP-GOBP–related classification is appropriate, with the caveat that D7s constitute a distinct OBP-like lineage specialized for anti-hemostatic ligand binding. (Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023; Sharma 2025, Sci Rep, https://doi.org/10.1038/s41598-025-21404-9, Oct 2025) (arora2023malariainfluenceof pages 6-7, sharma2025olfactorygenedynamics pages 5-6, sharma2025olfactorygenedynamics pages 6-9)
- Biochemical function and substrate specificity: Direct, gene-specific ligand-binding data for AngaD7L3 in An. gambiae were not identified in the sources retrieved here. By homology to other D7 long forms, AngaD7L3 most likely functions as a kratagonist that binds host hemostatic agonists. Long forms typically possess two domains that can bind: (i) biogenic amines (histamine, serotonin, norepinephrine/epinephrine) and/or (ii) eicosanoids (e.g., cysteinyl leukotrienes, thromboxane analogs); in some lineages, long forms evolved high‑affinity binding to adenine nucleotides/nucleosides (ADP/ATP/adenosine), directly inhibiting platelet aggregation. Definitive substrate specificity for AngaD7L3 remains to be experimentally defined. (Martin‑Martin 2020, Nat Commun, https://doi.org/10.1038/s41467-020-16665-z, Jun 2020; Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023; Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (martinmartin2020adpbindingby pages 1-2, martinmartin2023aedesaegyptid7 pages 1-2, arora2023malariainfluenceof pages 6-7)
- Localization and secretion: D7 proteins are expressed in female salivary glands and secreted in saliva; imaging in related species localizes D7s primarily to distal lateral lobes of the salivary glands. During feeding, they are injected into the bite site and may be partially reingested, potentially acting in the midgut. These features are well-documented for D7 long forms in Aedes and are broadly consistent across mosquitoes, including Anopheles. (Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023; Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023; Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022) (martinmartin2023aedesaegyptid7 pages 1-2, arora2023malariainfluenceof pages 6-7, oseno2022characterizationofanopheles pages 1-2)
- Pathway/physiological role: AngaD7L3, as a D7 long-form salivary protein, likely contributes to inhibition of vasoconstriction and platelet aggregation and dampening of inflammation/itch/pain at the bite site by scavenging host agonists. These actions facilitate blood acquisition and can influence early events in Plasmodium transmission. While AngaD7L3-specific evidence is lacking, this role is strongly supported for D7 long forms. (Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023; Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023; Martin‑Martin 2020, Nat Commun, https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (arora2023malariainfluenceof pages 6-7, martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2020adpbindingby pages 1-2)
- Evidence limitations and symbol verification: The symbol “7DL3/AngaD7L3” is used in An. gambiae literature to denote one of the long-form D7 genes, and the organism identity (An. gambiae) is correct. However, we did not retrieve D7L3-specific biochemical data (ligand-binding or structure) in the 2020–2024 window; functional inference is based on the D7 long-form family. (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022; Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (oseno2022characterizationofanopheles pages 1-2, arora2023malariainfluenceof pages 6-7)

Translational opportunities and implementations
- Serological surveillance: Anti-D7 IgG responses can index human exposure to Anopheles bites and track intervention impact (e.g., bed net usage). Given immunogenicity of An. gambiae D7 long forms and family members, AngaD7L3-derived antigens could be evaluated as additional biomarkers alongside D7L2. (Oseno 2022, Parasites & Vectors, https://doi.org/10.1186/s13071-021-05130-5, Jan 2022) (oseno2022characterizationofanopheles pages 1-2)
- Vaccine/therapeutic concepts: D7 long forms’ capacity to neutralize host hemostatic mediators is a mechanistic basis for considering anti-saliva vaccination or therapeutic mimetics; genetic or immunological targeting of D7 long forms modulates probing and parasite infection in Aedes models, motivating analogous evaluation in Anopheles for AngaD7L3. (Martin‑Martin 2023, mBio, https://doi.org/10.1128/mbio.02289-23, Dec 2023; Arora 2023, Trends in Immunology, https://doi.org/10.1016/j.it.2023.02.005, Apr 2023) (martinmartin2023aedesaegyptid7 pages 1-2, arora2023malariainfluenceof pages 6-7)

Study and source summary
| Reference | Species / Protein focus | Main findings relevant to D7L3 functional annotation | Relevance to AngaD7L3 | URL / DOI | Publication date |
|---|---|---|---|---|---|
| Oseno et al., 2022 (Parasites & Vectors) (oseno2022characterizationofanopheles pages 1-2) | Anopheles gambiae — D7 family (D7L1, D7L2, D7L3; D7r1–D7r5) | Defines D7 multigene family in An. gambiae; reports three long forms (D7L1–D7L3) and abundance in female salivary glands; implicates D7s in inhibiting platelet aggregation/coagulation and as serological markers of bite exposure (D7L2 data shown). (oseno2022characterizationofanopheles pages 1-2) | Confirms nomenclature and salivary-gland localization for AngaD7L3; supports inference that AngaD7L3 is a secreted anti-hemostatic salivary protein. (oseno2022characterizationofanopheles pages 1-2) | https://doi.org/10.1186/s13071-021-05130-5 | Jan 2022 |
| Arora et al., 2023 (Trends in Immunology) (arora2023malariainfluenceof pages 6-7) | Anopheles spp. — salivary proteins (including D7s) | Review: D7 proteins are abundant in Anopheles saliva, were initially characterized as odorant‑binding protein–like, and long/short forms act as kratagonists that scavenge host hemostatic/inflammatory agonists at the bite site. (arora2023malariainfluenceof pages 6-7) | Provides authoritative review support that AngaD7L3 likely functions as a ligand‑binding anti‑hemostatic salivary protein affecting host inflammation/hemostasis. (arora2023malariainfluenceof pages 6-7) | https://doi.org/10.1016/j.it.2023.02.005 | Apr 2023 |
| Martin‑Martin et al., 2020 (Nature Communications) (martinmartin2020adpbindingby pages 1-2) | Culex quinquefasciatus — D7 long forms (CxD7L1, CxD7L2) | High‑quality structural/functional work: CxD7L2 binds biogenic amines and eicosanoids; CxD7L1 binds adenine nucleotides (ADP/ATP) with solved crystal structure (1.97 Å); both inhibit hemostasis in ex vivo/in vivo assays — demonstrates D7L ligand diversity and anti‑platelet activity. (martinmartin2020adpbindingby pages 1-2) | Demonstrates that D7 long forms can bind biogenic amines, eicosanoids, or nucleotides; supports inference that AngaD7L3 may bind similar host agonists (kratagonist function) although direct binding data for D7L3 are lacking. (martinmartin2020adpbindingby pages 1-2) | https://doi.org/10.1038/s41467-020-16665-z | Jun 2020 |
| Martin‑Martin et al., 2023 (mBio) (martinmartin2023aedesaegyptid7 pages 1-2) | Aedes aegypti — D7 long forms (D7L1, D7L2) | In vivo functional genetics: D7L long‑form knockouts have prolonged probing times; D7Ls bind biogenic amines and eicosanoids and modulate Plasmodium infection (fewer oocysts in KO). Demonstrates physiological roles in feeding and pathogen dynamics. (martinmartin2023aedesaegyptid7 pages 1-2) | Provides experimental evidence that D7 long forms modulate probing/feeding and pathogen infection — supports likely biological consequences if AngaD7L3 binds analogous ligands in An. gambiae. (martinmartin2023aedesaegyptid7 pages 1-2) | https://doi.org/10.1128/mbio.02289-23 | Dec 2023 |
| Sharma et al., 2025 (Scientific Reports) (sharma2025olfactorygenedynamics pages 6-9, sharma2025olfactorygenedynamics pages 5-6) | Comparative structural analysis — OBP (PBP/GOBP), OSD, D7 domains | Structural comparison: D7 domains are OBP‑related (alpha‑helical architecture) but show low sequence identity and distinguishable folds vs canonical PBP_GOBP; D7s have larger ligand cavities suggesting broader ligand repertoire. (sharma2025olfactorygenedynamics pages 6-9, sharma2025olfactorygenedynamics pages 5-6) | Supports UniProt/domain annotation (PBP_GOBP‑like) while noting D7 divergence — useful for inferring ligand‑binding possibilities for AngaD7L3 from domain architecture but cautions against simple transfer of OBP function. (sharma2025olfactorygenedynamics pages 6-9, sharma2025olfactorygenedynamics pages 5-6) | https://doi.org/10.1038/s41598-025-21404-9 | Oct 2025 |

Table: Compact table of recent, authoritative sources on mosquito D7 long-form salivary proteins, summarizing findings relevant to AngaD7L3 (7DL3, UniProt A0A1S4HE90) to support functional annotation and translational relevance.

Conclusion
AngaD7L3 (7DL3; UniProt A0A1S4HE90) is one of the three Anopheles gambiae D7 long-form salivary proteins. While direct ligand-specific data for D7L3 in An. gambiae were not retrieved in 2020–2024 sources, convergent evidence from closely related D7 long forms shows that long-form D7s are secreted, OBP-like kratagonists that facilitate blood feeding by scavenging biogenic amines, eicosanoids, and, in some lineages, adenine nucleotides. They are abundant in female salivary glands/saliva, act at the bite site to counter hemostasis and inflammation, and serve as immunogenic biomarkers of exposure with translational potential in surveillance and, prospectively, in vector-targeted interventions. Future work should define AngaD7L3’s precise ligand specificity and in vivo roles using biochemical binding assays and functional genetics in Anopheles. (oseno2022characterizationofanopheles pages 1-2, arora2023malariainfluenceof pages 6-7, martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2020adpbindingby pages 1-2)

References

1. (oseno2022characterizationofanopheles pages 1-2): Brenda Oseno, Faith Marura, Rodney Ogwang, Martha Muturi, James Njunge, Irene Nkumama, Robert Mwakesi, Kennedy Mwai, Martin K. Rono, Ramadhan Mwakubambanya, Faith Osier, and James Tuju. Characterization of anopheles gambiae d7 salivary proteins as markers of human–mosquito bite contact. Parasites & Vectors, Jan 2022. URL: https://doi.org/10.1186/s13071-021-05130-5, doi:10.1186/s13071-021-05130-5. This article has 11 citations and is from a peer-reviewed journal.

2. (arora2023malariainfluenceof pages 6-7): Gunjan Arora, Yu-Min Chuang, Photini Sinnis, George Dimopoulos, and Erol Fikrig. Malaria: influence of anopheles mosquito saliva on plasmodium infection. Trends in Immunology, 44:256-265, Apr 2023. URL: https://doi.org/10.1016/j.it.2023.02.005, doi:10.1016/j.it.2023.02.005. This article has 50 citations and is from a domain leading peer-reviewed journal.

3. (sharma2025olfactorygenedynamics pages 5-6): Arvind Sharma, Bhuvan Dixit, Bharti Goyal, Renuka Harit, Jatin Kumar, Shibani Biswas, Ritu Goswami, Kailash C. Pandey, S. Noushin Emami, and Soumyananda Chakraborti. Olfactory gene dynamics in invasive indian and non-invasive african malaria vectors at the crossroads of development, infection and resistance. Scientific Reports, Oct 2025. URL: https://doi.org/10.1038/s41598-025-21404-9, doi:10.1038/s41598-025-21404-9. This article has 1 citations and is from a peer-reviewed journal.

4. (sharma2025olfactorygenedynamics pages 6-9): Arvind Sharma, Bhuvan Dixit, Bharti Goyal, Renuka Harit, Jatin Kumar, Shibani Biswas, Ritu Goswami, Kailash C. Pandey, S. Noushin Emami, and Soumyananda Chakraborti. Olfactory gene dynamics in invasive indian and non-invasive african malaria vectors at the crossroads of development, infection and resistance. Scientific Reports, Oct 2025. URL: https://doi.org/10.1038/s41598-025-21404-9, doi:10.1038/s41598-025-21404-9. This article has 1 citations and is from a peer-reviewed journal.

5. (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.

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Citations

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