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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:** Q9Y6H3
- **Protein Description:** RecName: Full=Mitochondrial inner membrane protease ATP23 homolog; EC=3.4.24.-; AltName: Full=Ku70-binding protein 3; AltName: Full=XRCC6-binding protein 1;
- **Gene Information:** Name=ATP23 {ECO:0000312|HGNC:HGNC:29452}; Synonyms=KUB3, XRCC6BP1;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the peptidase M76 family. .
- **Key Domains:** Peptidase_M76_ATP23. (IPR019165); Peptidase_M76 (PF09768)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "ATP23" 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 'ATP23' 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 **ATP23** (gene ID: ATP23, UniProt: Q9Y6H3) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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:** Q9Y6H3
- **Protein Description:** RecName: Full=Mitochondrial inner membrane protease ATP23 homolog; EC=3.4.24.-; AltName: Full=Ku70-binding protein 3; AltName: Full=XRCC6-binding protein 1;
- **Gene Information:** Name=ATP23 {ECO:0000312|HGNC:HGNC:29452}; Synonyms=KUB3, XRCC6BP1;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the peptidase M76 family. .
- **Key Domains:** Peptidase_M76_ATP23. (IPR019165); Peptidase_M76 (PF09768)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "ATP23" 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 'ATP23' 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 **ATP23** (gene ID: ATP23, UniProt: Q9Y6H3) 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.

# Research report: Human **ATP23** (UniProt **Q9Y6H3**; gene **ATP23**, synonyms **KUB3**, **XRCC6BP1**) — functional annotation with evidence

## 1) Target verification and nomenclature/identity risks

The UniProt target provided (Q9Y6H3) is described as a “mitochondrial inner membrane protease ATP23 homolog” and is annotated as a member of the peptidase **M76** family. In the primary literature retrieved here, the strongest mechanistic characterization of “Atp23/ATP23” is from *Saccharomyces cerevisiae*, where **ATP23 (YNR020c)** encodes an M76 metalloprotease acting at the mitochondrial inner membrane with intermembrane-space (IMS) exposure and a role in ATP synthase subunit 6 (Atp6) processing and assembly. (zeng2007themetalloproteaseencoded pages 1-2, zeng2007themetalloproteaseencoded pages 8-9, osman2007prohibitinsinteractgenetically pages 2-3)

However, there is **naming ambiguity**: a human glioblastoma study uses the name **KUB3** and explicitly states “KUB3 also termed **XRCC6BP1** (X-ray repair cross-complementation group 6 binding protein 1)” and discusses binding to **Ku70** (XRCC6) and effects on DNA double-strand break (DSB) repair. That paper excerpt does **not** mention ATP23, UniProt Q9Y6H3, ENSG00000166896, mitochondria, or M76 protease features. Therefore, while KUB3/XRCC6BP1 is a documented alias pair in human cancer/DNA-repair literature, **the retrieved evidence does not allow a definitive statement that the Ku70-binding/nuclear DSB-repair role refers to the same protein as mitochondrial ATP23 (Q9Y6H3)**. Any functional annotation must explicitly separate (i) robust mitochondrial Atp23 ortholog biology from (ii) KUB3/XRCC6BP1 nuclear DNA-repair reports until mapping is confirmed by a source that links these identifiers directly. (fischer2013gliomaamplifiedsequencekub3 pages 1-2, fischer2013gliomaamplifiedsequencekub3 pages 2-4)

## 2) Key concepts and definitions (current understanding)

### 2.1 What is “ATP23/Atp23” as a functional class?

**Atp23 is an M76-family metalloprotease and ATP synthase biogenesis factor.** In yeast, ATP23 encodes a metalloprotease with a conserved **HEXXH** motif typical of metalloprotease active sites and is conserved across eukaryotes (“from yeast to humans” in the yeast studies’ comparative statements). (zeng2007themetalloproteaseencoded pages 4-6)

### 2.2 Dual function concept: protease activity vs assembly/chaperone activity

A central concept emerging from independent yeast studies is that Atp23 has **two separable functions**:

1) **Proteolytic processing (maturation)** of ATP synthase subunit 6 (**Atp6**) by removing an N-terminal extension after membrane insertion. (zeng2007themetalloproteaseencoded pages 1-2, zeng2007themetalloproteaseencoded pages 8-9)

2) A **protease-independent assembly/chaperone-like role** that promotes incorporation of Atp6 into the F1Fo-ATP synthase, particularly steps involving association with the **Atp9 ring** (FO channel formation). Protease-dead mutants can still allow assembly of a functional ATP synthase and restore respiratory growth, implying the assembly role is not simply a consequence of cleavage. (osman2007prohibitinsinteractgenetically pages 6-7, zeng2007themetalloproteaseencoded pages 8-9)

This dual-function model is important for human annotation because it predicts that even if a human ortholog has reduced/altered substrate processing requirements (e.g., differences in ATP6 N-termini across species), an **assembly factor function may be retained**.

## 3) Biological role, pathways, and mechanistic evidence (with emphasis on what is experimentally supported)

### 3.1 Subcellular localization and topology

In yeast, Atp23 is localized to the mitochondrial **intermembrane space (IMS)** and is associated with the inner membrane such that the **C-terminus is exposed to the IMS**, supported by protease-protection experiments and biochemical extraction behavior. (osman2007prohibitinsinteractgenetically pages 2-3)

This IMS-facing topology is consistent with how Atp23 can access and cleave an N-terminal segment of Atp6 that becomes IMS-accessible after membrane insertion. (osman2007prohibitinsinteractgenetically pages 7-8, zeng2007themetalloproteaseencoded pages 8-9)

**Implication for human ATP23 (Q9Y6H3):** the most defensible model—based on orthology—is that human ATP23 is an inner-membrane–associated M76 metalloprotease with an IMS-exposed catalytic region, participating in complex V (ATP synthase) biogenesis/quality control. This is inference, not direct human experimental proof in the retrieved corpus.

### 3.2 Enzymatic activity, reaction, and substrate specificity

**Reaction type (ortholog evidence):** Atp23 is a **metalloprotease** that cleaves a peptide bond to remove an N-terminal extension from Atp6 (ATP synthase subunit 6) in yeast. (zeng2007themetalloproteaseencoded pages 1-2, zeng2007themetalloproteaseencoded pages 8-9)

**Substrate specificity:** The directly supported substrate is the **Atp6 precursor N-terminus**, where ~10 residues are removed. The mechanistic requirement for the metal-binding motif is supported by mutagenesis (e.g., mutation of the key glutamate within the HEXXH region abolishing processing). (zeng2007themetalloproteaseencoded pages 8-9, zeng2007themetalloproteaseencoded pages 4-6)

**Protease-independent activity:** Multiple protease-inactive mutants retain the ability to support assembly of a functional F1Fo ATP synthase, underscoring that “substrate specificity” for the processing reaction does not fully define Atp23’s physiological importance. (osman2007prohibitinsinteractgenetically pages 6-7)

**Human caveat:** The Osman study notes that the human Atp6 lacks the yeast N-terminal extension that is cleaved in yeast, implying that if human ATP23 is enzymatically active as a protease, its native substrate(s) could differ or the cleavage event could be absent/modified in mammals. This again supports prioritizing the **assembly/biogenesis** function for human annotation unless a human substrate is experimentally identified. (osman2007prohibitinsinteractgenetically pages 6-7)

### 3.3 Role in ATP synthase (Complex V) biogenesis and mitochondrial pathways

**ATP synthase assembly step:** Yeast studies support a role for Atp23 in mediating Atp6 assembly with the Atp9 oligomer/ring during FO channel formation. (osman2007prohibitinsinteractgenetically pages 7-8, zeng2007themetalloproteaseencoded pages 8-9)

**Genetic interaction/mitochondrial membrane proteostasis context:** Atp23 genetically interacts with prohibitins (PHB1/PHB2). Synthetic sickness/lethality indicates that Atp23 function intersects with inner membrane scaffolding/proteostasis systems important for respiratory function and ATP synthase biogenesis. (osman2007prohibitinsinteractgenetically pages 2-2)

**Human context (assembly literature):** A PNAS paper on human ATP synthase membrane-domain assembly cites yeast ATP23/Atp23 as an ATP6/ATP8-related assembly factor (contextualizing how ATP6 is handled in yeast). In the excerpt available, it does not provide direct experiments on human ATP23 itself, but it confirms ATP23’s canonical placement among ATP synthase assembly factors in the field’s conceptual framework. (he2018assemblyofthe pages 6-6)

## 4) Recent developments and latest research (prioritize 2023–2024)

### 4.1 2024: mitochondrial proteolysis as a modifier of protein-toxicity phenotypes (Atp23 included in screen)

A 2024 NPJ Parkinson’s Disease study tested whether enhancing mitochondrial proteolysis alleviates α-synuclein toxicity. In a yeast screen using moderate copy-number increases of mitochondrial proteases, **Atp23** was among the proteases showing the **highest inhibitory effects on α-synuclein accumulation in mitochondria**, and protease copy-number increases (including Atp23) helped **rescue growth defects** and restore mitochondrial membrane potential in α-syn-expressing cells. This result expands the functional context of Atp23-family enzymes beyond ATP synthase assembly to broader **mitochondrial proteostasis capacity**, though the evidence for Atp23 specifically is in yeast. (zhang2024enhancingmitochondrialproteolysis pages 4-5)

### 4.2 Human genetics aggregation (hypothesis-generating)

OpenTargets aggregates human genetic association evidence for ATP23 (ENSG00000166896) across multiple phenotypes/diseases. In the retrieved OpenTargets output, ATP23 shows association entries (each with **5 evidence items**) and moderate overall scores (≈0.20–0.30) for traits including **Sjögren syndrome**, **gout**, and **myasthenia gravis**, among others. These are not mechanistic demonstrations of ATP23 function, but they are relevant for prioritizing ATP23 in downstream functional follow-up or variant interpretation workflows. (OpenTargets Search: -ATP23)

## 5) Current applications and real-world implementations

### 5.1 Translational implication: boosting mitochondrial proteostasis

The 2024 α-synuclein study supports a broader therapeutic concept: **increasing activity or abundance of specific mitochondrial proteases can reduce mitochondrial α-synuclein accumulation and improve cellular fitness**. While the most emphasized proteases in that paper include NLN and PITRM1 in mammalian contexts (not ATP23), Atp23’s inclusion among top-performing yeast proteases suggests that proteases involved in inner-membrane proteostasis/assembly may contribute to protecting mitochondria from proteotoxic stress—an angle potentially relevant to neurodegeneration research. (zhang2024enhancingmitochondrialproteolysis pages 4-5)

### 5.2 Cancer biology context for the KUB3/XRCC6BP1 alias

In glioblastoma models, KUB3 (also termed XRCC6BP1) amplification/expression correlates with improved DSB repair after irradiation; knockdown reduces repair efficiency, and the authors discuss Ku70/DNA-PK pathway context. These findings have potential implications for radiation response in tumors. Importantly, this literature does not establish mitochondrial localization or peptidase activity and should not be used alone to annotate mitochondrial ATP23/Q9Y6H3 function without identifier reconciliation. (fischer2013gliomaamplifiedsequencekub3 pages 1-2)

## 6) Expert opinions/authoritative synthesis

The Atp23 role as an IMS protease required for Atp6 processing during ATP synthase biogenesis is reiterated in a mitochondrial biogenesis/redox review, reflecting a consensus placement of Atp23 among mitochondrial IMS-associated factors supporting complex V maturation. (osman2007prohibitinsinteractgenetically pages 2-3)

## 7) Statistics and data highlights (from retrieved sources)

- **Atp6 processing event size:** yeast Atp6 is synthesized with an ~10-residue N-terminal extension that is removed in an Atp23-dependent manner. (osman2007prohibitinsinteractgenetically pages 7-8)
- **Genetic evidence strength:** protease-dead Atp23 mutants (multiple active-site substitutions) can still support assembly of functional ATP synthase, demonstrating functional separability and arguing that “processing” is not the only essential role. (osman2007prohibitinsinteractgenetically pages 6-7)
- **OpenTargets association metrics:** ATP23 has aggregated association scores ~0.20–0.30 for several traits, with **5 evidence items** per listed disease in the retrieved output. (OpenTargets Search: -ATP23)

## 8) Consolidated evidence table

| Evidence item (function/localization) | Species/context | Key finding | Experimental basis (brief) | Citation (first author year) | Publication date (month/year) | URL |
|---|---|---|---|---|---|---|
| Dual function in Atp6 processing and ATP synthase assembly | *Saccharomyces cerevisiae* Atp23; used as orthologous functional evidence for human ATP23/Q9Y6H3 | ATP23 encodes a conserved metalloprotease required to remove the ~10-residue N-terminal presequence from Atp6/subunit 6; protease-dead mutant still supports assembly/respiratory growth, implying a second assembly/chaperone-like role. Atp23 is associated with the inner membrane and its C-terminus faces the IMS. (zeng2007themetalloproteaseencoded pages 1-2, zeng2007themetalloproteaseencoded pages 8-9, zeng2007themetalloproteaseencoded pages 4-6) | Yeast genetics, catalytic-site mutagenesis (E168Q), mitochondrial translation/assembly assays, respiratory growth rescue, biochemical topology/processing analysis | Zeng 2007 | Feb 2007 | https://doi.org/10.1091/mbc.e06-09-0801 |
| IMS localization and separable protease vs chaperone functions | *S. cerevisiae* Atp23; strongest mechanistic evidence for ATP23-family role | Atp23 localizes to the mitochondrial intermembrane space; protease-protection and alkaline extraction place the HA-tagged C-terminus in the IMS. Protease activity is required for Atp6 maturation, but protease-inactive mutants still allow assembly of functional F1FO-ATP synthase, separating Atp23's processing and chaperone/assembly roles. Genetic interaction with prohibitins links Atp23 to inner-membrane proteostasis/ATP synthase biogenesis. (osman2007prohibitinsinteractgenetically pages 2-2, osman2007prohibitinsinteractgenetically pages 7-8, osman2007prohibitinsinteractgenetically pages 6-7, osman2007prohibitinsinteractgenetically pages 2-3) | Protease protection, alkaline extraction, BN-PAGE, co-immunoprecipitation with Atp6, site-directed mutagenesis, yeast genetic interaction analysis | Osman 2007 | Feb 2007 | https://doi.org/10.1091/mbc.e06-09-0839 |
| Human ATP synthase assembly context | Human mitochondria; ATP23 discussed as yeast assembly factor context rather than directly functionally tested in human cells in the cited excerpt | Human ATP synthase membrane-domain assembly paper cites yeast ATP23/Atp23 as an assembly factor associated with ATP6/ATP8 biogenesis. The excerpt supports relevance of ATP23 to ATP synthase assembly models, but does not provide direct experimental characterization of human ATP23 in that paper excerpt. (he2018assemblyofthe pages 6-6) | Human ATP synthase assembly study with citation-based contextual comparison to yeast ATP23 literature | He 2018 | Feb 2018 | https://doi.org/10.1073/pnas.1722086115 |
| Review statement: IMS protease role in ATP synthase biogenesis | Yeast/human mitochondrial biogenesis review | Review identifies Atp23 as an IMS protease required for processing Atp6 during ATP synthase biogenesis, reinforcing the submitochondrial localization and functional model derived from yeast primary studies. (osman2007prohibitinsinteractgenetically pages 2-3) | Review synthesis of prior mitochondrial biogenesis/protease literature | Geldon 2021 | Sep 2021 | https://doi.org/10.3389/fcell.2021.720656 |
| KUB3/XRCC6BP1 naming and DNA double-strand break repair claim | Human glioblastoma; same symbol/synonym space relevant to ATP23 alias ambiguity | KUB3 is explicitly described as Ku70-binding protein 3 and also termed XRCC6BP1; elevated KUB3 amplification/expression correlated with more efficient DNA double-strand break repair after ionizing radiation, and prior Ku70 binding was noted/confirmed. The paper excerpt does not mention ATP23, ENSG00000166896, or mitochondrial localization, so it should be treated cautiously as alias-linked but functionally distinct literature relative to mitochondrial ATP23 annotation. (fischer2013gliomaamplifiedsequencekub3 pages 2-4, fischer2013gliomaamplifiedsequencekub3 pages 1-2) | Glioma cell expression/amplification analyses, siRNA knockdown, ectopic expression, DSB-repair assays after irradiation, co-immunoprecipitation with Ku70 | Fischer 2013 | May 2013 | https://doi.org/10.3892/ijo.2013.1937 |
| Atp23 in mitochondrial proteolysis screen for α-synuclein toxicity | Yeast mitochondrial protease overexpression screen | Atp23 was one of the yeast mitochondrial proteases whose increased copy number reduced mitochondrial α-synuclein accumulation; Atp23 grouped with Cym1, Prd1, and Imp2 among the strongest inhibitors of α-syn accumulation and helped rescue growth and membrane-potential defects in the yeast model. This is indirect, non-human evidence linking Atp23-family activity to mitochondrial proteostasis. (zhang2024enhancingmitochondrialproteolysis pages 7-9, zhang2024enhancingmitochondrialproteolysis pages 4-5) | Yeast MoBY plasmid overexpression screen, α-syn spGFP quantification, immunoblotting, growth rescue, membrane-potential assays | Zhang 2024 | Jun 2024 | https://doi.org/10.1038/s41531-024-00733-y |


*Table: This table compiles the most relevant evidence for annotating human ATP23/Q9Y6H3, separating direct human alias literature from stronger mechanistic ortholog evidence in yeast. It is useful for clarifying localization, catalytic/assembly roles, and naming ambiguity involving KUB3/XRCC6BP1.*

## 9) Summary functional annotation (best-supported)

**Most defensible functional model for human ATP23/Q9Y6H3 (based on ortholog evidence):** a conserved **M76 metalloprotease** associated with the **mitochondrial inner membrane** with IMS exposure, functioning in **mitochondrial ATP synthase (complex V) biogenesis**, including (at least in yeast) proteolytic processing of ATP6/Atp6 and a separable **assembly/chaperone-like role** promoting incorporation of ATP6/Atp6 into the FO sector. (zeng2007themetalloproteaseencoded pages 8-9, osman2007prohibitinsinteractgenetically pages 2-3)

**What remains unresolved in the retrieved corpus:** direct experimental confirmation of (i) human ATP23 submitochondrial topology, (ii) native human substrate(s) and cleavage events, and (iii) whether the nuclear DNA-repair literature on KUB3/XRCC6BP1/Ku70 binding is indeed about the same gene product as UniProt Q9Y6H3. (fischer2013gliomaamplifiedsequencekub3 pages 1-2, osman2007prohibitinsinteractgenetically pages 6-7)


References

1. (zeng2007themetalloproteaseencoded pages 1-2): Xiaomei Zeng, Walter Neupert, and Alexander Tzagoloff. The metalloprotease encoded by<i>atp23</i>has a dual function in processing and assembly of subunit 6 of mitochondrial atpase. Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0801, doi:10.1091/mbc.e06-09-0801. This article has 151 citations and is from a domain leading peer-reviewed journal.

2. (zeng2007themetalloproteaseencoded pages 8-9): Xiaomei Zeng, Walter Neupert, and Alexander Tzagoloff. The metalloprotease encoded by<i>atp23</i>has a dual function in processing and assembly of subunit 6 of mitochondrial atpase. Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0801, doi:10.1091/mbc.e06-09-0801. This article has 151 citations and is from a domain leading peer-reviewed journal.

3. (osman2007prohibitinsinteractgenetically pages 2-3): Christof Osman, Claudia Wilmes, Takashi Tatsuta, and Thomas Langer. Prohibitins interact genetically with atp23, a novel processing peptidase and chaperone for the f<sub>1</sub>f<sub>o</sub>-atp synthase. Molecular Biology of the Cell, 18:627-635, Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0839, doi:10.1091/mbc.e06-09-0839. This article has 179 citations and is from a domain leading peer-reviewed journal.

4. (fischer2013gliomaamplifiedsequencekub3 pages 1-2): ULRIKE FISCHER, STEFANIE RHEINHEIMER, ANDREA KREMPLER, MARKUS LÖBRICH, and ECKART MEESE. Glioma-amplified sequence kub3 influences double-strand break repair after ionizing radiation. International Journal of Oncology, 43:50-56, May 2013. URL: https://doi.org/10.3892/ijo.2013.1937, doi:10.3892/ijo.2013.1937. This article has 15 citations and is from a peer-reviewed journal.

5. (fischer2013gliomaamplifiedsequencekub3 pages 2-4): ULRIKE FISCHER, STEFANIE RHEINHEIMER, ANDREA KREMPLER, MARKUS LÖBRICH, and ECKART MEESE. Glioma-amplified sequence kub3 influences double-strand break repair after ionizing radiation. International Journal of Oncology, 43:50-56, May 2013. URL: https://doi.org/10.3892/ijo.2013.1937, doi:10.3892/ijo.2013.1937. This article has 15 citations and is from a peer-reviewed journal.

6. (zeng2007themetalloproteaseencoded pages 4-6): Xiaomei Zeng, Walter Neupert, and Alexander Tzagoloff. The metalloprotease encoded by<i>atp23</i>has a dual function in processing and assembly of subunit 6 of mitochondrial atpase. Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0801, doi:10.1091/mbc.e06-09-0801. This article has 151 citations and is from a domain leading peer-reviewed journal.

7. (osman2007prohibitinsinteractgenetically pages 6-7): Christof Osman, Claudia Wilmes, Takashi Tatsuta, and Thomas Langer. Prohibitins interact genetically with atp23, a novel processing peptidase and chaperone for the f<sub>1</sub>f<sub>o</sub>-atp synthase. Molecular Biology of the Cell, 18:627-635, Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0839, doi:10.1091/mbc.e06-09-0839. This article has 179 citations and is from a domain leading peer-reviewed journal.

8. (osman2007prohibitinsinteractgenetically pages 7-8): Christof Osman, Claudia Wilmes, Takashi Tatsuta, and Thomas Langer. Prohibitins interact genetically with atp23, a novel processing peptidase and chaperone for the f<sub>1</sub>f<sub>o</sub>-atp synthase. Molecular Biology of the Cell, 18:627-635, Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0839, doi:10.1091/mbc.e06-09-0839. This article has 179 citations and is from a domain leading peer-reviewed journal.

9. (osman2007prohibitinsinteractgenetically pages 2-2): Christof Osman, Claudia Wilmes, Takashi Tatsuta, and Thomas Langer. Prohibitins interact genetically with atp23, a novel processing peptidase and chaperone for the f<sub>1</sub>f<sub>o</sub>-atp synthase. Molecular Biology of the Cell, 18:627-635, Feb 2007. URL: https://doi.org/10.1091/mbc.e06-09-0839, doi:10.1091/mbc.e06-09-0839. This article has 179 citations and is from a domain leading peer-reviewed journal.

10. (he2018assemblyofthe pages 6-6): Jiuya He, Holly C. Ford, Joe Carroll, Corsten Douglas, Evvia Gonzales, Shujing Ding, Ian M. Fearnley, and John E. Walker. Assembly of the membrane domain of atp synthase in human mitochondria. Proceedings of the National Academy of Sciences, 115:2988-2993, Feb 2018. URL: https://doi.org/10.1073/pnas.1722086115, doi:10.1073/pnas.1722086115. This article has 269 citations and is from a highest quality peer-reviewed journal.

11. (zhang2024enhancingmitochondrialproteolysis pages 4-5): Xi Zhang, Linhao Ruan, Hu Wang, Jin Zhu, Taibo Li, Gordon Sun, Yi Dong, Yuhao Wang, Gil Berreby, Ashley Shay, Rong Chen, Sreekumar Ramachandran, Valina L. Dawson, Ted M. Dawson, and Rong Li. Enhancing mitochondrial proteolysis alleviates alpha-synuclein-mediated cellular toxicity. NPJ Parkinson's Disease, Jun 2024. URL: https://doi.org/10.1038/s41531-024-00733-y, doi:10.1038/s41531-024-00733-y. This article has 17 citations and is from a domain leading peer-reviewed journal.

12. (OpenTargets Search: -ATP23): Open Targets Query (-ATP23, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

13. (zhang2024enhancingmitochondrialproteolysis pages 7-9): Xi Zhang, Linhao Ruan, Hu Wang, Jin Zhu, Taibo Li, Gordon Sun, Yi Dong, Yuhao Wang, Gil Berreby, Ashley Shay, Rong Chen, Sreekumar Ramachandran, Valina L. Dawson, Ted M. Dawson, and Rong Li. Enhancing mitochondrial proteolysis alleviates alpha-synuclein-mediated cellular toxicity. NPJ Parkinson's Disease, Jun 2024. URL: https://doi.org/10.1038/s41531-024-00733-y, doi:10.1038/s41531-024-00733-y. This article has 17 citations and is from a domain leading peer-reviewed journal.

## Artifacts

- [Edison artifact artifact-00](ATP23-deep-research-falcon_artifacts/artifact-00.md)

## Citations

1. zeng2007themetalloproteaseencoded pages 4-6
2. osman2007prohibitinsinteractgenetically pages 2-3
3. osman2007prohibitinsinteractgenetically pages 6-7
4. osman2007prohibitinsinteractgenetically pages 2-2
5. he2018assemblyofthe pages 6-6
6. zhang2024enhancingmitochondrialproteolysis pages 4-5
7. osman2007prohibitinsinteractgenetically pages 7-8
8. zeng2007themetalloproteaseencoded pages 1-2
9. zeng2007themetalloproteaseencoded pages 8-9
10. zhang2024enhancingmitochondrialproteolysis pages 7-9
11. https://doi.org/10.1091/mbc.e06-09-0801
12. https://doi.org/10.1091/mbc.e06-09-0839
13. https://doi.org/10.1073/pnas.1722086115
14. https://doi.org/10.3389/fcell.2021.720656
15. https://doi.org/10.3892/ijo.2013.1937
16. https://doi.org/10.1038/s41531-024-00733-y
17. https://doi.org/10.1091/mbc.e06-09-0801,
18. https://doi.org/10.1091/mbc.e06-09-0839,
19. https://doi.org/10.3892/ijo.2013.1937,
20. https://doi.org/10.1073/pnas.1722086115,
21. https://doi.org/10.1038/s41531-024-00733-y,