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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: P42943
• Protein Description: RecName: Full=T-complex protein 1 subunit eta; Short=TCP-1-eta; AltName: Full=CCT-eta;
• Gene Information: Name=CCT7; OrderedLocusNames=YJL111W; ORFNames=J0804;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_eta. (IPR012720); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT7" 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 'CCT7' 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 CCT7 (gene ID: CCT7, UniProt: P42943) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P42943
• Protein Description: RecName: Full=T-complex protein 1 subunit eta; Short=TCP-1-eta; AltName: Full=CCT-eta;
• Gene Information: Name=CCT7; OrderedLocusNames=YJL111W; ORFNames=J0804;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_eta. (IPR012720); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT7" 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 'CCT7' 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 CCT7 (gene ID: CCT7, UniProt: P42943) 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.

Comprehensive Research Report: Yeast CCT7 (UniProt P42943; SGD ORF YJL111W)—Functional Annotation

Executive summary

CCT7 encodes T-complex protein 1 subunit eta (Cct7p), one of the eight distinct subunits (CCT1–CCT8) that assemble into the eukaryotic group II chaperonin TRiC/CCT. In budding yeast, Cct7p’s primary function is ATP-dependent folding of cytosolic client proteins as part of this ~1 MDa, double-ring (16-subunit) machine. Experimental genetics demonstrate that CCT7 is essential for viability, and perturbation of its conserved ATP-binding pocket causes growth defects and proteostasis collapse (protein aggregation) and alters stress responses, consistent with impaired chaperonin activity. Recent (2023–2024) cryo-EM and biochemical studies (primarily in mammalian systems but mechanistically conserved) refine how TRiC cycles through open/closed states to fold obligate substrates (actin/tubulin) and how co-chaperones (prefoldin, PhLP2A) engage TRiC during the ATP-driven cycle, providing a modern framework for interpreting subunit contributions including CCT7.

1) Verification of gene/protein identity (critical disambiguation)

The target in this report is yeast CCT7 (YJL111W; UniProt P42943) encoding T-complex protein 1 subunit eta, a TCP-1 chaperonin family component of TRiC/CCT. The yeast-specific experimental literature explicitly refers to CCT7 as an essential gene in S. cerevisiae and studies Cct7p as a TRiC subunit (not to be confused with human CCT7 studies, which are orthologous context only) (dube2021chaperoninpointmutation pages 4-7, liu2021cryoemstudyon pages 1-4).

2) Key concepts and definitions (current understanding)

2.1 TRiC/CCT: definition, architecture, and folding mechanism

TRiC/CCT (TCP-1 Ring Complex / Chaperonin Containing TCP-1) is a eukaryotic cytosolic chaperonin that is ATP-dependent and forms a ring-shaped, double-ring assembly. A recent review summarizes it as an ~1 MDa complex of 16 subunits arranged as two stacked rings, each ring containing eight distinct subunits (CCT1–CCT8) (que2024theroleof pages 2-4). The folding mechanism is fundamentally ATP-driven: ATP binding/hydrolysis drives conformational changes (opening/closure of the folding chamber) that encapsulate non-native substrates to limit conformational space, thereby promoting productive folding and reducing aggregation (que2024theroleof pages 2-4).

At the subunit level, TRiC subunits share a conserved chaperonin fold with three domains: equatorial (ATP-binding), intermediate, and apical (substrate-binding), which provides a structure–function rationale for why ATP-pocket mutations in Cct7p lead to proteostasis phenotypes (dube2021chaperoninpointmutation pages 1-4, que2024theroleof pages 2-4).

2.2 Where CCT7 fits: subunit composition and arrangement

A yeast-relevant review/experimental synthesis reports a consensus TRiC ring order CCT1-4-2-5-7-8-6-3, placing CCT7 at a defined position within each ring, with evidence supporting near equal stoichiometry of the eight subunits in mature TRiC (sergeeva2019coexpressionofcct pages 1-2). This is consistent with CCT7’s role as a structural and functional component of the machine rather than a stand-alone enzyme.

2.3 Cellular localization

Group II TRiC/CCT is classically described as cytosolic, implying that yeast Cct7p primarily functions in the cytosol as part of the TRiC complex (kabir2005physiologicaleffectsof pages 1-2). Recent broader chaperonin literature also supports potential nuclear-associated roles for TRiC/CCT (e.g., regulation of RNA polymerase II activity), but this evidence is not specific to yeast CCT7 and should be interpreted cautiously when assigning CCT7 localization/functions in budding yeast (gvozdenov2024triccctchaperoningoverns pages 33-36).

3) Gene product function: molecular function, pathways, and clients

3.1 Primary molecular function

Cct7p’s primary molecular function is ATP-dependent molecular chaperone activity as part of TRiC/CCT. It does not catalyze a discrete chemical transformation; instead, it contributes to substrate binding/encapsulation and allosteric conformational cycling required for folding (que2024theroleof pages 2-4, kelly2020structuralandfunctional pages 28-35).

3.2 Pathways/processes influenced (mechanistically proximal)

Because TRiC folds proteins that are difficult to fold spontaneously, its most direct pathway role is in cytosolic proteostasis, particularly folding of essential cytoskeletal proteins and other complex clients. Yeast-/TRiC-level client examples include actin and tubulin; the yeast mutant data also connect CCT activity to mitotic checkpoint complex (MCC) disassembly and cell-cycle regulation through client folding/complex remodeling (liu2021cryoemstudyon pages 1-4, dube2021chaperoninpointmutation pages 4-7).

3.3 Client scope: fraction of the proteome

Multiple sources converge on the estimate that TRiC/CCT assists folding of approximately ~10% of cytosolic proteins (often stated as “a tenth of the proteins in the cell”) (que2024theroleof pages 2-4, sergeeva2019coexpressionofcct pages 1-2). This provides a scale-of-function context for why CCT7 is essential.

4) Yeast CCT7-specific experimental evidence (essentiality, phenotypes, mechanistic inference)

4.1 Essentiality

A plasmid-shuffling strategy in S. cerevisiae demonstrated that CCT7 is essential: CCT7 deletant mutants do not grow on FOA plates, indicating inviability when the wild-type covering plasmid is lost (dube2021chaperoninpointmutation pages 4-7). This aligns with TRiC being a core proteostasis machine required for folding essential clients.

4.2 ATP-pocket mutation phenotypes (proteostasis and stress)

A targeted point mutation in the conserved ATP-binding region of Cct7p (reported as G412E; mutation of the conserved GGG motif region) produced hallmark chaperonin-defect phenotypes:

• Growth retardation: doubling time increased from 2.05 ± 0.2 h (WT) to 3.47 ± 0.2 h (mutant) (dube2021chaperoninpointmutation pages 4-7).
• Proteostasis collapse / aggregation: mutant cells showed protein aggregates, visualized indirectly using Hsp104-GFP as an aggregation marker (dube2021chaperoninpointmutation pages 4-7).
• Stress-response alterations: mutant was lethal under arsenite (As3+) but showed improved growth under cadmium stress (Cd2+) and altered cadmium handling (dube2021chaperoninpointmutation pages 1-4, dube2021chaperoninpointmutation pages 4-7).

Quantitative cadmium-related measures included:
* Cadmium uptake efficiency: 10.54 µg Cd/mg (mutant) vs 9.05 µg Cd/mg (WT) (dube2021chaperoninpointmutation pages 4-7).
* Cadmium removal capacity: 42.75%, 46.70%, 65.17% at 16, 24, 48 h; and pH dependence (e.g., 48.97% at pH 4 vs 42.75% at pH 6) (dube2021chaperoninpointmutation pages 4-7).

Mechanistically, these phenotypes are consistent with impaired ATP-driven TRiC cycling, leading to widespread client misfolding/aggregation and strong secondary effects on stress adaptation.

4.3 Assembly-related mechanistic evidence involving CCT7

A yeast TRiC assembly study reported subunit-specific behaviors: when expressed individually in E. coli, CCT3/4/7/8 could not form homo-oligomeric TRiC-like rings, unlike certain other subunits. This suggests that CCT7 is not sufficient alone to build ring-like assemblies and that its productive function depends on hetero-oligomeric assembly pathways (liu2021cryoemstudyon pages 1-4). While heterologous expression is not the native context, it supports a model where subunit specialization underlies TRiC assembly and allostery.

5) Recent developments (prioritizing 2023–2024) relevant to yeast CCT7 functional interpretation

5.1 2023: Cryo-EM of TRiC-mediated tubulin folding along the ATPase cycle

A 2023 cryo-EM/XL-MS study (endogenous human TRiC) captured multiple substrate-engaged states across the ATPase cycle, providing quantitative mechanistic data that informs conserved TRiC principles relevant to subunits such as yeast CCT7:

• Open-state populations: 61.6% and 38.4% particle classes for distinct open maps (liu2023pathwayandmechanism pages 1-2).
• High-resolution reconstructions: 3.1 Å and 4.1 Å maps (liu2023pathwayandmechanism pages 1-2).
• Client–subunit contacts: five XL-MS cross-links between tubulin and specific subunits (CCT3/4/6/8 in that study) and a pathway of substrate translocation/stabilization during ring closure (liu2023pathwayandmechanism pages 1-2).

Although CCT7 was not the primary contacting subunit in the reported tubulin interface summary, the study’s central insight—that TRiC folding is coordinated with ATP-driven conformational changes and specific subunit surfaces—provides a modern interpretive frame for yeast CCT7’s ATP-pocket mutation phenotypes (liu2023pathwayandmechanism pages 1-2).

Visual evidence (from this 2023 work): a cropped figure region showing TRiC architecture with labeled subunits and the folding-state pathway across the ATPase cycle is available (liu2023pathwayandmechanism media 86d3cbff, liu2023pathwayandmechanism media 483af941).

5.2 2024: Co-chaperone cooperation (Prefoldin and PhLP2A) during the ATP-driven cycle

A 2024 Nature Communications study defined an ATP-driven cycle of TRiC cooperation with cochaperones prefoldin (PFD) and PhLP2A, including mechanistic steps for cofactor binding and displacement during TRiC conformational transitions (junsun2024astructuralvista pages 1-2). These findings strengthen the prevailing view that TRiC function in vivo is embedded in a multi-chaperone network, and that subunit-specific surfaces coordinate co-chaperone binding and allosteric transitions—concepts directly relevant for functional annotation of yeast subunits including CCT7 (junsun2024astructuralvista pages 1-2).

5.3 2024: Disease genetics underscores conserved essentiality (“TRiCopathies”)

A 2024 Science paper reported that TRiC is an obligate hetero-oligomer and that variants in seven of eight subunits can impair TRiC function/assembly, causing severe neurodevelopmental phenotypes in humans (kraft2024brainmalformationsand pages 1-3). While not yeast-specific, it provides expert-level reinforcement that subunit integrity is critical and that subunits can be differentially sensitive to mutation.

5.4 2024 review perspectives linking TRiC to translation and broader proteostasis

A 2024 review emphasizes TRiC/CCT roles in translation-associated proteostasis, including interactions with nascent chains and broader regulatory implications for translation elongation (que2024theroleof pages 7-9). For yeast CCT7 annotation, this supports a contemporary systems-level view: TRiC is not merely a refolding machine but part of a cotranslational folding network (que2024theroleof pages 7-9).

6) Current applications and real-world implementations

6.1 Yeast as a platform for TRiC/CCT mechanistic dissection

Yeast remains a key model for dissecting TRiC function via genetics and quantitative phenotyping. The CCT7 plasmid-shuffle/point-mutation strategy illustrates how essential chaperonin subunits can be experimentally perturbed while maintaining viability, enabling mechanistic inference from growth, proteostasis, and stress phenotypes (dube2021chaperoninpointmutation pages 4-7).

6.2 Biotechnology/bioprocess relevance (stress tolerance engineering)

The CCT7 ATP-pocket mutant’s altered heavy-metal phenotypes (cadmium uptake/removal metrics) suggest that TRiC perturbations can shift stress response landscapes in ways that could be exploited or must be controlled in industrial yeast contexts (e.g., fermentation under stress), although these are likely indirect effects mediated by global proteostasis changes rather than a dedicated “cadmium pathway” role for Cct7p (dube2021chaperoninpointmutation pages 4-7).

6.3 Translational relevance (outside yeast): TRiC as a therapeutic/diagnostic target concept

Recent structural studies explicitly note that understanding TRiC–substrate interfaces may inform therapeutic agent design targeting these interactions (liu2023pathwayandmechanism pages 1-2), and human genetics highlights clinical consequences of TRiC impairment (kraft2024brainmalformationsand pages 1-3). These are not yeast applications per se, but they contextualize why subunit-specific mechanisms (including CCT7/eta) remain an active research area.

7) Expert opinion and analysis (authoritative synthesis)

Across reviews and structural work, an expert-consensus picture emerges:

1. TRiC/CCT is essential and specialized compared to bacterial GroEL, with eight distinct subunits whose sequence divergence enables subunit-specific client interactions and allosteric behavior (que2024theroleof pages 2-4, sergeeva2019coexpressionofcct pages 1-2).
2. The ATP-driven open/close cycle is central; therefore, conserved ATP-pocket motifs in subunits like Cct7p are expected to be critical. Yeast G412E phenotypes are consistent with this model, linking ATPase-cycle defects to global aggregation and growth defects (que2024theroleof pages 2-4, dube2021chaperoninpointmutation pages 4-7).
3. Subunit arrangement and equal stoichiometry are recurring themes, supporting the interpretation of CCT7 as a fixed architectural element with a defined position within the ring, not a transient accessory factor (sergeeva2019coexpressionofcct pages 1-2).
4. The 2023–2024 wave of cryo-EM studies increasingly describes TRiC function as a networked process involving co-chaperones (PFD, PhLPs) and structural “trajectories” of client folding, pushing the field from descriptive architecture to mechanistic cycles and state populations (liu2023pathwayandmechanism pages 1-2, junsun2024astructuralvista pages 1-2).

8) Evidence summary table

The following table consolidates the core functional annotation for yeast CCT7 with best supporting citations.

Table: This table condenses the main functional-annotation points for yeast CCT7/YJL111W, including identity verification, role in the TRiC/CCT chaperonin, localization, mechanism, phenotypes, and recent advances. It is useful as a quick evidence-backed summary before reading the full narrative report.

9) Limitations and evidence gaps (yeast CCT7-specific)

• Direct yeast Cct7p client lists: The retrieved evidence supports TRiC-level clients (actin/tubulin) and mechanistic roles, but does not provide a curated, yeast CCT7-specific client interactome. Assigning specific clients uniquely to CCT7 would require additional yeast proteomics/biochemical studies not captured in the current corpus.
• Direct localization experiments for yeast Cct7p: The strongest statement available here is TRiC’s cytosolic classification; direct Cct7p imaging/localization in yeast is not provided in the retrieved text (kabir2005physiologicaleffectsof pages 1-2).

Key URLs and publication dates (selected)

• Que et al., 2024-04 (Heliyon) “The role of molecular chaperone CCT/TRiC in translation elongation” https://doi.org/10.1016/j.heliyon.2024.e29029 (que2024theroleof pages 2-4)
• Park et al., 2024-02 (Nature Communications) “A structural vista of PhLP2A–TRiC cooperation…” https://doi.org/10.1038/s41467-024-45242-x (junsun2024astructuralvista pages 1-2)
• Liu et al., 2023-05 (Communications Biology) “Pathway and mechanism of tubulin folding…” https://doi.org/10.1038/s42003-023-04915-x (liu2023pathwayandmechanism pages 1-2)
• Kraft et al., 2024-11 (Science) “Brain malformations and seizures by impaired chaperonin function of TRiC” https://doi.org/10.1126/science.adp8721 (kraft2024brainmalformationsand pages 1-3)
• Dube & Kabir, 2021-05 (Biotechnology Letters) “Chaperonin point mutation enhances cadmium endurance…” https://doi.org/10.1007/s10529-021-03151-9 (dube2021chaperoninpointmutation pages 4-7)

Figure evidence

• Cropped panels showing TRiC double-ring architecture with labeled subunits and tubulin-folding pathway schematic across ATPase-cycle states (from Liu et al., 2023) (liu2023pathwayandmechanism media 86d3cbff, liu2023pathwayandmechanism media 483af941).

References

1. (dube2021chaperoninpointmutation pages 4-7): Ankita Dube and M. Anaul Kabir. Chaperonin point mutation enhances cadmium endurance in saccharomyces cerevisiae. Biotechnology Letters, 43:1735-1745, May 2021. URL: https://doi.org/10.1007/s10529-021-03151-9, doi:10.1007/s10529-021-03151-9. This article has 2 citations and is from a peer-reviewed journal.

2. (liu2021cryoemstudyon pages 1-4): Caixuan Liu, Huping Wang, Mingliang Jin, Wenyu Han, Shutian Wang, Yanxing Wang, Fangfang Wang, Chun Su, Xiaoyu Hong, Qiaoyu Zhao, and Yao Cong. Cryo-em study on the homo-oligomeric ring formation of yeast tric/cct subunits reveals tric ring assembly mechanism. bioRxiv, Feb 2021. URL: https://doi.org/10.1101/2021.02.24.432666, doi:10.1101/2021.02.24.432666. This article has 8 citations.

3. (que2024theroleof pages 2-4): Yueyue Que, Yudan Qiu, Zheyu Ding, Shanshan Zhang, Rong Wei, Jianing Xia, and Yingying Lin. The role of molecular chaperone cct/tric in translation elongation: a literature review. Heliyon, 10:e29029, Apr 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e29029, doi:10.1016/j.heliyon.2024.e29029. This article has 12 citations.

4. (dube2021chaperoninpointmutation pages 1-4): Ankita Dube and M. Anaul Kabir. Chaperonin point mutation enhances cadmium endurance in saccharomyces cerevisiae. Biotechnology Letters, 43:1735-1745, May 2021. URL: https://doi.org/10.1007/s10529-021-03151-9, doi:10.1007/s10529-021-03151-9. This article has 2 citations and is from a peer-reviewed journal.

5. (sergeeva2019coexpressionofcct pages 1-2): Oksana A. Sergeeva, Cameron Haase-Pettingell, and Jonathan A. King. Co-expression of cct subunits hints at tric assembly. Cell Stress and Chaperones, 24:1055-1065, Nov 2019. URL: https://doi.org/10.1007/s12192-019-01028-5, doi:10.1007/s12192-019-01028-5. This article has 18 citations and is from a peer-reviewed journal.

6. (kabir2005physiologicaleffectsof pages 1-2): M. Anaul Kabir, Joanna Kaminska, George B. Segel, Gabor Bethlendy, Paul Lin, Flavio Della Seta, Casey Blegen, Kristine M. Swiderek, Teresa ?o??dek, Kim T. Arndt, and Fred Sherman. Physiological effects of unassembled chaperonin cct subunits in the yeast saccharomyces cerevisiae. Yeast, 22:219-239, Feb 2005. URL: https://doi.org/10.1002/yea.1210, doi:10.1002/yea.1210. This article has 60 citations and is from a peer-reviewed journal.

7. (gvozdenov2024triccctchaperoningoverns pages 33-36): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

8. (kelly2020structuralandfunctional pages 28-35): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

9. (liu2023pathwayandmechanism pages 1-2): Caixuan Liu, Mingliang Jin, Shutian Wang, Wenyu Han, Qiaoyu Zhao, Yifan Wang, Cong Xu, Lei Diao, Yue Yin, Chao Peng, Lan Bao, Yanxing Wang, and Yao Cong. Pathway and mechanism of tubulin folding mediated by tric/cct along its atpase cycle revealed using cryo-em. Communications Biology, May 2023. URL: https://doi.org/10.1038/s42003-023-04915-x, doi:10.1038/s42003-023-04915-x. This article has 28 citations and is from a peer-reviewed journal.

10. (liu2023pathwayandmechanism media 86d3cbff): Caixuan Liu, Mingliang Jin, Shutian Wang, Wenyu Han, Qiaoyu Zhao, Yifan Wang, Cong Xu, Lei Diao, Yue Yin, Chao Peng, Lan Bao, Yanxing Wang, and Yao Cong. Pathway and mechanism of tubulin folding mediated by tric/cct along its atpase cycle revealed using cryo-em. Communications Biology, May 2023. URL: https://doi.org/10.1038/s42003-023-04915-x, doi:10.1038/s42003-023-04915-x. This article has 28 citations and is from a peer-reviewed journal.

11. (liu2023pathwayandmechanism media 483af941): Caixuan Liu, Mingliang Jin, Shutian Wang, Wenyu Han, Qiaoyu Zhao, Yifan Wang, Cong Xu, Lei Diao, Yue Yin, Chao Peng, Lan Bao, Yanxing Wang, and Yao Cong. Pathway and mechanism of tubulin folding mediated by tric/cct along its atpase cycle revealed using cryo-em. Communications Biology, May 2023. URL: https://doi.org/10.1038/s42003-023-04915-x, doi:10.1038/s42003-023-04915-x. This article has 28 citations and is from a peer-reviewed journal.

12. (junsun2024astructuralvista pages 1-2): Junsun Park, Hyunmin Kim, Daniel Gestaut, Seyeon Lim, Kwadwo A. Opoku-Nsiah, Alexander Leitner, Judith Frydman, and Soung-Hun Roh. A structural vista of phosducin-like phlp2a-chaperonin tric cooperation during the atp-driven folding cycle. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45242-x, doi:10.1038/s41467-024-45242-x. This article has 16 citations and is from a highest quality peer-reviewed journal.

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