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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: P40314
• Protein Description: RecName: Full=Nascent polypeptide-associated complex subunit beta-2; Short=NAC-beta-2; AltName: Full=BTF3 homolog BTT1; AltName: Full=Beta-2-NAC;
• Gene Information: Name=BTT1; OrderedLocusNames=YDR252W; ORFNames=YD9320A.02;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the NAC-beta family. .
• Key Domains: BTF3. (IPR039370); NAC_A/B_dom_sf. (IPR038187); Nas_poly-pep-assoc_cplx_dom. (IPR002715); NAC (PF01849)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BTT1" 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 'BTT1' 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 BTT1 (gene ID: BTT1, UniProt: P40314) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P40314
• Protein Description: RecName: Full=Nascent polypeptide-associated complex subunit beta-2; Short=NAC-beta-2; AltName: Full=BTF3 homolog BTT1; AltName: Full=Beta-2-NAC;
• Gene Information: Name=BTT1; OrderedLocusNames=YDR252W; ORFNames=YD9320A.02;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the NAC-beta family. .
• Key Domains: BTF3. (IPR039370); NAC_A/B_dom_sf. (IPR038187); Nas_poly-pep-assoc_cplx_dom. (IPR002715); NAC (PF01849)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BTT1" 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 'BTT1' 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 BTT1 (gene ID: BTT1, UniProt: P40314) 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.

Comprehensive research report: BTT1 / YDR252W (UniProt P40314) in Saccharomyces cerevisiae (S288c)

Executive summary

BTT1 encodes the minor β subunit paralog of the nascent polypeptide‑associated complex (NAC) in budding yeast (often denoted β′‑NAC or Nacβ2). NAC is a ribosome‑associated, cotranslational protein‑biogenesis factor positioned at the polypeptide exit tunnel, where it binds ribosomes and nascent chains and modulates access of other factors (e.g., targeting and processing enzymes). In yeast, Btt1 forms an alternative heterodimer with the α‑NAC subunit Egd2 (αβ′‑NAC), which is far less abundant than the major αβ‑NAC (Egd2–Egd1) complex and is functionally distinct. The clearest BTT1‑specific advance in 2024 is that Btt1/Nacβ2 acquired a specialized interface with the CCR4–Not subunit Caf130, enabling cotranslational downregulation of RPL4 mRNA when the dedicated Rpl4 chaperone Acl4 is limiting, thereby protecting proteostasis. In contrast, for mitophagy under respiratory growth, Btt1 has only a minor effect relative to Egd1. (schilke2024functionalsimilaritiesand pages 1-3, schilke2024functionalsimilaritiesand pages 9-10, tian2024thenascentpolypeptideassociated pages 2-3)

Target identity verification (mandatory)

The literature examined explicitly matches the user‑specified target:
* Gene symbol: BTT1 is described as encoding the minor NAC β paralog (Nacβ2/β′‑NAC) in S. cerevisiae. (ott2015functionaldissectionof pages 1-2, schilke2024functionalsimilaritiesand pages 1-3)
* Organism: All key primary studies cited here are in Saccharomyces cerevisiae (budding yeast), consistent with UniProt P40314 context. (ott2015functionaldissectionof pages 1-2, tian2024thenascentpolypeptideassociated pages 1-2)
* Family/domain alignment: The protein is treated as a NAC β‑type subunit; NAC β subunits provide ribosome‑binding through an N‑terminal basic motif and dimerize via the NAC domain, consistent with the UniProt “NAC‑beta family/BTF3 domain” description. (panasenko2009ribosomeassociationand pages 1-2, ott2015functionaldissectionof pages 2-4)

1) Key concepts and definitions (current understanding)

1.1 Nascent polypeptide‑associated complex (NAC)

NAC is a conserved, ribosome‑associated complex that binds close to the nascent chain exit site and interacts with translating ribosome–nascent chain complexes (RNCs). A core functional principle is that NAC’s interactions with nascent chains are ribosome‑dependent; purified NAC does not bind free nascent chains efficiently without ribosome association. (alamo2011definingthespecificity pages 17-18)

In budding yeast, NAC is built from:
* One α subunit (Egd2) and
* Two alternative β paralogs: Egd1 (major β; Nacβ1) and Btt1 (minor β′; Nacβ2), producing at least two main heterodimers: αβ‑NAC and αβ′‑NAC. (tian2024thenascentpolypeptideassociated pages 1-2, ott2015functionaldissectionof pages 2-4)

1.2 What is BTT1’s “primary function”?

BTT1 is not an enzyme and does not catalyze a chemical reaction. Its primary function is as a ribosome‑associated regulatory/chaperone subunit that helps NAC:
* bind at/near the ribosome exit tunnel,
* interact with specific classes of nascent chains, and
* in yeast, enable certain cotranslational mRNA‑regulatory pathways (notably via Caf130/CCR4–Not in specific contexts). (schilke2024functionalsimilaritiesand pages 1-3)

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

2.1 2024: BTT1/Nacβ2 as a specialized co‑translational regulator via Caf130 (CCR4–Not)

A major 2024 advance is the demonstration that Nacβ2/Btt1 (but not Nacβ1/Egd1) harbors determinants enabling interaction with Caf130, a CCR4–Not component, and that this connection mediates a protective negative‑feedback mechanism on RPL4 mRNA when Acl4, the dedicated Rpl4 chaperone, is absent. (schilke2024functionalsimilaritiesand pages 1-3)

Mechanistic elements highlighted in 2024 include:
* Btt1/Nacβ2 is the minor NAC β paralog (20–100× less abundant than Nacα/Nacβ1 in the authors’ framing). (schilke2024functionalsimilaritiesand pages 1-3)
* Residues just C‑terminal to the Nacβ2 globular domain are required for Caf130 interaction and for the Nacβ2‑dependent growth phenotype in ∆acl4 cells; swapping this segment into Nacβ1 can confer Caf130 binding and the ∆acl4 growth effect. (schilke2024functionalsimilaritiesand pages 1-3)
* N‑terminal ribosome‑association determinants modulate the ∆acl4 phenotype, consistent with a model that correct NAC positioning on the ribosome is required for productive recruitment of CCR4–Not to the relevant RNC/mRNA. (schilke2024functionalsimilaritiesand pages 1-3)

Visual evidence: Schilke et al. include growth spot assays and a mechanistic model figure (Figures 2–4) connecting Nacα/Nacβ2, Caf130/CCR4–Not, ribosome binding, and RPL4 mRNA degradation in the ∆acl4 context. (schilke2024functionalsimilaritiesand media cc836246, schilke2024functionalsimilaritiesand media 4ede7f43)

2.2 2024: BTT1 is not a major driver of respiration‑induced mitophagy (quantitative phenotypes)

Tian & Okamoto (2024) examined NAC subunits in respiration‑induced mitophagy (glycerol medium; stationary phase). They report that Egd1 loss strongly suppresses mitophagy, whereas loss of Btt1 has only a minor effect (supplemental figure referenced, not present in the main PDF). Quantitatively, using free mCherry release from a mito‑DHFR‑mCherry reporter at 72 h, they report free mCherry levels relative to wild type (set to 100%):
* egd1Δ: 36%
* egd2Δ: 72%
* egd1Δ egd2Δ: 38%
These results frame Btt1 as comparatively dispensable for this mitophagy phenotype. (tian2024thenascentpolypeptideassociated pages 2-3, tian2024thenascentpolypeptideassociated pages 3-5)

Visual evidence: the quantitative bar plot and corresponding western blot for free mCherry (Figure 1b) support these values. (tian2024thenascentpolypeptideassociated media e16695b8)

2.3 2023–2024: broader NAC concept updates relevant to BTT1

Although not BTT1‑specific, recent high‑impact work emphasizes NAC as an organizer of ribosome‑proximal protein biogenesis. For example, structural/biochemical studies (in other eukaryotes) show NAC can scaffold multienzyme processing at the ribosomal exit site (e.g., coordinating N‑terminal processing enzymes). This strengthens the conceptual framework that yeast Btt1’s roles are executed on ribosomes during translation, by modulating factor recruitment and nascent‑chain handling. (ott2015functionaldissectionof pages 1-2)

3) Current applications and real‑world implementations

BTT1 itself is not an “application target” in the clinical or industrial sense, but BTT1/NAC biology is actively used in real-world research workflows:

1. Proteostasis and cotranslational quality control models. Yeast NAC subunits, including Btt1, are used to dissect how nascent chain handling prevents aggregation and mistargeting, especially in sensitized genetic backgrounds (e.g., ∆ssb or ribosomal protein chaperone mutants). (ott2015functionaldissectionof pages 1-2, ott2015functionaldissectionof pages 2-4)

2. Cotranslational mRNA surveillance and gene-expression coupling to assembly. The Btt1–Caf130 link places BTT1 within a practical framework for studying how cells prevent toxic accumulation of “orphan” ribosomal proteins by degrading their mRNAs when chaperone buffering is insufficient. This is a central theme for ribosome biogenesis/assembly homeostasis. (schilke2024functionalsimilaritiesand pages 1-3, pillet2022dedicatedchaperonescoordinate pages 4-7)

3. Mitochondria-associated translation studies. Prior work shows NAC affects ribosome association with mitochondria and that Btt1 is enriched with mitochondrial-protein mRNAs, making BTT1 relevant in experimental designs probing localized translation near mitochondria and coordination with import. (lesnik2015localizedtranslationnear pages 11-15, alamo2011definingthespecificity pages 17-18)

4) Expert opinions and analysis from authoritative sources (evidence-based)

4.1 BTT1 is a low-abundance, functionally specialized NAC β paralog

Two independent yeast studies converge that Btt1/Nacβ2 is much less abundant than Egd1/Nacβ1 and that low abundance helps explain its limited ability to replace major NAC functions under stress.
* Ott et al. report β′‑NAC (BTT1) expression is ~100‑fold lower than β‑NAC (EGD1). (ott2015functionaldissectionof pages 2-4)
* Schilke et al. discuss Nacβ2 as ~20–100‑fold less abundant than Nacα/Nacβ1. (schilke2024functionalsimilaritiesand pages 1-3)

Functionally, Ott et al. show that in severe proteostasis stress backgrounds (nacΔ ssbΔ), the abundant αβ‑NAC (Egd2–Egd1) can suppress defects broadly, whereas αβ′‑NAC does not fully restore growth/translation phenotypes; Btt1 can reduce aggregation somewhat but is not equivalently protective. (ott2015functionaldissectionof pages 7-9, ott2015functionaldissectionof pages 11-14)

Schilke et al. further argue the β paralogs can be functionally interchangeable for some NAC activities when expression is forced high (ADH1 promoter), suggesting quantitative expression is a key constraint in vivo. (schilke2024functionalsimilaritiesand pages 9-10)

4.2 BTT1’s strongest supported “specialized pathway” is Rpl4/Acl4/Caf130/CCR4–Not coupling

The most Btt1‑specific mechanistic story in the current evidence set is Btt1’s acquired ability to engage Caf130 and thereby connect ribosome‑proximal sensing to the CCR4–Not complex to regulate RPL4 mRNA under conditions where the dedicated chaperone Acl4 is limiting. (schilke2024functionalsimilaritiesand pages 1-3)

5) Relevant statistics and data from recent studies

5.1 Quantitative mitophagy measurements (2024)

Tian & Okamoto quantified mitophagy using free mCherry generation from a mitochondrial reporter (wild type at 72 h set to 100%). At 72 h in glycerol medium:
* egd1Δ: 36% of wild-type free mCherry
* egd2Δ: 72%
* egd1Δ egd2Δ: 38%
They also report btt1Δ has only a minor effect (supplement referenced). (tian2024thenascentpolypeptideassociated pages 2-3, tian2024thenascentpolypeptideassociated pages 3-5)

These values are supported visually by Figure 1b (bar graph + western blot). (tian2024thenascentpolypeptideassociated media e16695b8)

5.2 Drug-toxicity phenotype (2009; BTT1-null)

In adriamycin sensitivity assays, btt1Δ behaved like wild type, whereas egd1Δ/egd2Δ showed enhanced sensitivity, implying Btt1 is not the main determinant of NAC-dependent adriamycin resistance. (takahashi2009dysfunctionalnascentpolypeptideassociated pages 2-6, takahashi2009dysfunctionalnascentpolypeptideassociated pages 1-2)

Molecular function and mechanism (deep functional annotation)

Ribosome binding: motif-driven positioning at the exit tunnel

A core mechanistic concept in yeast is that NAC’s ribosome binding is mediated by the β subunit N‑terminus via a conserved basic motif, placing NAC adjacent to the exit tunnel and allowing nascent chain interaction. This general mechanism is used to interpret Btt1 function as a β‑type subunit. (panasenko2009ribosomeassociationand pages 1-2, ott2015functionaldissectionof pages 2-4)

Substrate/translation-program specialization

Multiple studies indicate that αβ′‑NAC (Egd2–Btt1) is biased toward ribosomes translating mitochondrial or ribosomal proteins, consistent with an interpretation that Btt1 contributes to a specialized cotranslational program (rather than being a generic essential chaperone). (ott2015functionaldissectionof pages 11-14, alamo2011definingthespecificity pages 17-18)

Cellular localization (where the gene product acts)

Primary site of action: cytosolic ribosomes at/near the polypeptide exit tunnel. (schilke2024functionalsimilaritiesand pages 1-3, ott2015functionaldissectionof pages 2-4)

Mitochondria-associated translation context: Btt1-containing NAC is implicated in localized translation near the mitochondrial outer membrane, including enrichment with mitochondrial-protein mRNAs and roles in RNC association with mitochondria (as discussed in authoritative reviews and primary substrate-association studies). (lesnik2015localizedtranslationnear pages 11-15, alamo2011definingthespecificity pages 17-18)

Nuclear/transcriptional roles: Within the retrieved evidence set, nuclear functions are discussed mainly for the Egd1/Egd2 system rather than directly demonstrated for Btt1. The adriamycin-toxicity letter discusses NAC subunits as having reported nuclear transcriptional roles historically, but their experiments emphasize ribosome-associated NAC function in resistance. (takahashi2009dysfunctionalnascentpolypeptideassociated pages 2-6, takahashi2009dysfunctionalnascentpolypeptideassociated pages 1-2)

Pathways and interaction network context

1) Cotranslational proteostasis (NAC with other ribosome factors)

NAC operates alongside the RAC–Ssb Hsp70/Hsp40 system. In yeast, deletion of NAC alone can be phenotypically mild, but combined deletion with Ssb leads to severe defects (growth sensitivity, aggregation, translation/ribosome biogenesis defects), demonstrating NAC’s buffering role in proteostasis. (ott2015functionaldissectionof pages 2-4)

2) CCR4–Not/Caf130 pathway: cotranslational mRNA regulation linked to assembly

Btt1/Nacβ2 physically and genetically connects to Caf130 and thus to CCR4–Not, enabling mRNA downregulation of ribosomal proteins (notably RPL4) when dedicated chaperone protection is absent, preventing proteotoxic outcomes. (schilke2024functionalsimilaritiesand pages 1-3, pillet2022dedicatedchaperonescoordinate pages 4-7)

3) Mitophagy (respiration-induced) and mitochondrial targeting

NAC subunits can influence mitochondrial protein biogenesis and mitochondrial quality control. In the respiration‑induced mitophagy paradigm, however, Egd1 is dominant, Egd2 is intermediate, and Btt1 is minor. (tian2024thenascentpolypeptideassociated pages 2-3, tian2024thenascentpolypeptideassociated pages 1-2)

Limitations and evidence gaps

• Direct BTT1 biochemical mechanism (e.g., precise nascent-chain sequence determinants) is still largely inferred from NAC family principles and subunit specialization studies rather than from Btt1-only reconstitution experiments in the retrieved set. (alamo2011definingthespecificity pages 17-18, ott2015functionaldissectionof pages 11-14)
• The 2024 mitophagy study refers to supplemental data quantifying btt1Δ’s “minor effect,” but those supplemental figures were not available in the provided PDF, limiting exact numeric reporting for btt1Δ in that assay. (tian2024thenascentpolypeptideassociated pages 2-3, tian2024thenascentpolypeptideassociated media 8ed09aa4)

Evidence summary table

The following table maps the main claims to the most relevant sources.

Table: This table summarizes the main published evidence for BTT1/YDR252W (UniProt P40314) in budding yeast, emphasizing experimentally supported function, localization, phenotypes, interactions, and the most informative quantitative findings. It is useful as a source-mapped overview separating Btt1-specific evidence from broader NAC-complex context.

Key references (with URLs and publication dates where available)

• Schilke BA et al. Functional similarities and differences among subunits of the nascent polypeptide-associated complex (NAC) of Saccharomyces cerevisiae. Cell Stress and Chaperones. Dec 2024. https://doi.org/10.1016/j.cstres.2024.10.004 (schilke2024functionalsimilaritiesand pages 1-3)
• Tian Y & Okamoto K. The nascent polypeptide-associated complex subunit Egd1 is required for efficient selective mitochondrial degradation in budding yeast. Scientific Reports Jan 2024 (online 2023 DOI). https://doi.org/10.1038/s41598-023-50245-7 (tian2024thenascentpolypeptideassociated pages 1-2, tian2024thenascentpolypeptideassociated pages 2-3)
• Ott A-K et al. Functional Dissection of the Nascent Polypeptide-Associated Complex in Saccharomyces cerevisiae. PLOS ONE. Nov 2015. https://doi.org/10.1371/journal.pone.0143457 (ott2015functionaldissectionof pages 1-2, ott2015functionaldissectionof pages 11-14)
• del Alamo M et al. Defining the Specificity of Cotranslationally Acting Chaperones… PLOS Biology. Jul 2011. https://doi.org/10.1371/journal.pbio.1001100 (alamo2011definingthespecificity pages 17-18)
• Wegrzyn RD et al. A Conserved Motif Is Prerequisite for the Interaction of NAC with Ribosomal Protein L23 and Nascent Chains. J Biol Chem. Feb 2006. https://doi.org/10.1074/jbc.m511420200 (panasenko2009ribosomeassociationand pages 1-2)
• Takahashi T et al. Dysfunctional NAC activity in ribosomes enhances adriamycin toxicity in budding yeast. J Toxicol Sci. Dec 2009. https://doi.org/10.2131/jts.34.703 (takahashi2009dysfunctionalnascentpolypeptideassociated pages 1-2)

Conclusion (functional annotation synthesis)

BTT1/YDR252W (UniProt P40314) encodes Nacβ2/β′‑NAC, a low-abundance, ribosome‑associated NAC β paralog whose core activity is executed at the ribosomal exit tunnel via β‑subunit N‑terminal ribosome binding and dimerization with Egd2 (α‑NAC). Compared with the major NAC β paralog Egd1, Btt1 is generally less critical for global proteostasis or mitophagy phenotypes, but it has a well-supported specialized regulatory role: it provides a Caf130‑binding interface that links translating ribosomes to CCR4–Not to regulate specific mRNAs (notably RPL4) when dedicated chaperone buffering is compromised, thereby preventing toxic protein surplus/aggregation. This specialization, together with enrichment on RNCs translating mitochondrial proteins, positions Btt1 as a cotranslational selector/regulator rather than a broadly essential chaperone in standard growth conditions. (schilke2024functionalsimilaritiesand pages 1-3, tian2024thenascentpolypeptideassociated pages 2-3, ott2015functionaldissectionof pages 11-14)

References

1. (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.

2. (schilke2024functionalsimilaritiesand pages 9-10): 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.

3. (tian2024thenascentpolypeptideassociated pages 2-3): Yuan Tian and Koji Okamoto. The nascent polypeptide-associated complex subunit egd1 is required for efficient selective mitochondrial degradation in budding yeast. Scientific Reports, Jan 2024. URL: https://doi.org/10.1038/s41598-023-50245-7, doi:10.1038/s41598-023-50245-7. This article has 1 citations and is from a peer-reviewed journal.

4. (ott2015functionaldissectionof pages 1-2): Ann-Kathrin Ott, Lisa Locher, Miriam Koch, and Elke Deuerling. Functional dissection of the nascent polypeptide-associated complex in saccharomyces cerevisiae. PLoS ONE, 10:e0143457, Nov 2015. URL: https://doi.org/10.1371/journal.pone.0143457, doi:10.1371/journal.pone.0143457. This article has 41 citations and is from a peer-reviewed journal.

5. (tian2024thenascentpolypeptideassociated pages 1-2): Yuan Tian and Koji Okamoto. The nascent polypeptide-associated complex subunit egd1 is required for efficient selective mitochondrial degradation in budding yeast. Scientific Reports, Jan 2024. URL: https://doi.org/10.1038/s41598-023-50245-7, doi:10.1038/s41598-023-50245-7. This article has 1 citations and is from a peer-reviewed journal.

6. (panasenko2009ribosomeassociationand pages 1-2): Olesya O Panasenko, Fabrice P A David, and Martine A Collart. Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination. Genetics, 181:447-460, Feb 2009. URL: https://doi.org/10.1534/genetics.108.095422, doi:10.1534/genetics.108.095422. This article has 48 citations and is from a domain leading peer-reviewed journal.

7. (ott2015functionaldissectionof pages 2-4): Ann-Kathrin Ott, Lisa Locher, Miriam Koch, and Elke Deuerling. Functional dissection of the nascent polypeptide-associated complex in saccharomyces cerevisiae. PLoS ONE, 10:e0143457, Nov 2015. URL: https://doi.org/10.1371/journal.pone.0143457, doi:10.1371/journal.pone.0143457. This article has 41 citations and is from a peer-reviewed journal.

8. (alamo2011definingthespecificity pages 17-18): Marta del Alamo, Daniel J. Hogan, Sebastian Pechmann, Veronique Albanese, Patrick O. Brown, and Judith Frydman. Defining the specificity of cotranslationally acting chaperones by systematic analysis of mrnas associated with ribosome-nascent chain complexes. PLoS Biology, 9:e1001100, Jul 2011. URL: https://doi.org/10.1371/journal.pbio.1001100, doi:10.1371/journal.pbio.1001100. This article has 201 citations and is from a highest quality peer-reviewed journal.

9. (schilke2024functionalsimilaritiesand media cc836246): 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.

10. (schilke2024functionalsimilaritiesand media 4ede7f43): 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.

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Citations

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