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gene_info: Name=ATP11; OrderedLocusNames=YNL315C; ORFNames=N0357;
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
protein_family: Belongs to the ATP11 family. .
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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: P32453
• Protein Description: RecName: Full=Protein ATP11, mitochondrial; Flags: Precursor;
• Gene Information: Name=ATP11; OrderedLocusNames=YNL315C; ORFNames=N0357;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the ATP11 family. .
• Key Domains: ATP11. (IPR010591); ATP11 (PF06644)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ATP11" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
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 'ATP11' 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 ATP11 (gene ID: ATP11, UniProt: P32453) in yeast.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P32453
• Protein Description: RecName: Full=Protein ATP11, mitochondrial; Flags: Precursor;
• Gene Information: Name=ATP11; OrderedLocusNames=YNL315C; ORFNames=N0357;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the ATP11 family. .
• Key Domains: ATP11. (IPR010591); ATP11 (PF06644)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ATP11" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
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 'ATP11' 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 ATP11 (gene ID: ATP11, UniProt: P32453) in yeast.

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: ATP11 (YNL315C; UniProt P32453) in Saccharomyces cerevisiae

Executive summary

ATP11 (YNL315C; UniProt P32453) encodes Atp11p, a mitochondrial-matrix, ATP-synthase–specific assembly chaperone that binds the F1 β subunit (Atp2) to prevent its nonproductive self-association and to promote formation of the F1 catalytic head (α3β3 hexamer) of mitochondrial F1FO-ATP synthase (Complex V). Atp11p is not a stoichiometric subunit of the mature enzyme but is required for efficient respiratory growth and correct mitochondrial ultrastructure; loss of ATP11 leads to α/β inclusion bodies in the matrix and impaired oxidative phosphorylation. Newer work (2023) adds mitochondrial Hsp70 as a cooperating factor with Atp11/Atp12 in F1 assembly and quality control. (franco2020modularassemblyof pages 7-10, hinton2003apurifiedsubfragment pages 1-2, lefebvrelegendre2005failuretoassemble pages 1-2, ludlam2009chaperonesoff1atpase pages 1-2, song2023themitochondrialhsp70 pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 What “ATP11” means in yeast (identity verification)

In S. cerevisiae, ATP11 (YNL315C) encodes Atp11p, a dedicated chaperone/assembly factor required for biogenesis of the F1 sector of mitochondrial ATP synthase. Its function is specific to ATP synthase assembly rather than broad protein import/folding, and it acts on unassembled F1 subunits in the matrix. (potocka2007assemblyfactorsin pages 17-21, franco2020modularassemblyof pages 7-10)

1.2 ATP synthase (Complex V) biogenesis and where ATP11 fits

Mitochondrial F1FO-ATP synthase is built from modular subassemblies. The F1 module (soluble catalytic head in the matrix) contains an α3β3 hexamer with the catalytic and noncatalytic nucleotide-binding interfaces. Dedicated assembly chaperones Atp11 and Atp12 bind newly imported F1 subunits to prevent aggregation and ensure productive oligomerization before integration with the stalk and FO membrane sector. (franco2020modularassemblyof pages 7-10, song2018assemblingthemitochondrial pages 1-2)

1.3 Assembly chaperone vs. enzyme: “substrate specificity” for ATP11

Atp11p is not an enzyme with a chemical substrate; its “substrate specificity” is client-protein specificity. The key client is the F1 β subunit, which Atp11p binds transiently during assembly. This binding prevents β from forming nonproductive complexes and promotes correct αβ interactions leading to the (αβ)3 hexamer. (hinton2003apurifiedsubfragment pages 1-2, ludlam2009chaperonesoff1atpase pages 1-2)

2) Molecular function, mechanism, and pathway placement (evidence-based)

2.1 Molecular function: a β-subunit assembly chaperone

Multiple experimental approaches support a direct Atp11p–β interaction: affinity tag pull-down and yeast two-hybrid assays showed Atp11p binds free/unassembled F1 β, and mechanistic interpretation is that Atp11p binding shields aggregation-prone surfaces to prevent β–β self-association and to facilitate productive formation of the (αβ)3 hexamer. (hinton2003apurifiedsubfragment pages 1-2, potocka2007assemblyfactorsin pages 17-21)

A structured chaperone-active truncation (removal of 67 N-terminal residues) retains chaperone activity in vitro (e.g., suppressing aggregation of reduced insulin B chain) and retains interaction with the natural F1 β client, indicating that a large portion of Atp11p’s functional chaperone surface resides outside the N-terminus. (hinton2003apurifiedsubfragment pages 1-2)

2.2 Binding interface and mechanistic models for chaperone release

Review synthesis and interaction mapping indicate Atp11p and Atp12p bind ~200-residue regions within nucleotide-binding domains of β and α, respectively, consistent with a model in which these assembly factors prevent premature α–β interface formation until appropriate assembly progression. (potocka2007assemblyfactorsin pages 17-21)

Earlier mechanistic models posited that the chaperones might resemble α/β; however, structural studies argue Atp11p/Atp12p do not mimic α or β. Instead, assembly progression involves release of the chaperones triggered by association of the γ subunit (central stalk), enabling maturation of the F1 hexamer. (ludlam2009chaperonesoff1atpase pages 1-2)

2.3 Pathway placement relative to general mitochondrial folding systems (Hsp60/Hsp70)

Atp11p is described as acting downstream of general chaperones (e.g., Hsp60/Hsp70) because atp11 mutants accumulate near-mature α and β subunits (processed/imported) but fail to assemble them, leading to aggregation rather than precursor accumulation—contrasting with general folding/import defects. (potocka2007assemblyfactorsin pages 17-21, franco2020modularassemblyof pages 7-10)

3) Subcellular localization and where the function occurs

Atp11p functions in the mitochondrial matrix, where the F1 catalytic head is assembled and where unassembled α and β subunits can otherwise aggregate. Mitochondrial targeting is supported by the use of leader peptides in constructs and by the matrix-localized phenotypes (matrix inclusion bodies). (hinton2003apurifiedsubfragment pages 1-2, ludlam2009chaperonesoff1atpase pages 3-4, lefebvrelegendre2005failuretoassemble pages 1-2)

4) Phenotypes, statistics, and quantitative data from experimental studies

4.1 Respiratory growth phenotypes

Loss of ATP11 impairs oxidative phosphorylation capacity and growth on nonfermentable carbon sources; in comparative phenotyping, atp11Δ can display a “leaky” respiratory phenotype, whereas atp12Δ can be fully defective on ethanol/glycerol (EG) medium under tested conditions. (ludlam2009chaperonesoff1atpase pages 3-4)

4.2 Inclusion bodies and mitochondrial ultrastructure (quantitative EM)

A key experimental signature of ATP11 loss is formation of electron-dense mitochondrial inclusion bodies enriched in F1 α/β proteins. In quantitative ultrastructural analysis, Δatp11 displayed inclusion bodies in 44.0% of cell sections and 23.5% of mitochondrial profiles, consistent with a strong block in α3β3 subcomplex assembly. (lefebvrelegendre2005failuretoassemble pages 1-2, lefebvrelegendre2005failuretoassemble media b3ecdee8)

These inclusion bodies are supported by EM and immunolabeling evidence and correlate with mitochondrial structural defects (including cristae abnormalities) when F1 assembly fails. (lefebvrelegendre2005failuretoassemble pages 1-2, lefebvrelegendre2005failuretoassemble media 33a6c4d5, lefebvrelegendre2005failuretoassemble media 5e421669)

5) Recent developments and latest research (prioritizing 2023–2024)

5.1 2023: mtHsp70 cooperates with Atp11/Atp12 and adds quality control

A 2023 Nature Communications study identified a dual role for mitochondrial Hsp70 (mtHsp70) in ATP synthase biogenesis: it (i) cooperates with Atp11 and Atp12 to form the F1 domain, and (ii) transfers Atp5/OSCP into the assembly line to connect the catalytic head to the peripheral stalk. Importantly, mtHsp70 inactivation permits incorporation of assembly-defective Atp5 variants into mature complexes, implying a quality-control checkpoint during ATP synthase assembly. (song2023themitochondrialhsp70 pages 1-2)

This reframes ATP11 action as part of a broader chaperone network: a specialized, client-specific assembly chaperone (Atp11) works alongside a general mitochondrial chaperone (mtHsp70) to coordinate formation and linkage of the F1 head. (song2023themitochondrialhsp70 pages 1-2)

5.2 2024: cross-species/clinical synthesis of ATP11 homolog ATPAF1

A 2024 systematic review of isolated ATP synthase defects explicitly identifies ATPAF1 as the human homolog of yeast ATP11, describing it as conserved and required for α3β3 hexamer formation. In the compiled variant landscape for isolated ATP synthase deficiency (total variants n = 63), ~60% (38/63) are nuclear-encoded; ATPAF1 is listed with 0 reported pathogenic variants in that review’s assembly-factor table, while other assembly factors (e.g., TMEM70) account for many cases. (tauchmannova2024variabilityofclinical pages 3-5)

While this is not a yeast functional discovery per se, it underscores ATP11’s mechanistic importance and conservation, and it motivates yeast ATP11 studies as models for fundamental assembly biology relevant to mitochondrial disease mechanisms. (tauchmannova2024variabilityofclinical pages 3-5, tauchmannova2024variabilityofclinical pages 1-3)

6) Current applications and real-world implementations

6.1 Yeast ATP11 as a mechanistic model system

ATP11 is widely used as a genetic and biochemical handle to:
- induce specific blocks in F1 assembly (yielding clean assembly intermediates/inclusion bodies),
- study the coupling of chaperone systems to respiratory complex biogenesis,
- and test cross-species complementation or structure–function relationships of ATP11-family proteins.

For example, structural/functional work showed that C. glabrata Atp11p can complement S. cerevisiae atp11Δ respiratory defects, supporting conserved chaperone function and enabling structure-informed mutational analysis. (ludlam2009chaperonesoff1atpase pages 3-4, ludlam2009chaperonesoff1atpase pages 4-5)

6.2 Structural biology of assembly factors

Atp11-family proteins have been purified and structurally characterized to inform mechanistic models of client binding and chaperone release during F1 assembly. Structural mapping also highlighted specific residues whose mutation inactivates Atp11p function, supporting a surface-mediated chaperone mechanism rather than catalytic chemistry. (ludlam2009chaperonesoff1atpase pages 4-5)

7) Expert opinions and analysis (authoritative syntheses)

7.1 Consensus view

Across reviews and primary literature, the consensus is that ATP11 encodes a specialized assembly chaperone for mitochondrial ATP synthase that:
- binds β (Atp2),
- prevents α/β aggregation,
- promotes (αβ)3 hexamer formation,
- and is released during later assembly steps (γ involvement),
while general chaperones (Hsp60/Hsp70) support upstream folding/import. (franco2020modularassemblyof pages 7-10, ludlam2009chaperonesoff1atpase pages 1-2, song2018assemblingthemitochondrial pages 1-2)

7.2 Conservation across genomes

Comparative-genomics analyses support conservation of Atp11p/Atp12p function across eukaryotes capable of oxidative phosphorylation, consistent with a conserved need to protect α/β subunits during assembly. (pickova2005assemblyfactorsof pages 1-2)

Evidence map (table)

Table: This table summarizes the main experimentally supported findings for Saccharomyces cerevisiae ATP11/YNL315C, including function, localization, binding specificity, mutant phenotypes, mechanistic models, and recent 2023 developments. It is useful as a compact evidence map linking each major claim to the assay type and primary literature source.

URLs and publication dates (key sources used)

• Hinton A, Zuiderweg ERP, Ackerman SH. 2003-09. J Biol Chem. “A Purified Subfragment of Yeast Atp11p Retains Full Molecular Chaperone Activity.” https://doi.org/10.1074/jbc.M305353200 (hinton2003apurifiedsubfragment pages 1-2)
• Lefebvre-Legendre L et al. 2005-05. J Biol Chem. “Failure to Assemble the α3β3 Subcomplex…” https://doi.org/10.1074/jbc.M410789200 (lefebvrelegendre2005failuretoassemble pages 1-2)
• Ludlam A et al. 2009-06. J Biol Chem. “Chaperones of F1-ATPase.” https://doi.org/10.1074/jbc.M109.002568 (ludlam2009chaperonesoff1atpase pages 1-2)
• Song J, Pfanner N, Becker T. 2018-03. PNAS. “Assembling the mitochondrial ATP synthase.” https://doi.org/10.1073/pnas.1801697115 (song2018assemblingthemitochondrial pages 1-2)
• Franco LVR, Su CH, Tzagoloff A. 2020-05. Biological Chemistry. “Modular assembly of yeast mitochondrial ATP synthase…” https://doi.org/10.1515/hsz-2020-0112 (franco2020modularassemblyof pages 7-10)
• Song J et al. 2023-01. Nature Communications. “The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase.” https://doi.org/10.1038/s41467-022-35720-5 (song2023themitochondrialhsp70 pages 1-2)
• Tauchmannová K et al. 2024-08. Physiological Research. “Variability of Clinical Phenotypes Caused by Isolated Defects of Mitochondrial ATP Synthase.” https://doi.org/10.33549/physiolres.935407 (tauchmannova2024variabilityofclinical pages 3-5)

Limitations / evidence gaps

Direct ATP11-focused yeast primary studies in 2023–2024 are limited in the retrieved corpus; the newest mechanistic advance relevant to ATP11 here is primarily the integration of Atp11/Atp12 into an mtHsp70-mediated assembly and quality-control framework. (song2023themitochondrialhsp70 pages 1-2)

References

1. (franco2020modularassemblyof pages 7-10): Leticia Veloso Ribeiro Franco, Chen Hsien Su, and Alexander Tzagoloff. Modular assembly of yeast mitochondrial atp synthase and cytochrome oxidase. Biological Chemistry, 401:835-853, May 2020. URL: https://doi.org/10.1515/hsz-2020-0112, doi:10.1515/hsz-2020-0112. This article has 35 citations and is from a peer-reviewed journal.

2. (hinton2003apurifiedsubfragment pages 1-2): Ayana Hinton, Erik R.P. Zuiderweg, and Sharon H. Ackerman. A purified subfragment of yeast atp11p retains full molecular chaperone activity*. Journal of Biological Chemistry, 278:34110-34113, Sep 2003. URL: https://doi.org/10.1074/jbc.m305353200, doi:10.1074/jbc.m305353200. This article has 10 citations and is from a domain leading peer-reviewed journal.

3. (lefebvrelegendre2005failuretoassemble pages 1-2): Linnka Lefebvre-Legendre, Bénédicte Salin, Jacques Schaëffer, Daniel Brèthes, Alain Dautant, Sharon H. Ackerman, and Jean-Paul di Rago. Failure to assemble the α3 β3 subcomplex of the atp synthase leads to accumulation of the α and β subunits within inclusion bodies and the loss of mitochondrial cristae in saccharomyces cerevisiae*. Journal of Biological Chemistry, 280:18386-18392, May 2005. URL: https://doi.org/10.1074/jbc.m410789200, doi:10.1074/jbc.m410789200. This article has 83 citations and is from a domain leading peer-reviewed journal.

4. (ludlam2009chaperonesoff1atpase pages 1-2): Anthony Ludlam, Joseph Brunzelle, Thomas Pribyl, Xingjue Xu, Domenico L. Gatti, and Sharon H. Ackerman. Chaperones of f1-atpase. Journal of Biological Chemistry, 284:17138-17146, Jun 2009. URL: https://doi.org/10.1074/jbc.m109.002568, doi:10.1074/jbc.m109.002568. This article has 40 citations and is from a domain leading peer-reviewed journal.

5. (song2023themitochondrialhsp70 pages 1-2): Jiyao Song, Liesa Steidle, Isabelle Steymans, Jasjot Singh, Anne Sanner, Lena Böttinger, Dominic Winter, and Thomas Becker. The mitochondrial hsp70 controls the assembly of the f1fo-atp synthase. Nature Communications, Jan 2023. URL: https://doi.org/10.1038/s41467-022-35720-5, doi:10.1038/s41467-022-35720-5. This article has 26 citations and is from a highest quality peer-reviewed journal.

6. (potocka2007assemblyfactorsin pages 17-21): A Potocká. Assembly factors in the biogenesis of mitochondrial atp synthase. Unknown journal, 2007.

7. (song2018assemblingthemitochondrial pages 1-2): Jiyao Song, Nikolaus Pfanner, and Thomas Becker. Assembling the mitochondrial atp synthase. Proceedings of the National Academy of Sciences, 115:2850-2852, Mar 2018. URL: https://doi.org/10.1073/pnas.1801697115, doi:10.1073/pnas.1801697115. This article has 84 citations and is from a highest quality peer-reviewed journal.

8. (ludlam2009chaperonesoff1atpase pages 3-4): Anthony Ludlam, Joseph Brunzelle, Thomas Pribyl, Xingjue Xu, Domenico L. Gatti, and Sharon H. Ackerman. Chaperones of f1-atpase. Journal of Biological Chemistry, 284:17138-17146, Jun 2009. URL: https://doi.org/10.1074/jbc.m109.002568, doi:10.1074/jbc.m109.002568. This article has 40 citations and is from a domain leading peer-reviewed journal.

9. (lefebvrelegendre2005failuretoassemble media b3ecdee8): Linnka Lefebvre-Legendre, Bénédicte Salin, Jacques Schaëffer, Daniel Brèthes, Alain Dautant, Sharon H. Ackerman, and Jean-Paul di Rago. Failure to assemble the α3 β3 subcomplex of the atp synthase leads to accumulation of the α and β subunits within inclusion bodies and the loss of mitochondrial cristae in saccharomyces cerevisiae*. Journal of Biological Chemistry, 280:18386-18392, May 2005. URL: https://doi.org/10.1074/jbc.m410789200, doi:10.1074/jbc.m410789200. This article has 83 citations and is from a domain leading peer-reviewed journal.

10. (lefebvrelegendre2005failuretoassemble media 33a6c4d5): Linnka Lefebvre-Legendre, Bénédicte Salin, Jacques Schaëffer, Daniel Brèthes, Alain Dautant, Sharon H. Ackerman, and Jean-Paul di Rago. Failure to assemble the α3 β3 subcomplex of the atp synthase leads to accumulation of the α and β subunits within inclusion bodies and the loss of mitochondrial cristae in saccharomyces cerevisiae*. Journal of Biological Chemistry, 280:18386-18392, May 2005. URL: https://doi.org/10.1074/jbc.m410789200, doi:10.1074/jbc.m410789200. This article has 83 citations and is from a domain leading peer-reviewed journal.

11. (lefebvrelegendre2005failuretoassemble media 5e421669): Linnka Lefebvre-Legendre, Bénédicte Salin, Jacques Schaëffer, Daniel Brèthes, Alain Dautant, Sharon H. Ackerman, and Jean-Paul di Rago. Failure to assemble the α3 β3 subcomplex of the atp synthase leads to accumulation of the α and β subunits within inclusion bodies and the loss of mitochondrial cristae in saccharomyces cerevisiae*. Journal of Biological Chemistry, 280:18386-18392, May 2005. URL: https://doi.org/10.1074/jbc.m410789200, doi:10.1074/jbc.m410789200. This article has 83 citations and is from a domain leading peer-reviewed journal.

12. (tauchmannova2024variabilityofclinical pages 3-5): K. Tauchmannová, A. Pecinová, J. Houštěk, and T. Mrázek. Variability of clinical phenotypes caused by isolated defects of mitochondrial atp synthase. Physiological Research, pages S243-S278, Aug 2024. URL: https://doi.org/10.33549/physiolres.935407, doi:10.33549/physiolres.935407. This article has 14 citations and is from a peer-reviewed journal.

13. (tauchmannova2024variabilityofclinical pages 1-3): K. Tauchmannová, A. Pecinová, J. Houštěk, and T. Mrázek. Variability of clinical phenotypes caused by isolated defects of mitochondrial atp synthase. Physiological Research, pages S243-S278, Aug 2024. URL: https://doi.org/10.33549/physiolres.935407, doi:10.33549/physiolres.935407. This article has 14 citations and is from a peer-reviewed journal.

14. (ludlam2009chaperonesoff1atpase pages 4-5): Anthony Ludlam, Joseph Brunzelle, Thomas Pribyl, Xingjue Xu, Domenico L. Gatti, and Sharon H. Ackerman. Chaperones of f1-atpase. Journal of Biological Chemistry, 284:17138-17146, Jun 2009. URL: https://doi.org/10.1074/jbc.m109.002568, doi:10.1074/jbc.m109.002568. This article has 40 citations and is from a domain leading peer-reviewed journal.

15. (pickova2005assemblyfactorsof pages 1-2): Andrea Pícková, Martin Potocký, and Josef Houštěk. Assembly factors of f1fo‐atp synthase across genomes. Proteins: Structure, 59:393-402, May 2005. URL: https://doi.org/10.1002/prot.20452, doi:10.1002/prot.20452. This article has 43 citations.

16. (lefebvrelegendre2001identificationofa pages 6-7): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 179 citations.

Citations

1. hinton2003apurifiedsubfragment pages 1-2
2. potocka2007assemblyfactorsin pages 17-21
3. tauchmannova2024variabilityofclinical pages 3-5
4. pickova2005assemblyfactorsof pages 1-2
5. lefebvrelegendre2005failuretoassemble pages 1-2
6. song2018assemblingthemitochondrial pages 1-2
7. franco2020modularassemblyof pages 7-10
8. tauchmannova2024variabilityofclinical pages 1-3
9. lefebvrelegendre2001identificationofa pages 6-7
10. https://doi.org/10.1074/jbc.M305353200;
11. https://doi.org/10.1074/jbc.M109.002568
12. https://doi.org/10.1074/jbc.M109.002568;
13. https://doi.org/10.1073/pnas.1801697115
14. https://doi.org/10.1074/jbc.M410789200;
15. https://doi.org/10.1074/jbc.M009557200
16. https://doi.org/10.1074/jbc.M410789200
17. https://doi.org/10.1073/pnas.1801697115;
18. https://doi.org/10.1515/hsz-2020-0112
19. https://doi.org/10.1515/hsz-2020-0112;
20. https://doi.org/10.1038/s41467-022-35720-5
21. https://doi.org/10.1074/jbc.M305353200
22. https://doi.org/10.33549/physiolres.935407
23. https://doi.org/10.1515/hsz-2020-0112,
24. https://doi.org/10.1074/jbc.m305353200,
25. https://doi.org/10.1074/jbc.m410789200,
26. https://doi.org/10.1074/jbc.m109.002568,
27. https://doi.org/10.1038/s41467-022-35720-5,
28. https://doi.org/10.1073/pnas.1801697115,
29. https://doi.org/10.33549/physiolres.935407,
30. https://doi.org/10.1002/prot.20452,
31. https://doi.org/10.1074/jbc.m009557200,