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protein_family: Belongs to the GroES chaperonin family. .
protein_domains: Chaperonin_GroES. (IPR020818); Chaperonin_GroES_sf. (IPR037124);
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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: P38910
• Protein Description: RecName: Full=10 kDa heat shock protein, mitochondrial; Short=HSP10; AltName: Full=10 kDa chaperonin;
• Gene Information: Name=HSP10; Synonyms=CPN10; OrderedLocusNames=YOR020C; ORFNames=OR26.10;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the GroES chaperonin family. .
• Key Domains: Chaperonin_GroES. (IPR020818); Chaperonin_GroES_sf. (IPR037124); Chaprnonin_Cpn10_CS. (IPR018369); GroES-like_sf. (IPR011032); Cpn10 (PF00166)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "HSP10" 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 'HSP10' 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 HSP10 (gene ID: HSP10, UniProt: P38910) 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: P38910
• Protein Description: RecName: Full=10 kDa heat shock protein, mitochondrial; Short=HSP10; AltName: Full=10 kDa chaperonin;
• Gene Information: Name=HSP10; Synonyms=CPN10; OrderedLocusNames=YOR020C; ORFNames=OR26.10;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the GroES chaperonin family. .
• Key Domains: Chaperonin_GroES. (IPR020818); Chaperonin_GroES_sf. (IPR037124); Chaprnonin_Cpn10_CS. (IPR018369); GroES-like_sf. (IPR011032); Cpn10 (PF00166)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "HSP10" 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 'HSP10' 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 HSP10 (gene ID: HSP10, UniProt: P38910) 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: Saccharomyces cerevisiae HSP10 (UniProt P38910; ORF YOR020C) — functional annotation

Executive summary

Yeast Hsp10 is a mitochondrial co-chaperonin (GroES/Cpn10 family) that acts with the mitochondrial chaperonin Hsp60 (GroEL/Cpn60 family) to enable ATP-dependent folding and assembly of a subset of imported mitochondrial matrix proteins and to support intramitochondrial sorting of selected substrates (notably the Rieske Fe/S protein) during transit through the matrix. Genetic studies show HSP10 is essential (loss requires complementation; temperature-sensitive alleles are lethal at non-permissive temperature), and biochemical work shows high-affinity nucleotide-dependent binding to Hsp60 and regulation of Hsp60 ATPase coupled to productive client folding. Substrate dependence is selective: some proteins fold largely independently of Hsp10/Hsp60, while other large enzymes (e.g., Ilv3p, aconitase homologs) strongly depend on them.

1. Target verification (critical identity checks)

The target described by UniProt accession P38910 (10 kDa heat shock protein, mitochondrial; GroES/Cpn10 family; yeast locus YOR020C) matches the gene/protein studied in classic yeast mitochondrial folding literature as Hsp10 / hsp10 / cochaperonin GroES homologue. Höhfeld & Hartl cloned yeast HSP10 and characterized it as the mitochondrial GroES homologue/cofactor of Hsp60, using temperature-sensitive lethal hspl0 mutants and mitochondrial import assays (publication date: 1994-07; URL: https://doi.org/10.1083/jcb.126.2.305) (hohfeld1994roleofthe pages 1-2). Dubaquié et al. subsequently used yeast mitochondrial hsp10(P36H) temperature-sensitive variants in biochemical and substrate-identification experiments, consistent with the GroES mobile loop region central to GroES/Cpn10 function (publication dates: 1997-08 and 1998-10; URLs: https://doi.org/10.1073/pnas.94.17.9011 and https://doi.org/10.1093/emboj/17.20.5868) (dubaquie1997significanceofchaperonin pages 1-2, dubaquie1998identificationofin pages 4-5).

2. Key concepts and definitions (current understanding)

2.1 What is Hsp10?

Hsp10 (also called Cpn10) is the co-chaperonin partner of Group I chaperonins. Group I chaperonins form a barrel-like chamber; the co-chaperonin forms a detachable “lid” that caps one end of the chamber to create a protected folding environment during an ATP-driven reaction cycle (singh2024molecularchaperoninhsp60 pages 2-4, boshoff2015chaperonincochaperonininteractions. pages 1-4).

2.2 Group I chaperonin/co-chaperonin mechanism

A recent review (publication date: 2024-05; URL: https://doi.org/10.3390/ijms25105483) summarizes the canonical Group I cycle: Hsp60/GroEL is a double-ring complex (two heptameric rings); co-chaperonin GroES/Hsp10 caps one ring to form an asymmetric “cis” folding chamber. ATP binding and hydrolysis coordinate encapsulation, client folding, and timed release through co-chaperonin dissociation (singh2024molecularchaperoninhsp60 pages 2-4, singh2024molecularchaperoninhsp60 pages 1-2). A dedicated review chapter similarly emphasizes that GroES/Hsp10 lid binding dislodges substrate into the chamber and ATP/co-chaperonin binding enlarges the chamber to allow folding (publication date: 2015-12; URL: https://doi.org/10.1007/978-3-319-11731-7_8) (boshoff2015chaperonincochaperonininteractions. pages 1-4).

3. Experimentally supported function in yeast

3.1 Essentiality

Höhfeld & Hartl generated temperature-sensitive lethal yeast hspl0 mutants and used genetic complementation logic indicating that loss of HSP10 function requires complementation for viability, supporting that HSP10 is essential under the tested conditions (hohfeld1994roleofthe pages 1-2, hohfeld1994roleofthe pages 2-3).

3.2 Subcellular localization and where Hsp10 acts

The yeast Hsp10 studied by Höhfeld & Hartl is a mitochondrial factor purified from mitochondria and investigated using isolated mitochondria import/folding/sorting assays, establishing its site of action in mitochondrial protein biogenesis (hohfeld1994roleofthe pages 2-3). Dubaquié et al. explicitly frame yeast hsp10 as a mitochondrial (matrix) co-chaperonin acting with hsp60 in folding of imported proteins (dubaquie1998identificationofin pages 1-2, dubaquie1998identificationofin pages 5-6).

3.3 Primary molecular function: co-chaperonin activity with Hsp60

Direct biochemical evidence demonstrates that yeast hsp10 is a heptameric co-chaperonin that binds nucleotide-dependently to the 14-mer hsp60 chaperonin and regulates its ATPase in a way coupled to productive folding.

• Binding affinity (ADP state): one hsp10 binding event has apparent Kd ~0.88–0.9 nM, with a second binding event Kd ~24 nM (dubaquie1997significanceofchaperonin pages 1-2).
• hsp10 inhibits hsp60 ATPase by ~40% (dubaquie1997significanceofchaperonin pages 1-2).
• In refolding of denatured mitochondrial malate dehydrogenase (mMDH), hsp60 + WT hsp10 yields ~40% refolding (150 min) at a 2–5× molar excess of hsp10 heptamer over hsp60 14-mer (dubaquie1997significanceofchaperonin pages 2-3).

These values support a model where hsp10 modulates the ATPase cycle of hsp60 and thereby gates productive folding (dubaquie1997significanceofchaperonin pages 1-2).

3.4 Mechanistic hotspot: GroES-like mobile loop (P36 region)

Both the yeast genetics and biochemistry converge on residues ~25–40 (mobile-loop-like region) as critical for chaperonin interaction.

• Höhfeld & Hartl mapped temperature-sensitive lesions to a region corresponding to the GroES mobile loop, and these mutations reduce chaperonin binding at non-permissive temperature (hohfeld1994roleofthe pages 1-2, hohfeld1994roleofthe pages 10-11).
• Dubaquié et al. characterized hsp10(P36H): binding to hsp60 is weakened (Kd shifts from ~0.88 nM to ~19.2 ± 1.6 nM) and the mutant fails to support hsp60-mediated mMDH refolding at elevated temperature (dubaquie1997significanceofchaperonin pages 2-3).

Figure evidence from Höhfeld & Hartl shows ATP-dependent complex formation between yeast Hsp10 and GroEL, and reduced binding of the P36>S mutant at non-permissive temperature (hohfeld1994roleofthe media 9f154887, hohfeld1994roleofthe media f10be0d9).

3.5 Substrate specificity: overlapping but non-identical requirement vs Hsp60

A key insight from Dubaquié et al. (publication date 1998-10; URL: https://doi.org/10.1093/emboj/17.20.5868) is that Hsp60 and Hsp10 requirements overlap but are not identical.

Quantitative folding and aggregation readouts include:

• Newly imported Hsp60 folding (protease-resistant after 30 min): >80% in WT, ~20% in hsp60-ts, and <5% in hsp10-ts mitochondria (dubaquie1998identificationofin pages 4-5).
• Detergent-insoluble pellet (%Pel; proxy for aggregation) for representative enzymes (hsp60-ts vs hsp10-ts): ILV3 100% vs 50%; ACO1 100% vs 80%; IDH1 95% vs <5%; MDH1 <20% vs <5% (dubaquie1998identificationofin pages 4-5).
• A subset of proteins folds largely independently: imported yeast malate dehydrogenase (y-mdh1) reaches protease-resistant state in ~70–90% of molecules regardless of hsp60/hsp10 status (dubaquie1998identificationofin pages 5-6).
• Import/folding kinetics example: yeast rhodanese folds in the matrix with half-time ~4 min (vs 15 min for bovine rhodanese) (dubaquie1998identificationofin pages 5-6).

These data support that Hsp10 is not a universal requirement for all matrix protein maturation but is essential overall because key substrates (and/or the folding system itself, including newly imported Hsp60) depend strongly on it (dubaquie1998identificationofin pages 4-5, dubaquie1998identificationofin pages 1-2).

3.6 Role in intramitochondrial sorting (Rieske Fe/S protein)

Höhfeld & Hartl provide in vivo/organellar evidence that Hsp10 contributes to sorting of certain proteins that transit the matrix en route to the intermembrane space, specifically the Rieske Fe/S protein. In hspl0 (P36>S) mutant mitochondria at non-permissive temperature, the Rieske Fe/S protein shows accumulation of processing intermediates and increased detergent-insoluble (aggregated) material, consistent with defective maturation/sorting (hohfeld1994roleofthe pages 8-9, hohfeld1994roleofthe pages 1-2).

4. Pathways and biological processes

Hsp10’s function is best placed within mitochondrial protein import and folding/proteostasis pathways: after nuclear-encoded precursors enter mitochondria, a subset require the Hsp60/Hsp10 chaperonin system to reach native structure or to remain competent for onward sorting steps (hohfeld1994roleofthe pages 1-2, dubaquie1998identificationofin pages 5-6, hohfeld1994roleofthe pages 8-9). Mechanistically, this maps to the conserved Group I cycle in which Hsp10 forms a lid to create a protected folding chamber and coordinate ATP-driven conformational transitions (singh2024molecularchaperoninhsp60 pages 2-4, boshoff2015chaperonincochaperonininteractions. pages 1-4).

5. Recent developments (prioritizing 2023–2024) and how they inform yeast Hsp10 annotation

Yeast-specific Hsp10 mechanistic experimentation is dominated by foundational 1990s work; however, recent studies refine the structural logic of the conserved mitochondrial Hsp60/Hsp10 system.

• Conserved lid and ATP-driven cycle (review, 2024-05): Singh et al. summarize GroES/Hsp10 as a heptameric lid that caps one end of the Group I chaperonin to form a cis chamber; ATP hydrolysis and ATP binding in the opposite ring coordinate lid dissociation and client release (https://doi.org/10.3390/ijms25105483) (singh2024molecularchaperoninhsp60 pages 2-4).
• Structural basis for client handling and co-chaperonin recruitment (preprint, 2024-05): A cryo-EM study reports that client density can be detected across multiple states and that asymmetric apical conformations can support simultaneous co-chaperonin recruitment and client retention before full encapsulation (https://doi.org/10.1101/2023.05.15.540872) (tascon2025structuralbasisfor pages 8-11).

These 2024 sources support an updated mechanistic framing for yeast Hsp10 as a conserved lid/cofactor that participates in dynamic conformational cycles and possibly asymmetric client-handling strategies, consistent with yeast genetic/biochemical evidence that different substrates have different dependencies on the co-chaperonin (dubaquie1998identificationofin pages 4-5, singh2024molecularchaperoninhsp60 pages 2-4).

6. Current applications and real-world implementations

6.1 Yeast Hsp10 as a model for conserved mitochondrial proteostasis

The yeast Hsp60/Hsp10 system provides a genetically tractable model to dissect mitochondrial protein folding, quality control, and sorting, using temperature-sensitive alleles in the conserved mobile-loop region (P36) to perturb function in vivo (hohfeld1994roleofthe pages 1-2, dubaquie1998identificationofin pages 4-5).

6.2 General translational relevance (conserved Hsp60/Hsp10 system)

Although not yeast-specific, recent and current reviews emphasize that mitochondrial Hsp60/Hsp10 systems are central to proteostasis and are being explored as targets/biomarkers in diverse disease contexts (e.g., via Hsp60-directed strategies), underscoring why mechanistic insights from yeast remain relevant to broader biology (singh2024molecularchaperoninhsp60 pages 2-4).

7. Expert synthesis and interpretation

7.1 Primary functional statement for annotation

Hsp10 (YOR020C; UniProt P38910) is an essential mitochondrial co-chaperonin that binds Hsp60 with high affinity in a nucleotide-dependent manner and regulates the Hsp60 ATPase-driven folding cycle to promote folding/assembly of a subset of imported matrix proteins and to support sorting of select substrates (e.g., Rieske Fe/S protein) during intramitochondrial trafficking. This statement is directly supported by yeast genetics and mitochondria import/sorting experiments (hohfeld1994roleofthe pages 1-2, hohfeld1994roleofthe pages 8-9) and by quantitative purified-protein binding/refolding assays (dubaquie1997significanceofchaperonin pages 1-2, dubaquie1997significanceofchaperonin pages 2-3).

7.2 Why essentiality can coexist with substrate-specific dependence

Dubaquié et al. show that some proteins fold with little dependence on Hsp10/Hsp60 (e.g., y-mdh1), yet newly imported Hsp60 itself is dramatically dependent on Hsp10 (<5% protease-resistant folding in hsp10-ts), implying a systems-level fragility where co-chaperonin dysfunction can compromise folding capacity broadly, even if a subset of substrates is intrinsically independent (dubaquie1998identificationofin pages 4-5, dubaquie1998identificationofin pages 5-6).

8. Key quantitative data (selected)

• HSP10 induction: ~2–3× at elevated temperature (hohfeld1994roleofthe pages 8-9).
• Hsp10–Hsp60 binding (ADP): Kd ~0.88–0.9 nM (first) and ~24 nM (second) (dubaquie1997significanceofchaperonin pages 1-2).
• Hsp10 inhibition of Hsp60 ATPase: ~40% (dubaquie1997significanceofchaperonin pages 1-2).
• mMDH refolding yield: ~40% (WT Hsp60/Hsp10); ~30% at 25°C and <10% at 30°C for Hsp10(P36H) with Hsp60 (dubaquie1997significanceofchaperonin pages 2-3).
• Newly imported Hsp60 folding (protease-resistant, 30 min): >80% WT; ~20% hsp60-ts; <5% hsp10-ts (dubaquie1998identificationofin pages 4-5).
• Aggregation proxy (%Pel): ILV3 100% vs 50% (hsp60-ts vs hsp10-ts); ACO1 100% vs 80%; IDH1 95% vs <5%; MDH1 <20% vs <5% (dubaquie1998identificationofin pages 4-5).
• Yeast rhodanese folding half-time in matrix: ~4 min (dubaquie1998identificationofin pages 5-6).

Visual evidence (from primary literature)

Key experimental figures from Höhfeld & Hartl (1994) show ATP-dependent complex formation between yeast Hsp10 and GroEL, the P36-region mutation mapping to the GroES-like mobile loop, reduced binding of the mutant at non-permissive temperature, and impaired assembly of an imported matrix protein (OTC) (hohfeld1994roleofthe media 9f154887, hohfeld1994roleofthe media f10be0d9, hohfeld1994roleofthe media 887c719f).

Evidence table

Table: This table summarizes primary-study evidence for the function of Saccharomyces cerevisiae mitochondrial Hsp10/YOR020C, including localization, mechanistic role with Hsp60, essentiality, and quantitative measurements from classic genetic and biochemical experiments.

Limitations of this report

Direct citations to UniProt or SGD web entries for P38910/YOR020C could not be ingested as citable sources with the available tools in this run; consequently, database-derived claims (e.g., specific GO terms, systematic name cross-references) were not used as primary evidence. The central functional, localization, and mechanistic assertions are instead grounded in peer-reviewed yeast primary literature and complemented by recent (2024) chaperonin reviews/structural work (hohfeld1994roleofthe pages 1-2, dubaquie1997significanceofchaperonin pages 2-3, dubaquie1998identificationofin pages 4-5, singh2024molecularchaperoninhsp60 pages 2-4).

References

1. (hohfeld1994roleofthe pages 1-2): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

2. (dubaquie1997significanceofchaperonin pages 1-2): Yves Dubaquié, Renate Looser, and Sabine Rospert. Significance of chaperonin 10-mediated inhibition of atp hydrolysis by chaperonin 60. Proceedings of the National Academy of Sciences of the United States of America, 94 17:9011-6, Aug 1997. URL: https://doi.org/10.1073/pnas.94.17.9011, doi:10.1073/pnas.94.17.9011. This article has 49 citations and is from a highest quality peer-reviewed journal.

3. (dubaquie1998identificationofin pages 4-5): Y. Dubaquié, R. Looser, U. Fünfschilling, P. Jenö, and S. Rospert. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non‐identical requirement for hsp60 and hsp10. The EMBO Journal, 17:5868-5876, Oct 1998. URL: https://doi.org/10.1093/emboj/17.20.5868, doi:10.1093/emboj/17.20.5868. This article has 130 citations.

4. (singh2024molecularchaperoninhsp60 pages 2-4): Manish Kumar Singh, Yoonhwa Shin, Sunhee Han, Joohun Ha, Pramod K. Tiwari, Sung Soo Kim, and Insug Kang. Molecular chaperonin hsp60: current understanding and future prospects. International Journal of Molecular Sciences, 25:5483, May 2024. URL: https://doi.org/10.3390/ijms25105483, doi:10.3390/ijms25105483. This article has 86 citations.

5. (boshoff2015chaperonincochaperonininteractions. pages 1-4): Aileen Boshoff. Chaperonin-co-chaperonin interactions. Sub-cellular biochemistry, 78:153-78, Dec 2015. URL: https://doi.org/10.1007/978-3-319-11731-7_8, doi:10.1007/978-3-319-11731-7_8. This article has 19 citations.

6. (singh2024molecularchaperoninhsp60 pages 1-2): Manish Kumar Singh, Yoonhwa Shin, Sunhee Han, Joohun Ha, Pramod K. Tiwari, Sung Soo Kim, and Insug Kang. Molecular chaperonin hsp60: current understanding and future prospects. International Journal of Molecular Sciences, 25:5483, May 2024. URL: https://doi.org/10.3390/ijms25105483, doi:10.3390/ijms25105483. This article has 86 citations.

7. (hohfeld1994roleofthe pages 2-3): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

8. (dubaquie1998identificationofin pages 1-2): Y. Dubaquié, R. Looser, U. Fünfschilling, P. Jenö, and S. Rospert. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non‐identical requirement for hsp60 and hsp10. The EMBO Journal, 17:5868-5876, Oct 1998. URL: https://doi.org/10.1093/emboj/17.20.5868, doi:10.1093/emboj/17.20.5868. This article has 130 citations.

9. (dubaquie1998identificationofin pages 5-6): Y. Dubaquié, R. Looser, U. Fünfschilling, P. Jenö, and S. Rospert. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non‐identical requirement for hsp60 and hsp10. The EMBO Journal, 17:5868-5876, Oct 1998. URL: https://doi.org/10.1093/emboj/17.20.5868, doi:10.1093/emboj/17.20.5868. This article has 130 citations.

10. (dubaquie1997significanceofchaperonin pages 2-3): Yves Dubaquié, Renate Looser, and Sabine Rospert. Significance of chaperonin 10-mediated inhibition of atp hydrolysis by chaperonin 60. Proceedings of the National Academy of Sciences of the United States of America, 94 17:9011-6, Aug 1997. URL: https://doi.org/10.1073/pnas.94.17.9011, doi:10.1073/pnas.94.17.9011. This article has 49 citations and is from a highest quality peer-reviewed journal.

11. (hohfeld1994roleofthe pages 10-11): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

12. (hohfeld1994roleofthe media 9f154887): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

13. (hohfeld1994roleofthe media f10be0d9): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

14. (hohfeld1994roleofthe pages 8-9): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

15. (tascon2025structuralbasisfor pages 8-11): Igor Tascón, Jorge P. López-Alonso, Yoel Shkolnisky, David Gil-Cartón, Jesús Vilchez-Garcia, Alberto G. Berruezo, Yacob Gómez-Llorente, Radhika Malik, Fady Jebara, Malay Patra, Joel A. Hirsch, Abdussalam Azem, and Iban Ubarretxena-Belandia. Structural basis for atp-driven double-ring assembly of the human mitochondrial hsp60 chaperonin. BioRxiv, Oct 2025. URL: https://doi.org/10.1101/2025.10.04.680452, doi:10.1101/2025.10.04.680452. This article has 2 citations.

16. (hohfeld1994roleofthe media 887c719f): J Höhfeld and F U Hartl. Role of the chaperonin cofactor hsp10 in protein folding and sorting in yeast mitochondria. The Journal of cell biology, 126:305-315, Jul 1994. URL: https://doi.org/10.1083/jcb.126.2.305, doi:10.1083/jcb.126.2.305. This article has 169 citations.

17. (dubaquie1998identificationofin pages 6-7): Y. Dubaquié, R. Looser, U. Fünfschilling, P. Jenö, and S. Rospert. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non‐identical requirement for hsp60 and hsp10. The EMBO Journal, 17:5868-5876, Oct 1998. URL: https://doi.org/10.1093/emboj/17.20.5868, doi:10.1093/emboj/17.20.5868. This article has 130 citations.

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