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gene_info: Name=PFD1; Synonyms=GIM6; OrderedLocusNames=YJL179W; ORFNames=J0488;
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
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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: P46988
• Protein Description: RecName: Full=Prefoldin subunit 1; AltName: Full=Genes involved in microtubule biogenesis protein 6; AltName: Full=Gim complex subunit 6; Short=GimC subunit 6;
• Gene Information: Name=PFD1; Synonyms=GIM6; OrderedLocusNames=YJL179W; ORFNames=J0488;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the prefoldin subunit beta family.
• Key Domains: PFD_beta-like. (IPR002777); Prefoldin. (IPR009053); Prefoldin_2 (PF01920)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PFD1" 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 'PFD1' 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 PFD1 (gene ID: PFD1, UniProt: P46988) 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: P46988
• Protein Description: RecName: Full=Prefoldin subunit 1; AltName: Full=Genes involved in microtubule biogenesis protein 6; AltName: Full=Gim complex subunit 6; Short=GimC subunit 6;
• Gene Information: Name=PFD1; Synonyms=GIM6; OrderedLocusNames=YJL179W; ORFNames=J0488;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the prefoldin subunit beta family.
• Key Domains: PFD_beta-like. (IPR002777); Prefoldin. (IPR009053); Prefoldin_2 (PF01920)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PFD1" 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 'PFD1' 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 PFD1 (gene ID: PFD1, UniProt: P46988) 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: PFD1 (GIM6 / YJL179W; UniProt P46988) in Saccharomyces cerevisiae (S288c)

Scope and identity verification (critical)

The literature retrieved here is consistent that S. cerevisiae PFD1 is the prefoldin subunit also called Gim6 (Genes Involved in Microtubule biogenesis), encoded by YJL179W, and corresponds to the canonical eukaryotic prefoldin subunit often denoted PFDN1 in cross-species nomenclature. This matches the UniProt-provided description (Prefoldin subunit 1; Gim complex subunit 6; prefoldin β-family member), and no conflicting “PFD1” identity from another organism was used for functional claims in this report. (millanzambrano2014nuclearfunctionsof pages 2-3, tahmaz2023prefoldin2contributes pages 1-2)

1) Key concepts and definitions (current understanding)

Prefoldin/GimC: a conserved cochaperone for cytoskeletal protein folding

Eukaryotic prefoldin (also termed GimC in yeast) is a heterohexameric cochaperone whose best-characterized role is to bind non-native nascent polypeptides—especially actin and tubulins—and deliver them to the cytosolic group II chaperonin CCT/TRiC for ATP-dependent folding. Prefoldin functions largely as an ATP-independent holdase, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC. (simons2004selectivecontributionof pages 1-2, millanzambrano2014nuclearfunctionsof pages 2-3, tahmaz2023prefoldin2contributes pages 1-2)

Subunit composition and the position of Pfd1/Gim6

Canonical eukaryotic prefoldin contains six distinct subunits (PFD1–PFD6), organized as two α-type and four β-type subunits. In budding yeast, the complex is described as containing α subunits Pac10/Pfd3 and Gim5/Pfd5, and β subunits Pfd1 (Gim6), Gim4/Pfd2, Gim3/Pfd4, and Yke2/Pfd6. (tahmaz2023prefoldin2contributes pages 1-2, millanzambrano2014nuclearfunctionsof pages 2-3)

Structural syntheses place PFD1 (with PFD5 and PFD6) on one side of the “jellyfish-like” prefoldin hexamer, opposite PFD2/PFD3/PFD4. This arrangement rationalizes how different subunits contribute to distinct client-binding surfaces while preserving a shared central cavity. (arranz2018structureandfunction pages 1-3, simons2004selectivecontributionof pages 7-8)

2) Primary molecular function of Pfd1 in yeast (functional annotation)

Function: chaperone-mediated biogenesis of actin and tubulin (not an enzyme)

Pfd1’s primary function is structural/cochaperone activity, not catalysis: as part of the prefoldin/GimC complex it captures and stabilizes unfolded actin and tubulin intermediates and hands them to CCT/TRiC for final folding, enabling cytoskeleton assembly. (simons2004selectivecontributionof pages 1-2, millanzambrano2014nuclearfunctionsof pages 2-3, tahmaz2023prefoldin2contributes pages 1-2)

Mechanistic evidence: physical and functional coupling to CCT/TRiC

Yeast prefoldin/GimC physically interacts with TRiC/CCT in vivo and in vitro, and gim deletion mutants exhibit actin and tubulin phenotypes resembling TRiC mutants, supporting a shared folding pathway. Importantly, in strains deleted for one or more GIM genes, actin folding by TRiC is slowed ~5-fold compared with wild type, consistent with prefoldin increasing folding efficiency by facilitating productive substrate handling/release. (leroux1999mtgimcanovel pages 1-2)

Substrate handling: “tentacle tips” and cavity-mediated capture

Biochemical reconstitution and binding assays support that prefoldin binds client proteins via the distal regions (“tentacle tips”) and/or the cavity of the hexamer. The tentacle tips are required for stable binary complexes with actin and tubulin, and different but overlapping sets of subunits contribute to actin vs tubulin binding, implying subunit-specific client-recognition contributions within the shared complex. (simons2004selectivecontributionof pages 8-8, simons2004selectivecontributionof pages 1-2)

3) Biological processes, pathways, and localization

Cytosolic proteostasis pathway: prefoldin → CCT/TRiC → cytoskeleton assembly

The central pathway involving Pfd1 is the cytosolic folding pipeline for cytoskeletal proteins: prefoldin binds nascent/non-native actin/tubulin and transfers them to CCT/TRiC for folding into assembly-competent monomers that form actin filaments and microtubules. This functional axis explains why prefoldin mutants show cytoskeletal abnormalities. (millanzambrano2014nuclearfunctionsof pages 2-3, leroux1999mtgimcanovel pages 1-2)

Nuclear/chromatin-associated roles: transcription elongation and chromatin dynamics

Beyond cytoskeletal folding, yeast prefoldin has a well-supported nuclear function: it is present in the nucleus, and a subset of prefoldin subunits is recruited to chromatin in a transcription-dependent manner. Functionally, prefoldin influences RNA polymerase II elongation rate, with pronounced effects on long genes and TATA-containing promoters, and is linked to histone dynamics after nucleosome remodeling (cotranscriptional histone eviction). (millanzambrano2013theprefoldincomplex pages 1-2)

For Pfd1 specifically, a prefoldin-focused review summarizes evidence that PFD1 deletion reduces RNAPII occupancy across gene bodies, consistent with an elongation/chromatin role for Pfd1-containing prefoldin in yeast. (tahmaz2022prefoldinfunctionin pages 3-5)

Subcellular localization (where Pfd1 acts)

The canonical prefoldin role implies predominant cytosolic localization (client binding and transfer to cytosolic CCT/TRiC), but multiple sources support that prefoldin subunits can also localize to the nucleus and associate with chromatin under transcriptional engagement and/or stress conditions. (millanzambrano2014nuclearfunctionsof pages 2-3, millanzambrano2013theprefoldincomplex pages 1-2, tahmaz2022prefoldinfunctionin pages 3-5)

4) Recent developments and latest research (prioritizing 2023–2024)

2023: prefoldin system expanded into mitochondrial-linked physiology (subunit-specific: Pfd2)

A 2023 study in BMC Biology extended yeast prefoldin biology beyond cytoskeleton folding by showing that loss of Pfd2/Gim4 affects mitochondrial morphology, respiratory growth, and abundance of some respiratory chain complexes, and that Pfd2 interacts with the mitochondrial import receptor Tom70. While this is not Pfd1-specific, it supports the emerging view that prefoldin supports broader cytosolic proteostasis relevant to organellar protein biogenesis and stress tolerance (consistent with prefoldin’s ATP-independent holdase activity). (tahmaz2023prefoldin2contributes pages 1-2)

Publication date/URL: Sep 2023, https://doi.org/10.1186/s12915-023-01695-y (tahmaz2023prefoldin2contributes pages 1-2)

2024: non-canonical prefoldin subunit function in proteasome assembly (subunit-specific: Pfd5)

A 2024 bioRxiv preprint reported a non-canonical role for yeast Pfd5 in 26S proteasome assembly, specifically affecting formation of the Rpt AAA+ ATPase ring (19S base). Only PFD5 deletion among single prefoldin subunit deletions reduced 26S activity in their assays, arguing for subunit-specific contributions to proteostasis machinery beyond canonical actin/tubulin delivery. This provides a contemporary example of prefoldin subunits acquiring additional functions, and contextualizes Pfd1’s established nuclear and cytoskeletal roles in a broader proteostasis network. (ghahe2024identificationofa pages 1-5, ghahe2024identificationofa pages 12-15)

Publication date/URL: Apr 2024, https://doi.org/10.1101/2024.04.22.590501 (ghahe2024identificationofa pages 1-5)

Limitation for 2023–2024 on Pfd1 specifically

Within the retrieved 2023–2024 corpus, no new Pfd1/Gim6-specific biochemical activity beyond the established canonical prefoldin role (actin/tubulin handoff to CCT) and prior-described nuclear/transcription functions was identified. This likely reflects either genuine research sparsity on Pfd1-specific mechanisms in that period or retrieval limitations. (tahmaz2023prefoldin2contributes pages 1-2, ghahe2024identificationofa pages 1-5)

5) Current applications and real-world implementations

Functional tool compounds that phenocopy prefoldin pathway disruption (conceptual application)

Recent pathway-level work (in fungal systems) supports the concept that disrupting GimC/prefoldin-dependent processes yields characteristic phenotypes (e.g., nuclear positioning and actin/cell wall defects) and can be exploited as a mechanistic probe for cytoskeleton-linked vulnerabilities. While not a Pfd1-specific application, this highlights prefoldin biology as actionable for functional dissection of cytoskeletal biogenesis pathways and antifungal target discovery approaches at the pathway level. (tahmaz2023prefoldin2contributes pages 1-2)

Widely used experimental application in yeast biology

Because prefoldin subunits are non-essential in yeast yet yield informative phenotypes in cytoskeleton and transcription, prefoldin mutants (including pfd1/gim6 perturbations) are useful for dissecting: (i) chaperone-assisted cytoskeletal biogenesis, (ii) coupling of proteostasis to transcription/chromatin dynamics, and (iii) stress responses that may involve nuclear relocalization of chaperone components. (millanzambrano2014nuclearfunctionsof pages 2-3, millanzambrano2013theprefoldincomplex pages 1-2, tahmaz2022prefoldinfunctionin pages 3-5)

6) Expert opinions and analysis (authoritative synthesis)

Canonical vs non-canonical prefoldin functions

Authoritative reviews emphasize that prefoldin’s canonical function—delivery of actin/tubulin to CCT/TRiC—is well established, but accumulating evidence supports broader roles in protein homeostasis, transcription regulation, and protein turnover, sometimes involving subunit-specific behavior and alternative assemblies. In yeast, this aligns with findings that prefoldin is present in the nucleus/chromatin and affects transcription elongation, and with more recent yeast studies demonstrating non-canonical subunit roles (e.g., Pfd5 in proteasome assembly; Pfd2 in mitochondrial-related phenotypes). (millanzambrano2014nuclearfunctionsof pages 2-3, tahmaz2023prefoldin2contributes pages 1-2, ghahe2024identificationofa pages 1-5)

Interpretation for Pfd1 functional annotation

Given the strongest direct evidence, Pfd1/Gim6 should be annotated primarily as a β-type canonical prefoldin subunit required for efficient actin/tubulin biogenesis via CCT/TRiC. A secondary, evidence-supported annotation is involvement in nuclear gene expression control, especially transcription elongation and chromatin/histone dynamics, likely reflecting either (i) nuclear localization of the prefoldin complex/subunits or (ii) a bridging role connecting proteostasis and transcriptional machinery under basal and stress conditions. (leroux1999mtgimcanovel pages 1-2, millanzambrano2013theprefoldincomplex pages 1-2, tahmaz2022prefoldinfunctionin pages 3-5)

7) Relevant statistics and data highlights

• Complex stoichiometry: eukaryotic prefoldin is a heterohexamer of six distinct subunits (PFD1–PFD6); two α-type and four β-type (including Pfd1). (tahmaz2023prefoldin2contributes pages 1-2, millanzambrano2014nuclearfunctionsof pages 2-3)
• Subunit sizes: eukaryotic prefoldin subunits are ~14–23 kDa each (reported generally for the complex). (simons2004selectivecontributionof pages 7-8)
• Folding efficiency: in yeast gim/prefoldin deletions, TRiC-mediated actin folding is ~5-fold slower, consistent with prefoldin enhancing cytoskeletal folding efficiency on the order of ~5-fold. (leroux1999mtgimcanovel pages 1-2, liang2020thefunctionsand pages 1-2)
• Mechanistic adjacency evidence: cross-linking data are consistent with PFD2 adjacent to PFD1 in the assembled complex. (simons2004selectivecontributionof pages 7-8)

Visual evidence (prefoldin architecture)

A representative structural schematic/model of the prefoldin hexamer showing the proposed arrangement of subunits (including PFD1) is available from Simons et al. (JBC 2004). (simons2004selectivecontributionof media b05b75fc)

Summary table (evidence map)

The following table consolidates identity, function, localization, pathways, and quantitative evidence for yeast PFD1/GIM6.

Table: This table summarizes the best-supported functional annotation points for yeast PFD1/GIM6/YJL179W, including its identity, canonical prefoldin role, localization, nuclear functions, and representative quantitative evidence. It is useful as a compact evidence map for interpreting UniProt P46988 in the context of yeast proteostasis and gene expression.

Key sources (URLs, dates)

• Leroux et al., EMBO J (1999-12): “MtGimC…” https://doi.org/10.1093/emboj/18.23.6730 (leroux1999mtgimcanovel pages 1-2)
• Simons et al., J Biol Chem (2004-02): “Selective Contribution…” https://doi.org/10.1074/jbc.m306053200 (simons2004selectivecontributionof pages 1-2, simons2004selectivecontributionof media b05b75fc)
• Millán-Zambrano et al., PLoS Genet (2013-09): “Prefoldin regulates chromatin…” https://doi.org/10.1371/journal.pgen.1003776 (millanzambrano2013theprefoldincomplex pages 1-2)
• Millán-Zambrano & Chávez, Open Biol (2014-07): “Nuclear functions of prefoldin” https://doi.org/10.1098/rsob.140085 (millanzambrano2014nuclearfunctionsof pages 2-3)
• Tahmaz et al., BMC Biology (2023-09): “Prefoldin 2 contributes…” https://doi.org/10.1186/s12915-023-01695-y (tahmaz2023prefoldin2contributes pages 1-2)
• Ghahe et al., bioRxiv preprint (2024-04): “Pfd5 in proteasome assembly” https://doi.org/10.1101/2024.04.22.590501 (ghahe2024identificationofa pages 1-5)

References

1. (millanzambrano2014nuclearfunctionsof pages 2-3): Gonzalo Millán-Zambrano and Sebastián Chávez. Nuclear functions of prefoldin. Open Biology, 4:140085, Jul 2014. URL: https://doi.org/10.1098/rsob.140085, doi:10.1098/rsob.140085. This article has 91 citations and is from a peer-reviewed journal.

2. (tahmaz2023prefoldin2contributes pages 1-2): Ismail Tahmaz, Somayeh Shahmoradi Ghahe, Monika Stasiak, Kamila P. Liput, Katarzyna Jonak, and Ulrike Topf. Prefoldin 2 contributes to mitochondrial morphology and function. BMC Biology, Sep 2023. URL: https://doi.org/10.1186/s12915-023-01695-y, doi:10.1186/s12915-023-01695-y. This article has 13 citations and is from a domain leading peer-reviewed journal.

3. (simons2004selectivecontributionof pages 1-2): C. Torrey Simons, An Staes, Heidi Rommelaere, Christophe Ampe, Sally A. Lewis, and Nicholas J. Cowan. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding*. Journal of Biological Chemistry, 279:4196-4203, Feb 2004. URL: https://doi.org/10.1074/jbc.m306053200, doi:10.1074/jbc.m306053200. This article has 75 citations and is from a domain leading peer-reviewed journal.

4. (arranz2018structureandfunction pages 1-3): Rocío Arranz, Jaime Martín-Benito, and José M. Valpuesta. Structure and function of the cochaperone prefoldin. Advances in experimental medicine and biology, 1106:119-131, Jan 2018. URL: https://doi.org/10.1007/978-3-030-00737-9_9, doi:10.1007/978-3-030-00737-9_9. This article has 32 citations and is from a peer-reviewed journal.

5. (simons2004selectivecontributionof pages 7-8): C. Torrey Simons, An Staes, Heidi Rommelaere, Christophe Ampe, Sally A. Lewis, and Nicholas J. Cowan. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding*. Journal of Biological Chemistry, 279:4196-4203, Feb 2004. URL: https://doi.org/10.1074/jbc.m306053200, doi:10.1074/jbc.m306053200. This article has 75 citations and is from a domain leading peer-reviewed journal.

6. (leroux1999mtgimcanovel pages 1-2): M. Leroux, M. Fändrich, D. Klunker, K. Siegers, A. Lupas, James R. Brown, E. Schiebel, C. Dobson, and F. Hartl. Mtgimc, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor gimc/prefoldin. The EMBO Journal, 18:6730-6743, Dec 1999. URL: https://doi.org/10.1093/emboj/18.23.6730, doi:10.1093/emboj/18.23.6730. This article has 178 citations.

7. (simons2004selectivecontributionof pages 8-8): C. Torrey Simons, An Staes, Heidi Rommelaere, Christophe Ampe, Sally A. Lewis, and Nicholas J. Cowan. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding*. Journal of Biological Chemistry, 279:4196-4203, Feb 2004. URL: https://doi.org/10.1074/jbc.m306053200, doi:10.1074/jbc.m306053200. This article has 75 citations and is from a domain leading peer-reviewed journal.

8. (millanzambrano2013theprefoldincomplex pages 1-2): Gonzalo Millán-Zambrano, Alfonso Rodríguez-Gil, Xenia Peñate, Lola de Miguel-Jiménez, Macarena Morillo-Huesca, Nevan Krogan, and Sebastián Chávez. The prefoldin complex regulates chromatin dynamics during transcription elongation. PLoS Genetics, 9:e1003776, Sep 2013. URL: https://doi.org/10.1371/journal.pgen.1003776, doi:10.1371/journal.pgen.1003776. This article has 64 citations and is from a domain leading peer-reviewed journal.

9. (tahmaz2022prefoldinfunctionin pages 3-5): Ismail Tahmaz, Somayeh Shahmoradi Ghahe, and Ulrike Topf. Prefoldin function in cellular protein homeostasis and human diseases. Frontiers in Cell and Developmental Biology, Jan 2022. URL: https://doi.org/10.3389/fcell.2021.816214, doi:10.3389/fcell.2021.816214. This article has 56 citations.

10. (ghahe2024identificationofa pages 1-5): Somayeh Shahmoradi Ghahe, Krzysztof Drabikowski, and Ulrike Topf. Identification of a non-canonical function of prefoldin subunit 5 in proteasome assembly. bioRxiv, Apr 2024. URL: https://doi.org/10.1101/2024.04.22.590501, doi:10.1101/2024.04.22.590501. This article has 3 citations.

11. (ghahe2024identificationofa pages 12-15): Somayeh Shahmoradi Ghahe, Krzysztof Drabikowski, and Ulrike Topf. Identification of a non-canonical function of prefoldin subunit 5 in proteasome assembly. bioRxiv, Apr 2024. URL: https://doi.org/10.1101/2024.04.22.590501, doi:10.1101/2024.04.22.590501. This article has 3 citations.

12. (liang2020thefunctionsand pages 1-2): Jiaxin Liang, Longzheng Xia, Linda Oyang, Jinguan Lin, Shiming Tan, Pin Yi, Yaqian Han, Xia Luo, Hui Wang, Lu Tang, Qing Pan, Yutong Tian, Shan Rao, Min Su, Yingrui Shi, Deliang Cao, Yujuan Zhou, and Qianjin Liao. The functions and mechanisms of prefoldin complex and prefoldin-subunits. Cell & Bioscience, Jul 2020. URL: https://doi.org/10.1186/s13578-020-00446-8, doi:10.1186/s13578-020-00446-8. This article has 71 citations and is from a peer-reviewed journal.

13. (simons2004selectivecontributionof media b05b75fc): C. Torrey Simons, An Staes, Heidi Rommelaere, Christophe Ampe, Sally A. Lewis, and Nicholas J. Cowan. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding*. Journal of Biological Chemistry, 279:4196-4203, Feb 2004. URL: https://doi.org/10.1074/jbc.m306053200, doi:10.1074/jbc.m306053200. This article has 75 citations and is from a domain leading peer-reviewed journal.

14. (yang2024prefoldinsubunitsand pages 2-4): Yi Yang, Gang Zhang, Mengyu Su, Qingbiao Shi, and Qingshuai Chen. Prefoldin subunits and its associate partners: conservations and specificities in plants. Plants, 13:556, Feb 2024. URL: https://doi.org/10.3390/plants13040556, doi:10.3390/plants13040556. This article has 0 citations.

15. (herranzmontoya2021acomprehensiveanalysis pages 5-7): Irene Herranz-Montoya, Solip Park, and Nabil Djouder. A comprehensive analysis of prefoldins and their implication in cancer. iScience, 24:103273, Nov 2021. URL: https://doi.org/10.1016/j.isci.2021.103273, doi:10.1016/j.isci.2021.103273. This article has 26 citations and is from a peer-reviewed journal.

16. (blancotourinan2021ageneticapproach pages 1-2): Noel Blanco-Touriñán, David Esteve-Bruna, Antonio Serrano-Mislata, Rosa María Esquinas-Ariza, Francesca Resentini, Javier Forment, Cristian Carrasco-López, Claudio Novella-Rausell, Alberto Palacios-Abella, Pedro Carrasco, Julio Salinas, Miguel Á Blázquez, and David Alabadí. A genetic approach reveals different modes of action of prefoldins. Plant Physiology, 187:1534-1550, Jul 2021. URL: https://doi.org/10.1093/plphys/kiab348, doi:10.1093/plphys/kiab348. This article has 24 citations and is from a highest quality peer-reviewed journal.

Citations

1. leroux1999mtgimcanovel pages 1-2
2. millanzambrano2013theprefoldincomplex pages 1-2
3. tahmaz2022prefoldinfunctionin pages 3-5
4. ghahe2024identificationofa pages 1-5
5. simons2004selectivecontributionof pages 7-8
6. millanzambrano2014nuclearfunctionsof pages 2-3
7. simons2004selectivecontributionof pages 1-2
8. arranz2018structureandfunction pages 1-3
9. simons2004selectivecontributionof pages 8-8
10. ghahe2024identificationofa pages 12-15
11. liang2020thefunctionsand pages 1-2
12. yang2024prefoldinsubunitsand pages 2-4
13. herranzmontoya2021acomprehensiveanalysis pages 5-7
14. blancotourinan2021ageneticapproach pages 1-2
15. https://doi.org/10.1186/s12915-023-01695-y
16. https://doi.org/10.1101/2024.04.22.590501
17. https://doi.org/10.1098/rsob.140085
18. https://doi.org/10.1007/978-3-030-00737-9_9
19. https://doi.org/10.1074/jbc.m306053200
20. https://doi.org/10.1186/s13578-020-00446-8
21. https://doi.org/10.3390/plants13040556
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