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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 SAS3 (UniProt P34218, ORF YBL052C) — Functional Annotation and Recent Literature

Executive summary

S. cerevisiae Sas3 is a MYST-family histone acetyltransferase (HAT) and the catalytic subunit of the NuA3 complex, which primarily acetylates histone H3 lysine 14 (H3K14) and is also associated with H3K23 acetylation in yeast chromatin. NuA3 integrates catalytic activity (Sas3) with multiple chromatin “reader” modules (e.g., Yng1 PHD binding H3K4 methylation; Pdp3 PWWP binding H3K36me3; Taf14 YEATS binding acyl-lysine marks) to target acetylation to active chromatin. Classic biochemical purification work established Sas3’s catalytic and structural role in NuA3 and revealed a physical/functional connection to the transcription-elongation factor FACT via Spt16. A major 2024 advance resolved how Taf14 helps organize NuA3 by binding short ET-binding motifs in both Sas3 and Yng1; mutations that disrupt these interfaces cause transcription-elongation stress sensitivity (6-AU) and increased sensitivity to replication/damage stresses (HU, MMS), connecting NuA3 assembly to genome maintenance. (john2000thesomethingabout pages 1-2, kim2020nua3hatantagonizes pages 1-2, taverna2006yng1phdfinger pages 1-2, nguyen2024molecularinsightinto pages 6-8)

1) Identity verification and disambiguation (critical)

The symbol SAS3 can refer to MYST-family HAT orthologs in other fungi (e.g., pathogens), but the target here is explicitly budding yeast SAS3 (P34218; YBL052C). Foundational yeast studies purifying NuA3 identified Sas3 as its catalytic HAT subunit and described Sas3 as the yeast homolog/counterpart of human MOZ/MORF-type MYST HATs, which provides a clear species/family/complex-based disambiguation. (john2000thesomethingabout pages 1-2, nguyen2024molecularinsightinto pages 1-2)

2) Key concepts and definitions (current understanding)

2.1 Histone acetyltransferase (HAT) activity of Sas3/NuA3

A HAT transfers an acetyl group from acetyl-CoA to the ε-amino group of a lysine residue on histones (a post-translational modification linked to chromatin accessibility and transcription). NuA3 is defined as a Gcn5-independent nucleosomal H3 HAT complex in yeast. (john2000thesomethingabout pages 2-4, john2000thesomethingabout pages 1-2)

2.2 NuA3 complex as a “writer + readers” chromatin machine

NuA3 combines:
- a writer: Sas3 (MYST catalytic subunit)
- multiple reader domains: Yng1 PHD (H3K4 methylation), Pdp3 PWWP (H3K36me3), Taf14 YEATS/ET (acyl-lysine binding and EBM binding), enabling chromatin-context-sensitive recruitment and regulation. (martin2017histoneh3k4and pages 1-2, kim2020nua3hatantagonizes pages 1-2, nguyen2024molecularinsightinto pages 1-2)

3) Primary biochemical function: reaction catalyzed and substrate specificity

3.1 Reaction catalyzed

Sas3 (as NuA3 catalytic subunit) catalyzes histone lysine acetylation using acetyl-CoA (EC 2.3.1.48 in UniProt context; mechanistically supported by HAT assays described in classic NuA3 purification studies). NuA3 is active on chromatin/nucleosomal templates and is positioned to acetylate nucleosomal H3. (john2000thesomethingabout pages 2-4, john2000thesomethingabout pages 1-2)

3.2 Substrate context: nucleosomes vs free histones

NuA3 is characterized as a complex that acetylates histone H3 on nucleosomal substrates, but can also acetylate H4 on free histones in vitro. Importantly, bacterially expressed Sas3 can acetylate free histones, whereas nucleosomal targeting/efficiency depends on NuA3 subunits that enable chromatin engagement. (john2000thesomethingabout pages 2-4, john2000thesomethingabout pages 6-8)

3.3 Site specificity on histone H3

Multiple independent yeast sources support H3K14 as the principal physiological site for NuA3/Sas3 action:
- NuA3 is described as primarily acetylating H3K14, and its transcriptional role is linked to reader-dependent stimulation (e.g., Yng1–H3K4me3). (kim2020nua3hatantagonizes pages 1-2, taverna2006yng1phdfinger pages 1-2)
- NuA3 is also associated with acetylation of H3K23 (reported in yeast NuA3 literature and summarized in Genetics work on recruitment). (martin2017histoneh3k4and pages 1-2)

4) Complex membership, assembly, and molecular interactions

4.1 Core/commonly cited subunits

Modern descriptions of NuA3 include Sas3 (catalytic), Nto1, Eaf6, Yng1, Taf14, and Pdp3; earlier biochemical purification also identified yTAFII30/TAF30 in NuA3 preparations. (john2000thesomethingabout pages 2-4, martin2017histoneh3k4and pages 1-2, john2000thesomethingabout pages 1-2)

4.2 Sas3 requirement for complex integrity

Deletion of SAS3 eliminates detectable NuA3 HAT activity and disrupts co-purification/co-elution of other NuA3 components (e.g., TAF30), supporting Sas3 as required for both activity and integrity of the complex. (john2000thesomethingabout pages 2-4, john2000thesomethingabout pages 1-2)

4.3 Coupling to transcription elongation machinery (FACT/Spt16)

A key mechanistic theme is physical coupling between NuA3 and the FACT complex:
- Sas3 mediates NuA3 interaction with Spt16 (in vivo and in vitro), through an acidic C-terminal region; genetic interaction includes enhanced 6-azauracil (6-AU) sensitivity when SAS3 is disrupted in an spt16-truncation background. This supports a role in transcription elongation through nucleosomes (and potentially replication-associated chromatin transactions). (john2000thesomethingabout pages 6-8, john2000thesomethingabout pages 8-9)

5) Localization and pathway-level function in the cell

5.1 Subcellular localization

NuA3 is a chromatin-associated nuclear complex (nucleosomal H3 acetyltransferase); genome-wide studies show Sas3 occupancy on genes and chromatin. (john2000thesomethingabout pages 1-2, vicentemunoz2014comprehensiveanalysisof pages 1-2)

5.2 Genome targeting patterns

Genome-wide chromatin mapping supports that Sas3/NuA3 localizes predominantly across transcribed gene bodies, often in mid-gene regions, consistent with a role in transcription-coupled chromatin regulation:
- Sas3 and Yng1 peaks reported ~750 bp and 657 bp downstream of the +1 nucleosome dyad, respectively, and correlate genome-wide (Spearman r = 0.48). (martin2018targetingofhistone pages 63-69)
- ChIP-on-chip mapping found Sas3 preferentially in the 5′ half of coding regions, supporting involvement in transcriptional elongation. (vicentemunoz2014comprehensiveanalysisof pages 1-2)

5.3 Recruitment logic (histone methylation cross-talk)

NuA3 recruitment is promoted by histone methylation marks associated with active transcription:
- H3K4 and H3K36 methylation independently support NuA3 recruitment via Yng1 (PHD) and Pdp3 (PWWP) modules. (martin2017histoneh3k4and pages 1-2, martin2016histoneh3k4and pages 14-18)
- Importantly, recruitment does not guarantee acetylation (“presence is insufficient”), implying additional regulation of enzymatic activity after binding. (martin2017histoneh3k4and pages 1-2)

6) Recent developments (priority 2023–2024)

6.1 2024: Structural and mechanistic assembly of NuA3 via Taf14–Sas3/Yng1 interfaces

A major 2024 Nature Communications study dissected how Taf14 binds short ET-binding motifs (EBMs) in Sas3 and Yng1, forming dimeric assemblies that enhance Taf14 DNA binding and are required for NuA3 function in transcription and genome maintenance. Key quantitative findings include:
- Taf14ET–Sas3EBM affinity Kd ≈ 18 μM (NMR) and Taf14FL–Sas3 peptide Kd ≈ 21 μM (fluorescence). (nguyen2024molecularinsightinto pages 3-6)
- Mutations in Sas3 EBM weaken/abrogate binding: L114D Kd ≈ 540 μM, while V116D/I118D disrupt binding. (nguyen2024molecularinsightinto pages 3-6)
- In vivo, Sas3 (I118D) or Yng1 (I120D) mutations that disrupt Taf14 binding cause strong sensitivity to transcription elongation stress (6-AU) and increased sensitivity to replication/damage stresses (HU, MMS). (nguyen2024molecularinsightinto pages 6-8)
- ChIP-exo promoter occupancy counts: Taf14 1096, Yng1 71, Sas3 9; 70/71 Yng1 promoters co-bound by Taf14; 6 promoters co-bound by all three. (nguyen2024molecularinsightinto pages 3-6)

These findings sharpen current understanding from “NuA3 has multiple subunits” to an explicit molecular assembly interface and provide a direct mechanistic route linking NuA3 architecture to transcription and DNA repair phenotypes. (nguyen2024molecularinsightinto pages 1-2, nguyen2024molecularinsightinto pages 6-8)

6.2 2024: Additional yeast literature signals

A 2024 bioRxiv histone-mutant screening study references reduced H3 acetylation including H3K14 and notes nucleosomes acetylated by Gcn5 and Sas3/NuA3 in transcriptional regulation contexts, suggesting Sas3 remains embedded as a standard component of chromatin functional interpretation in contemporary yeast epigenetics. (singh2024screeningofhistone; retrieved but not deeply evidenced beyond snippet in this corpus)

7) Current applications and real-world implementations

7.1 Yeast Sas3/NuA3 as a model for human MYST HATs (MOZ/MORF)

Authoritative review literature frames yeast MYST HATs—including Sas3—as a tractable system to illuminate mechanisms relevant to human disease-associated MYST enzymes (e.g., MOZ/MORF), leveraging yeast genetics, biochemistry, and interaction assays. (lafon2007mystopportunitiesfor pages 1-2, lafon2007mystopportunitiesfor pages 2-3)

7.2 Studying transcription elongation through nucleosomes

The Sas3–Spt16/FACT linkage provides a platform to study how acetylation is coupled to chromatin transactions during elongation, with phenotypes such as 6-AU sensitivity serving as functional readouts in standard laboratory workflows. (john2000thesomethingabout pages 6-8, john2000thesomethingabout pages 8-9)

7.3 Modular “reader–writer” logic for chromatin targeting

NuA3 embodies a widely used conceptual framework in epigenetics—writer enzymes guided by reader domains recognizing pre-existing histone marks (H3K4 methylation, H3K36me3, acyl marks). This supports experimental designs that perturb reader interactions (e.g., Yng1 PHD mutants) to test causality between histone PTMs, recruitment, and downstream acetylation/transcription. (taverna2006yng1phdfinger pages 1-2, martin2017histoneh3k4and pages 1-2, nguyen2024molecularinsightinto pages 1-2)

8) Expert opinions and analysis (authoritative synthesis)

• “Yeast genes illuminate human cancer gene functions”: Sas3/NuA3 is presented as a key yeast MYST system that connects conserved domain architecture and complex subunits to transcriptional regulation and growth control, supporting its translational relevance to MOZ/MORF biology. (lafon2007mystopportunitiesfor pages 1-2, lafon2007mystopportunitiesfor pages 3-4)
• Modern consensus on multi-layer control: recruitment of NuA3 by active chromatin marks is necessary but not sufficient for acetylation output, implying regulation at the level of complex assembly, chromatin engagement geometry, and/or competing chromatin modifiers (e.g., Rpd3 HDAC pathways). (martin2017histoneh3k4and pages 1-2, kim2020nua3hatantagonizes pages 1-2)
• 2024 mechanistic refinement: NuA3 function depends on defined Taf14-mediated interactions with both Sas3 and Yng1, linking a specific physical interface to transcription and DNA repair phenotypes; this strengthens causal inference beyond correlational chromatin localization. (nguyen2024molecularinsightinto pages 6-8, nguyen2024molecularinsightinto pages 1-2)

9) Relevant statistics and data highlights (from cited studies)

• NuA3 substrate context: NuA3 acetylates H3 on nucleosomal substrates and can acetylate H4 on free histones in vitro. (john2000thesomethingabout pages 2-4)
• Genome targeting metrics: Sas3 peak enrichment ~750 bp downstream of +1 dyad; Yng1 ~657 bp; Sas3–Yng1 occupancy correlation Spearman r = 0.48. (martin2018targetingofhistone pages 63-69)
• 2024 affinities: Taf14FL–Sas3 peptide Kd ~21 μM; Taf14ET–Sas3 EBM Kd ~18 μM; Sas3 L114D mutant Kd ~540 μM. (nguyen2024molecularinsightinto pages 3-6)
• 2024 occupancy counts: Taf14 1096 promoters; Yng1 71; Sas3 9; triple overlap 6. (nguyen2024molecularinsightinto pages 3-6)
• 2024 phenotypes: Disruption of Taf14–Sas3 or Taf14–Yng1 binding increases sensitivity to 6-AU, HU, MMS, linking NuA3 assembly to elongation stress and genome maintenance. (nguyen2024molecularinsightinto pages 6-8)

10) Key figure evidence (2024)

Nguyen et al. provide direct figure-level evidence for Taf14–Sas3/Yng1 binding energetics, structural overlap, and stress phenotypes.
- Binding curves and mutant effects (Fig. 5 panels) and structural overlays (Fig. 6c). (nguyen2024molecularinsightinto media 3daaaaa8)
- Spot assays showing growth sensitivity with interface-disrupting mutations under 6-AU, HU, and MMS. (nguyen2024molecularinsightinto media cea32fb1)

11) Limitations and evidence gaps

Within the retrieved corpus, 2023–2024 yeast-specific Sas3/NuA3 primary literature beyond Nguyen et al. (2024) is limited. Ortholog papers (2023–2024) in fungal pathogens exist but should not be used as direct evidence for S. cerevisiae P34218 function; they mainly support evolutionary conservation of a nuclear MYST-HAT role.

Consolidated evidence table

Table: This table condenses yeast-specific evidence for SAS3/P34218 function, substrates, complex organization, chromatin targeting, and 2024 mechanistic advances from Nguyen et al. It also flags ortholog-only Sas3 literature to avoid conflating non-yeast findings with the target protein.

Selected key references (URLs; publication dates)

• John S. et al. “The Something About Silencing protein, Sas3, is the catalytic subunit of NuA3…” Genes & Development May 2000. https://doi.org/10.1101/gad.14.10.1196 (john2000thesomethingabout pages 1-2)
• Taverna S.D. et al. “Yng1 PHD finger binding to H3K4me3 promotes NuA3 HAT activity at K14…” Molecular Cell Dec 2006. https://doi.org/10.1016/j.molcel.2006.10.026 (taverna2006yng1phdfinger pages 1-2)
• Lafon A. et al. “MYST opportunities for growth control: yeast genes illuminate human cancer gene functions.” Oncogene Aug 2007. https://doi.org/10.1038/sj.onc.1210606 (lafon2007mystopportunitiesfor pages 1-2)
• Vicente-Muñoz S. et al. “Comprehensive analysis… Sas3-dependent NuA3…” FEBS Open Bio Nov 2014. https://doi.org/10.1016/j.fob.2014.11.001 (vicentemunoz2014comprehensiveanalysisof pages 1-2)
• Martin B.J.E. et al. “Histone H3K4 and H3K36 methylation independently recruit the NuA3 HAT…” Genetics Mar 2017. https://doi.org/10.1534/genetics.116.199422 (martin2017histoneh3k4and pages 1-2)
• Kim J.H. et al. “NuA3 HAT antagonizes the Rpd3S and Rpd3L HDACs…” Nucleic Acids Research Oct 2020. https://doi.org/10.1093/nar/gkaa781 (kim2020nua3hatantagonizes pages 1-2)
• Nguyen M.C. et al. “Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex.” Nature Communications Jun 2024. https://doi.org/10.1038/s41467-024-49730-y (nguyen2024molecularinsightinto pages 1-2)

References

1. (john2000thesomethingabout pages 1-2): Sam John, LeAnn Howe, Stefan T. Tafrov, Patrick A. Grant, Rolf Sternglanz, and Jerry L. Workman. The something about silencing protein, sas3, is the catalytic subunit of nua3, a ytaf_ii30-containing hat complex that interacts with the spt16 subunit of the yeast cp (cdc68/pob3)–fact complex. Genes & Development, 14:1196-1208, May 2000. URL: https://doi.org/10.1101/gad.14.10.1196, doi:10.1101/gad.14.10.1196. This article has 316 citations and is from a highest quality peer-reviewed journal.

2. (kim2020nua3hatantagonizes pages 1-2): Ji Hyun Kim, Chae Young Yoon, Yukyung Jun, Bo Bae Lee, Ji Eun Lee, So Dam Ha, Hyeonju Woo, Ahyoung Choi, Sanghyuk Lee, Woojin Jeong, Ji Hyung Kim, and TaeSoo Kim. Nua3 hat antagonizes the rpd3s and rpd3l hdacs to optimize mrna and lncrna expression dynamics. Nucleic Acids Research, 48:10753-10767, Oct 2020. URL: https://doi.org/10.1093/nar/gkaa781, doi:10.1093/nar/gkaa781. This article has 16 citations and is from a highest quality peer-reviewed journal.

3. (taverna2006yng1phdfinger pages 1-2): Sean D. Taverna, Serge Ilin, Richard S. Rogers, Jason C. Tanny, Heather Lavender, Haitao Li, Lindsey Baker, John Boyle, Lauren P. Blair, Brian T. Chait, Dinshaw J. Patel, John D. Aitchison, Alan J. Tackett, and C. David Allis. Yng1 phd finger binding to h3 trimethylated at k4 promotes nua3 hat activity at k14 of h3 and transcription at a subset of targeted orfs. Molecular cell, 24 5:785-796, Dec 2006. URL: https://doi.org/10.1016/j.molcel.2006.10.026, doi:10.1016/j.molcel.2006.10.026. This article has 418 citations and is from a highest quality peer-reviewed journal.

4. (nguyen2024molecularinsightinto pages 6-8): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

5. (nguyen2024molecularinsightinto pages 1-2): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

6. (john2000thesomethingabout pages 2-4): Sam John, LeAnn Howe, Stefan T. Tafrov, Patrick A. Grant, Rolf Sternglanz, and Jerry L. Workman. The something about silencing protein, sas3, is the catalytic subunit of nua3, a ytaf_ii30-containing hat complex that interacts with the spt16 subunit of the yeast cp (cdc68/pob3)–fact complex. Genes & Development, 14:1196-1208, May 2000. URL: https://doi.org/10.1101/gad.14.10.1196, doi:10.1101/gad.14.10.1196. This article has 316 citations and is from a highest quality peer-reviewed journal.

7. (martin2017histoneh3k4and pages 1-2): Benjamin J E Martin, Kristina L McBurney, Vicki E Maltby, Kristoffer N Jensen, Julie Brind’Amour, and LeAnn J Howe. Histone h3k4 and h3k36 methylation independently recruit the nua3 histone acetyltransferase in saccharomyces cerevisiae. Genetics, 205:1113-1123, Mar 2017. URL: https://doi.org/10.1534/genetics.116.199422, doi:10.1534/genetics.116.199422. This article has 39 citations and is from a domain leading peer-reviewed journal.

8. (john2000thesomethingabout pages 6-8): Sam John, LeAnn Howe, Stefan T. Tafrov, Patrick A. Grant, Rolf Sternglanz, and Jerry L. Workman. The something about silencing protein, sas3, is the catalytic subunit of nua3, a ytaf_ii30-containing hat complex that interacts with the spt16 subunit of the yeast cp (cdc68/pob3)–fact complex. Genes & Development, 14:1196-1208, May 2000. URL: https://doi.org/10.1101/gad.14.10.1196, doi:10.1101/gad.14.10.1196. This article has 316 citations and is from a highest quality peer-reviewed journal.

9. (john2000thesomethingabout pages 8-9): Sam John, LeAnn Howe, Stefan T. Tafrov, Patrick A. Grant, Rolf Sternglanz, and Jerry L. Workman. The something about silencing protein, sas3, is the catalytic subunit of nua3, a ytaf_ii30-containing hat complex that interacts with the spt16 subunit of the yeast cp (cdc68/pob3)–fact complex. Genes & Development, 14:1196-1208, May 2000. URL: https://doi.org/10.1101/gad.14.10.1196, doi:10.1101/gad.14.10.1196. This article has 316 citations and is from a highest quality peer-reviewed journal.

10. (vicentemunoz2014comprehensiveanalysisof pages 1-2): Sara Vicente-Muñoz, Paco Romero, Lorena Magraner-Pardo, Celia P. Martinez-Jimenez, Vicente Tordera, and Mercè Pamblanco. Comprehensive analysis of interacting proteins and genome-wide location studies of the sas3-dependent nua3 histone acetyltransferase complex. FEBS Open Bio, 4:996-1006, Nov 2014. URL: https://doi.org/10.1016/j.fob.2014.11.001, doi:10.1016/j.fob.2014.11.001. This article has 21 citations and is from a peer-reviewed journal.

11. (martin2018targetingofhistone pages 63-69): Benjamin John Elwood Martin. Targeting of histone acetylation to transcribed chromatin. ArXiv, Jan 2018. URL: https://doi.org/10.14288/1.0364673, doi:10.14288/1.0364673. This article has 0 citations.

12. (martin2016histoneh3k4and pages 14-18): Benjamin J.E. Martin, Kristina L. McBurney, Vicki E. Maltby, Kristoffer N. Jensen, Julie Brind’Amour, and LeAnn J. Howe. Histone h3k4 and h3k36 methylation promotes recruitment, but not activity, of the nua3 histone acetyltransferase complex in s. cerevisiae. bioRxiv, Dec 2016. URL: https://doi.org/10.1101/096511, doi:10.1101/096511. This article has 0 citations.

13. (nguyen2024molecularinsightinto pages 3-6): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

14. (lafon2007mystopportunitiesfor pages 1-2): Anne Lafon, Christie S. Chang, E. Scott, Sandra J. Jacobson, and L. Pillus. Myst opportunities for growth control: yeast genes illuminate human cancer gene functions. Oncogene, 26:5373-5384, Aug 2007. URL: https://doi.org/10.1038/sj.onc.1210606, doi:10.1038/sj.onc.1210606. This article has 82 citations and is from a domain leading peer-reviewed journal.

15. (lafon2007mystopportunitiesfor pages 2-3): Anne Lafon, Christie S. Chang, E. Scott, Sandra J. Jacobson, and L. Pillus. Myst opportunities for growth control: yeast genes illuminate human cancer gene functions. Oncogene, 26:5373-5384, Aug 2007. URL: https://doi.org/10.1038/sj.onc.1210606, doi:10.1038/sj.onc.1210606. This article has 82 citations and is from a domain leading peer-reviewed journal.

16. (lafon2007mystopportunitiesfor pages 3-4): Anne Lafon, Christie S. Chang, E. Scott, Sandra J. Jacobson, and L. Pillus. Myst opportunities for growth control: yeast genes illuminate human cancer gene functions. Oncogene, 26:5373-5384, Aug 2007. URL: https://doi.org/10.1038/sj.onc.1210606, doi:10.1038/sj.onc.1210606. This article has 82 citations and is from a domain leading peer-reviewed journal.

17. (nguyen2024molecularinsightinto media 3daaaaa8): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

18. (nguyen2024molecularinsightinto media cea32fb1): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

19. (martin2018targetingofhistone pages 69-78): Benjamin John Elwood Martin. Targeting of histone acetylation to transcribed chromatin. ArXiv, Jan 2018. URL: https://doi.org/10.14288/1.0364673, doi:10.14288/1.0364673. This article has 0 citations.

20. (nguyen2024molecularinsightinto pages 2-3): Minh Chau Nguyen, Hosein Rostamian, Ana Raman, Pengcheng Wei, Dustin C. Becht, Annette H. Erbse, Brianna J. Klein, Tonya M. Gilbert, Gongyi Zhang, M. Andres Blanco, Brian D. Strahl, Sean D. Taverna, and Tatiana G. Kutateladze. Molecular insight into interactions between the taf14, yng1 and sas3 subunits of the nua3 complex. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49730-y, doi:10.1038/s41467-024-49730-y. This article has 3 citations and is from a highest quality peer-reviewed journal.

Artifacts

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Citations

1. martin2018targetingofhistone pages 63-69
2. vicentemunoz2014comprehensiveanalysisof pages 1-2
3. nguyen2024molecularinsightinto pages 3-6
4. nguyen2024molecularinsightinto pages 6-8
5. john2000thesomethingabout pages 2-4
6. john2000thesomethingabout pages 1-2
7. lafon2007mystopportunitiesfor pages 2-3
8. nguyen2024molecularinsightinto pages 1-2
9. lafon2007mystopportunitiesfor pages 1-2
10. john2000thesomethingabout pages 6-8
11. john2000thesomethingabout pages 8-9
12. lafon2007mystopportunitiesfor pages 3-4
13. martin2018targetingofhistone pages 69-78
14. nguyen2024molecularinsightinto pages 2-3
15. https://doi.org/10.1101/gad.14.10.1196;
16. https://doi.org/10.1038/sj.onc.1210606;
17. https://doi.org/10.1016/j.molcel.2006.10.026;
18. https://doi.org/10.1534/genetics.116.199422;
19. https://doi.org/10.1093/nar/gkaa781;
20. https://doi.org/10.1038/s41467-024-49730-y;
21. https://doi.org/10.1101/096511;
22. https://doi.org/10.14288/1.0364673;
23. https://doi.org/10.1016/j.fob.2014.11.001;
24. https://doi.org/10.1128/mbio.01386-23;
25. https://doi.org/10.1128/aem.01885-23;
26. https://doi.org/10.1101/gad.14.10.1196
27. https://doi.org/10.1016/j.molcel.2006.10.026
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