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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
CCT6 (YDR188W; UniProt P39079) encodes T-complex protein 1 subunit zeta (Cct6p; also called CCT-ζ), one of eight paralogous subunits that assemble into the essential cytosolic group II chaperonin TRiC/CCT. TRiC/CCT is a ~1 MDa ATP-dependent double-ring folding machine required for maturation of a specific subset of eukaryotic proteins—classically actin and tubulin—and is estimated to mediate folding of roughly ~10% of newly synthesized polypeptides in yeast. Yeast genetics further indicates that CCT6 is essential, and that excess/unassembled Cct6p (produced by overexpression) can suppress multiple conditional growth defects in otherwise unrelated pathways (TOR signaling, trafficking/vacuole/cell wall, ubiquitin ligase function), implying physiologically meaningful activity beyond (or in addition to) the assembled TRiC complex. Recent 2023–2024 studies refine TRiC allostery/ATPase kinetics, connect TRiC malfunction to stress-response pathways (e.g., cell-wall integrity MAPK signaling), and expand the functional landscape to include nuclear roles for TRiC in transcriptional homeostasis; however, these advances are mostly complex-level and not uniquely CCT6-subunit–specific. (grantham2020themolecularchaperone pages 1-2, dube2023saccharomycescerevisiaesurvival pages 1-4, kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)
| Claim/Topic | Key evidence (short) | Organism/system | Source (author year) | Publication date | URL/DOI | Notes/caveats |
|---|---|---|---|---|---|---|
| Identity / disambiguation | Yeast CCT6 / YDR188W / UniProt P39079 encodes T-complex protein 1 subunit zeta (Cct6p), one of the eight paralogous subunits of the eukaryotic cytosolic group II chaperonin TRiC/CCT; literature here refers to the yeast chaperonin subunit, not mammalian CCT6A/B paralogs (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4) | Saccharomyces cerevisiae | Kabir et al. 2005 | 2005-02 | https://doi.org/10.1002/yea.1210 | Older but yeast-specific foundational annotation; important because CCT6 is ambiguous across organisms. |
| Complex membership | TRiC/CCT is a ~1 MDa double-ring complex with two stacked octameric rings; each ring contains CCT1–CCT8 in fixed order, with CCT6 as one subunit (grantham2020themolecularchaperone pages 1-2, zang2018developmentofa pages 1-2) | Yeast TRiC/CCT / eukaryotic TRiC | Grantham 2020; Zang et al. 2018 | 2020-03; 2018-02 | https://doi.org/10.3389/fgene.2020.00172 ; https://doi.org/10.1038/s41598-017-18962-y | Complex-level function is better established than isolated Cct6p-specific biochemistry. |
| Essentiality | All eight yeast CCT1–CCT8 genes are essential; disruption experiments showed each is required, including CCT6 (kabir2008overexpressedribosomalproteins pages 1-2, kabir2005physiologicaleffectsof pages 2-4) | S. cerevisiae | Kabir & Sherman 2008; Kabir et al. 2005 | 2008-12; 2005-02 | https://doi.org/10.1111/j.1567-1364.2008.00425.x ; https://doi.org/10.1002/yea.1210 | Essentiality is gene-level; not every subunit’s ATPase chemistry is equally essential. |
| Canonical substrates / primary function | TRiC/CCT performs ATP-dependent folding of obligate cytosolic substrates, especially actin and tubulin; CCT is required for tubulin biogenesis and actin folding, providing the main functional context for CCT6 (grantham2020themolecularchaperone pages 1-2, kelly2020structuralandfunctional pages 18-23, willison2018thestructureand pages 1-2) | Eukaryotic cytosol; yeast-focused review context | Grantham 2020; Kelly 2020; Willison 2018 | 2020-03; 2020; 2018-10 | https://doi.org/10.3389/fgene.2020.00172 ; n/a ; https://doi.org/10.1042/BCJ20170378 | Evidence is strongest at complex level; direct yeast Cct6-substrate specificity remains less resolved than for the complex as a whole. |
| ATPase / hemisphere specialization | CCT6 belongs to the low-ATP-affinity hemisphere (with CCT3/6/7/8); sequence divergence near the nucleotide pocket and structural analyses suggest lower nucleotide exchange, and P-loop alanine substitutions in low-affinity subunits had little growth effect relative to high-affinity subunits (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48) | Yeast TRiC/CCT | Kelly 2020 | 2020 | n/a | Strong structural/kinetic inference; thesis source, but evidence summarized from cryo-EM, nucleotide assays, and yeast mutational work. |
| CCT6-specific ATP-cycle nuance | Cct6p is described as a low-affinity/low-turnover subunit; one source notes Cct6p and Cct8p remain ADP-bound and do not participate like high-affinity subunits, and a glycine-motif mutation analogous to ts mutations in other subunits did not impair growth when introduced in Cct6p (dube2021chaperoninpointmutation pages 1-4) | S. cerevisiae CCT | Dube & Kabir 2021 | 2021-05 | https://doi.org/10.1007/s10529-021-03151-9 | Useful subunit-specific nuance, but based on synthesis of prior work rather than a direct dedicated CCT6 biochemical paper. |
| Subunit position / structure | Cryo-EM with internal eGFP labeling (YISEL) assigned CCT6 as an on-axis subunit (a5 / subunit 6) in yeast TRiC and helped define full subunit order; CCT6 contributes to the characteristic Z-shaped on-axis pair geometry (zang2018developmentofa pages 1-2, zang2018developmentofa media 20a150a9) | Yeast TRiC/CCT | Zang et al. 2018 | 2018-02 | https://doi.org/10.1038/s41598-017-18962-y | Structural assignment is direct and yeast-specific. |
| Inter-ring structural role | Structural analyses indicate the N-terminus of CCT6 participates in inter-ring interactions/stacking during TRiC closure, supporting a role in conformational locking rather than being a dominant ATP-hydrolyzing driver (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48) | Yeast TRiC/CCT | Kelly 2020 | 2020 | n/a | Mechanistic inference from structures and comparative mutational studies. |
| Unassembled Cct6 suppressor activity | Overexpression of CCT6 increases unassociated Cct6p, not total assembled CCT complex, and this excess subunit suppresses diverse conditional phenotypes (tor2-21, lst8-2, rsp5-9, [SIT4 SAP155]N) (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4) | S. cerevisiae genetics | Kabir et al. 2005 | 2005-02 | https://doi.org/10.1002/yea.1210 | Important evidence that Cct6p may have physiologically relevant extra-complex activity or sequestration/competition effects. |
| Requirement for ATP-binding motif in suppressor function | The cct6-24 mutant with GDGTT→AAAAA replacement in the conserved ATP-binding motif was unable to suppress those conditional traits, despite supporting growth, implying suppression depends on a specific functional state of unassembled Cct6p (kabir2005physiologicaleffectsof pages 1-2) | S. cerevisiae | Kabir et al. 2005 | 2005-02 | https://doi.org/10.1002/yea.1210 | Strong evidence for separable roles: viability of mutant allele vs loss of suppressor activity. |
| Genetic phenotypes / ts alleles | Multiple temperature-sensitive cct6 alleles were reported (e.g., cct6-14, -18, -27, -74, -85, -93, -97), many with TBZ sensitivity and some with NaCl sensitivity, consistent with roles in microtubule/actin-related processes (kabir2008overexpressedribosomalproteins pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3) | S. cerevisiae | Kabir & Sherman 2008 | 2008-12 | https://doi.org/10.1111/j.1567-1364.2008.00425.x | Phenotypes derive from legacy allele collections; not all were mechanistically dissected. |
| Multicopy suppressors of cct defects | Kabir & Sherman isolated 22 multicopy suppressors of a cct4 ts allele; 14 encoded ribosomal proteins, and some suppressors also acted on certain cct6 mutants, suggesting overexpressed ribosomal proteins can weakly buffer defective chaperonins (kabir2008overexpressedribosomalproteins pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3) | S. cerevisiae | Kabir & Sherman 2008 | 2008-12 | https://doi.org/10.1111/j.1567-1364.2008.00425.x | Indirectly informative for CCT6 buffering/genetic interaction space. |
| CCT6 vs CCT3 subunit-specific interactome effects | A conserved ATP-site Glu→Asp mutation in CCT6 was compared with CCT3 in high-throughput microscopy; each mutant produced distinct proteome-level effects, and CCT3 showed stronger association with Q/N-rich proteins/P-body phenotypes than CCT6 (nadlerholly2012interactionsofsubunit pages 1-2) | S. cerevisiae | Nadler-Holly et al. 2012 | 2012-11 | https://doi.org/10.1073/pnas.1209277109 | Useful because it argues subunit specialization; CCT6 phenotype was milder/different than CCT3 for this substrate class. |
| Cytosolic localization / classical role | TRiC/CCT is classically a cytosolic folding machine in yeast/eukaryotes, accounting for ~10% of new polypeptide maturation; this is the best-supported localization/function for Cct6p as part of the holo-complex (gvozdenov2024triccctchaperoningoverns pages 1-6, dube2023saccharomycescerevisiaesurvival pages 1-4) | Yeast / eukaryotic cytosol | Gvozdenov et al. 2024; Dube et al. 2023 | 2024-09-26; 2023-11 | https://doi.org/10.1101/2024.09.26.615188 ; https://doi.org/10.1007/s42977-023-00192-1 | Dube 2023 is about CCT7 mutant, but explicitly states yeast TRiC/CCT is cytosolic and folds ~10% of polypeptides. |
| Nuclear localization / emerging role | Recent work shows TRiC/CCT is also present in the nucleus and can regulate RNA polymerase II activity and nascent RNA homeostasis; this extends likely functional context for all subunits including CCT6, though not yet CCT6-specific (gvozdenov2024triccctchaperoningoverns pages 1-6) | S. cerevisiae | Gvozdenov et al. 2024 | 2024-09-26 | https://doi.org/10.1101/2024.09.26.615188 | Preprint; compelling for nuclear TRiC, but not direct evidence that CCT6 alone mediates the effect. |
| Recent development: stress/pathway crosstalk | A 2023 yeast study showed a cct7 folding-defective mutant is heat- and cell-wall-stress sensitive and is rescued by PKC1/SLT2, supporting crosstalk between CCT proteostasis and the cell wall integrity (CWI) MAPK pathway (dube2023saccharomycescerevisiaesurvival pages 1-4) | S. cerevisiae | Dube et al. 2023 | 2023-11 | https://doi.org/10.1007/s42977-023-00192-1 | Not CCT6-specific, but relevant recent pathway context for the complex in yeast. |
| Recent development: kinetic mechanism | A 2023 yeast study on CCT2 found reduced ADP off-rate in a disease-linked mutant and quantified WT ATPase behavior (K1 ~8.3 µM, K2 ~110 µM; kcat ~0.043–0.053 s^-1), reinforcing asymmetric ATPase cycling within yeast TRiC relevant to low-affinity subunits such as CCT6 (roy2023reducedadpoffrate pages 1-2, kelly2020structuralandfunctional pages 42-48) | Yeast TRiC/CCT | Roy et al. 2023; Kelly 2020 | 2023-08; 2020 | https://doi.org/10.1038/s42003-023-05261-8 ; n/a | Quantitative kinetics are for CCT2/whole complex, not directly for CCT6, but they support the asymmetric ring model. |
| Recent development: cochaperone cooperation | 2024 cryo-EM/XL-MS work showed PhLP2A and substrate actin occupy opposing TRiC chambers; actin/PhLP2A contact positively charged inner-surface residues from CCT1/3/6/8, implicating CCT6 directly in the substrate/cochaperone folding chamber interface (junsun2024astructuralvista pages 1-2) | Purified TRiC system | Park et al. 2024 | 2024-02 | https://doi.org/10.1038/s41467-024-45242-x | Strong recent mechanistic evidence, though not yeast-specific in organism designation. |
Table: This table summarizes experimentally supported functional annotation evidence for yeast CCT6/YDR188W/P39079, emphasizing identity verification, complex role, subunit specialization, genetics, localization, and 2023-2024 developments. It is useful as a compact evidence map for building a narrative report while keeping organism-specific claims separate from broader TRiC/CCT findings.
The target is yeast CCT6 (ordered locus name YDR188W; UniProt P39079), a TRiC/CCT subunit (Cct6p). Yeast-focused primary literature explicitly treats CCT6 as a chaperonin subunit gene and performs yeast genetics with cct6 alleles and CCT6 overexpression constructs, consistent with the UniProt record and domain/family assignment (TCP-1 chaperonin family). (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)
TRiC/CCT (TCP-1 Ring Complex / Chaperonin Containing TCP-1) is an essential eukaryotic chaperonin that forms two stacked rings, each ring containing eight different subunits (CCT1–CCT8) in a fixed arrangement, producing a central chamber where folding can proceed under “caged” conditions coupled to an ATP-driven conformational cycle. (grantham2020themolecularchaperone pages 1-2, gvozdenov2024triccctchaperoningoverns pages 1-6)
For functional annotation, the most defensible “primary function” for CCT6 is: a structural/ATPase subunit of the TRiC/CCT chaperonin that contributes to ATP-dependent folding and maturation of obligate cytosolic substrates, especially actin and tubulin, and other topologically complex clients. Reviews emphasize that actin and tubulin are core/obligate CCT substrates, and TRiC also contributes to assembly of select multiprotein complexes (e.g., VHL–Elongin) and interacts with regulators (e.g., gelsolin) in a non-classical chaperoning mode. (grantham2020themolecularchaperone pages 1-2, willison2018thestructureand pages 1-2)
Unlike bacterial GroEL (homooligomer), TRiC is heterooligomeric, allowing subunit-specific substrate contacts and asymmetric ATPase/allosteric behavior. Experimental and structural analyses (summarized in yeast TRiC-focused work) group subunits into two “hemispheres” with differing nucleotide affinity and ATPase roles. CCT6 is consistently placed in the low ATP-affinity hemisphere (with CCT3/6/7/8), with sequence divergence near the nucleotide pocket proposed to reduce nucleotide exchange/ATP binding; yeast mutational data indicate that ATPase/P-loop disruption is more deleterious in high-affinity subunits than in low-affinity ones. (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48)
A yeast internal-subunit eGFP labeling strategy combined with cryo-EM (YISEL) enabled unambiguous subunit assignment in yeast TRiC, including CCT6. This work assigns CCT6 as an on-axis subunit and places it at a defined position in the ring architecture (Figure evidence). (zang2018developmentofa pages 1-2, zang2018developmentofa media 20a150a9)
Structural analyses summarized for yeast TRiC indicate that the N-terminus of CCT6 participates in an inter-ring interaction network during closure, stacking with the trans ring alongside other low-affinity hemisphere subunits. This supports the view that CCT6 contributes importantly to mechanical/structural coupling of the two rings through the ATP-driven cycle, even if its own ATPase contribution is reduced relative to high-affinity subunits. (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48)
TRiC/CCT is classically considered a cytosolic folding machine that supports co-/post-translational maturation of a substantial fraction of the proteome. Yeast-focused work explicitly reiterates TRiC/CCT as a cytosolic cylindrical complex encoded by eight essential genes and contributing to folding of ~10% of yeast cellular polypeptides. (dube2023saccharomycescerevisiaesurvival pages 1-4)
A 2024 preprint reports TRiC/CCT is present in the nucleus and proposes a direct role in regulating RNA polymerase II activity and nascent RNA production (with effects persisting when TRiC is restricted to the cytoplasm, supporting a direct nuclear role in their model). This expands likely functional contexts for all TRiC subunits (including CCT6), although it does not isolate a CCT6-specific nuclear mechanism. (gvozdenov2024triccctchaperoningoverns pages 1-6)
Yeast gene disruption experiments and genetic summaries state that all eight CCT genes (CCT1–CCT8) are essential, which includes CCT6. (kabir2008overexpressedribosomalproteins pages 1-2, kabir2005physiologicaleffectsof pages 2-4)
A panel of temperature-sensitive cct6 alleles has been described (e.g., cct6-14, -18, -27, -74, -85, -93, -97). Reported phenotypes include TBZ sensitivity (consistent with microtubule-associated stress) and in some alleles NaCl sensitivity (often used as an actin/cytoskeleton stress readout in these legacy screens). (kabir2008overexpressedribosomalproteins pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3)
A central yeast-specific insight is that overexpression of CCT6 can suppress diverse conditional phenotypes, including defects caused by tor2-21, lst8-2, rsp5-9, and growth inhibition caused by concomitant overexpression of Sit4p and Sap155p. Importantly, fractionation/abundance analysis indicates that overexpressing CCT6 increases the level of unassociated (unassembled) Cct6p, while the assembled TRiC/CCT complex remains at normal levels—supporting a model where unassembled Cct6p has physiological effects (e.g., substrate sequestration/competition for modifying activities) beyond simply boosting holo-complex abundance. (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)
Kabir et al. examined many altered forms of Cct6p and report that a CCT6 allele with GDGTT→AAAAA substitutions in the conserved ATP-binding motif (cct6-24) is unable to suppress the above traits, yet is functional for growth. This strongly supports that (i) Cct6p has separable functional states and (ii) suppression by unassembled Cct6p likely requires a specific ATP-associated conformation or activity. (kabir2005physiologicaleffectsof pages 1-2)
High-throughput microscopy profiling comparing ATP-site mutants in different TRiC subunits found that CCT subunits can have distinguishable in vivo consequences; in particular, the study emphasizes that the CCT3 mutant showed stronger associations with Q/N-rich proteins and P-body phenotypes than the CCT6 mutant, consistent with subunit-specific substrate/interactome specialization. (nadlerholly2012interactionsofsubunit pages 1-2)
Overexpression of CCT6 suppresses tor2-21 conditional phenotypes and is linked to partial restoration of actin cytoskeleton polarization in that genetic background, tying TRiC/CCT (and/or unassembled Cct6p) to a TOR2-dependent actin organization pathway. (kabir2005physiologicaleffectsof pages 2-4)
CCT6 overexpression suppresses phenotypes of lst8-2 (a TOR-associated factor required for sorting of diverse proteins at the Golgi and associated with cell wall integrity) and rsp5-9 (an essential ubiquitin–protein ligase with broad roles including endocytosis and actin dynamics). These suppression relationships suggest that TRiC/CCT proteostasis capacity and/or Cct6p-mediated sequestration can buffer defects in trafficking, membrane protein turnover, and cell surface/cell wall regulation. (kabir2005physiologicaleffectsof pages 2-4)
A 2023 yeast study using a folding-defective cct7 mutant reports temperature and cell-wall-stressor sensitivity and rescue by overexpression of PKC1 and SLT2 (MAPK cell wall integrity pathway components), supporting a functional interface between TRiC/CCT-dependent folding and cell-wall integrity signaling under heat stress. While not CCT6-specific, it is relevant to interpreting downstream consequences of impaired TRiC activity in yeast and potential contexts where CCT6 alleles may manifest. (dube2023saccharomycescerevisiaesurvival pages 1-4)
A 2023 study analyzing yeast TRiC with disease-associated mutations in CCT2 quantified ATPase behavior and reported apparent ATP binding constants and turnover (e.g., WT K1 ~8.3 μM, K2 ~110 μM; kcat ~0.043–0.053 s−1 under their fitted model) and showed that a double mutation reduces ADP off-rate, stabilizing closed states. This strengthens the mechanistic framework in which different subunits contribute differently to allosteric cycling—contextually relevant to CCT6 as a low-affinity hemisphere member—even though the mutation is in CCT2 rather than CCT6. (roy2023reducedadpoffrate pages 1-2, kelly2020structuralandfunctional pages 42-48)
A 2024 cryo-EM/XL-MS study of TRiC cooperation with PhLP2A (phosducin-like protein) in the folding cycle reports that in the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding positively charged inner surface residues from CCT1/3/6/8. This provides modern structural evidence that CCT6 contributes directly to the physicochemical environment and binding surfaces engaged during actin folding intermediates. (junsun2024astructuralvista pages 1-2)
A 2024 yeast study proposes TRiC/CCT has a direct nuclear role modulating RNA polymerase II activity and nascent RNA output, suggesting TRiC contributes to cell homeostasis beyond canonical cytosolic folding. This is a notable expansion of functional annotation scope for the complex and likely relevant to CCT6 as a subunit, but remains preprint-stage and not subunit-resolved. (gvozdenov2024triccctchaperoningoverns pages 1-6)
CCT6 is used experimentally as (i) a genetically essential proteostasis component (ts alleles) and (ii) a multicopy suppressor whose overexpression reveals buffering relationships across major pathways (TOR signaling, trafficking/cell wall, ubiquitin-mediated regulation). This makes CCT6 a practical tool for dissecting genetic robustness and proteostasis-pathway crosstalk in an industrially and medically relevant model organism. (kabir2005physiologicaleffectsof pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3)
The YISEL internal labeling method demonstrated in yeast TRiC enables precise subunit assignment in challenging hetero-oligomeric complexes and is itself an implementation with broader utility for macromolecular complex annotation and cryo-EM mapping—directly leveraging yeast CCT6 subunit labeling/assignment. (zang2018developmentofa pages 1-2, zang2018developmentofa media 20a150a9)
While human disease phenotypes are not part of yeast CCT6 annotation per se, yeast TRiC studies (e.g., kinetic analysis of disease-linked CCT2 mutations) illustrate how yeast TRiC serves as a mechanistic model for conserved chaperonin function and allosteric defects. Any extension to CCT6-related human disease or therapeutic targeting should be made cautiously and requires direct evidence not provided here. (roy2023reducedadpoffrate pages 1-2)
References
(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.
(dube2023saccharomycescerevisiaesurvival pages 1-4): Ankita Dube, Dileep Pullepu, and M. Anaul Kabir. Saccharomyces cerevisiae survival against heat stress entails a communication between cct and cell wall integrity pathway. Biologia futura, 74:519-527, Nov 2023. URL: https://doi.org/10.1007/s42977-023-00192-1, doi:10.1007/s42977-023-00192-1. This article has 2 citations and is from a peer-reviewed journal.
(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.
(kabir2005physiologicaleffectsof pages 2-4): 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.
(zang2018developmentofa pages 1-2): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.
(kabir2008overexpressedribosomalproteins pages 1-2): M. Anaul Kabir and Fred Sherman. Overexpressed ribosomal proteins suppress defective chaperonins in saccharomyces cerevisiae. FEMS yeast research, 8 8:1236-44, Dec 2008. URL: https://doi.org/10.1111/j.1567-1364.2008.00425.x, doi:10.1111/j.1567-1364.2008.00425.x. This article has 21 citations and is from a peer-reviewed journal.
(kelly2020structuralandfunctional pages 18-23): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.
(willison2018thestructureand pages 1-2): Keith Robert Willison. The structure and evolution of eukaryotic chaperonin-containing tcp-1 and its mechanism that folds actin into a protein spring. The Biochemical journal, 475 19:3009-3034, Oct 2018. URL: https://doi.org/10.1042/bcj20170378, doi:10.1042/bcj20170378. This article has 42 citations.
(kelly2020structuralandfunctionala pages 42-48): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.
(kelly2020structuralandfunctional pages 42-48): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.
(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.
(zang2018developmentofa media 20a150a9): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.
(kabir2008overexpressedribosomalproteins pages 2-3): M. Anaul Kabir and Fred Sherman. Overexpressed ribosomal proteins suppress defective chaperonins in saccharomyces cerevisiae. FEMS yeast research, 8 8:1236-44, Dec 2008. URL: https://doi.org/10.1111/j.1567-1364.2008.00425.x, doi:10.1111/j.1567-1364.2008.00425.x. This article has 21 citations and is from a peer-reviewed journal.
(nadlerholly2012interactionsofsubunit pages 1-2): Michal Nadler-Holly, Michal Breker, Ranit Gruber, Ariel Azia, Melissa Gymrek, Miriam Eisenstein, Keith R. Willison, Maya Schuldiner, and Amnon Horovitz. Interactions of subunit cct3 in the yeast chaperonin cct/tric with q/n-rich proteins revealed by high-throughput microscopy analysis. Proceedings of the National Academy of Sciences, 109:18833-18838, Oct 2012. URL: https://doi.org/10.1073/pnas.1209277109, doi:10.1073/pnas.1209277109. This article has 52 citations and is from a highest quality peer-reviewed journal.
(gvozdenov2024triccctchaperoningoverns pages 1-6): 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.
(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.
(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.