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gene_id: TCP1
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gene_info: Name=TCP1; Synonyms=CCT1; OrderedLocusNames=YDR212W; ORFNames=YD8142.13,
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organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
protein_family: Belongs to the TCP-1 chaperonin family. .
protein_domains: Chap_CCT_alpha. (IPR012715); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS.
(IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)
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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: P12612
• Protein Description: RecName: Full=T-complex protein 1 subunit alpha; Short=TCP-1-alpha; AltName: Full=CCT-alpha;
• Gene Information: Name=TCP1; Synonyms=CCT1; OrderedLocusNames=YDR212W; ORFNames=YD8142.13, YD8142B.04;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_alpha. (IPR012715); 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 "TCP1" 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 'TCP1' 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 TCP1 (gene ID: TCP1, UniProt: P12612) 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: P12612
• Protein Description: RecName: Full=T-complex protein 1 subunit alpha; Short=TCP-1-alpha; AltName: Full=CCT-alpha;
• Gene Information: Name=TCP1; Synonyms=CCT1; OrderedLocusNames=YDR212W; ORFNames=YD8142.13, YD8142B.04;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_alpha. (IPR012715); 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 "TCP1" 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 'TCP1' 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 TCP1 (gene ID: TCP1, UniProt: P12612) 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 TCP1/CCT1 (UniProt P12612) — functional annotation

0) Target verification (critical disambiguation)

The UniProt entry provided (P12612) describes T-complex protein 1 subunit alpha (also called TCP-1-alpha, CCT-alpha) encoded by TCP1 (synonym CCT1) in Saccharomyces cerevisiae S288c. The literature gathered here consistently uses TCP1/CCT1 to refer to the CCT/TRiC cytosolic group II chaperonin subunit (not unrelated “TCP1” symbols in other organisms), including yeast genetics that explicitly uses a cct1-2 temperature-sensitive allele to perturb TRiC/CCT function. (gvozdenov2024triccctchaperoningoverns pages 30-33, narayanan2021sorbitolandpkc1 pages 1-3)

Limitation: within the retrieved full-text corpus, I did not find an explicit string mapping (e.g., “UniProt P12612” or “YDR212W”) inside the papers; thus, the identifier-level mapping to P12612/YDR212W is taken from the user-provided UniProt record, while mechanistic/functional claims are supported by peer-reviewed literature on yeast CCT1/TCP1. (gvozdenov2024triccctchaperoningoverns pages 30-33, narayanan2021sorbitolandpkc1 pages 1-3)

1) Key concepts and current understanding (definitions and mechanism)

1.1 What TCP1/CCT1 is

TCP1/CCT1 encodes CCT1 (TCP-1; CCT-alpha), one of eight paralogous subunits that assemble into the eukaryotic cytosolic chaperonin TRiC/CCT. TRiC/CCT is a ~1 MDa ATP-dependent double-ring machine, with eight distinct subunits per ring (CCT1–CCT8), and each subunit has apical/intermediate/equatorial domains; the equatorial domain binds ATP and supports ring assembly, while apical surfaces mediate substrate recognition and the built-in lid. (gestaut2019theatppoweredgymnastics pages 1-2, que2024theroleof pages 2-4, willison2018thesubstratespecificity pages 1-2)

1.2 What TRiC/CCT does (primary molecular function)

TRiC/CCT’s primary biological function is ATP-coupled folding (and in some cases assembly/biogenesis) of a select set of cytosolic proteins, especially those that are topologically complex and aggregation-prone. Substrates bind TRiC in non-native conformations; ATP binding/hydrolysis drives conformational changes that close the chamber and promote productive folding. (gestaut2019theatppoweredgymnastics pages 1-2, gestaut2019theatppoweredgymnastics pages 4-5)

Quantitatively, TRiC/CCT is commonly estimated to engage on the order of ~10% of cytosolic proteins (review-level estimate), reflecting a substantial but selective role in proteostasis. (que2024theroleof pages 2-4, gestaut2019theatppoweredgymnastics pages 4-5)

1.3 Subunit specialization and what “CCT1-specific” means

TRiC/CCT subunits are not redundant: subunit diversification creates asymmetry in ATP binding/allostery and in substrate-recognition surfaces. A key mechanistic concept is a hierarchy of ATP affinities across subunits; in one model, the “high-affinity hemisphere” includes CCT5, CCT4, CCT1, and CCT2, which initiates ATP-driven conformational transitions. (gestaut2019theatppoweredgymnastics pages 4-5)

2) Molecular function and substrate/client specificity (yeast-focused)

2.1 Core/obligate clients

In budding yeast and across eukaryotes, the most established obligate clients of TRiC/CCT are actin and tubulin, which require TRiC/CCT to reach native, functional states. (willison2018thesubstratespecificity pages 1-2, gestaut2019theatppoweredgymnastics pages 4-5)

2.2 WD40/β-propeller proteins and cell-cycle regulation

A major additional client class is WD40-repeat β-propeller proteins. In yeast, TRiC/CCT is reported as the only known folding pathway producing functional, active Cdh1p and Cdc20p (APC/C coactivators that are WD40 propellers), linking TRiC directly to cell-cycle control via APC/C regulation. (willison2018thesubstratespecificity pages 6-6, willison2018thesubstratespecificity pages 1-2)

In a targeted analysis of yeast 7-bladed WD40 proteins (plus one 8-bladed WD40 protein), many showed some binding to CCT, but only a subset were strong interactors (including Cdh1p and Cdc20p), consistent with a restricted substrate spectrum rather than generic folding of all WD40 proteins. (willison2018thesubstratespecificity pages 5-6)

2.3 Substrate-binding logic

Substrate specificity is driven largely by apical domain surfaces that differ among subunits, enabling polyvalent, subunit-selective binding. Review synthesis emphasizes that TRiC tends to fold proteins enriched in β-structure/topological complexity and that it can act as a folding machine and/or a regulated holding/assembly platform for some propellers. (gestaut2019theatppoweredgymnastics pages 4-5, willison2018thesubstratespecificity pages 5-6, monkemeyer2019structuralandfunctional pages 29-31)

3) Cellular localization and where TCP1/CCT1 acts

3.1 Canonical localization: cytosol

TRiC/CCT is classically a cytosolic chaperonin, functioning co- and post-translationally in general proteostasis and in cytoskeletal protein biogenesis (actin/tubulin). (que2024theroleof pages 2-4, willison2018thesubstratespecificity pages 1-2)

3.2 Emerging localization/function: nucleus (2024 preprint)

Recent work in budding yeast reports an assembled TRiC/CCT pool in the nucleus (supported by GFP-tagged subunits and biochemical fractionation/SEC consistent with a ~1 MDa holo-complex in nuclear fractions), and uses the cct1-2 allele to show nuclear TRiC/CCT modulates RNA polymerase II activity and RNA homeostasis. (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 13-17)

4) Pathways and biological processes involving TCP1/CCT1

4.1 Proteostasis networks and translation-coupled folding

CCT/TRiC is discussed as a major ribosome-associated chaperone within the CLIPS (Chaperones Linked to Protein Synthesis) network, connecting TCP1/CCT1 function to translation elongation and nascent-chain maturation. (que2024theroleof pages 2-4)

4.2 Cell cycle control via folding of APC/C coactivators

By folding the WD40 propeller proteins Cdh1p and Cdc20p, TRiC/CCT contributes directly to APC/C function and thus cell-cycle progression. (willison2018thesubstratespecificity pages 6-6, willison2018thesubstratespecificity pages 1-2)

4.3 Cell wall integrity and stress signaling (phenotype-based linkage)

A yeast cct1-2 mutant shows sensitivity to cell-wall stress agents (SDS, congo red), and its temperature sensitivity is suppressed by 1 M sorbitol or PKC1 overexpression (PKC1 is a key regulator of the yeast cell wall integrity pathway). This supports a functional link between TRiC/CCT proteostasis and maintenance of cell wall integrity, likely via folding/biogenesis of proteins required for cell wall homeostasis. (narayanan2021sorbitolandpkc1 pages 1-3)

4.4 RNA homeostasis / transcriptional control (2024 preprint)

In the 2024 preprint, TRiC/CCT inactivation using cct1-2 causes widespread transcriptional/RNA anomalies, including extensive accumulation of cryptic/noncoding RNAs and increased intergenic transcription. The authors propose TRiC acts as an RNAPII “rheostat” linking proteostasis state to transcriptional output. (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 13-17)

5) Recent developments (prioritizing 2023–2024)

5.1 ATP-driven folding cycle and cochaperone coordination (2024)

High-resolution cryo-EM and crosslinking mass spectrometry has advanced mechanistic understanding of how TRiC cooperates with cochaperones (e.g., prefoldin and phosducin-like proteins). In particular, 2024 structural work shows an ATP-driven cycle in which PhLP2A binds open TRiC via subunit-selective contacts and rearranges upon chamber closure; in substrate-containing complexes, inner-surface contacts involve a subset of subunits including CCT1. (junsun2024astructuralvista pages 1-2)

5.2 Subunit-specific contacts involving CCT1 (2024)

The 2024 Nature Communications study reports that actin and/or PhLP2A engage positively charged chamber-facing residues from CCT1/CCT3/CCT6/CCT8, and crosslinks can place cochaperone helices proximal to CCT1 cavity-facing residues, supporting direct involvement of CCT1 surfaces in substrate/cochaperone positioning inside the folding chamber. (junsun2024astructuralvista pages 1-2)

5.3 Mechanochemistry in yeast: nucleotide exchange kinetics (2023)

A 2023 yeast kinetic analysis of a disease-linked CCT2 double mutation shows that slowing ADP off-rate can stabilize the closed state and that TRiC ATPase activity is stimulated by a non-folded substrate. Although this work is on CCT2, it strengthens the mechanistic framework for how the TRiC ATPase cycle (in which CCT1 is part of the high-affinity hemisphere) couples nucleotide exchange to folding output. (roy2023reducedadpoffrate pages 1-2, gestaut2019theatppoweredgymnastics pages 4-5)

5.4 Substrate folding intermediates visualized by cryo-EM (2023)

A 2023 cryo-EM ensemble of substrate-engaged TRiC states (human endogenous TRiC with tubulin) provides a modern reference trajectory for how substrates move and stabilize during ring closure across the ATPase cycle. While not yeast-specific, the mechanism supports functional inference for yeast TCP1/CCT1 as part of the conserved folding machine for tubulin-class substrates. (liu2023pathwayandmechanism pages 1-2)

6) Quantitative data and statistics (from recent and authoritative sources)

6.1 Client fraction / proteome coverage

CCT/TRiC is commonly estimated to assist folding/maturation of ~10% of cytoplasmic proteins (review synthesis). (que2024theroleof pages 2-4, gestaut2019theatppoweredgymnastics pages 4-5)

6.2 Yeast expression proxies (mRNA copy number estimates)

A quantitative figure caption in an authoritative substrate-specificity review reports yeast mRNA copy-number estimates: TCP1 ~1.81 mRNA copies/cell, with similar magnitudes for other CCT subunits, and much higher values for abundant clients such as ACT1 ~28.97 and TUB2 ~5.94. (willison2018thesubstratespecificity media 549e9c0a, willison2018thesubstratespecificity media 4a831a29)

6.3 Yeast nuclear transcription phenotypes (2024 preprint)

In the cct1-2 mutant background, the preprint reports strong genome-wide RNA effects. Examples include: intergenic coverage increasing dramatically, and a substantial fraction of the genome exhibiting strong nascent-RNA increases (e.g., ~22.8% of the genome meeting a ≥4-fold threshold for increased nascent RNAs in one analysis), plus measurable readthrough/termination defects at subsets of snoRNA loci. (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 13-17)

7) Current applications and real-world implementations

7.1 Yeast as an experimental platform for chaperonin biology (and disease-linked mechanisms)

Temperature-sensitive yeast TRiC mutants (including cct1-2) are used as tractable tools for genetic suppression screens and pathway probing, as demonstrated by suppression of cct phenotypes via osmotic stabilization or PKC1 overexpression. This is a concrete real-world implementation of TCP1/CCT1 genetics for dissecting cellular proteostasis and stress pathways. (narayanan2021sorbitolandpkc1 pages 1-3)

7.2 Informing intervention strategies by resolving substrate-specific interactions

Modern structural studies of TRiC with clients/cochaperones are explicitly discussed as informing design of agents targeting TRiC–substrate interactions (e.g., in tubulin folding contexts). While this is largely developed in mammalian systems, it represents translationally oriented use of TRiC mechanistic knowledge enabled by conserved chaperonin architecture that includes CCT1/CCT-alpha. (liu2023pathwayandmechanism pages 1-2)

8) Expert synthesis and interpretation (authoritative perspectives)

A consistent expert view is that TRiC/CCT is a specialist folding machine (not a generalist chaperone), focusing on a restricted client set enriched for difficult-to-fold, aggregation-prone, β-structure-rich proteins, and that subunit diversification (including CCT1) is central to this specialization via asymmetric ATP allostery and subunit-specific binding surfaces. (gestaut2019theatppoweredgymnastics pages 4-5, willison2018thesubstratespecificity pages 7-8, monkemeyer2019structuralandfunctional pages 29-31)

9) Summary evidence map (key sources)

The following table lists the most relevant recent and foundational sources used for this annotation, emphasizing 2023–2024 where available.

Table: This table summarizes the most relevant recent and foundational sources for annotating yeast TCP1/CCT1 as a TRiC/CCT subunit. It highlights what each paper contributes to understanding molecular function, subunit-specific roles, and cellular pathways.

A yeast-focused evidence map of TCP1/CCT1 functional annotation categories is provided here.

Table: This table summarizes the most relevant functional annotation points for yeast TCP1/CCT1, organized by molecular role, clients, localization, pathways, phenotypes, and quantitative evidence. It is designed as a compact evidence map for building the final research report.

10) References (URLs and dates from retrieved corpus)

• Willison KR. 2018-06. Phil Trans R Soc B “The substrate specificity of eukaryotic cytosolic chaperonin CCT”. https://doi.org/10.1098/rstb.2017.0192 (willison2018thesubstratespecificity pages 6-6, willison2018thesubstratespecificity pages 1-2)
• Gestaut D, Limatola A, Joachimiak L, Frydman J. 2019-04. Curr Opin Struct Biol “The ATP-powered gymnastics of TRiC/CCT…”. https://doi.org/10.1016/j.sbi.2019.03.002 (gestaut2019theatppoweredgymnastics pages 1-2, gestaut2019theatppoweredgymnastics pages 4-5)
• Liu C 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)
• Roy M et al. 2023-08. Communications Biology “Reduced ADP off-rate by the yeast CCT2 double mutation…”. https://doi.org/10.1038/s42003-023-05261-8 (roy2023reducedadpoffrate pages 1-2)
• Park J 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)
• Que Y et al. 2024-04. Heliyon “The role of molecular chaperone CCT/TRiC in translation elongation: A literature review”. https://doi.org/10.1016/j.heliyon.2024.e29029 (que2024theroleof pages 2-4)
• Gvozdenov Z et al. 2024-09. bioRxiv preprint “TRiC/CCT chaperonin governs RNA polymerase II activity in the nucleus…”. https://doi.org/10.1101/2024.09.26.615188 (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 13-17)
• Narayanan A, Kabir MA. 2021-08. microPublication Biology “Sorbitol and PKC1 overexpression alleviate temperature sensitivity in chaperonin mutants…”. https://doi.org/10.17912/micropub.biology.000440 (narayanan2021sorbitolandpkc1 pages 1-3)

References

1. (gvozdenov2024triccctchaperoningoverns pages 30-33): 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.

2. (narayanan2021sorbitolandpkc1 pages 1-3): Aswathy Narayanan and M. Anaul Kabir. Sorbitol and pkc1 overexpression alleviate temperature sensitivity in chaperonin mutants of saccharomyces cerevisiae. microPublication Biology, Aug 2021. URL: https://doi.org/10.17912/micropub.biology.000440, doi:10.17912/micropub.biology.000440. This article has 1 citations.

3. (gestaut2019theatppoweredgymnastics pages 1-2): Daniel Gestaut, Antonio Limatola, Lukasz Joachimiak, and Judith Frydman. The atp-powered gymnastics of tric/cct: an asymmetric protein folding machine with a symmetric origin story. Current opinion in structural biology, 55:50-58, Apr 2019. URL: https://doi.org/10.1016/j.sbi.2019.03.002, doi:10.1016/j.sbi.2019.03.002. This article has 106 citations and is from a peer-reviewed journal.

4. (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.

5. (willison2018thesubstratespecificity pages 1-2): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

6. (gestaut2019theatppoweredgymnastics pages 4-5): Daniel Gestaut, Antonio Limatola, Lukasz Joachimiak, and Judith Frydman. The atp-powered gymnastics of tric/cct: an asymmetric protein folding machine with a symmetric origin story. Current opinion in structural biology, 55:50-58, Apr 2019. URL: https://doi.org/10.1016/j.sbi.2019.03.002, doi:10.1016/j.sbi.2019.03.002. This article has 106 citations and is from a peer-reviewed journal.

7. (willison2018thesubstratespecificity pages 6-6): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

8. (willison2018thesubstratespecificity pages 5-6): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

9. (monkemeyer2019structuralandfunctional pages 29-31): Leonie Mönkemeyer. Structural and functional studies on the eukaryotic chaperonin tric/cct and its cooperating chaperone hgh1. Dissertation, Jan 2019. URL: https://doi.org/10.5282/edoc.23750, doi:10.5282/edoc.23750. This article has 0 citations.

10. (gvozdenov2024triccctchaperoningoverns pages 6-9): 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.

11. (gvozdenov2024triccctchaperoningoverns pages 13-17): 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.

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.

13. (roy2023reducedadpoffrate pages 1-2): Mousam Roy, Rachel C. Fleisher, Alexander I. Alexandrov, and Amnon Horovitz. Reduced adp off-rate by the yeast cct2 double mutation t394p/r510h which causes leber congenital amaurosis in humans. Communications Biology, Aug 2023. URL: https://doi.org/10.1038/s42003-023-05261-8, doi:10.1038/s42003-023-05261-8. This article has 9 citations and is from a peer-reviewed journal.

14. (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.

15. (willison2018thesubstratespecificity media 549e9c0a): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

16. (willison2018thesubstratespecificity media 4a831a29): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

17. (willison2018thesubstratespecificity pages 7-8): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

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