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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: P46683
• Protein Description: RecName: Full=Ankyrin repeat-containing protein YAR1;
• Gene Information: Name=YAR1; OrderedLocusNames=YPL239W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Ankyrin_rpt. (IPR002110); Ankyrin_rpt-contain_sf. (IPR036770); Ank_2 (PF12796)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "YAR1" 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 'YAR1' 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 YAR1 (gene ID: YAR1, UniProt: P46683) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P46683
• Protein Description: RecName: Full=Ankyrin repeat-containing protein YAR1;
• Gene Information: Name=YAR1; OrderedLocusNames=YPL239W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Ankyrin_rpt. (IPR002110); Ankyrin_rpt-contain_sf. (IPR036770); Ank_2 (PF12796)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "YAR1" 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 'YAR1' 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 YAR1 (gene ID: YAR1, UniProt: P46683) 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 YAR1 (UniProt P46683; SGD locus YPL239W) — Functional Annotation

0. Target verification (critical disambiguation)

The gene/protein reviewed here is YAR1 / YPL239W from Saccharomyces cerevisiae strain S288c, matching UniProt accession P46683 and the protein name “Ankyrin repeat-containing protein Yar1”. Primary yeast studies explicitly refer to Yar1 as an ankyrin-repeat protein and experimentally connect it to ribosomal protein Rps3 (uS3) as its dedicated chaperone, aligning with the UniProt description and expected ankyrin-repeat domain function (protein–protein interaction) (koch2012yar1protectsthe pages 1-2, koch2012yar1protectsthe pages 1-1, pillet2017holdonto pages 3-4).

1. Key concepts and definitions (current understanding)

1.1 Dedicated ribosomal-protein chaperones

A central concept for YAR1 is the class of “dedicated chaperones”: specialized factors that bind a specific ribosomal protein (r-protein) to prevent its aggregation/misinteraction and to promote proper delivery to the ribosome assembly pathway. Reviews cite Yar1 as a canonical dedicated chaperone for Rps3/uS3, binding the Rps3 N-terminus (aa ~14–29) (pillet2017holdonto pages 3-4).

1.2 What Yar1 is (and is not)

Yar1 is not an enzyme and no catalytic reaction has been assigned in the cited primary literature; rather, it is best understood as an anti-aggregation, escort-type chaperone whose function is implemented by direct binding to its client ribosomal protein Rps3 (koch2012yar1protectsthe pages 1-2, koch2012yar1protectsthe pages 2-3).

2. Molecular function and mechanism

2.1 Primary molecular function: Rps3 anti-aggregation chaperone

Direct Yar1–Rps3 binding is supported by in vivo affinity purification (near-stoichiometric co-purification) and in vitro complex formation (co-expression/co-elution), consistent with a dedicated chaperone–client relationship (koch2012yar1protectsthe pages 2-3, koch2012yar1protectsthe pages 3-4). Yar1 increases Rps3 solubility and prevents Rps3 aggregation in vitro and in vivo, including experiments where Rps3 is largely insoluble unless Yar1 is present/co-expressed (koch2012yar1protectsthe pages 8-9, koch2012yar1protectsthe pages 2-3, koch2012yar1protectsthe pages 7-8). Mechanistically, an “RNA-mimic/shielding” interpretation has been proposed based on charge complementarity: Rps3 is highly basic while Yar1 is acidic, consistent with shielding basic rRNA-binding surfaces from aberrant interactions (koch2012yar1protectsthe pages 8-9).

2.2 Co-translational capture of nascent Rps3

A 2015 Nature Communications study tested the general hypothesis that dedicated r-protein chaperones capture their clients co-translationally. In that work, affinity purification of Yar1 enriched the mRNA encoding its client Rps3, supporting co-translational association of Yar1 with nascent Rps3 (publication date: 2015-06-26; URL: https://doi.org/10.1038/ncomms8494) (pausch2015cotranslationalcapturingof pages 1-2).

2.3 Nuclear import and handoff: coupling chaperoning to karyopherins

A 2016 Scientific Reports paper provides a detailed model for nuclear import of Rps3 together with Yar1. Key points:

• Rps3 contains an N-terminal monopartite NLS (reported motif 7–10: KKRK) adjacent to the Yar1-binding region (publication date: 2016-11; URL: https://doi.org/10.1038/srep36714) (mitterer2016nuclearimportof pages 1-2, mitterer2016nuclearimportof pages 2-4).
• The major import route is Kap60/Kap95 (importin α/β), with additional karyopherins contributing redundantly (mitterer2016nuclearimportof pages 1-2, mitterer2016nuclearimportof pages 2-4).
• Kap60 and Yar1 compete for binding on the Rps3 N-domain in vitro, yet Kap60 is still found in Rps3/Yar1 complexes in vivo; this is explained by the fact that Rps3 is dimeric, allowing Yar1 to occupy one Rps3 N-domain while Kap60 binds the other, coordinating import while maintaining protection (mitterer2016nuclearimportof pages 1-2, mitterer2016nuclearimportof pages 2-4).

The key biochemical evidence for importin competition and the co-import model is shown in figures from this paper (mitterer2016nuclearimportof media 8e76864a, mitterer2016nuclearimportof media 4e812712).

3. Cellular localization

Steady-state localization of Yar1 is predominantly cytoplasmic, with evidence that Yar1 transiently enters the nucleus and is exported via Xpo1/CRM1 (based on nuclear accumulation upon Xpo1 inhibition). Because no Yar1 NLS was identified whereas Rps3’s N-terminus acts as an NLS, Yar1 is inferred to piggyback with Rps3 into the nucleus (koch2012yar1protectsthe pages 4-6, koch2012yar1protectsthe pages 3-4).

4. Biological role and pathways

4.1 Role in 40S small subunit biogenesis

Loss of YAR1 produces clear 40S ribosome biogenesis/maturation phenotypes. Yar1 acts upstream of Rps3 incorporation by ensuring a soluble supply of Rps3 for assembly. Consistent phenotypes reported include:

• Accumulation of 20S pre-rRNA and defects consistent with impaired cytoplasmic maturation/export of pre-40S particles (koch2012yar1protectsthe pages 4-6, koch2012yar1protectsthe pages 6-7, koch2012yar1protectsthe pages 1-1).
• Polysome/ribosome profile alterations: reduced 40S peak with excess free 60S and reduced polysomes (koch2012yar1protectsthe pages 6-7, loar2004geneticandbiochemical pages 9-11).

4.2 Genetic interaction network centered on RPS3 (and links to LTV1)

A 2004 Genetics paper reported that Yar1 physically and genetically interacts with Rps3 and functionally relates to the 40S biogenesis factor Ltv1, with both yar1 and ltv1 mutants showing 40S production defects and stress-sensitive phenotypes (publication date: 2004-12; URL: https://doi.org/10.1534/genetics.104.032656) (loar2004geneticandbiochemical pages 8-9, loar2004geneticandbiochemical pages 9-11). Importantly, RPS3 overexpression suppresses yar1 mutant phenotypes, supporting a model where Yar1’s key role is maintaining Rps3 function/availability (loar2004geneticandbiochemical pages 8-9, loar2004geneticandbiochemical pages 9-11).

5. Phenotypes and quantitative/statistical findings

5.1 Essentiality and growth

YAR1 is non-essential, but yar1Δ cells show slow growth, particularly at lower temperature, and phenotypes similar to compromised Rps3 function; combining yar1Δ with defective rps3 alleles can produce stronger defects including synthetic sickness/lethality (koch2012yar1protectsthe pages 4-6, koch2012yar1protectsthe pages 6-7).

5.2 Quantitative data (selected)

• In early genetic/biochemical analyses, yar1 and ltv1 mutants exhibited an approximately ~50% reduction in the 40S:60S ratio relative to wild type (loar2004geneticandbiochemical pages 9-11).
• In vitro anti-aggregation assays for Rps3 used ultracentrifugation (reported 200,000 g) and showed that Yar1 keeps Rps3 in the supernatant (soluble fraction) (koch2012yar1protectsthe pages 2-3, koch2012yar1protectsthe pages 7-8).
• Dedicated-chaperone biology is motivated by very high ribosome production demand: exponentially growing yeast produce about ~2,000 ribosomes/min and thus must synthesize >160,000 ribosomal proteins/min (publication date: 2015-06-26; URL: https://doi.org/10.1038/ncomms8494) (pausch2015cotranslationalcapturingof pages 1-2).

6. Recent developments (prioritizing 2023–2024)

6.1 Ribosome repair under oxidative stress: Yar1 as a negative control for repair activity

A 2023 Molecular Cell study discovered a chaperone-directed ribosome repair mechanism in yeast for oxidatively damaged ribosomal proteins (notably Tsr2/Rps26). In that context, the authors report that chaperone-dependent release was specific to Tsr2/Rps26, because neither Rps2 nor Rps3 were released by their chaperones (Tsr4 and Yar1, respectively). Additionally, H2O2 exposure increased ribosome association for Tsr2 but not for Yar1, supporting that Yar1 is not acting as the cognate “release/repair” factor for oxidized Rps3 in the tested system (publication date: 2023-05; URL: https://doi.org/10.1016/j.molcel.2023.03.030) (yang2023chaperonedirectedribosomerepair pages 5-7).

6.2 Reviews (2024) integrating Yar1 into ribosome assembly/repair landscape

A 2024 Annual Review of Cell and Developmental Biology review synthesizes progress in ribosome assembly and repair and frames dedicated r-protein chaperones (including the Rps3 system) as part of broader ribosome homeostasis (publication date: 2024-10; URL: https://doi.org/10.1146/annurev-cellbio-111822-113326) (yang2024ribosomeassemblyand pages 8-9). A 2024 Biomolecules review focusing on the 40S “beak” region also discusses Rps3/uS3-centric pathways (including quality control and collision signaling at/near uS3) and notes the role of Yar1 in the assembly context (publication date: 2024-07; URL: https://doi.org/10.3390/biom14070882) (martinvillanueva2024thebeakof pages 10-11).

Overall, the 2023–2024 literature primarily extends context (ribosome repair and quality control; assembly–stress interfaces) rather than redefining Yar1’s core, best-supported role as the dedicated chaperone for Rps3 (yang2024ribosomeassemblyand pages 8-9, yang2023chaperonedirectedribosomerepair pages 5-7).

7. Current applications and real-world implementations

YAR1 is widely used as a model factor to study:

• Protein quality control of ribosomal proteins (anti-aggregation strategies for basic r-proteins) (koch2012yar1protectsthe pages 1-2, koch2012yar1protectsthe pages 7-8).
• Co-translational chaperoning (mRNA enrichment and nascent-chain capture paradigms) (pausch2015cotranslationalcapturingof pages 1-2).
• Coordination between chaperoning and nuclear transport (handoff/competition between dedicated chaperone Yar1 and importin Kap60/Kap95) (mitterer2016nuclearimportof pages 1-2, mitterer2016nuclearimportof pages 2-4).

No Yar1-specific industrial or therapeutic application was identified in the retrieved evidence; its “real-world” impact is primarily as an experimentally tractable paradigm for eukaryotic ribosome biogenesis and proteostasis (pillet2017holdonto pages 3-4, yang2024ribosomeassemblyand pages 8-9).

8. Expert opinion and synthesis (authoritative interpretation)

The most consistent expert-level synthesis across primary and review sources is that Yar1’s primary, evolutionarily motivated job is to shield the aggregation-prone, basic N-terminal region of Rps3/uS3 from nonspecific interactions until it is safely delivered for 40S assembly (koch2012yar1protectsthe pages 1-2, pillet2017holdonto pages 3-4). The 2016 mechanistic import model further suggests that Yar1’s function is integrated into nucleocytoplasmic transport by an elegant “division of labor” on an Rps3 dimer: one N-domain protected by Yar1 while the other is engaged by Kap60 for import, enabling both protection and transport (mitterer2016nuclearimportof pages 2-4, mitterer2016nuclearimportof media 4e812712).

Evidence summary table

The following table consolidates key findings (function, partners, localization, phenotypes, quantitative data, and 2023–2024 context) with publication dates and URLs.

Table: This table summarizes the most relevant evidence for the identity, function, mechanism, localization, phenotypes, and recent literature context of S. cerevisiae YAR1 (P46683/YPL239W). It is designed as a compact, citation-ready reference for the final research report.

Key primary sources (with publication dates and URLs)

• Loar et al. 2004-12, Genetics: https://doi.org/10.1534/genetics.104.032656 (loar2004geneticandbiochemical pages 8-9, loar2004geneticandbiochemical pages 9-11)
• Koch et al. 2012-06, J Biol Chem: https://doi.org/10.1074/jbc.m112.365791 (koch2012yar1protectsthe pages 4-6, koch2012yar1protectsthe pages 2-3)
• Pausch et al. 2015-06-26, Nat Commun: https://doi.org/10.1038/ncomms8494 (pausch2015cotranslationalcapturingof pages 1-2)
• Mitterer et al. 2016-11, Sci Rep: https://doi.org/10.1038/srep36714 (mitterer2016nuclearimportof pages 1-2, mitterer2016nuclearimportof media 4e812712)
• Yang et al. 2023-05, Mol Cell: https://doi.org/10.1016/j.molcel.2023.03.030 (yang2023chaperonedirectedribosomerepair pages 5-7)
• Yang & Karbstein 2024-10, Annu Rev Cell Dev Biol: https://doi.org/10.1146/annurev-cellbio-111822-113326 (yang2024ribosomeassemblyand pages 8-9)
• Martín‑Villanueva et al. 2024-07, Biomolecules: https://doi.org/10.3390/biom14070882 (martinvillanueva2024thebeakof pages 10-11)

References

1. (koch2012yar1protectsthe pages 1-2): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

2. (koch2012yar1protectsthe pages 1-1): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

3. (pillet2017holdonto pages 3-4): Benjamin Pillet, Valentin Mitterer, Dieter Kressler, and Brigitte Pertschy. Hold on to your friends: dedicated chaperones of ribosomal proteins. BioEssays, 39:1-12, Jan 2017. URL: https://doi.org/10.1002/bies.201600153, doi:10.1002/bies.201600153. This article has 93 citations and is from a peer-reviewed journal.

4. (koch2012yar1protectsthe pages 2-3): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

5. (koch2012yar1protectsthe pages 3-4): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

6. (koch2012yar1protectsthe pages 8-9): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

7. (koch2012yar1protectsthe pages 7-8): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

8. (pausch2015cotranslationalcapturingof pages 1-2): Patrick Pausch, Ujjwala Singh, Yasar Luqman Ahmed, Benjamin Pillet, Guillaume Murat, Florian Altegoer, Gunter Stier, Matthias Thoms, Ed Hurt, Irmgard Sinning, Gert Bange, and Dieter Kressler. Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nature Communications, Jun 2015. URL: https://doi.org/10.1038/ncomms8494, doi:10.1038/ncomms8494. This article has 93 citations and is from a highest quality peer-reviewed journal.

9. (mitterer2016nuclearimportof pages 1-2): Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Nuclear import of dimerized ribosomal protein rps3 in complex with its chaperone yar1. Scientific Reports, Nov 2016. URL: https://doi.org/10.1038/srep36714, doi:10.1038/srep36714. This article has 38 citations and is from a peer-reviewed journal.

10. (mitterer2016nuclearimportof pages 2-4): Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Nuclear import of dimerized ribosomal protein rps3 in complex with its chaperone yar1. Scientific Reports, Nov 2016. URL: https://doi.org/10.1038/srep36714, doi:10.1038/srep36714. This article has 38 citations and is from a peer-reviewed journal.

11. (mitterer2016nuclearimportof media 8e76864a): Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Nuclear import of dimerized ribosomal protein rps3 in complex with its chaperone yar1. Scientific Reports, Nov 2016. URL: https://doi.org/10.1038/srep36714, doi:10.1038/srep36714. This article has 38 citations and is from a peer-reviewed journal.

12. (mitterer2016nuclearimportof media 4e812712): Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Nuclear import of dimerized ribosomal protein rps3 in complex with its chaperone yar1. Scientific Reports, Nov 2016. URL: https://doi.org/10.1038/srep36714, doi:10.1038/srep36714. This article has 38 citations and is from a peer-reviewed journal.

13. (koch2012yar1protectsthe pages 4-6): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

14. (koch2012yar1protectsthe pages 6-7): Barbara Koch, Valentin Mitterer, Johannes Niederhauser, Tamsyn Stanborough, Guillaume Murat, Gerald Rechberger, Helmut Bergler, Dieter Kressler, and Brigitte Pertschy. Yar1 protects the ribosomal protein rps3 from aggregation. Journal of Biological Chemistry, 287:21806-21815, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.365791, doi:10.1074/jbc.m112.365791. This article has 78 citations and is from a domain leading peer-reviewed journal.

15. (loar2004geneticandbiochemical pages 9-11): Jesse W Loar, Robert M Seiser, Alexandra E Sundberg, Holly J Sagerson, Nasreen Ilias, Pamela Zobel-Thropp, Elizabeth A Craig, and Deborah E Lycan. Genetic and biochemical interactions among yar1, ltv1 and rps3 define novel links between environmental stress and ribosome biogenesis in saccharomyces cerevisiae. Genetics, 168:1877-1889, Dec 2004. URL: https://doi.org/10.1534/genetics.104.032656, doi:10.1534/genetics.104.032656. This article has 70 citations and is from a domain leading peer-reviewed journal.

16. (loar2004geneticandbiochemical pages 8-9): Jesse W Loar, Robert M Seiser, Alexandra E Sundberg, Holly J Sagerson, Nasreen Ilias, Pamela Zobel-Thropp, Elizabeth A Craig, and Deborah E Lycan. Genetic and biochemical interactions among yar1, ltv1 and rps3 define novel links between environmental stress and ribosome biogenesis in saccharomyces cerevisiae. Genetics, 168:1877-1889, Dec 2004. URL: https://doi.org/10.1534/genetics.104.032656, doi:10.1534/genetics.104.032656. This article has 70 citations and is from a domain leading peer-reviewed journal.

17. (yang2023chaperonedirectedribosomerepair pages 5-7): Yoon-Mo Yang, Youngeun Jung, Daniel Abegg, Alexander Adibekian, Kate S. Carroll, and Katrin Karbstein. Chaperone-directed ribosome repair after oxidative damage. Molecular Cell, 83:1527-1537.e5, May 2023. URL: https://doi.org/10.1016/j.molcel.2023.03.030, doi:10.1016/j.molcel.2023.03.030. This article has 70 citations and is from a highest quality peer-reviewed journal.

18. (yang2024ribosomeassemblyand pages 8-9): 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.

19. (martinvillanueva2024thebeakof pages 10-11): Sara Martín-Villanueva, Carla V. Galmozzi, Carmen Ruger-Herreros, Dieter Kressler, and Jesús de la Cruz. The beak of eukaryotic ribosomes: life, work and miracles. Biomolecules, 14:882, Jul 2024. URL: https://doi.org/10.3390/biom14070882, doi:10.3390/biom14070882. This article has 4 citations.

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