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gene_id: ACL4
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gene_info: Name=ACL4 {ECO:0000303|PubMed:25936803}; OrderedLocusNames=YDR161W {ECO:0000312|SGD:S000002568};
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
protein_family: Belongs to the ACL4 family. .
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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: Q03771
• Protein Description: RecName: Full=Assembly chaperone of RPL4 {ECO:0000303|PubMed:25936803};
• Gene Information: Name=ACL4 {ECO:0000303|PubMed:25936803}; OrderedLocusNames=YDR161W {ECO:0000312|SGD:S000002568};
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the ACL4 family. .
• Key Domains: TPR-like_helical_dom_sf. (IPR011990)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ACL4" 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 'ACL4' 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 ACL4 (gene ID: ACL4, UniProt: Q03771) 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: Q03771
• Protein Description: RecName: Full=Assembly chaperone of RPL4 {ECO:0000303|PubMed:25936803};
• Gene Information: Name=ACL4 {ECO:0000303|PubMed:25936803}; OrderedLocusNames=YDR161W {ECO:0000312|SGD:S000002568};
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the ACL4 family. .
• Key Domains: TPR-like_helical_dom_sf. (IPR011990)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ACL4" 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 'ACL4' 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 ACL4 (gene ID: ACL4, UniProt: Q03771) 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 ACL4 (YDR161W; UniProt Q03771)

Executive summary

Acl4 is a dedicated assembly chaperone for the 60S large-subunit ribosomal protein Rpl4 (uL4) in Saccharomyces cerevisiae (strain S288c). It binds a defined segment of the Rpl4 long internal loop, keeps nascent/unassembled Rpl4 soluble, and escorts it to the nuclear pre-60S assembly site, coordinating with the importin Kap104. Loss of ACL4 causes a severe slow-growth phenotype with hallmark 60S biogenesis defects (60S shortage and half-mers). More recent work (2022–2024) extends Acl4 biology to cotranslational regulation of RPL4 mRNA abundance via NAC/Caf130/Ccr4–Not circuitry, and links Acl4-limited conditions to aggregation/quality control networks that include the E3 ligase Tom1. (pillet2015thededicatedchaperone pages 1-2, huber2017molecularbasisfor pages 1-2, pillet2015thededicatedchaperone pages 10-12, schilke2024functionalsimilaritiesand pages 1-3, pillet2022dedicatedchaperonescoordinate pages 14-16, pillet2022dedicatedchaperonescoordinate pages 20-22)

1) Identity verification and key definitions

1.1 Target identity (mandatory verification)

Primary literature explicitly identifies Acl4 as yeast YDR161W and characterizes it as the dedicated chaperone for Rpl4, matching the UniProt target Q03771 and the stated domain annotation (TPR-like helical domain superfamily). (stelter2015coordinatedribosomall4 pages 3-3, pillet2015thededicatedchaperone pages 1-2, huber2017molecularbasisfor pages 1-2)

1.2 Key concepts (current understanding)

• Dedicated ribosomal-protein (RP) chaperone: A specialized factor that binds one (or a small set of) ribosomal protein(s) to prevent aggregation/mislocalization and to promote safe delivery to the assembly site. Acl4 is dedicated for Rpl4. (pillet2015thededicatedchaperone pages 18-20, yang2024ribosomeassemblyand pages 1-3)
• Pre-60S assembly: Stepwise nuclear maturation of the large ribosomal subunit, involving incorporation of RPs into pre-ribosomal particles and transient binding of biogenesis factors; Acl4 acts at the stage of delivering Rpl4 to early nuclear pre-60S particles. (pillet2015thededicatedchaperone pages 18-20, pillet2015thededicatedchaperone pages 20-21)
• Cotranslational capture: Binding of a chaperone to a nascent client during translation; Acl4 enriches RPL4 mRNA in pull-downs, consistent with cotranslational engagement. (pillet2015thededicatedchaperone pages 17-18)

2) Molecular function and mechanism

2.1 Core function: chaperoning and escort of Rpl4/uL4

Acl4 binds newly synthesized, free Rpl4, enabling soluble expression of Rpl4 and escorting it from cytoplasm to nuclear pre-60S assembly sites; Acl4 is not stably associated with mature 60S particles, consistent with a transient escort. (pillet2015thededicatedchaperone pages 1-2, pillet2015thededicatedchaperone pages 10-12)

2.2 Client-binding site on Rpl4

Mapping in yeast indicates Acl4 recognizes the C-terminal region of the long internal loop of Rpl4, with functional mapping to approximately aa 88–114 (and emphasis around ~101–114). Multiple alanine-block substitutions in this segment abolish the Acl4–Rpl4 interaction. (pillet2015thededicatedchaperone pages 14-17, pillet2015thededicatedchaperone pages 20-21)

2.3 Structural basis (TPR fold; sequestration of exposed residues)

A high-resolution structure of the Acl4–RpL4 complex shows that Acl4 adopts an α-helical TPR fold (reported as seven TPRs plus a C-terminal helix) and uses its concave surface to sequester ~70 exposed residues of the elongated RpL4 loop, providing a mechanistic basis for preventing degradation/aggregation of unassembled L4. (huber2017molecularbasisfor pages 1-2, huber2017molecularbasisfor media 4aaddfb0, huber2017molecularbasisfor media cb2e78f3)

2.4 Nuclear import and Kap104 coupling

A central mechanistic insight is that the eukaryote-specific extension of Rpl4 contains overlapping determinants for Acl4 binding and the nuclear import factor Kap104, enabling continuous protection during import. In vitro, Kap104 can form a stoichiometric Acl4–Rpl4–Kap104 trimer, and a schematic map of overlapping binding sites is provided in the structural work. (huber2017molecularbasisfor pages 1-2, pillet2015thededicatedchaperone pages 20-21, huber2017molecularbasisfor media e4ea49ee)

3) Subcellular localization and pathway placement

3.1 Localization

Fluorescent tagging and fractionation show Acl4 is present in both cytoplasm and nucleus and is recovered in soluble fractions, not as a stable component of pre-60S or mature 60S particles. This supports a “carrier/escort” rather than “structural subunit” model. (pillet2015thededicatedchaperone pages 10-12)

3.2 Pathway role in large-subunit biogenesis

Deletion of ACL4 causes a defect in 60S subunit production and characteristic half-mer polysomes, consistent with impaired assembly or supply of an essential large-subunit RP to the nucleus and pre-60S particles. (stelter2015coordinatedribosomall4 pages 3-3, pillet2015thededicatedchaperone pages 10-12)

4) Phenotypes, statistics, and quantitative evidence

4.1 Growth and ribosome biogenesis phenotypes

• acl4Δ is viable but has severe slow growth across tested temperatures and shows a shortage of free 60S subunits, half-mer polysomes, and reduced overall polysomes. (pillet2015thededicatedchaperone pages 10-12)
• Growth and 60S defects can be partially rescued by extra RPL4, and deletion of ACL4 impairs 60S synthesis and yields half-mers. (stelter2015coordinatedribosomall4 pages 3-3, pillet2015thededicatedchaperone pages 14-17)

4.2 Cotranslational evidence (mRNA enrichment)

Acl4 affinity purification shows strong enrichment of RPL4 mRNA (~150-fold), supporting cotranslational recognition of nascent Rpl4. (pillet2015thededicatedchaperone pages 17-18)

4.3 RPL4 mRNA regulation (Acl4 availability as a rheostat)

Recent work indicates Acl4 availability feeds back on RPL4 expression:
- RPL4 mRNA abundance is almost ~2-fold lower in Δacl4 cells versus wild type, consistent with an Acl4-dependent stabilization effect. (pillet2022dedicatedchaperonescoordinate pages 14-16)
- When Acl4 is absent/limiting, ribosome-associated Rpl4 nascent chain becomes accessible to regulatory machinery involving NAC and Caf130-associated Ccr4–Not, which promotes RPL4 mRNA degradation, limiting accumulation of aggregation-prone excess Rpl4. (pillet2022dedicatedchaperonescoordinate pages 1-4, schilke2024functionalsimilaritiesand pages 1-3)

4.4 Proteostasis/quality control linkage (Tom1)

Deregulated Rpl4 expression promotes aggregation and proteostasis defects, particularly in tom1Δ backgrounds; in such assays, wild-type proteins show nucle(ol)ar signal in <20% of Δtom1 cells, whereas deregulated variants show strong nucle(ol)ar compartment signals in most Δtom1 cells. These observations link Acl4-dependent homeostasis to ubiquitin-ligase-dependent quality control. (pillet2022dedicatedchaperonescoordinate pages 20-22)

4.5 System-level scale statistics (context for why Acl4 matters)

• In an exponentially growing yeast cell, there are ~200,000 ribosomes, requiring synthesis of >2,000 ribosomes/minute (≈160,000 ribosomal proteins per minute) to maintain growth—illustrating why tight control of RP supply (including Acl4-mediated handling of Rpl4) is crucial. (pillet2022dedicatedchaperonescoordinate pages 1-4)
• Across eukaryotes, ribosome assembly requires several hundred ribosome biogenesis factors (RBFs), compared with ~50 in bacteria, reflecting increased complexity and the need for specialized factors such as dedicated RP chaperones. (dorner2023ribosomebiogenesisfactors—from pages 1-2)
• Yeast ribosomes contain 79 ribosomal proteins, while humans have ~80; the 60S contains 46 RPs in yeast and 47 in humans. (dorner2023ribosomebiogenesisfactors—from pages 1-2, yang2024ribosomeassemblyand pages 1-3)
• Ribosome production is extremely resource-intensive (yeast allocation estimates include ~60% of transcription and ~50% of translation events, among others), motivating quality-control and repair/assembly-control systems. (yang2024ribosomeassemblyand pages 1-3)

5) Recent developments (prioritizing 2023–2024)

5.1 2024: Integration of Acl4 into cotranslational regulatory networks

A 2024 study of NAC subunits in S. cerevisiae explicitly frames Acl4 as the specialized chaperone for Rpl4, noting that without Acl4 Rpl4 is aggregation-prone and cells grow very slowly. It further places Acl4-limited states into a regulatory pathway where Rpl4 mRNA is targeted for degradation via the CCR4–Not complex, and highlights quantitative NAC subunit abundance differences (Nacβ2 is ~20–100× less abundant than the major NAC subunits). (schilke2024functionalsimilaritiesand pages 1-3)

5.2 2023: Expert synthesis on why mechanistic annotation matters

A high-citation 2023 EMBO Journal review argues that assigning detailed molecular functions to ribosome biogenesis factors is essential for understanding and treating diseases linked to disturbed ribosome assembly, including ribosomopathies and cancers. While Acl4 is not the focus, this review provides field-level justification for precise mechanistic annotation of factors like Acl4. (dorner2023ribosomebiogenesisfactors—from pages 1-2)

5.3 2024: Assembly and repair framework (expert view)

A 2024 Annual Review article frames dedicated chaperones as part of the cellular strategy to manage small, basic, aggregation-prone RPs and maintain ribosome integrity through quality control and repair, with dedicated RP chaperones known for at least ~13 RPs. This strengthens the conceptual placement of Acl4 as a dedicated RP chaperone integrating assembly and proteostasis. (yang2024ribosomeassemblyand pages 1-3)

6) Current applications and real-world implementations

6.1 Yeast Acl4 as a model for conserved principles

Acl4 exemplifies how eukaryotes solve the “RP handling problem” created by (i) cytoplasmic synthesis but nuclear assembly and (ii) aggregation propensity of basic RPs. Structural definition of the Acl4–L4 interface provides a mechanistic template for understanding analogous dedicated-chaperone systems and their coupling to nuclear import pathways (e.g., overlapping chaperone/importin binding sites). (huber2017molecularbasisfor pages 1-2, huber2017molecularbasisfor media e4ea49ee)

6.2 Disease relevance via ribosome biogenesis concepts

Although Acl4 itself is a yeast protein, authoritative reviews stress that detailed knowledge of ribosome assembly factors is key for understanding disease states (ribosomopathies, cancers) linked to perturbed ribosome assembly and quality control, supporting the broader translational relevance of dissecting dedicated-chaperone mechanisms in model organisms. (dorner2023ribosomebiogenesisfactors—from pages 1-2, yang2024ribosomeassemblyand pages 1-3)

7) Visual evidence (structure and import coupling)

Figures from the Acl4–RpL4 structural study show (i) the overall complex architecture, (ii) the interaction interface/hotspots, and (iii) a schematic of overlapping Acl4 and Kap104 binding sites on RpL4 (supporting the escort/import model). (huber2017molecularbasisfor media 4aaddfb0, huber2017molecularbasisfor media cb2e78f3, huber2017molecularbasisfor media e4ea49ee)

Evidence summary table

Table: This table summarizes the core functional-annotation evidence for Saccharomyces cerevisiae Acl4/YDR161W, including identity verification, mechanism, localization, pre-60S role, and recent regulatory insights. It is useful as a compact evidence-backed reference for gene/protein annotation.

Key references (with URLs and publication dates)

• Pillet B. et al. The Dedicated Chaperone Acl4 Escorts Ribosomal Protein Rpl4 to Its Nuclear Pre-60S Assembly Site. PLOS Genetics (Oct 2015). https://doi.org/10.1371/journal.pgen.1005565 (pillet2015thededicatedchaperone pages 1-2, pillet2015thededicatedchaperone pages 10-12)
• Stelter P. et al. Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension. Molecular Cell (Jun 2015). https://doi.org/10.1016/j.molcel.2015.03.029 (stelter2015coordinatedribosomall4 pages 3-3)
• Huber F.M., Hoelz A. Molecular basis for protection of ribosomal protein L4 from cellular degradation. Nature Communications (Feb 2017). https://doi.org/10.1038/ncomms14354 (huber2017molecularbasisfor pages 1-2)
• Pillet B. et al. Dedicated chaperones coordinate co-translational regulation of ribosomal protein production with ribosome assembly to preserve proteostasis. bioRxiv (posted Oct 2022). https://doi.org/10.1101/2021.10.05.463164 (pillet2022dedicatedchaperonescoordinate pages 1-4, pillet2022dedicatedchaperonescoordinate pages 14-16)
• Dörner K. et al. Ribosome biogenesis factors—from names to functions. The EMBO Journal (Feb 2023). https://doi.org/10.15252/embj.2022112699 (dorner2023ribosomebiogenesisfactors—from pages 1-2)
• Schilke B.A. et al. Functional similarities and differences among subunits of the NAC of Saccharomyces cerevisiae. Cell Stress and Chaperones (Dec 2024). https://doi.org/10.1016/j.cstres.2024.10.004 (schilke2024functionalsimilaritiesand pages 1-3)
• Yang Y.-M., Karbstein K. Ribosome Assembly and Repair. Annual Review of Cell and Developmental Biology (Oct 2024). https://doi.org/10.1146/annurev-cellbio-111822-113326 (yang2024ribosomeassemblyand pages 1-3)

References

1. (pillet2015thededicatedchaperone pages 1-2): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

2. (huber2017molecularbasisfor pages 1-2): Ferdinand M. Huber and André Hoelz. Molecular basis for protection of ribosomal protein l4 from cellular degradation. Nature Communications, Feb 2017. URL: https://doi.org/10.1038/ncomms14354, doi:10.1038/ncomms14354. This article has 37 citations and is from a highest quality peer-reviewed journal.

3. (pillet2015thededicatedchaperone pages 10-12): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

4. (schilke2024functionalsimilaritiesand pages 1-3): Brenda A. Schilke, Thomas Ziegelhoffer, Przemyslaw Domanski, Jaroslaw Marszalek, Bartlomiej Tomiczek, and Elizabeth A. Craig. Functional similarities and differences among subunits of the nascent polypeptide-associated complex (nac) of saccharomyces cerevisiae. Cell Stress and Chaperones, 29:721-734, Dec 2024. URL: https://doi.org/10.1016/j.cstres.2024.10.004, doi:10.1016/j.cstres.2024.10.004. This article has 1 citations and is from a peer-reviewed journal.

5. (pillet2022dedicatedchaperonescoordinate pages 14-16): Benjamin Pillet, Alfonso Méndez-Godoy, Guillaume Murat, Sébastien Favre, Michael Stumpe, Laurent Falquet, and Dieter Kressler. Dedicated chaperones coordinate co-translational regulation of ribosomal protein production with ribosome assembly to preserve proteostasis. BioRxiv, Oct 2022. URL: https://doi.org/10.1101/2021.10.05.463164, doi:10.1101/2021.10.05.463164. This article has 30 citations.

6. (pillet2022dedicatedchaperonescoordinate pages 20-22): Benjamin Pillet, Alfonso Méndez-Godoy, Guillaume Murat, Sébastien Favre, Michael Stumpe, Laurent Falquet, and Dieter Kressler. Dedicated chaperones coordinate co-translational regulation of ribosomal protein production with ribosome assembly to preserve proteostasis. BioRxiv, Oct 2022. URL: https://doi.org/10.1101/2021.10.05.463164, doi:10.1101/2021.10.05.463164. This article has 30 citations.

7. (stelter2015coordinatedribosomall4 pages 3-3): Philipp Stelter, Ferdinand M. Huber, Ruth Kunze, Dirk Flemming, André Hoelz, and Ed Hurt. Coordinated ribosomal l4 protein assembly into the pre-ribosome is regulated by its eukaryote-specific extension. Molecular cell, 58 5:854-62, Jun 2015. URL: https://doi.org/10.1016/j.molcel.2015.03.029, doi:10.1016/j.molcel.2015.03.029. This article has 78 citations and is from a highest quality peer-reviewed journal.

8. (pillet2015thededicatedchaperone pages 18-20): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

9. (yang2024ribosomeassemblyand pages 1-3): Yoon-Mo Yang and Katrin Karbstein. Ribosome assembly and repair. Annual Review of Cell and Developmental Biology, 40:241-264, Oct 2024. URL: https://doi.org/10.1146/annurev-cellbio-111822-113326, doi:10.1146/annurev-cellbio-111822-113326. This article has 18 citations and is from a domain leading peer-reviewed journal.

10. (pillet2015thededicatedchaperone pages 20-21): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

11. (pillet2015thededicatedchaperone pages 17-18): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

12. (pillet2015thededicatedchaperone pages 14-17): Benjamin Pillet, Juan J. García-Gómez, Patrick Pausch, Laurent Falquet, Gert Bange, Jesús de la Cruz, and Dieter Kressler. The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLOS Genetics, 11:e1005565, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005565, doi:10.1371/journal.pgen.1005565. This article has 84 citations and is from a domain leading peer-reviewed journal.

13. (huber2017molecularbasisfor media 4aaddfb0): Ferdinand M. Huber and André Hoelz. Molecular basis for protection of ribosomal protein l4 from cellular degradation. Nature Communications, Feb 2017. URL: https://doi.org/10.1038/ncomms14354, doi:10.1038/ncomms14354. This article has 37 citations and is from a highest quality peer-reviewed journal.

14. (huber2017molecularbasisfor media cb2e78f3): Ferdinand M. Huber and André Hoelz. Molecular basis for protection of ribosomal protein l4 from cellular degradation. Nature Communications, Feb 2017. URL: https://doi.org/10.1038/ncomms14354, doi:10.1038/ncomms14354. This article has 37 citations and is from a highest quality peer-reviewed journal.

15. (huber2017molecularbasisfor media e4ea49ee): Ferdinand M. Huber and André Hoelz. Molecular basis for protection of ribosomal protein l4 from cellular degradation. Nature Communications, Feb 2017. URL: https://doi.org/10.1038/ncomms14354, doi:10.1038/ncomms14354. This article has 37 citations and is from a highest quality peer-reviewed journal.

16. (pillet2022dedicatedchaperonescoordinate pages 1-4): Benjamin Pillet, Alfonso Méndez-Godoy, Guillaume Murat, Sébastien Favre, Michael Stumpe, Laurent Falquet, and Dieter Kressler. Dedicated chaperones coordinate co-translational regulation of ribosomal protein production with ribosome assembly to preserve proteostasis. BioRxiv, Oct 2022. URL: https://doi.org/10.1101/2021.10.05.463164, doi:10.1101/2021.10.05.463164. This article has 30 citations.

17. (dorner2023ribosomebiogenesisfactors—from pages 1-2): Kerstin Dörner, Chiara Ruggeri, Ivo Zemp, and Ulrike Kutay. Ribosome biogenesis factors—from names to functions. The EMBO Journal, Feb 2023. URL: https://doi.org/10.15252/embj.2022112699, doi:10.15252/embj.2022112699. This article has 201 citations.

Citations

1. pillet2015thededicatedchaperone pages 17-18
2. pillet2015thededicatedchaperone pages 10-12
3. pillet2022dedicatedchaperonescoordinate pages 14-16
4. pillet2022dedicatedchaperonescoordinate pages 20-22
5. pillet2022dedicatedchaperonescoordinate pages 1-4
6. yang2024ribosomeassemblyand pages 1-3
7. schilke2024functionalsimilaritiesand pages 1-3
8. huber2017molecularbasisfor pages 1-2
9. pillet2015thededicatedchaperone pages 1-2
10. pillet2015thededicatedchaperone pages 18-20
11. pillet2015thededicatedchaperone pages 20-21
12. pillet2015thededicatedchaperone pages 14-17
13. https://doi.org/10.1371/journal.pgen.1005565;
14. https://doi.org/10.1016/j.molcel.2015.03.029
15. https://doi.org/10.1038/ncomms14354
16. https://doi.org/10.1016/j.molcel.2015.03.029;
17. https://doi.org/10.1371/journal.pgen.1005565
18. https://doi.org/10.1038/ncomms14354;
19. https://doi.org/10.1101/2021.10.05.463164;
20. https://doi.org/10.1016/j.cstres.2024.10.004
21. https://doi.org/10.1101/2021.10.05.463164
22. https://doi.org/10.15252/embj.2022112699
23. https://doi.org/10.1146/annurev-cellbio-111822-113326
24. https://doi.org/10.1371/journal.pgen.1005565,
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