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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:** O00170
- **Protein Description:** RecName: Full=AH receptor-interacting protein; Short=AIP; AltName: Full=Aryl-hydrocarbon receptor-interacting protein; AltName: Full=HBV X-associated protein 2; Short=XAP-2; AltName: Full=Immunophilin homolog ARA9;
- **Gene Information:** Name=AIP; Synonyms=XAP2;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Not specified in UniProt
- **Key Domains:** AIP/AIPL1/TTC9. (IPR039663); PPIase_AIP. (IPR056277); PPIase_dom_sf. (IPR046357); PPIase_FKBP_dom. (IPR001179); TPR-like_helical_dom_sf. (IPR011990)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "AIP" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
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 'AIP' 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 **AIP** (gene ID: AIP, UniProt: O00170) in human.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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:** O00170
- **Protein Description:** RecName: Full=AH receptor-interacting protein; Short=AIP; AltName: Full=Aryl-hydrocarbon receptor-interacting protein; AltName: Full=HBV X-associated protein 2; Short=XAP-2; AltName: Full=Immunophilin homolog ARA9;
- **Gene Information:** Name=AIP; Synonyms=XAP2;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Not specified in UniProt
- **Key Domains:** AIP/AIPL1/TTC9. (IPR039663); PPIase_AIP. (IPR056277); PPIase_dom_sf. (IPR046357); PPIase_FKBP_dom. (IPR001179); TPR-like_helical_dom_sf. (IPR011990)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "AIP" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
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 'AIP' 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 **AIP** (gene ID: AIP, UniProt: O00170) in human.

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.

Title: Functional Annotation Research Report — Human AIP (AH receptor-interacting protein; UniProt O00170)

Publication window emphasized: 2023–2024 clinical genetics/guidelines; 2022 structural biology; foundational mechanistic work prior.

1. Executive summary (gene/protein verified)

AIP (aryl hydrocarbon receptor-interacting protein) in Homo sapiens is a ~37 kDa, 330-aa cytoplasmic co-chaperone also known as XAP2 and ARA9 (UniProt O00170). It is best understood as a scaffold/co-chaperone that stabilizes specific client proteins—most prominently the aryl hydrocarbon receptor (AHR)—within an HSP90-based cytosolic chaperone complex, influencing AHR stability, cytosolic retention, and ligand-triggered nuclear signaling. In humans, germline loss-of-function AIP variants predispose to pituitary neuroendocrine tumors (PitNETs; especially somatotroph and lactotroph lineages) with incomplete penetrance, and AIP behaves as a tumor suppressor consistent with a two-hit model (loss of heterozygosity in tumors). (trivellin2011evaluationofthe pages 34-37, cain2010roleofthe pages 2-3)

2. Gene/protein identity, synonyms, and disambiguation

2.1 Verified identity

The literature retrieved explicitly uses AIP synonymy consistent with UniProt O00170: AIP is also called XAP2 and ARA9, and is described as a 330-aa (~37 kDa) protein. (trivellin2011evaluationofthe pages 34-37, cain2010roleofthe pages 2-3)

2.2 Common aliases used in the literature

AIP is repeatedly referred to as XAP2/ARA9 and described as “immunophilin-like” due to an FKBP-like N-terminus, although it does not behave as a classical FKBP immunophilin (see §3.3). (cain2010roleofthe pages 2-3, trivellin2011evaluationofthe pages 34-37)

3. Key concepts, definitions, and current mechanistic understanding

3.1 Domain architecture and structural definitions

AIP is composed of:

• An N-terminal FKBP-type peptidyl-prolyl isomerase (PPIase)-like domain (often called “PPIase-like” or “FKBP-type”), and 
• A C-terminal tetratricopeptide repeat (TPR) region containing three TPR motifs plus a terminal α-helix (often discussed as an α-7 helix) important for protein–protein interactions and client binding. (trivellin2011evaluationofthe pages 34-37, hernandezramirez2018multichaperonefunctionmodulation pages 1-2, cain2010roleofthe pages 2-3)

3.2 Core biochemical function: co-chaperone/scaffold in the AHR–HSP90 complex

AIP participates in a cytosolic multiprotein complex with AHR and HSP90 (and p23), regulating AHR stability/cytosolic retention and nuclear translocation following ligand activation. (cain2010roleofthe pages 2-3, cain2010roleofthe pages 12-13)

Interaction mapping supports a model in which AIP binds the HSP90 C-terminus through its TPR-containing C-terminal half (residues ~154–330), and the terminal residues/helix are critical for AHR association. (trivellin2011evaluationofthe pages 41-44, cain2010roleofthe pages 2-3)

3.3 Is AIP an enzyme? (PPIase activity and substrate specificity)

Although AIP contains an FKBP-like “PPIase-like” domain, multiple sources indicate it does not function as an immunophilin and lacks detectable PPIase enzymatic activity; it also lacks binding to FKBP ligands (FK506/rapamycin) that typify catalytically active FKBPs. Therefore, AIP is best annotated as a non-enzymatic immunophilin-like co-chaperone/scaffold, not a PPIase enzyme with a defined substrate. (trivellin2011evaluationofthe pages 34-37, hernandezramirez2018multichaperonefunctionmodulation pages 1-2, cain2010roleofthe pages 2-3)

3.4 Subcellular localization (where AIP carries out function)

AIP is described as a cytoplasmic protein and as part of the cytoplasmic AHR/HSP90/p23 complex; this complex translocates to the nucleus upon AHR ligand binding, enabling AHR to dimerize with ARNT and act as a transcription factor. (cain2010roleofthe pages 4-5)

In pituitary-focused proteomic work, AIP additionally co-localized with HSPA9 in the mitochondrial network, consistent with broader chaperone-network associations beyond the AHR complex. (hernandezramirez2018multichaperonefunctionmodulation pages 1-2)

3.5 Pathway context: AHR signaling and cAMP modulation (PDE interactions)

AIP’s best-established pathway context is AHR signaling via its co-chaperone role in the AHR cytosolic complex. (cain2010roleofthe pages 2-3, cain2010roleofthe pages 12-13)

AIP also binds phosphodiesterases (notably PDE4A5 and PDE2A3 are reported interactors), linking it to localized cAMP regulation and potentially to modulation of AHR nuclear translocation and pituitary tumor biology. (trivellin2011evaluationofthe pages 34-37, cain2010roleofthe pages 12-13)

4. Structural biology and molecular mechanism (notable developments)

4.1 Cryo-EM architecture of the HSP90–AIP(XAP2)–AHR cytosolic complex

A high-resolution cryo-EM structure of the human agonist-bound AHR cytosolic complex with Hsp90 and XAP2/AIP provides a concrete architectural model: AIP/XAP2 acts as a brace associated with the Hsp90 dimer and the AHR client. This structure also shows the Hsp90 C-terminal MEEVD motif docked into the TPR domain region of AIP/XAP2, consistent with canonical TPR-mediated recruitment of HSP90 co-chaperones. (gruszczyk2022cryoemstructureof media 0a99161a, gruszczyk2022cryoemstructureof media a4609a97)

Interpretation for functional annotation: these structural data strongly support annotating AIP as an HSP90 co-chaperone/scaffold that physically stabilizes the AHR client complex in the cytosol and helps govern the activation-ready state. (gruszczyk2022cryoemstructureof media 0a99161a, gruszczyk2022cryoemstructureof media a4609a97)

5. Human genetics and disease association: pituitary tumor predisposition

5.1 Tumor suppressor role and “two-hit” behavior

AIP is widely described as a tumor suppressor in familial isolated pituitary adenoma (FIPA), supported by loss of heterozygosity at the AIP locus in tumors consistent with a two-hit model. (trivellin2011evaluationofthe pages 34-37, cain2010roleofthe pages 2-3)

5.2 Penetrance (current estimates and variability)

Penetrance among AIP variant carriers is incomplete and variable. Reported penetrance ranges in the literature include ~12–30% overall for pituitary adenomas among AIP variant carriers, with some variants/families reported as low as ~6% penetrance. (trofimiukmuldner2023aipgenegermline pages 9-10)

A 2024 review similarly summarizes limited penetrance estimates in the ~20–33% range and notes that onset is typically young (<30 years). (balinisteanu2024unlockingthegenetic pages 5-6)

5.3 Recent (2023–2024) statistics: prevalence of germline pathogenic variants in clinical cohorts

5.3.1 Prolactinomas (large 2023 cohort study)

In a multicenter cohort of 506 patients with isolated prolactinomas undergoing germline testing (MEN1, AIP, CDKN1B; plus SF3B1 in genetically negative cases), 14/506 (2.8%) carried a pathogenic/likely pathogenic germline variant in MEN1 or AIP. All mutation-positive cases were macroprolactinomas diagnosed before age 30. (boukerrouni2023genetictestingin pages 1-5)

In sporadic isolated macroprolactinomas diagnosed ≤30 years, the germline pathogenic/likely pathogenic variant prevalence was 4.3% (11/258) overall, split into 2.3% MEN1 (6/258) and 1.9% AIP (5/258). (boukerrouni2023genetictestingin pages 8-11)

Age-stratified risk was strong: sporadic macroprolactinoma diagnosed before age 18 had ~9-fold higher odds of carrying a germline mutation than diagnosis at 18–30 (OR 9; 95% CI 2.3–43; p=0.0016). (boukerrouni2023genetictestingin pages 8-11)

The same study found no pathogenic/likely pathogenic variants in sporadic microprolactinomas (including <30 years), and no (likely) pathogenic variants in macroprolactinomas diagnosed after age 30, supporting a targeted (not universal) testing approach. (boukerrouni2023genetictestingin pages 11-13)

5.3.2 Sporadic pituitary adenomas (2024 WES cohort)

In a 2024 whole-exome sequencing study of 134 apparently sporadic pituitary adenomas, one AIP variant (p.S256F) was considered VUS by ACMG but “likely pathogenic” by AlphaMissense (1/134, ~0.7%), illustrating an emerging trend: integrating AI-based variant effect prediction may change the set of candidates requiring follow-up functional/clinical validation. (alzahrani2024germlinevariantsin pages 4-5)

5.3.3 Pediatric/high-risk contexts (2024 consensus guideline)

A 2024 Nature Reviews Endocrinology consensus guideline reports that among childhood-onset GH-secreting pituitary tumours presenting as gigantism, AIP mutations account for ~29% of cases. (korbonits2024consensusguidelinefor pages 6-7)

For macroprolactinomas presenting before age 20, the guideline reports a genetic aetiology in ~14% (9% AIP, 5% MEN1). (korbonits2024consensusguidelinefor pages 6-7)

6. Current applications and real-world implementations

6.1 Genetic testing strategies (who to test)

Real-world testing criteria are increasingly risk-stratified by age, tumor size/behavior, and family history:

• In isolated prolactinoma care, a large 2023 cohort supports focusing germline testing on young patients with macroprolactinomas (especially <18 years) and/or familial context; the study does not support routine testing for sporadic microprolactinomas even in younger adults. (boukerrouni2023genetictestingin pages 11-13, boukerrouni2023genetictestingin pages 8-11)

• In pediatric/adolescent pituitary adenomas, a 2024 consensus guideline strongly recommends offering genetic testing to all children and young people with GH or prolactin excess, reflecting the higher yield and important implications for family counseling and surveillance. (korbonits2024consensusguidelinefor pages 6-7)

6.2 Surveillance of carriers

The 2024 pediatric guideline emphasizes that genetic assessment of potential carriers should occur before typical symptom onset, and that follow-up may include yearly clinical and biochemical review. It also cautions that if known genes are ruled out in the proband, routine family clinical assessment is not recommended because penetrance is incomplete and screening can cause harm. (korbonits2024consensusguidelinefor pages 6-7)

6.3 Variant interpretation as an implementation challenge

Clinical implementation depends heavily on rigorous variant classification. Recent cohort work highlights that variant reclassification (e.g., when a once-suspected pathogenic variant is found to be common in population databases) can substantially alter prevalence estimates and downstream family management. This is one reason some cohorts report lower pathogenic-variant frequencies than earlier literature. (trofimiukmuldner2023aipgenegermline pages 9-10)

7. Expert opinion and authoritative synthesis

Authoritative reviews and guidelines converge on two major, mechanistically grounded interpretations:

(1) AIP is primarily a co-chaperone/scaffold that binds HSP90 (via TPR interactions) and stabilizes client protein complexes, notably AHR; and 
(2) germline AIP loss-of-function predisposes to pituitary tumors with incomplete penetrance, with highest diagnostic yield of testing in young-onset, macroadenoma, gigantism, and familial contexts. (cain2010roleofthe pages 2-3, korbonits2024consensusguidelinefor pages 6-7)

8. Practical functional annotation (recommended concise ontology-style statements)

Protein class/function:

• Non-enzymatic immunophilin-like co-chaperone/scaffold protein; binds HSP90 via TPR motifs and participates in client protein stabilization complexes; lacks demonstrable PPIase catalytic activity despite FKBP-like fold homology. (trivellin2011evaluationofthe pages 34-37, hernandezramirez2018multichaperonefunctionmodulation pages 1-2, cain2010roleofthe pages 2-3)

Key pathway/process:

• AHR signaling: component of cytosolic AHR–HSP90–AIP/p23 complex controlling AHR stability/cytosolic retention and ligand-dependent nuclear signaling. (cain2010roleofthe pages 4-5, cain2010roleofthe pages 12-13)

Localization:

• Primarily cytoplasmic as part of AHR chaperone complex; association with chaperone networks may extend to mitochondrial-associated chaperones (co-localization with HSPA9 in proteomic validation). (cain2010roleofthe pages 4-5, hernandezramirez2018multichaperonefunctionmodulation pages 1-2)

Disease association:

• Tumor suppressor in pituitary tumor predisposition (FIPA/PitNET), with incomplete penetrance; testing yield highest in childhood-onset GH excess/gigantism and early-onset macroprolactinoma. (trivellin2011evaluationofthe pages 34-37, korbonits2024consensusguidelinefor pages 6-7)

9. Key source list (URLs and publication dates)

• Korbonits et al. “Consensus guideline for the diagnosis and management of pituitary adenomas in childhood and adolescence: Part 1, general recommendations.” Nature Reviews Endocrinology. Published Feb 2024. https://doi.org/10.1038/s41574-023-00948-8 (korbonits2024consensusguidelinefor pages 6-7)

• Boukerrouni et al. “Genetic testing in prolactinomas: a cohort study.” European Journal of Endocrinology. Published Nov 2023. https://doi.org/10.1093/ejendo/lvad148 (boukerrouni2023genetictestingin pages 8-11, boukerrouni2023genetictestingin pages 11-13)

• Trofimiuk-Müldner et al. “AIP gene germline variants in adult Polish patients with apparently sporadic pituitary macroadenomas.” Frontiers in Endocrinology. Published Feb 2023. https://doi.org/10.3389/fendo.2023.1098367 (trofimiukmuldner2023aipgenegermline pages 9-10)

• Alzahrani et al. “Germline Variants in Sporadic Pituitary Adenomas.” Journal of the Endocrine Society. Published Apr 2024. https://doi.org/10.1210/jendso/bvae085 (alzahrani2024germlinevariantsin pages 4-5)

• Balinisteanu et al. “Unlocking the Genetic Secrets of Acromegaly: Exploring the Role of Genetics in a Rare Disorder.” Current Issues in Molecular Biology. Published Aug 2024. https://doi.org/10.3390/cimb46080538 (balinisteanu2024unlockingthegenetic pages 5-6)

• Cain et al. “Role of the aryl hydrocarbon receptor-interacting protein in familial isolated pituitary adenoma.” Expert Review of Endocrinology & Metabolism. Published Sep 2010. https://doi.org/10.1586/eem.10.42 (cain2010roleofthe pages 4-5, cain2010roleofthe pages 2-3)

• Hernández-Ramírez et al. “Multi-chaperone function modulation and association with cytoskeletal proteins are key features of the function of AIP in the pituitary gland.” Oncotarget. Published Jan 2018. https://doi.org/10.18632/oncotarget.24183 (hernandezramirez2018multichaperonefunctionmodulation pages 1-2)

• Cryo-EM figure evidence for complex architecture (human Hsp90–XAP2/AIP–AHR complex; AIP domains and Hsp90 MEEVD docking in TPR): (gruszczyk2022cryoemstructureof media 0a99161a, gruszczyk2022cryoemstructureof media a4609a97)


References

1. (trivellin2011evaluationofthe pages 34-37): G Trivellin. Evaluation of the role of aip, cdkn1b, mir-107 and ahrr in the pathogenesis of sporadic and familial pituitary adenomas. Unknown journal, 2011.

2. (cain2010roleofthe pages 2-3): Joshua W Cain, Dragana Miljic, Vera Popovic, and Márta Korbonits. Role of the aryl hydrocarbon receptor-interacting protein in familial isolated pituitary adenoma. Expert Review of Endocrinology & Metabolism, 5:681-695, Sep 2010. URL: https://doi.org/10.1586/eem.10.42, doi:10.1586/eem.10.42. This article has 19 citations and is from a peer-reviewed journal.

3. (hernandezramirez2018multichaperonefunctionmodulation pages 1-2): Laura C. Hernández-Ramírez, Rhodri M.L. Morgan, Sayka Barry, Fulvio D’Acquisto, Chrisostomos Prodromou, and Márta Korbonits. Multi-chaperone function modulation and association with cytoskeletal proteins are key features of the function of aip in the pituitary gland. Oncotarget, 9:9177-9198, Jan 2018. URL: https://doi.org/10.18632/oncotarget.24183, doi:10.18632/oncotarget.24183. This article has 50 citations.

4. (cain2010roleofthe pages 12-13): Joshua W Cain, Dragana Miljic, Vera Popovic, and Márta Korbonits. Role of the aryl hydrocarbon receptor-interacting protein in familial isolated pituitary adenoma. Expert Review of Endocrinology & Metabolism, 5:681-695, Sep 2010. URL: https://doi.org/10.1586/eem.10.42, doi:10.1586/eem.10.42. This article has 19 citations and is from a peer-reviewed journal.

5. (trivellin2011evaluationofthe pages 41-44): G Trivellin. Evaluation of the role of aip, cdkn1b, mir-107 and ahrr in the pathogenesis of sporadic and familial pituitary adenomas. Unknown journal, 2011.

6. (cain2010roleofthe pages 4-5): Joshua W Cain, Dragana Miljic, Vera Popovic, and Márta Korbonits. Role of the aryl hydrocarbon receptor-interacting protein in familial isolated pituitary adenoma. Expert Review of Endocrinology & Metabolism, 5:681-695, Sep 2010. URL: https://doi.org/10.1586/eem.10.42, doi:10.1586/eem.10.42. This article has 19 citations and is from a peer-reviewed journal.

7. (gruszczyk2022cryoemstructureof media 0a99161a): Jakub Gruszczyk, Loic Grandvuillemin, Josephine Lai-Kee-Him, Matteo Paloni, Christos G. Savva, Pierre Germain, Marina Grimaldi, Abdelhay Boulahtouf, Hok-Sau Kwong, Julien Bous, Aurelie Ancelin, Cherine Bechara, Alessandro Barducci, Patrick Balaguer, and William Bourguet. Cryo-em structure of the agonist-bound hsp90-xap2-ahr cytosolic complex. Nature Communications, Jun 2022. URL: https://doi.org/10.1038/s41467-022-34773-w, doi:10.1038/s41467-022-34773-w. This article has 114 citations and is from a highest quality peer-reviewed journal.

8. (gruszczyk2022cryoemstructureof media a4609a97): Jakub Gruszczyk, Loic Grandvuillemin, Josephine Lai-Kee-Him, Matteo Paloni, Christos G. Savva, Pierre Germain, Marina Grimaldi, Abdelhay Boulahtouf, Hok-Sau Kwong, Julien Bous, Aurelie Ancelin, Cherine Bechara, Alessandro Barducci, Patrick Balaguer, and William Bourguet. Cryo-em structure of the agonist-bound hsp90-xap2-ahr cytosolic complex. Nature Communications, Jun 2022. URL: https://doi.org/10.1038/s41467-022-34773-w, doi:10.1038/s41467-022-34773-w. This article has 114 citations and is from a highest quality peer-reviewed journal.

9. (trofimiukmuldner2023aipgenegermline pages 9-10): Małgorzata Trofimiuk-Müldner, Bartosz Domagała, Grzegorz Sokołowski, Anna Skalniak, and Alicja Hubalewska-Dydejczyk. Aip gene germline variants in adult polish patients with apparently sporadic pituitary macroadenomas. Frontiers in Endocrinology, Feb 2023. URL: https://doi.org/10.3389/fendo.2023.1098367, doi:10.3389/fendo.2023.1098367. This article has 6 citations.

10. (balinisteanu2024unlockingthegenetic pages 5-6): Ioana Balinisteanu, Lavinia Caba, Andreea Florea, Roxana Popescu, Laura Florea, Maria-Christina Ungureanu, Letitia Leustean, Eusebiu Vlad Gorduza, and Cristina Preda. Unlocking the genetic secrets of acromegaly: exploring the role of genetics in a rare disorder. Current Issues in Molecular Biology, 46:9093-9121, Aug 2024. URL: https://doi.org/10.3390/cimb46080538, doi:10.3390/cimb46080538. This article has 6 citations.

11. (boukerrouni2023genetictestingin pages 1-5): Amina Boukerrouni, Thomas Cuny, Thibaut Anjou, Isabelle Raingeard, Amandine Ferrière, Solange Grunenwald, Jean-Christophe Maïza, Emeline Marquant, Nicolas Sahakian, Sarah Fodil-Cherif, Laurence Salle, Patricia Niccoli, Hanitra Randrianaivo, Emmanuel Sonnet, Nicolas Chevalier, Philippe Thuillier, Delphine Vezzosi, Rachel Reynaud, Henry Dufour, Thierry Brue, Antoine Tabarin, Brigitte Delemer, Véronique Kerlan, Frédéric Castinetti, Anne Barlier, and Pauline Romanet. Genetic testing in prolactinomas: a cohort study. European journal of endocrinology, 189:567-574, Nov 2023. URL: https://doi.org/10.1093/ejendo/lvad148, doi:10.1093/ejendo/lvad148. This article has 6 citations and is from a highest quality peer-reviewed journal.

12. (boukerrouni2023genetictestingin pages 8-11): Amina Boukerrouni, Thomas Cuny, Thibaut Anjou, Isabelle Raingeard, Amandine Ferrière, Solange Grunenwald, Jean-Christophe Maïza, Emeline Marquant, Nicolas Sahakian, Sarah Fodil-Cherif, Laurence Salle, Patricia Niccoli, Hanitra Randrianaivo, Emmanuel Sonnet, Nicolas Chevalier, Philippe Thuillier, Delphine Vezzosi, Rachel Reynaud, Henry Dufour, Thierry Brue, Antoine Tabarin, Brigitte Delemer, Véronique Kerlan, Frédéric Castinetti, Anne Barlier, and Pauline Romanet. Genetic testing in prolactinomas: a cohort study. European journal of endocrinology, 189:567-574, Nov 2023. URL: https://doi.org/10.1093/ejendo/lvad148, doi:10.1093/ejendo/lvad148. This article has 6 citations and is from a highest quality peer-reviewed journal.

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