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gene_id: TEP2
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gene_info: Name=TEP2 {ECO:0000313|EMBL:EAL39586.4}; Synonyms=3291704 {ECO:0000313|EnsemblMetazoa:AGAP008366-PA};
ORFNames=AgaP_AGAP008366 {ECO:0000313|EMBL:EAL39586.4};
organism_full: Anopheles gambiae (African malaria mosquito).
protein_family: Belongs to the protease inhibitor I39 (alpha-2-
protein_domains: A-macroglobulin_rcpt-bd. (IPR009048); A-macroglobulin_rcpt-bd_sf.
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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: Q5TQC0
• Protein Description: RecName: Full=TEP1-F {ECO:0000256|ARBA:ARBA00078071};
• Gene Information: Name=TEP2 {ECO:0000313|EMBL:EAL39586.4}; Synonyms=3291704 {ECO:0000313|EnsemblMetazoa:AGAP008366-PA}; ORFNames=AgaP_AGAP008366 {ECO:0000313|EMBL:EAL39586.4};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the protease inhibitor I39 (alpha-2-
• Key Domains: A-macroglobulin_rcpt-bd. (IPR009048); A-macroglobulin_rcpt-bd_sf. (IPR036595); A2M/Complement_sys. (IPR050473); A2M_N_BRD. (IPR011625); A2M_TED. (IPR041813)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "TEP2" 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 'TEP2' 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 TEP2 (gene ID: TEP2, UniProt: Q5TQC0) 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: Q5TQC0
• Protein Description: RecName: Full=TEP1-F {ECO:0000256|ARBA:ARBA00078071};
• Gene Information: Name=TEP2 {ECO:0000313|EMBL:EAL39586.4}; Synonyms=3291704 {ECO:0000313|EnsemblMetazoa:AGAP008366-PA}; ORFNames=AgaP_AGAP008366 {ECO:0000313|EMBL:EAL39586.4};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the protease inhibitor I39 (alpha-2-
• Key Domains: A-macroglobulin_rcpt-bd. (IPR009048); A-macroglobulin_rcpt-bd_sf. (IPR036595); A2M/Complement_sys. (IPR050473); A2M_N_BRD. (IPR011625); A2M_TED. (IPR041813)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "TEP2" 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 'TEP2' 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 TEP2 (gene ID: TEP2, UniProt: Q5TQC0) 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 overview
- Verified identity and scope: The target is Anopheles gambiae TEP2 (AGAP008366), a thioester-containing protein (TEP) of the alpha-2-macroglobulin/complement-like family, UniProt Q5TQC0. The gene resides in a TEP cluster on chromosome 3R and carries an intact thioester (TE) motif. To avoid symbol ambiguity, all functional inferences below pertain to An. gambiae TEP2, not Drosophila Tep2 or vertebrate TEPs (christophides2002immunityrelatedgenesand pages 4-6, christophides2002immunityrelatedgenesand pages 6-7).

1) Key concepts and definitions
- Thioester-containing proteins (TEPs): Secreted innate immune effectors with a reactive thioester (GCGEQ) that can form covalent bonds with microbial surfaces. In insects, TEPs are functionally analogous to vertebrate complement factors (e.g., C3), contributing to recognition, opsonization, and clearance by phagocytosis and/or lysis. The family also includes alpha-2-macroglobulin-like protease inhibitors with related architectural features (shokal2017evolutionandfunction pages 2-4, shokal2017evolutionandfunction pages 1-2). URL: https://doi.org/10.3389/fimmu.2017.00759 (published Jun 29, 2017).
- Anopheles TEP system: In A. gambiae, the complement-like pathway centers on TEP1, which circulates in hemolymph, is proteolytically processed (TEP1cut), and is stabilized by the LRIM1/APL1C heterodimeric complex until deployment on pathogen surfaces. These interactions exemplify core principles likely shared across mosquito TEPs, including secretion to hemolymph and regulated activation on target surfaces (baxter2010aheterodimericcomplex pages 1-2). URL: https://doi.org/10.1073/pnas.1010575107 (published Sep 28, 2010).
- Target identity and genomic context: TEP2 is a distinct An. gambiae TEP gene in a multi-gene cluster on chromosome arm 3R (29A–30E). TEP2 lies very close to TEP15, with other TEPs (TEP12–14) located farther within the same region. TEP2 is annotated with a present thioester (TE) motif, consistent with complement-like opsonin function (christophides2002immunityrelatedgenesand pages 4-6, christophides2002immunityrelatedgenesand pages 6-7). URL: https://doi.org/10.1126/science.1077136 (published Oct 4, 2002).

2) Recent developments and latest research (priority 2023–2024)
- Transcriptomic regulation linking TEP2 to immune and reproductive physiology: In gene-edited mosGILT-null A. gambiae, whole-body RNA-seq revealed significant upregulation of TEP2 (AGAP008366) by ~9-fold (p=0.0001), alongside other TEPs. The study connects mosGILT to modulation of complement activity and innate immunity, providing contemporary evidence that TEP2 is dynamically regulated with immune pathway perturbations (arora2024mosgiltcontrolsinnate pages 5-7). URL: https://doi.org/10.1186/s12864-023-09887-0 (published Jan 2024).
- Preprint corroboration: The same research group’s 2023 preprint similarly reported increased expression of TEP2 (AGAP008366) in mosGILT-null mosquitoes, reinforcing the regulatory link across datasets (arora2023anophelesgambiaemosgilt pages 10-15). URL: https://doi.org/10.1101/2023.08.01.551536 (posted Aug 2023).
- Population genomics context: A multi-country GWAS of insecticide resistance in A. gambiae/coluzzii detected cross-insecticide association signals spanning regions containing Tep family genes (e.g., Tep1/Tep4), highlighting immune gene neighborhoods as potential contributors to complex resistance phenotypes. While not isolating TEP2 specifically, the findings implicate TEP loci as potential hubs under selection in contemporary field populations (lucas2023genomewideassociationstudies pages 7-8). URL: https://doi.org/10.1038/s41467-023-40693-0 (published Aug 2023).

3) Function, mechanism, and pathways (integrating precise evidence and inference)
- Domain architecture and inferred mechanism: TEP2 belongs to the A2M/TEP family and contains the conserved thioester motif. By analogy to complement-like TEPs in mosquitoes, the active thioester can mediate covalent attachment to microbial surfaces, serving as an opsonin that promotes downstream effector outcomes such as phagocytosis or killing. This mechanistic inference is grounded in the conserved TEP architecture and well-characterized TEP1 biology in An. gambiae (shokal2017evolutionandfunction pages 2-4, shokal2017evolutionandfunction pages 1-2, baxter2010aheterodimericcomplex pages 1-2). URLs: 2017 review https://doi.org/10.3389/fimmu.2017.00759; 2010 structural/biochemical study https://doi.org/10.1073/pnas.1010575107.
- Pathway integration and interacting modules: In the canonical mosquito complement-like pathway, TEP1 is stabilized and delivered by LRIM1/APL1C until deposition on pathogens; SPCLIP1 regulates TEP1 recruitment to microbial surfaces. While direct biochemical interaction data for TEP2 with LRIM1/APL1C are not available in the gathered sources, the shared TEP architecture and clustered genomic organization suggest that TEP2 likely participates in extracellular complement-like immunity in hemolymph, potentially coordinated with LRIM/APL1 modules. This is an informed inference based on TEP family principles and the Anopheles complement-like paradigm (baxter2010aheterodimericcomplex pages 1-2, shokal2017evolutionandfunction pages 2-4). URL: https://doi.org/10.1073/pnas.1010575107; https://doi.org/10.3389/fimmu.2017.00759.
- Specific roles: There is strong evidence for TEP1-mediated opsonization and parasite killing in A. gambiae, and for TEP family roles in opsonization and melanization cascades in insects. However, direct phenotypic evidence uniquely assigning opsonization, melanization, or phagocytosis roles to An. gambiae TEP2 was not identified in the 2023–2024 literature sampled here. Thus, TEP2’s primary function is best described as a secreted, thioester-bearing complement-like protein with predicted opsonin activity by homology, pending direct experimental validation (shokal2017evolutionandfunction pages 2-4, shokal2017evolutionandfunction pages 1-2). URL: https://doi.org/10.3389/fimmu.2017.00759.

4) Localization, expression, and regulation
- Extracellular localization: Mosquito complement-like TEPs (exemplified by TEP1) are secreted into the hemolymph, where they circulate and are activated/targeted to pathogen surfaces. Given TEP2’s conserved signal features within the TEP family and genomic clustering with other secreted TEPs, TEP2 is expected to be a secreted hemolymph protein (inference from family and TEP1 data) (baxter2010aheterodimericcomplex pages 1-2, shokal2017evolutionandfunction pages 2-4). URL: https://doi.org/10.1073/pnas.1010575107; https://doi.org/10.3389/fimmu.2017.00759.
- Tissue expression and inducibility: RNA-seq in mosGILT-null mosquitoes shows whole-body upregulation of TEP2 (~9×), suggesting responsiveness to immune pathway perturbation. Earlier work cited therein noted midgut TEP gene upregulation upon Plasmodium falciparum infection, consistent with infection-inducible regulation in the epithelium/hemolymph interface. Direct tissue-specific expression for TEP2 (e.g., fat body vs. hemocytes) was not explicitly reported in the 2023–2024 sources queried here (arora2024mosgiltcontrolsinnate pages 5-7, arora2023anophelesgambiaemosgilt pages 10-15). URL: https://doi.org/10.1186/s12864-023-09887-0; https://doi.org/10.1101/2023.08.01.551536.
- Genomic organization: TEP2 is part of a TEP cluster on 3R (29A–30E), lying very close to TEP15; the cluster organization supports coordinated evolution and possibly co-regulation within the family (christophides2002immunityrelatedgenesand pages 4-6, christophides2002immunityrelatedgenesand pages 6-7). URL: https://doi.org/10.1126/science.1077136.

5) Applications and real-world implementations
- Vector control and surveillance implications: Complement-like genes are major determinants of vector competence and are under selection in wild populations. The 2023 GWAS highlights Tep family regions exhibiting cross-insecticide associations, suggesting immune gene neighborhoods—including TEPs—may influence or correlate with resistance phenotypes, informing genomic surveillance strategies. While TEP2-specific selection was not isolated, Tep regions appear as multi-allelic, population-variable signals, cautioning that monitoring should account for local haplotypes and CNVs (lucas2023genomewideassociationstudies pages 7-8). URL: https://doi.org/10.1038/s41467-023-40693-0 (Aug 2023).
- Research utility: The robust upregulation of TEP2 in mosGILT-null mosquitoes links TEP2 expression to innate immune modulation and reproductive biology, providing an entry point for functional genetic tests in A. gambiae strains used by vector biology labs (arora2024mosgiltcontrolsinnate pages 5-7, arora2023anophelesgambiaemosgilt pages 10-15). URL: https://doi.org/10.1186/s12864-023-09887-0; https://doi.org/10.1101/2023.08.01.551536.

6) Expert opinions and analysis
- Complement-like architecture as a guide to function: Reviews and structural work emphasize that insect TEPs are secreted, hemolymph-borne effectors with regulated activation, covalent target tagging via a transient thioester, and interactions with LRIM/APL1 complexes. For An. gambiae, this framework is best characterized for TEP1 and provides the most reliable mechanistic scaffold for TEP2 functional hypotheses until TEP2-specific experiments are available (shokal2017evolutionandfunction pages 2-4, baxter2010aheterodimericcomplex pages 1-2). URLs: https://doi.org/10.3389/fimmu.2017.00759; https://doi.org/10.1073/pnas.1010575107.
- Gene family context and diversification: The Anopheles genome encodes an expanded TEP repertoire relative to Drosophila, with multiple clustered loci and some members lacking a TE motif. TEP2 is among the thioester-positive members, consistent with complement-like opsonin potential in Anopheles immunity (christophides2002immunityrelatedgenesand pages 4-6, christophides2002immunityrelatedgenesand pages 6-7). URL: https://doi.org/10.1126/science.1077136.

7) Quantitative data and statistics
- TEP2 expression change: In A. gambiae mosGILT-null, TEP2 (AGAP008366) whole-body transcript levels increased ~9-fold versus wild type (p=0.0001), indicating strong inducibility under immune/reproductive pathway perturbation (arora2024mosgiltcontrolsinnate pages 5-7, arora2023anophelesgambiaemosgilt pages 10-15). URLs: 2024 article https://doi.org/10.1186/s12864-023-09887-0; 2023 preprint https://doi.org/10.1101/2023.08.01.551536.
- GWAS signals: Cross-insecticide resistance association peaks were reported in genomic regions encompassing Tep family genes (not isolating TEP2), underscoring potential relevance of complement-like immunity loci to adaptive traits in field populations (lucas2023genomewideassociationstudies pages 7-8). URL: https://doi.org/10.1038/s41467-023-40693-0.

Ambiguity and limitations explicitly addressed
- Symbol ambiguity: “TEP2” is used in multiple insects; here it denotes Anopheles gambiae TEP2 (AGAP008366; UniProt Q5TQC0). Reviews that discuss “Tep2” in Drosophila are not directly applicable; where family-level mechanisms are invoked, they are explicitly identified as inferences from conserved architecture and A. gambiae TEP1 biology (shokal2017evolutionandfunction pages 2-4, christophides2002immunityrelatedgenesand pages 4-6).
- Evidence gaps: No 2023–2024 primary experimental study providing direct biochemical function, substrate specificity, hemolymph proteomics confirmation, or genetic loss-of-function phenotypes for An. gambiae TEP2 was found in the gathered sources. Functional roles are therefore inferred from TEP family principles, genomic context, and expression regulation, and should be validated with TEP2-specific perturbation studies in A. gambiae (shokal2017evolutionandfunction pages 2-4, arora2024mosgiltcontrolsinnate pages 5-7).

Concise functional annotation for An. gambiae TEP2 (AGAP008366; UniProt Q5TQC0)
- Molecular function: Predicted complement-like opsonin with a reactive thioester; covalent tagging of pathogen surfaces is inferred by homology to An. gambiae TEP1 and conserved domain features (shokal2017evolutionandfunction pages 2-4, baxter2010aheterodimericcomplex pages 1-2).
- Biological processes: Innate immune response in hemolymph; likely contributes to pathogen recognition/opsonization and downstream effector mechanisms (phagocytosis or melanization) as part of the mosquito complement-like pathway; inducible in immune pathway perturbation (shokal2017evolutionandfunction pages 2-4, arora2024mosgiltcontrolsinnate pages 5-7).
- Cellular/extracellular localization: Secreted to hemolymph (inferred from TEP family and TEP1 paradigm) (baxter2010aheterodimericcomplex pages 1-2, shokal2017evolutionandfunction pages 2-4).
- Pathways: Mosquito complement-like cascade coordinated by LRIM1/APL1C carrier complex and serine protease regulators; direct interaction of TEP2 with LRIM/APL1 not yet reported in the sources gathered here; genomic clustering suggests shared regulation with neighboring TEPs (baxter2010aheterodimericcomplex pages 1-2, christophides2002immunityrelatedgenesand pages 4-6).

Citations
- Shokal U, Eleftherianos I. Evolution and Function of Thioester-Containing Proteins and the Complement System in the Innate Immune Response. Front Immunol. 2017;8:759. https://doi.org/10.3389/fimmu.2017.00759 (Jun 29, 2017) (shokal2017evolutionandfunction pages 2-4, shokal2017evolutionandfunction pages 1-2).
- Baxter RHG, et al. A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae. PNAS. 2010;107(39):16817–16822. https://doi.org/10.1073/pnas.1010575107 (Sep 28, 2010) (baxter2010aheterodimericcomplex pages 1-2).
- Christophides GK, et al. Immunity-Related Genes and Gene Families in Anopheles gambiae. Science. 2002;298(5591):159–165. https://doi.org/10.1126/science.1077136 (Oct 4, 2002) (christophides2002immunityrelatedgenesand pages 4-6, christophides2002immunityrelatedgenesand pages 6-7).
- Arora G, et al. mosGILT controls innate immunity and germ cell development in Anopheles gambiae. BMC Genomics. 2024;25:1–12. https://doi.org/10.1186/s12864-023-09887-0 (Jan 2024) (arora2024mosgiltcontrolsinnate pages 5-7).
- Arora G, et al. Anopheles gambiae mosGILT regulates innate immune genes and zpg expression. bioRxiv. 2023. https://doi.org/10.1101/2023.08.01.551536 (Aug 2023) (arora2023anophelesgambiaemosgilt pages 10-15).
- Lucas ER, et al. Genome-wide association studies reveal novel loci associated with pyrethroid and organophosphate resistance in Anopheles gambiae and Anopheles coluzzii. Nat Commun. 2023;14:4946. https://doi.org/10.1038/s41467-023-40693-0 (Aug 2023) (lucas2023genomewideassociationstudies pages 7-8).

References

1. (christophides2002immunityrelatedgenesand pages 4-6): George K. Christophides, Evgeny Zdobnov, Carolina Barillas-Mury, Ewan Birney, Stephanie Blandin, Claudia Blass, Paul T. Brey, Frank H. Collins, Alberto Danielli, George Dimopoulos, Charles Hetru, Ngo T. Hoa, Jules A. Hoffmann, Stefan M. Kanzok, Ivica Letunic, Elena A. Levashina, Thanasis G. Loukeris, Gareth Lycett, Stephan Meister, Kristin Michel, Luis F. Moita, Hans-Michael Müller, Mike A. Osta, Susan M. Paskewitz, Jean-Marc Reichhart, Andrey Rzhetsky, Laurent Troxler, Kenneth D. Vernick, Dina Vlachou, Jennifer Volz, Christian von Mering, Jiannong Xu, Liangbiao Zheng, Peer Bork, and Fotis C. Kafatos. Immunity-related genes and gene families in anopheles gambiae. Science, 298:159-165, Oct 2002. URL: https://doi.org/10.1126/science.1077136, doi:10.1126/science.1077136. This article has 1191 citations and is from a highest quality peer-reviewed journal.

2. (christophides2002immunityrelatedgenesand pages 6-7): George K. Christophides, Evgeny Zdobnov, Carolina Barillas-Mury, Ewan Birney, Stephanie Blandin, Claudia Blass, Paul T. Brey, Frank H. Collins, Alberto Danielli, George Dimopoulos, Charles Hetru, Ngo T. Hoa, Jules A. Hoffmann, Stefan M. Kanzok, Ivica Letunic, Elena A. Levashina, Thanasis G. Loukeris, Gareth Lycett, Stephan Meister, Kristin Michel, Luis F. Moita, Hans-Michael Müller, Mike A. Osta, Susan M. Paskewitz, Jean-Marc Reichhart, Andrey Rzhetsky, Laurent Troxler, Kenneth D. Vernick, Dina Vlachou, Jennifer Volz, Christian von Mering, Jiannong Xu, Liangbiao Zheng, Peer Bork, and Fotis C. Kafatos. Immunity-related genes and gene families in anopheles gambiae. Science, 298:159-165, Oct 2002. URL: https://doi.org/10.1126/science.1077136, doi:10.1126/science.1077136. This article has 1191 citations and is from a highest quality peer-reviewed journal.

3. (shokal2017evolutionandfunction pages 2-4): Upasana Shokal and Ioannis Eleftherianos. Evolution and function of thioester-containing proteins and the complement system in the innate immune response. Frontiers in Immunology, Jun 2017. URL: https://doi.org/10.3389/fimmu.2017.00759, doi:10.3389/fimmu.2017.00759. This article has 138 citations and is from a peer-reviewed journal.

4. (shokal2017evolutionandfunction pages 1-2): Upasana Shokal and Ioannis Eleftherianos. Evolution and function of thioester-containing proteins and the complement system in the innate immune response. Frontiers in Immunology, Jun 2017. URL: https://doi.org/10.3389/fimmu.2017.00759, doi:10.3389/fimmu.2017.00759. This article has 138 citations and is from a peer-reviewed journal.

5. (baxter2010aheterodimericcomplex pages 1-2): Richard H. G. Baxter, Stefanie Steinert, Yogarany Chelliah, Gloria Volohonsky, Elena A. Levashina, and Johann Deisenhofer. A heterodimeric complex of the lrr proteins lrim1 and apl1c regulates complement-like immunity in anopheles gambiae. Proceedings of the National Academy of Sciences, 107:16817-16822, Sep 2010. URL: https://doi.org/10.1073/pnas.1010575107, doi:10.1073/pnas.1010575107. This article has 76 citations and is from a highest quality peer-reviewed journal.

6. (arora2024mosgiltcontrolsinnate pages 5-7): Gunjan Arora, Xiaotian Tang, Yingjun Cui, Jing Yang, Yu-Min Chuang, Jayadev Joshi, Andaleeb Sajid, Yuemei Dong, Peter Cresswell, George Dimopoulos, and Erol Fikrig. Mosgilt controls innate immunity and germ cell development in anopheles gambiae. BMC Genomics, 25:1-12, Jan 2024. URL: https://doi.org/10.1186/s12864-023-09887-0, doi:10.1186/s12864-023-09887-0. This article has 8 citations and is from a peer-reviewed journal.

7. (arora2023anophelesgambiaemosgilt pages 10-15): Gunjan Arora, Xiaotian Tang, Yingjun Cui, Jing Yang, Yu-Min Chuang, Jayadev Joshi, Andaleeb Sajid, Yuemei Dong, Peter Cresswell, George Dimopoulos, and Erol Fikrig. Anopheles gambiae mosgilt regulates innate immune genes and zpg expression. bioRxiv, Aug 2023. URL: https://doi.org/10.1101/2023.08.01.551536, doi:10.1101/2023.08.01.551536. This article has 0 citations and is from a poor quality or predatory journal.

8. (lucas2023genomewideassociationstudies pages 7-8): Eric R. Lucas, Sanjay C. Nagi, Alexander Egyir-Yawson, John Essandoh, Samuel Dadzie, Joseph Chabi, Luc S. Djogbénou, Adandé A. Medjigbodo, Constant V. Edi, Guillaume K. Kétoh, Benjamin G. Koudou, Arjen E. Van’t Hof, Emily J. Rippon, Dimitra Pipini, Nicholas J. Harding, Naomi A. Dyer, Louise T. Cerdeira, Chris S. Clarkson, Dominic P. Kwiatkowski, Alistair Miles, Martin J. Donnelly, and David Weetman. Genome-wide association studies reveal novel loci associated with pyrethroid and organophosphate resistance in anopheles gambiae and anopheles coluzzii. Nature Communications, Aug 2023. URL: https://doi.org/10.1038/s41467-023-40693-0, doi:10.1038/s41467-023-40693-0. This article has 70 citations and is from a highest quality peer-reviewed journal.

Citations

1. baxter2010aheterodimericcomplex pages 1-2
2. arora2024mosgiltcontrolsinnate pages 5-7
3. arora2023anophelesgambiaemosgilt pages 10-15
4. lucas2023genomewideassociationstudies pages 7-8
5. christophides2002immunityrelatedgenesand pages 4-6
6. christophides2002immunityrelatedgenesand pages 6-7
7. shokal2017evolutionandfunction pages 2-4
8. shokal2017evolutionandfunction pages 1-2
9. https://doi.org/10.3389/fimmu.2017.00759
10. https://doi.org/10.1073/pnas.1010575107
11. https://doi.org/10.1126/science.1077136
12. https://doi.org/10.1186/s12864-023-09887-0
13. https://doi.org/10.1101/2023.08.01.551536
14. https://doi.org/10.1038/s41467-023-40693-0
15. https://doi.org/10.3389/fimmu.2017.00759;
16. https://doi.org/10.1073/pnas.1010575107.
17. https://doi.org/10.1073/pnas.1010575107;
18. https://doi.org/10.3389/fimmu.2017.00759.
19. https://doi.org/10.1186/s12864-023-09887-0;
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