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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_epsi. (IPR012718); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS.
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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: P40413
• Protein Description: RecName: Full=T-complex protein 1 subunit epsilon; Short=TCP-1-epsilon; AltName: Full=CCT-epsilon;
• Gene Information: Name=CCT5; Synonyms=TCP5; OrderedLocusNames=YJR064W; ORFNames=J1752;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_epsi. (IPR012718); 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 "CCT5" 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 'CCT5' 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 CCT5 (gene ID: CCT5, UniProt: P40413) 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: P40413
• Protein Description: RecName: Full=T-complex protein 1 subunit epsilon; Short=TCP-1-epsilon; AltName: Full=CCT-epsilon;
• Gene Information: Name=CCT5; Synonyms=TCP5; OrderedLocusNames=YJR064W; ORFNames=J1752;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_epsi. (IPR012718); 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 "CCT5" 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 'CCT5' 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 CCT5 (gene ID: CCT5, UniProt: P40413) 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: Functional Annotation of CCT5 (UniProt P40413) in Saccharomyces cerevisiae (S288c)

Executive summary

CCT5 (ORF YJR064W, synonym TCP5) encodes the epsilon subunit of the cytosolic group II chaperonin TRiC/CCT (also called the TCP‑1 ring complex). CCT5 is not an enzyme with a unique small-molecule substrate; rather, it is an ATP-binding/ATPase chaperonin subunit that contributes to an essential hetero-oligomeric folding machine that supports eukaryotic proteostasis, with strongest evidence for folding/biogenesis of actin and tubulin and for broad roles in assembly of WD40/propeller proteins and other complexes. Yeast genetic and structural studies implicate ATPase-competent CCT5 as critical for viability and for the ATP-driven conformational cycle of the TRiC/CCT chamber. Recent 2023–2024 cryo-EM work in the field (mostly in mammalian TRiC, plus yeast mechanistic cryo-EM studies) refined models for how the ATPase cycle drives substrate translocation and how co-chaperones (prefoldin, phosducin-like proteins) control substrate delivery and chamber occupancy—mechanistic context directly relevant to interpreting yeast CCT5’s function as part of TRiC/CCT. (stoldt1996reviewthecct pages 1-2, grantham2020themolecularchaperone pages 1-2, kelly2020structuralandfunctionala pages 42-48, liu2023pathwayandmechanism pages 1-2, junsun2024astructuralvista pages 1-2)

1. Target verification (critical identity disambiguation)

1.1 Verified gene/protein identity

The literature and yeast-specific reviews identify the S. cerevisiae epsilon subunit of the CCT/TRiC chaperonin as CCT5 (historical names include Cctε, TCP1E/TCP5) and explicitly map it to ORF YJR064W in S288c. (Publication date: 1996-05; URL: https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c) (stoldt1996reviewthecct pages 1-2)

1.2 Avoiding symbol ambiguity

The symbol CCT5 is also used for orthologous TRiC/CCT subunit 5 proteins in animals, where variants are associated with disease (e.g., hereditary sensory neuropathy). Such papers inform conserved structure/function of CCT5-family proteins but are not yeast-specific functional genetics and should not be conflated with S. cerevisiae phenotypes. (pereira2017structureofthe pages 1-2, kelly2020structuralandfunctionala pages 23-28)

2. Key concepts and definitions (current understanding)

2.1 TRiC/CCT: a eukaryotic group II chaperonin

TRiC/CCT is a group II chaperonin localized to the eukaryotic cytosol, consisting of two stacked rings with eight distinct paralogous subunits per ring (CCT1–CCT8; CCT5 is the epsilon/“subunit 5” paralog). The complex couples ATP binding/hydrolysis to large conformational changes that close a built-in lid over a central folding cavity (unlike bacterial GroEL, which requires GroES). (ghozlan2022thetrickybusiness pages 1-2, kabir2011functionalsubunitsof pages 1-2, kelly2020structuralandfunctionala pages 14-18)

2.2 What CCT5 “does” at the molecular level

CCT5 is best defined as a structural and catalytic component (ATPase + substrate-interaction surface) of TRiC/CCT rather than a standalone enzyme. TRiC/CCT’s strongest obligate substrates are actin and tubulin, which require TRiC/CCT to reach native conformations/assembly-competent states; CCT5 contributes one of the eight distinct apical-domain surfaces that form the composite substrate-binding environment within the chamber. (grantham2020themolecularchaperone pages 1-2, willison2018thesubstratespecificity pages 1-2)

2.3 Conserved domain architecture

CCT5-family subunits have a canonical chaperonin architecture with equatorial (ATP binding and ring contacts), intermediate (hinge/transmission), and apical (substrate recognition/lid) domains. The ATP-binding region is relatively conserved across paralogs, whereas apical domains are more divergent and contribute to subunit-specific substrate recognition properties. (ghozlan2022thetrickybusiness pages 1-2, pereira2017structureofthe pages 1-2)

3. Yeast-specific functional annotation of CCT5

3.1 Complex membership, subunit arrangement, and chamber electrostatics

Yeast TRiC/CCT structural work places subunits in a defined ring order and groups them into electrostatic “hemispheres” within the chamber; CCT5 sits in the CCT2 hemisphere alongside CCT4 and CCT2, contributing to a positively charged partition of the folding environment. (kelly2020structuralandfunctional pages 35-42)

3.2 ATPase asymmetry and subunit-specific conformational role of CCT5

In yeast structural/functional analyses, CCT5 belongs to a high ATP-affinity set of subunits (CCT1/2/4/5), with CCT5 (and CCT4) described as having the highest ATP affinities in one model. CCT5’s apical domain undergoes substantial nucleotide-linked motion (reported as ~14° rotation toward the folding cavity upon nucleotide binding), and CCT5 is among the subunits showing larger conformational changes than others in the ring. (kelly2020structuralandfunctionala pages 42-48)

3.3 Essentiality and viability-relevant mutations

Yeast-focused synthesis indicates that all eight CCT genes are essential and that even relatively small perturbations in ATP-binding motifs/ATPase kinetics can cause severe growth and morphology defects. (willison2018thesubstratespecificity pages 2-3)

More directly subunit-linked evidence indicates that mutating the P-loop ATP-binding motif (GDGTT→AAAAA) in high-affinity subunits leads to lethal phenotypes in yeast, implicating ATPase competence of high-affinity subunits including CCT5 as critical for viability. (kelly2020structuralandfunctionala pages 42-48)

3.4 Biological processes and pathway context inferred from yeast CCT/TRiC biology

Because CCT5 functions as an obligate TRiC/CCT subunit, yeast process annotations are best supported at the complex level:

• Actin and microtubule assembly / cytoskeletal organization: Yeast conditional mutant studies link the Cct complex to in vivo assembly of microtubules and actin, consistent with conserved TRiC/CCT roles in actin and tubulin folding. (1996-05; URL above) (stoldt1996reviewthecct pages 1-2)
• Genetic interactions with cytoskeletal alleles: Allele-specific synthetic interactions between CCT subunit mutants and actin/tubulin alleles (e.g., inviability of a cct1-1 tub2-402 double mutant) support close functional coupling between CCT and cytoskeletal components. (stoldt1996reviewthecct pages 5-6)
• Cell cycle regulation via folding of APC/C activators: A yeast CCT interactome/functional synthesis indicates that WD40/propeller proteins and specific cell-cycle regulators such as APC activators Cdc20p and Cdh1p are obligate CCT substrates in yeast. (willison2018thesubstratespecificity pages 1-2)
• Growth/nutrient signaling linkage (TOR pathway): Expert synthesis highlights TRiC/CCT’s functional linkage to TOR signaling in yeast, including growth defects when CCT activity is reduced and altered phosphorylation of TOR pathway outputs (S6K/S6). (kelly2020structuralandfunctionalb pages 23-28)

3.5 Subcellular localization

CCT5 acts primarily in the cytosol as part of the cytosolic TRiC/CCT folding machine. Current evidence in the retrieved set supports this cytosolic role; no strong evidence was retrieved for a stable organellar or secreted localization for yeast CCT5. (kabir2011functionalsubunitsof pages 1-2, kelly2020structuralandfunctionala pages 14-18)

4. Recent developments (prioritizing 2023–2024)

Recent high-resolution structural and mechanistic work has focused on TRiC/CCT’s ATP-driven cycle and co-chaperone coordination; while much of this is performed on mammalian TRiC, the mechanisms are widely treated as conserved and provide direct interpretive context for yeast subunit roles (including CCT5).

4.1 2023: Cryo-EM delineation of tubulin folding pathway along the ATPase cycle

A 2023 cryo-EM + XL-MS study captured multiple TRiC states with endogenously engaged tubulin and quantified state occupancies. Key reported quantitative findings include open-state classification with 61.6% empty and 38.4% tubulin-like density, and a trapped population with 27.2% both-rings-closed under ATP-AlFx. The work describes gradual substrate translocation/stabilization during ring closure and a near-native tubulin captured in the closed chamber; notably, the tubulin I domain is reported to associate more loosely with the CCT2 hemisphere subunits (CCT7/5/2/4)—the same hemisphere that includes yeast CCT5. (Publication date: 2023-05; URL: https://doi.org/10.1038/s42003-023-04915-x) (liu2023pathwayandmechanism pages 1-2, liu2023pathwayandmechanism pages 6-7)

4.2 2024: Structural mechanism for PhLP2A–TRiC coordination and prefoldin displacement

A 2024 Nature Communications cryo-EM/biochemical study resolved how PhLP2A binds open TRiC, how an N-terminal helix engages CCT3/CCT4 apical domains to displace prefoldin, and how ATP-induced closure rearranges PhLP2A contacts. The authors reiterate that TRiC facilitates folding of ~10% of the eukaryotic proteome and show a mechanistic model in which co-chaperones and substrates can segregate into opposing chambers during the folding cycle. (Publication date: 2024-02; URL: https://doi.org/10.1038/s41467-024-45242-x) (junsun2024astructuralvista pages 1-2)

Visual evidence: the paper includes a labeled cryo-EM view of the TRiC ring with subunits CCT1–CCT8 annotated, supporting the defined subunit arrangement that underpins any subunit-specific annotation. (junsun2024astructuralvista media 0880aeaf)

4.3 Yeast-focused mechanistic cryo-EM: ring opening intermediates (context)

A yeast TRiC cryo-EM study of ADP-bound ensembles reports a stepwise ring-opening model in which outward leaning involves consecutive subunits including CCT6/8/7/5, placing CCT5 on a mechanically relevant trajectory during nucleotide-dependent reopening and (putative) substrate release. (Publication: 2025; URL: https://doi.org/10.1017/qrd.2024.17) (jin2025theconformationallandscape pages 1-2)

5. Current applications and real-world implementations

Although yeast CCT5 itself is primarily a basic-science target, TRiC/CCT research has translational applications; yeast is often the model for mechanistic/functional dissection.

5.1 Therapeutic targeting and chemical modulation of TRiC/CCT

Expert syntheses describe TRiC/CCT as a potential therapeutic target in cancer and proteostasis-related diseases. Examples discussed include a TRiC-inhibiting peptide (CT20p) tested in cancer cell line contexts and small molecules/lipids reported to modulate TRiC-mediated folding (e.g., clemastine; 1-deoxydihydroceramide), as well as modulation by stress-response-linked factors (e.g., HSF1A). These applications are complex-level rather than yeast-CCT5-specific but rely on understanding subunit-specific assembly/ATPase features (including those involving CCT5). (kelly2020structuralandfunctionala pages 23-28, shen2025proteinfoldingby pages 5-7)

5.2 Proteostasis engineering and mechanistic tool development in yeast

Yeast serves as an engineering and discovery platform for TRiC/CCT structure-function studies, including strategies for subunit identification in cryo-EM maps by endogenous tagging approaches. Such methods enable subunit-resolved mechanistic annotation of components like CCT5 without overexpression artifacts. (Publication date: 2018-02; URL: https://doi.org/10.1038/s41598-017-18962-y) (context: subunit identification strategy applied to TRiC; CCT5 used as tagged subunit) (from retrieved paper list; not directly evidenced in snippets beyond abstract)

6. Statistics and quantitative data relevant to yeast CCT5 annotation

• Proteome fraction: TRiC/CCT is widely described as folding roughly ~10% of cytosolic proteins. (junsun2024astructuralvista pages 1-2, liu2023pathwayandmechanism pages 1-2)
• Yeast transcript estimate for CCT5: A yeast-focused synthesis reports an estimated CCT5 mRNA copy number ~2.24 per cell (derived from global transcript counts at 30°C) and notes low variance among CCT subunits in abundance. (Publication date: 2018-06; URL: https://doi.org/10.1098/rstb.2017.0192) (willison2018thesubstratespecificity pages 7-8)
• Yeast interactome scale: The yeast CCT interactome is summarized as roughly ~300 members, with many being cofactors/effectors rather than direct folding substrates, indicating extensive pathway connectivity beyond actin/tubulin. (willison2018thesubstratespecificity pages 2-3)

7. Interpretation and expert analysis (what is well-supported vs. uncertain for yeast CCT5)

7.1 High-confidence statements (supported directly)

• CCT5 is the S. cerevisiae TRiC/CCT epsilon subunit encoded by YJR064W. (stoldt1996reviewthecct pages 1-2)
• CCT5 participates in a cytosolic group II chaperonin complex essential for folding/biogenesis of actin and tubulin (complex-level function with strong yeast linkage). (stoldt1996reviewthecct pages 1-2, willison2018thesubstratespecificity pages 1-2)
• Yeast structural/functional analyses place CCT5 in a high ATP-affinity hemisphere and show large nucleotide-linked conformational change; yeast viability depends on ATPase-competent high-affinity subunits including CCT5 (P-loop mutant lethality). (kelly2020structuralandfunctionala pages 42-48)

7.2 Medium-confidence/inference statements

• Subunit-specific substrate recognition: Reviews emphasize that divergence in apical domains across the eight subunits confers substrate selectivity, implying that CCT5 contributes unique binding determinants. However, the retrieved yeast literature did not provide a CCT5-only substrate list; most substrate specificity is attributed to the assembled chamber interface. (willison2018thesubstratespecificity pages 1-2, ghozlan2022thetrickybusiness pages 1-2)

7.3 Not resolved in the retrieved corpus

• A dedicated, yeast-only experimental characterization of CCT5-specific phenotypes (e.g., temperature-sensitive cct5 alleles) was not retrieved here; available yeast phenotypes in the evidence largely pertain to the TRiC/CCT complex broadly or to other subunits. Accordingly, CCT5-specific phenotype statements above are restricted to ATP-binding motif perturbations and subunit-resolved structural dynamics. (kelly2020structuralandfunctionala pages 42-48, willison2018thesubstratespecificity pages 2-3)

Summary table

Table: This table summarizes verified identity, function, localization, and mechanistic evidence for Saccharomyces cerevisiae CCT5/YJR064W, emphasizing what is directly supported for the yeast subunit versus what is inferred from the TRiC/CCT complex. It also highlights recent 2023-2024 developments that refine the current mechanistic annotation of CCT5 within TRiC.

Key figures (visual evidence)

• Labeled TRiC subunit arrangement and PhLP2A-bound open-state structure (useful for orienting where CCT5 sits in the ring and how cochaperones engage the complex). (junsun2024astructuralvista media 0880aeaf)
• Comparative schematics of prefoldin and PhLP2A interactions with TRiC (relevant to understanding co-chaperone regulated folding pathways). (junsun2024astructuralvista media 774d2963, junsun2024astructuralvista media e727d38e)

References (URLs and publication dates from evidence)

• Stoldt V. et al. “Review: The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts.” Yeast 1996-05. https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c (stoldt1996reviewthecct pages 1-2)
• Willison K.R. “The substrate specificity of eukaryotic cytosolic chaperonin CCT.” Phil. Trans. R. Soc. B 2018-06. https://doi.org/10.1098/rstb.2017.0192 (willison2018thesubstratespecificity pages 7-8, willison2018thesubstratespecificity pages 2-3, willison2018thesubstratespecificity pages 1-2)
• Grantham J. “The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation.” Front. Genet. 2020-03. https://doi.org/10.3389/fgene.2020.00172 (grantham2020themolecularchaperone pages 1-2)
• Liu C. et al. “Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.” Communications Biology 2023-05. https://doi.org/10.1038/s42003-023-04915-x (liu2023pathwayandmechanism pages 1-2, liu2023pathwayandmechanism pages 6-7)
• Park J. et al. “A structural vista of phosducin-like PhLP2A–chaperonin TRiC cooperation during the ATP-driven folding cycle.” Nature Communications 2024-02. https://doi.org/10.1038/s41467-024-45242-x (junsun2024astructuralvista pages 1-2, junsun2024astructuralvista media 0880aeaf)

References

1. (stoldt1996reviewthecct pages 1-2): Volker Stoldt, Felicitas Rademacher, Verena Kehren, Joachim F. Ernst, David A. Pearce, and Fred Sherman. Review: the cct eukaryotic chaperonin subunits of saccharomyces cerevisiae and other yeasts. Yeast, 12:523-529, May 1996. URL: https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c, doi:10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c. This article has 153 citations and is from a peer-reviewed journal.

2. (grantham2020themolecularchaperone pages 1-2): Julie Grantham. The molecular chaperone cct/tric: an essential component of proteostasis and a potential modulator of protein aggregation. Frontiers in Genetics, Mar 2020. URL: https://doi.org/10.3389/fgene.2020.00172, doi:10.3389/fgene.2020.00172. This article has 139 citations and is from a peer-reviewed journal.

3. (kelly2020structuralandfunctionala pages 42-48): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

4. (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.

5. (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.

6. (pereira2017structureofthe pages 1-2): Jose H. Pereira, Ryan P. McAndrew, Oksana A. Sergeeva, Corie Y. Ralston, Jonathan A. King, and Paul D. Adams. Structure of the human tric/cct subunit 5 associated with hereditary sensory neuropathy. Scientific Reports, Jun 2017. URL: https://doi.org/10.1038/s41598-017-03825-3, doi:10.1038/s41598-017-03825-3. This article has 43 citations and is from a peer-reviewed journal.

7. (kelly2020structuralandfunctionala pages 23-28): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

8. (ghozlan2022thetrickybusiness pages 1-2): Heba Ghozlan, Amanda Cox, Daniel Nierenberg, Stephen King, and Annette R. Khaled. The tricky business of protein folding in health and disease. Frontiers in Cell and Developmental Biology, May 2022. URL: https://doi.org/10.3389/fcell.2022.906530, doi:10.3389/fcell.2022.906530. This article has 34 citations.

9. (kabir2011functionalsubunitsof pages 1-2): M. Anaul Kabir, Wasim Uddin, Aswathy Narayanan, Praveen Kumar Reddy, M. Aman Jairajpuri, Fred Sherman, and Zulfiqar Ahmad. Functional subunits of eukaryotic chaperonin cct/tric in protein folding. Journal of Amino Acids, 2011:1-16, Jul 2011. URL: https://doi.org/10.4061/2011/843206, doi:10.4061/2011/843206. This article has 62 citations.

10. (kelly2020structuralandfunctionala pages 14-18): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

11. (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.

12. (kelly2020structuralandfunctional pages 35-42): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

13. (willison2018thesubstratespecificity pages 2-3): 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.

14. (stoldt1996reviewthecct pages 5-6): Volker Stoldt, Felicitas Rademacher, Verena Kehren, Joachim F. Ernst, David A. Pearce, and Fred Sherman. Review: the cct eukaryotic chaperonin subunits of saccharomyces cerevisiae and other yeasts. Yeast, 12:523-529, May 1996. URL: https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c, doi:10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c. This article has 153 citations and is from a peer-reviewed journal.

15. (kelly2020structuralandfunctionalb pages 23-28): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

16. (liu2023pathwayandmechanism pages 6-7): 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.

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