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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: P25040
• Protein Description: RecName: Full=uS5 assembly chaperone {ECO:0000305}; AltName: Full=20S rRNA accumulation protein 4;
• Gene Information: Name=TSR4; OrderedLocusNames=YOL022C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TSR4 family. .
• Key Domains: PDCD2_C. (IPR007320); PDCD2_C (PF04194)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "TSR4" 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 'TSR4' 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 TSR4 (gene ID: TSR4, UniProt: P25040) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P25040
• Protein Description: RecName: Full=uS5 assembly chaperone {ECO:0000305}; AltName: Full=20S rRNA accumulation protein 4;
• Gene Information: Name=TSR4; OrderedLocusNames=YOL022C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TSR4 family. .
• Key Domains: PDCD2_C. (IPR007320); PDCD2_C (PF04194)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "TSR4" 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 'TSR4' 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 TSR4 (gene ID: TSR4, UniProt: P25040) 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 TSR4 (UniProt P25040; YOL022C)

0) Target verification (gene/protein identity)

The yeast gene TSR4 (ordered locus YOL022C; UniProt P25040) corresponds to the ribosome biogenesis factor historically described as “20S rRNA accumulation protein 4” and is now experimentally established as a uS5 (Rps2) assembly chaperone. Primary yeast studies that biochemically and genetically characterize Tsr4 (the protein product of TSR4) identify its client as the small-subunit ribosomal protein Rps2/uS5 and show a cytoplasmic chaperone role (black2019tsr4isa pages 1-3, black2019tsr4isa pages 15-17).

Domain/family verification matches the UniProt context: a comparative genomics analysis reports that yeast TSR4 is annotated in Pfam as containing a C-terminal PDCD2_C domain and unifies TSR4 with eukaryotic homologs PDCD2/PDCD2L (and related proteins) into a larger duplicated-repeat superfamily termed TYPP, proposed to mediate protein–protein interactions consistent with chaperone-like function (burroughs2014analysisoftwo pages 3-5, burroughs2014analysisoftwo pages 5-7).

1) Key concepts and current understanding

1.1 Dedicated ribosomal-protein chaperones (concept)

Eukaryotic ribosome biogenesis requires safe handling of newly synthesized ribosomal proteins (RPs), many of which are highly basic and/or contain intrinsically disordered, eukaryote-specific extensions that are aggregation-prone. Dedicated RP chaperones are specialized factors that bind specific RPs to promote solubility, prevent nonproductive interactions, and enable correct delivery/assembly (rossler2019tsr4andnap1 pages 1-2, black2019tsr4isa pages 1-3).

TSR4/Tsr4 is a canonical example of this class: it is described as a dedicated chaperone that binds Rps2/uS5 and promotes its solubility and productive assembly into 40S subunits (rossler2019tsr4andnap1 pages 14-15, black2019tsr4isa pages 15-17).

1.2 What TSR4 does at a molecular level

Molecular function (best-supported): Tsr4 binds nascent Rps2/uS5 co-translationally in the cytoplasm and acts as a client-specific chaperone to stabilize Rps2 and support 40S biogenesis (black2019tsr4isa pages 1-3, rossler2019tsr4andnap1 pages 12-13).

Client recognition: Multiple experiments map Tsr4 recognition primarily to the eukaryote-specific N-terminal extension of Rps2, with the first ~42 amino acids sufficient/required for robust interaction (rossler2019tsr4andnap1 pages 12-13). This binding is consistent with the general principle that dedicated chaperones often recognize eukaryote-specific RP extensions (rossler2019tsr4andnap1 pages 1-2).

Chaperone effect on solubility: Rps2 expressed alone is aggregation-prone, while co-expression with Tsr4 keeps Rps2 soluble and supports complex formation in vitro and in vivo (rossler2019tsr4andnap1 pages 14-15).

1.3 Cellular process and pathway context

TSR4 acts within small (40S) ribosomal subunit biogenesis, specifically by enabling accumulation and assembly of Rps2/uS5 into pre-40S particles. Loss of TSR4 phenocopies reduced uS5 availability, producing severe 40S defects and pre-40S export problems (black2019tsr4isa pages 15-17, rossler2019tsr4andnap1 pages 15-16).

A 2023 review synthesizing cross-species evidence frames TSR4/PDCD2 as an evolutionarily conserved uS5 chaperone module that monitors uS5 availability/folding and supports pre-rRNA maturation outcomes consistent with 40S assembly (e.g., accumulation of 20S/21S pre-rRNAs and reduced uS5 incorporation when the module is perturbed) (landryvoyer2023ribosomalproteinus5 pages 6-8, landryvoyer2023ribosomalproteinus5 pages 8-10).

2) Experimentally supported biology of yeast TSR4/Tsr4

2.1 Binding partners and mechanism

Primary binding partner: Rps2/uS5.

Co-translational association: Tsr4 purifications enrich RPS2 mRNA, consistent with binding to nascent chains during translation; interaction mapping supports specificity for the Rps2 N-terminus (rossler2019tsr4andnap1 pages 12-13). Black et al. likewise report co-translational association and dependence on the eukaryote-specific Rps2 N-terminal extension (black2019tsr4isa pages 1-3).

Key mechanistic inference: Tsr4 appears to act upstream of nuclear pre-40S assembly, stabilizing Rps2 before (or during) handoff to nuclear import/assembly pathways, rather than being a stable component of nuclear pre-ribosomes (black2019tsr4isa pages 17-20, black2019tsr4isa pages 15-17).

2.2 Subcellular localization (where it acts)

Multiple lines of evidence support that yeast Tsr4 is predominantly cytoplasmic and does not undergo obvious Crm1-dependent shuttling:

• Black et al. performed a Crm1 inhibition assay (leptomycin B in a Crm1-sensitized strain) where the Crm1 cargo control Nmd3 relocalizes to the nucleus, but Tsr4 remains cytoplasmic, arguing against Crm1-dependent nucleocytoplasmic shuttling (black2019tsr4isa media 141d3d19).
• Functional mutation of a predicted NLS in Tsr4 still complements loss of Tsr4, consistent with the idea that nuclear entry is not required for its essential function (black2019tsr4isa pages 15-17).

2.3 Consequences of TSR4 loss: phenotypes and readouts

Ribosome biogenesis output (polysome profiling): Loss of Tsr4 produces a dramatic small subunit defect described as a missing 40S peak, increased free 60S, and reduced 80S/polysomes (rossler2019tsr4andnap1 pages 15-16).

Pre-40S export / nuclear accumulation: Repression of TSR4 (or RPS2) causes nuclear accumulation of ITS1, interpreted as a block in pre-40S export (black2019tsr4isa pages 15-17).

Rps2 abundance: Perturbation of Tsr4 reduces Rps2 levels and phenocopies Rps2 depletion, consistent with a stabilizing chaperone function (black2019tsr4isa pages 1-3).

Genetic suppression: Increasing RPS2 dosage can partially bypass TSR4 loss (viability rescue), supporting a direct client-chaperone relationship; however, the rescued strains have impaired growth (growth defects at 25–30°C; inviability at 37°C), consistent with incomplete restoration of robust biogenesis (rossler2019tsr4andnap1 pages 15-16).

Quantitative notes:
* Estimated abundance: ~1,500 Tsr4 molecules/cell (black2019tsr4isa pages 6-8).
* Rps2-GFP steady-state localization: in wild-type, ~72% of cells show nuclear exclusion of Rps2-GFP; in the absence of Tsr4, Rps2 reporters show nuclear signal/accumulation (rossler2019tsr4andnap1 pages 15-16, rossler2019tsr4andnap1 pages 16-16).

3) Recent developments and latest research (2023–2024 prioritized)

3.1 2023: Nuclear import of Rps2/uS5 is Tsr4-independent

A focused mechanistic study (Steiner et al., July 2023) dissected nuclear import signals of yeast Rps2/uS5. Key findings:

• An internal region Rps2(76–145) is sufficient for nuclear targeting and contains a critical basic cluster R95/R97/K99; mutation of these residues strongly disrupts nuclear localization (steiner2023dissectingthenuclear pages 6-9, steiner2023dissectingthenuclear pages 1-2).
• A second nuclear targeting element lies in the N-terminal region (~10–28) (RG-rich/basic), which overlaps the Tsr4-binding region (steiner2023dissectingthenuclear pages 1-2, steiner2023dissectingthenuclear pages 15-18).
• Importin Pse1 (Kap121) interacts with and contributes to import of the internal NLS, but import is not exclusively Pse1-dependent, consistent with redundancy among importins (steiner2023dissectingthenuclear pages 2-4, steiner2023dissectingthenuclear pages 15-18).
• Critically, nuclear import via either the internal or N-terminal element does not require Tsr4, supporting a model where Tsr4’s essential function is chaperoning/assembly competence rather than serving as the import adaptor (steiner2023dissectingthenuclear pages 2-4, steiner2023dissectingthenuclear pages 13-15).

This resolves an important mechanistic ambiguity noted in reviews: because Tsr4 binds near an NLS, it was plausible that Tsr4 was required for import; instead, import can occur without it, while assembly remains defective (steiner2023dissectingthenuclear pages 2-4, rossler2019tsr4andnap1 pages 16-16).

3.2 2023: Consolidation of the conserved uS5 interactome

A 2023 review (Landry-Voyer et al., May 2023) synthesizes evidence that PDCD2 and its homologs (including yeast Tsr4) are dedicated uS5 chaperones that recognize nascent uS5 co-translationally and whose perturbation phenocopies uS5 deficiency (landryvoyer2023ribosomalproteinus5 pages 6-8, landryvoyer2023ribosomalproteinus5 pages 8-10). The review also highlights unanswered questions, including how the chaperone–uS5 complex is disassembled and coordinated with import/assembly (landryvoyer2023ribosomalproteinus5 pages 8-10).

3.3 2024: Framing Tsr4 in modern “chaperome” and coordination questions

A 2024 Biomolecules editorial (Pertschy & Zierler, Dec 2024) highlights the open question created by overlap of Tsr4 binding and an N-terminal uS5 NLS: how are chaperoning and import coordinated in space and time? (pertschy2024ribosomalproteinsin pages 1-2).

A 2024 Annual Review (Yang & Karbstein, Oct 2024) places dedicated RP chaperones (including the Tsr4/Nap1 chaperome work) into a broader conceptual framework where specialized chaperones can contribute to assembly and potentially to maintenance/repair processes (yang2024ribosomeassemblyand pages 20-21, yang2024ribosomeassemblyand pages 11-13).

3.4 2023: Ribosome repair after oxidative damage—Tsr4 does not extract Rps2

Yang et al. (Molecular Cell, May 2023) demonstrated chaperone-mediated extraction of oxidized Rps26 by Tsr2 during oxidative stress, but explicitly report that neither Rps2 nor Rps3 were released by their chaperones (Tsr4 and Yar1) in their in vitro extraction assays (yang2023chaperonedirectedribosomerepair pages 3-5, yang2023chaperonedirectedribosomerepair pages 5-7). This suggests that, unlike Tsr2–Rps26, the Tsr4–Rps2 pair is not (or is not readily) deployed for extraction-based repair under those experimental conditions.

4) Applications and real-world implementations

4.1 TSR4 as an experimental handle for uS5 handling and 40S biogenesis

In yeast, TSR4 is used as a mechanistic probe to study co-translational RP capture, client stabilization, and the pathway linking RP availability to pre-40S export. The strong, diagnostic phenotypes (missing 40S peak; nuclear ITS1 accumulation) provide clear, implementation-ready assays for perturbations in the uS5 supply chain (rossler2019tsr4andnap1 pages 15-16, black2019tsr4isa pages 15-17).

4.2 Translational relevance via conserved homologs (PDCD2/PDCD2L)

While the present target is yeast TSR4, the TSR4–PDCD2/PDCD2L homology provides direct translational relevance: PDCD2 is described as a conserved uS5 chaperone that underlies essential roles in proliferation and development, and has reported associations with human disease contexts (as summarized in the 2023 uS5 review) (landryvoyer2023ribosomalproteinus5 pages 6-8, landryvoyer2023ribosomalproteinus5 pages 8-10). PDCD2L is discussed as a candidate late-acting uS5 interactor and potential pre-40S export adaptor (XPO1/CRM1-associated via an NES), supporting a conserved “uS5 handling network” spanning chaperoning and nucleocytoplasmic trafficking (landryvoyer2023ribosomalproteinus5 pages 8-10, landryvoyer2023ribosomalproteinus5 pages 10-12).

5) Expert synthesis and open questions

Collectively, the best-supported model is that Tsr4 is a cytoplasmic, co-translational uS5 chaperone that captures the eukaryote-specific N-terminus of Rps2, promotes soluble/assembly-competent Rps2 accumulation, and enables downstream 40S assembly and pre-40S export. Nuclear import of Rps2 proceeds via at least two NLS elements and importin-β pathways that do not require Tsr4, implying a handoff step from Tsr4-bound uS5 to importins and/or other factors remains to be mechanistically defined (black2019tsr4isa pages 17-20, steiner2023dissectingthenuclear pages 2-4).

Key unresolved areas highlighted across primary studies and recent reviews include (i) how the limited pool of Tsr4 efficiently targets nascent Rps2 (possible mRNA targeting), (ii) what triggers Tsr4 release from Rps2, and (iii) how binding overlaps with N-terminal targeting signals without blocking productive import/assembly (black2019tsr4isa pages 17-20, landryvoyer2023ribosomalproteinus5 pages 8-10, pertschy2024ribosomalproteinsin pages 1-2).

Evidence summary table

The following table consolidates major conclusions, assays, and quantitative notes.

Table: This table condenses the main experimentally supported findings for Saccharomyces cerevisiae TSR4 (UniProt P25040), including its chaperone function, binding to Rps2/uS5, localization, and role in 40S ribosome biogenesis. It also highlights useful quantitative observations and cites the supporting evidence by context ID.

Visual evidence

A key localization control supporting cytoplasmic restriction of Tsr4 is shown in Black et al. 2019 Figure 8B: in a leptomycin B Crm1 export-blocking assay, the Crm1 cargo control Nmd3 accumulates in the nucleus while Tsr4 remains cytoplasmic (black2019tsr4isa media 141d3d19).

Key references (with URLs and publication dates)

• Black JJ, Musalgaonkar S, Johnson AW. Tsr4 Is a Cytoplasmic Chaperone for the Ribosomal Protein Rps2 in Saccharomyces cerevisiae. Molecular and Cellular Biology. Sep 2019. https://doi.org/10.1128/mcb.00094-19 (black2019tsr4isa pages 1-3)
• Rössler I et al. Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME. Nucleic Acids Research. May 2019. https://doi.org/10.1093/nar/gkz317 (rossler2019tsr4andnap1 pages 1-2)
• Steiner A et al. Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5). Biomolecules. Jul 2023. https://doi.org/10.3390/biom13071127 (steiner2023dissectingthenuclear pages 1-2)
• Landry-Voyer A-M et al. Ribosomal Protein uS5 and Friends: Protein–Protein Interactions Involved in Ribosome Assembly and Beyond. Biomolecules. May 2023. https://doi.org/10.3390/biom13050853 (landryvoyer2023ribosomalproteinus5 pages 6-8)
• Yang Y-M et al. Chaperone-directed ribosome repair after oxidative damage. Molecular Cell. May 2023. https://doi.org/10.1016/j.molcel.2023.03.030 (yang2023chaperonedirectedribosomerepair pages 3-5)
• 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)
• Pertschy B, Zierler I. Ribosomal Proteins in Ribosome Assembly. Biomolecules. Dec 2024. https://doi.org/10.3390/biom15010013 (pertschy2024ribosomalproteinsin pages 1-2)

References

1. (black2019tsr4isa pages 1-3): Joshua J. Black, Sharmishtha Musalgaonkar, and Arlen W. Johnson. Tsr4 is a cytoplasmic chaperone for the ribosomal protein rps2 in saccharomyces cerevisiae. Molecular and Cellular Biology, Sep 2019. URL: https://doi.org/10.1128/mcb.00094-19, doi:10.1128/mcb.00094-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

2. (black2019tsr4isa pages 15-17): Joshua J. Black, Sharmishtha Musalgaonkar, and Arlen W. Johnson. Tsr4 is a cytoplasmic chaperone for the ribosomal protein rps2 in saccharomyces cerevisiae. Molecular and Cellular Biology, Sep 2019. URL: https://doi.org/10.1128/mcb.00094-19, doi:10.1128/mcb.00094-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

3. (burroughs2014analysisoftwo pages 3-5): A. M. Burroughs, L. Aravind, and R. Emes. Analysis of two domains with novel rna-processing activities throws light on the complex evolution of ribosomal rna biogenesis. Frontiers in Genetics, Dec 2014. URL: https://doi.org/10.3389/fgene.2014.00424, doi:10.3389/fgene.2014.00424. This article has 26 citations and is from a peer-reviewed journal.

4. (burroughs2014analysisoftwo pages 5-7): A. M. Burroughs, L. Aravind, and R. Emes. Analysis of two domains with novel rna-processing activities throws light on the complex evolution of ribosomal rna biogenesis. Frontiers in Genetics, Dec 2014. URL: https://doi.org/10.3389/fgene.2014.00424, doi:10.3389/fgene.2014.00424. This article has 26 citations and is from a peer-reviewed journal.

5. (rossler2019tsr4andnap1 pages 1-2): Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, and Brigitte Pertschy. Tsr4 and nap1, two novel members of the ribosomal protein chaperome. Nucleic Acids Research, 47:6984-7002, May 2019. URL: https://doi.org/10.1093/nar/gkz317, doi:10.1093/nar/gkz317. This article has 38 citations and is from a highest quality peer-reviewed journal.

6. (rossler2019tsr4andnap1 pages 14-15): Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, and Brigitte Pertschy. Tsr4 and nap1, two novel members of the ribosomal protein chaperome. Nucleic Acids Research, 47:6984-7002, May 2019. URL: https://doi.org/10.1093/nar/gkz317, doi:10.1093/nar/gkz317. This article has 38 citations and is from a highest quality peer-reviewed journal.

7. (rossler2019tsr4andnap1 pages 12-13): Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, and Brigitte Pertschy. Tsr4 and nap1, two novel members of the ribosomal protein chaperome. Nucleic Acids Research, 47:6984-7002, May 2019. URL: https://doi.org/10.1093/nar/gkz317, doi:10.1093/nar/gkz317. This article has 38 citations and is from a highest quality peer-reviewed journal.

8. (rossler2019tsr4andnap1 pages 15-16): Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, and Brigitte Pertschy. Tsr4 and nap1, two novel members of the ribosomal protein chaperome. Nucleic Acids Research, 47:6984-7002, May 2019. URL: https://doi.org/10.1093/nar/gkz317, doi:10.1093/nar/gkz317. This article has 38 citations and is from a highest quality peer-reviewed journal.

9. (landryvoyer2023ribosomalproteinus5 pages 6-8): Anne-Marie Landry-Voyer, Zabih Mir Hassani, Mariano Avino, and François Bachand. Ribosomal protein us5 and friends: protein–protein interactions involved in ribosome assembly and beyond. Biomolecules, 13:853, May 2023. URL: https://doi.org/10.3390/biom13050853, doi:10.3390/biom13050853. This article has 20 citations.

10. (landryvoyer2023ribosomalproteinus5 pages 8-10): Anne-Marie Landry-Voyer, Zabih Mir Hassani, Mariano Avino, and François Bachand. Ribosomal protein us5 and friends: protein–protein interactions involved in ribosome assembly and beyond. Biomolecules, 13:853, May 2023. URL: https://doi.org/10.3390/biom13050853, doi:10.3390/biom13050853. This article has 20 citations.

11. (black2019tsr4isa pages 17-20): Joshua J. Black, Sharmishtha Musalgaonkar, and Arlen W. Johnson. Tsr4 is a cytoplasmic chaperone for the ribosomal protein rps2 in saccharomyces cerevisiae. Molecular and Cellular Biology, Sep 2019. URL: https://doi.org/10.1128/mcb.00094-19, doi:10.1128/mcb.00094-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

12. (black2019tsr4isa media 141d3d19): Joshua J. Black, Sharmishtha Musalgaonkar, and Arlen W. Johnson. Tsr4 is a cytoplasmic chaperone for the ribosomal protein rps2 in saccharomyces cerevisiae. Molecular and Cellular Biology, Sep 2019. URL: https://doi.org/10.1128/mcb.00094-19, doi:10.1128/mcb.00094-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

13. (black2019tsr4isa pages 6-8): Joshua J. Black, Sharmishtha Musalgaonkar, and Arlen W. Johnson. Tsr4 is a cytoplasmic chaperone for the ribosomal protein rps2 in saccharomyces cerevisiae. Molecular and Cellular Biology, Sep 2019. URL: https://doi.org/10.1128/mcb.00094-19, doi:10.1128/mcb.00094-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

14. (rossler2019tsr4andnap1 pages 16-16): Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, and Brigitte Pertschy. Tsr4 and nap1, two novel members of the ribosomal protein chaperome. Nucleic Acids Research, 47:6984-7002, May 2019. URL: https://doi.org/10.1093/nar/gkz317, doi:10.1093/nar/gkz317. This article has 38 citations and is from a highest quality peer-reviewed journal.

15. (steiner2023dissectingthenuclear pages 6-9): Andreas Steiner, Sébastien Favre, Maximilian Mack, Annika Hausharter, Benjamin Pillet, Jutta Hafner, Valentin Mitterer, Dieter Kressler, Brigitte Pertschy, and Ingrid Zierler. Dissecting the nuclear import of the ribosomal protein rps2 (us5). Biomolecules, 13:1127, Jul 2023. URL: https://doi.org/10.3390/biom13071127, doi:10.3390/biom13071127. This article has 7 citations.

16. (steiner2023dissectingthenuclear pages 1-2): Andreas Steiner, Sébastien Favre, Maximilian Mack, Annika Hausharter, Benjamin Pillet, Jutta Hafner, Valentin Mitterer, Dieter Kressler, Brigitte Pertschy, and Ingrid Zierler. Dissecting the nuclear import of the ribosomal protein rps2 (us5). Biomolecules, 13:1127, Jul 2023. URL: https://doi.org/10.3390/biom13071127, doi:10.3390/biom13071127. This article has 7 citations.

17. (steiner2023dissectingthenuclear pages 15-18): Andreas Steiner, Sébastien Favre, Maximilian Mack, Annika Hausharter, Benjamin Pillet, Jutta Hafner, Valentin Mitterer, Dieter Kressler, Brigitte Pertschy, and Ingrid Zierler. Dissecting the nuclear import of the ribosomal protein rps2 (us5). Biomolecules, 13:1127, Jul 2023. URL: https://doi.org/10.3390/biom13071127, doi:10.3390/biom13071127. This article has 7 citations.

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Citations

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3. yang2023chaperonedirectedribosomerepair pages 3-5
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