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template_file: templates/gene_research_go_focused.md
template_variables:
organism: yeast
gene_id: HST3
gene_symbol: HST3
uniprot_accession: P53687
protein_description: 'RecName: Full=NAD-dependent histone deacetylase HST3; EC=2.3.1.286
{ECO:0000255|PROSITE-ProRule:PRU00236}; AltName: Full=Homologous to SIR2 protein
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gene_info: Name=HST3; OrderedLocusNames=YOR025W; ORFNames=OR26.15;
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
protein_family: Belongs to the sirtuin family. Class I subfamily.
protein_domains: DHS-like_NAD/FAD-binding_dom. (IPR029035); NAD-dep_sirtuin_deacylases.
(IPR050134); Sirtuin. (IPR003000); Sirtuin_cat_small_dom_sf. (IPR026591); Ssirtuin_cat_dom.
(IPR026590)
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allowed_domains: []
temperature: 0.1
citation_count: 29

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: P53687
• Protein Description: RecName: Full=NAD-dependent histone deacetylase HST3; EC=2.3.1.286 {ECO:0000255|PROSITE-ProRule:PRU00236}; AltName: Full=Homologous to SIR2 protein 3; AltName: Full=Regulatory protein SIR2 homolog 3;
• Gene Information: Name=HST3; OrderedLocusNames=YOR025W; ORFNames=OR26.15;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the sirtuin family. Class I subfamily.
• Key Domains: DHS-like_NAD/FAD-binding_dom. (IPR029035); NAD-dep_sirtuin_deacylases. (IPR050134); Sirtuin. (IPR003000); Sirtuin_cat_small_dom_sf. (IPR026591); Ssirtuin_cat_dom. (IPR026590)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "HST3" 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 'HST3' 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 HST3 (gene ID: HST3, UniProt: P53687) 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: P53687
• Protein Description: RecName: Full=NAD-dependent histone deacetylase HST3; EC=2.3.1.286 {ECO:0000255|PROSITE-ProRule:PRU00236}; AltName: Full=Homologous to SIR2 protein 3; AltName: Full=Regulatory protein SIR2 homolog 3;
• Gene Information: Name=HST3; OrderedLocusNames=YOR025W; ORFNames=OR26.15;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the sirtuin family. Class I subfamily.
• Key Domains: DHS-like_NAD/FAD-binding_dom. (IPR029035); NAD-dep_sirtuin_deacylases. (IPR050134); Sirtuin. (IPR003000); Sirtuin_cat_small_dom_sf. (IPR026591); Ssirtuin_cat_dom. (IPR026590)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "HST3" 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 'HST3' 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 HST3 (gene ID: HST3, UniProt: P53687) 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: Functional annotation of Saccharomyces cerevisiae HST3 (UniProt P53687, ORF YOR025W)

1) Target verification and disambiguation

The literature extracted in this run consistently defines Hst3 as a budding yeast sirtuin-family, NAD+-dependent histone deacetylase that—together with its paralog Hst4—erases histone H3 lysine 56 acetylation (H3K56ac). Key primary evidence comes from S. cerevisiae studies explicitly using HST3/HST4 deletion strains, H3K56 mutant histones, and Hst3-tagged expression time courses during the cell cycle and after DNA damage (maas2006cellcycleand pages 8-9, maas2006cellcycleand pages 2-3, maas2006cellcycleand pages 5-6). This functional profile matches the user-specified UniProt identity for HST3 (YOR025W; P53687) as an NAD-dependent histone deacetylase in the sirtuin family.

2) Key concepts and definitions (current understanding)

2.1 Sirtuins and NAD+-dependent lysine deacetylation

Hst3 belongs to the sirtuin class of deacetylases whose activity depends on NAD+; in vitro, recombinant/full-length Hst3/Hst4 require NAD+ to deacetylate H3K56ac and are inhibited by nicotinamide, consistent with canonical sirtuin biochemistry (delgoshaie2013studyofhistone pages 39-44). Functionally, this places Hst3 within metabolic–epigenetic coupling, since NAD+ availability can constrain enzymatic flux through deacetylation reactions.

2.2 The H3K56 acetylation/deacetylation cycle

H3K56ac is a cell-cycle regulated histone modification that is enriched in S phase (new histone deposition during DNA replication) and removed as cells enter G2/M (maas2006cellcycleand pages 5-6, maas2006cellcycleand pages 8-9). In wild-type logarithmically growing yeast, H3K56ac constitutes approximately ~20% of total H3, with most acetylated H3K56 present during S phase (maas2006cellcycleand pages 8-9).

Hst3 and Hst4 act as the primary “erasers” of this mark: deletion of both enzymes increases H3K56ac by >4-fold (maas2006cellcycleand pages 8-9), and genetic epistasis experiments indicate H3K56 is the dominant functional substrate of Hst3/Hst4 (maas2006cellcycleand pages 1-2, maas2006cellcycleand pages 8-9).

3) Primary molecular function: enzymatic activity and substrate specificity

3.1 Reaction and substrate specificity

Primary demonstrated enzymatic activity: Hst3 catalyzes deacetylation of acetylated histone H3 lysine 56 (H3K56ac) in an NAD+-dependent manner (maas2006cellcycleand pages 1-2, delgoshaie2013studyofhistone pages 39-44). Multiple lines of evidence support high substrate specificity and functional dominance of H3K56:

• Genetic epistasis: An H3 K56R substitution (non-acetylatable) is epistatic to phenotypes caused by HST3/HST4 deletion and HST3 overexpression, implying H3K56 is the major physiologic target site driving those phenotypes (maas2006cellcycleand pages 1-2, maas2006cellcycleand pages 8-9).
• In vivo acetylation pattern: Loss of Hst3/Hst4 does not comparably increase other H3/H4 N-terminal acetylation sites in the summarized evidence, supporting that H3K56ac is the key substrate in vivo (delgoshaie2013studyofhistone pages 39-44).
• Direct deacetylation behavior: De novo expression of Hst3 in arrested cells leads to rapid removal of detectable H3K56ac, supporting that Hst3 can directly drive H3K56 deacetylation (gershon2021theamazingacrobat pages 4-5).

3.2 Quantitative measures relevant to substrate occupancy

Several quantitative observations help bound the magnitude and kinetics of the mark:

• WT log-phase: ~20% of total H3 is H3K56-acetylated (maas2006cellcycleand pages 8-9).
• Double deletion: >4-fold increase in H3K56ac (maas2006cellcycleand pages 8-9).
• Cell-cycle timing: H3K56ac peaks around ~30–40 minutes after G1 release in the Maas et al. synchronization framework (maas2006cellcycleand pages 5-6, maas2006cellcycleand pages 2-3).
• In the absence of Hst3 for one cell cycle: approximately ~50% of histones carry H3K56ac (gershon2021theamazingacrobat pages 4-5).
• In extreme hyperacetylation backgrounds (hst3Δ hst4Δ) the H3K56ac stoichiometry can reach ~98–100% (delgoshaie2013studyofhistone pages 51-56, delgoshaie2013studyofhistone pages 39-44).

4) Biological processes and pathway context

4.1 DNA replication and replication-coupled chromatin assembly

H3K56ac is linked to replication-coupled chromatin assembly, and the timely removal of this mark by Hst3/Hst4 is required for genome integrity. In hst3Δ hst4Δ mutants, essentially all H3 becomes K56-acetylated throughout the genome and cell cycle, and this hyperacetylation is associated with replication-associated stress phenotypes and genome instability (delgoshaie2013studyofhistone pages 79-83, delgoshaie2013studyofhistone pages 75-79). The toxicity of excessive H3K56ac is further supported by the observation that many defects in hst3Δ hst4Δ cells are attenuated by H3K56R (delgoshaie2013studyofhistone pages 79-83).

4.2 DNA damage response (DDR) and checkpoint signaling

A central theme in the literature is that Hst3 is itself regulated by DNA damage checkpoints, which tune H3K56ac levels during replication stress.

In the highly cited primary study by Maas et al. (Molecular Cell, July 2006; https://doi.org/10.1016/j.molcel.2006.06.006), Hst3 is downregulated by checkpoint signaling in response to replication stressors MMS and HU (maas2006cellcycleand pages 8-9, maas2006cellcycleand pages 2-3). Importantly:

• Downregulation is checkpoint-dependent and requires MEC1 and RAD53, but not DUN1 or CRT1 (maas2006cellcycleand pages 2-3, maas2006cellcycleand pages 6-8).
• In these experiments, MMS blocks the normal accumulation of HST3 transcript after release from G1, indicating transcriptional repression as a major mode of downregulation (maas2006cellcycleand pages 2-3).
• Hst3 downregulation is most evident in conditions that activate the DNA replication checkpoint (MMS, HU) and not with other agents in that study’s comparisons (maas2006cellcycleand pages 8-9).

Conceptually, this checkpoint-mediated repression is interpreted as adaptive: forced/constitutive expression of Hst3 reduces H3K56ac and makes cells more damage sensitive, and overexpression sensitizes growth on CPT in the cited work (maas2006cellcycleand pages 5-6, maas2006cellcycleand pages 8-9).

4.3 Chromatin landscape at double-strand breaks (DSBs)

A 2023 review on yeast DSB chromatin (International Journal of Molecular Sciences, Feb 2023; https://doi.org/10.3390/ijms24043248) frames Hst3/Hst4 as key deacetylases of H3K56ac in DNA repair contexts and cites studies in which Mec1-dependent proteolysis of Hst3 links H3K56 deacetylation to S-phase checkpoint control and sister chromatid cohesion (frigerio2023thechromatinlandscape pages 23-24).

4.4 Transcriptional homeostasis (connection to RNA decay machinery)

A 2023 review on mRNA homeostasis (Transcription, Feb 2023; https://doi.org/10.1080/21541264.2023.2183684) cites prior work linking Hst3 to transcriptional homeostasis through a functional interaction with the RNA exosome, positioning Hst3 beyond histone-only models and into coordination of transcription with RNA decay pathways (bryll2023thecircularlogic pages 8-9).

5) Regulation of Hst3: cell cycle, protein stability, and stress-triggered downregulation

5.1 Cell-cycle expression and timing

Hst3 is cell-cycle regulated, with highest expression in G2/M and low levels in G1 (maas2006cellcycleand pages 5-6, maas2006cellcycleand pages 2-3). In the Maas et al. time course experiments, H3K56ac peaks at ~30–40 minutes after G1 release and then declines, consistent with Hst3 induction later in the cycle (maas2006cellcycleand pages 5-6).

5.2 Protein turnover and phosphorylation-dependent degradation

A 2021 review synthesis of the H3K56ac field (Genes, Feb 2021; https://doi.org/10.3390/genes12030342) highlights a strong layer of post-translational regulation: Hst3 has a very short half-life (reported as ~8–9 minutes in the cited synthesis), and mutation of key C-terminal phosphorylation sites can increase its half-life from ~8 minutes to 45 minutes, consistent with CDK/SCF-mediated degradation control (gershon2021theamazingacrobat pages 4-5). This complements the core 2006 checkpoint–transcription model by emphasizing rapid protein-level reset.

5.3 Replication-stress response and nuclear proteasome dependence (2024 proteomics)

A 2024 proteome-wide study of ubiquitylation and DNA damage responses in yeast (Molecular & Cellular Proteomics, Jan 2024; https://doi.org/10.1016/j.mcpro.2023.100695) reiterates that Hst3 is “well known to be rapidly degraded upon MMS” and experimentally shows that when nuclear proteasome function is perturbed (anchor-away approach), Hst3 accumulates and is not degraded under rapamycin treatment in their turnover assays (blaszczak2024dissectingubiquitylationand pages 7-9). Although the authors did not capture Hst3 ubiquitination sites in their K-ε-GG enrichment dataset, they observed strong MMS-induced ubiquitination behavior for Hst4, highlighting paralog differences while reinforcing proteolysis as a regulatory axis (blaszczak2024dissectingubiquitylationand pages 7-9).

6) Subcellular localization and site of action

The evidence assembled here strongly supports Hst3 acting on chromatin-associated nuclear histone H3, because its primary substrate is H3K56ac and its phenotypes are chromatin/replication/checkpoint linked (maas2006cellcycleand pages 1-2, maas2006cellcycleand pages 8-9, delgoshaie2013studyofhistone pages 75-79). However, the specific excerpts retrieved in this run do not contain an explicit microscopy- or fractionation-based localization statement for Hst3 protein. Therefore, nuclear/chromatin site of action is inferred from substrate and pathway context rather than directly demonstrated within the extracted text (gershon2021theamazingacrobat pages 4-5).

7) Current applications and real-world implementations

7.1 Yeast as an experimental platform to engineer histone modification states

HST3 is routinely used in yeast genetics and chromatin biology as a “control knob” for global H3K56ac abundance: deletion of HST3/HST4 drives hyperacetylation, while HST3 forced expression reduces the mark and can sensitize cells to replication stress (maas2006cellcycleand pages 5-6, maas2006cellcycleand pages 8-9). This enables tractable perturbation of replication-coupled chromatin maturation, checkpoint signaling, and genome stability mechanisms.

7.2 Proteomics and systems biology of DDR pathways (2024)

The 2024 Molecular & Cellular Proteomics work demonstrates a practical implementation: integrating protein turnover assays with nuclear proteasome perturbation to evaluate stress-triggered degradation programs, including Hst3 behavior during MMS response (blaszczak2024dissectingubiquitylationand pages 7-9). This situates Hst3 among proteins whose abundance is tuned by nuclear proteostasis during genotoxic stress.

7.3 Conceptual translation: checkpoint-controlled chromatin-state persistence

A widely adopted conceptual application is the checkpoint logic documented by Maas et al.: replication stress represses HST3 so that H3K56ac persists during stress, supporting survival, whereas inappropriate Hst3 activity under stress is detrimental (maas2006cellcycleand pages 2-3, maas2006cellcycleand pages 6-8).

8) Expert opinion and authoritative synthesis

Expert synthesis in the 2021 review emphasizes that H3K56ac sits at a “balance point” in genome maintenance: both insufficient acetylation (writer-side defects) and insufficient deacetylation (eraser-side defects) generate genome instability, and Hst3 is presented as the dominant deacetylase whose precise temporal control is essential (gershon2021theamazingacrobat pages 4-5).

Recent reviews (2023) reinforce this view by incorporating Hst3/Hst4 into broader chromatin–DDR frameworks (DSB chromatin landscape, pathway choice, checkpoint coupling), while also pointing to additional regulatory outcomes such as cohesion control (frigerio2023thechromatinlandscape pages 23-24).

9) Recent developments (prioritizing 2023–2024)

Recent (2023–2024) sources in this run mainly extend systems-level context rather than redefining enzymology:

• DSB chromatin review (Feb 2023): re-contextualizes Hst3/Hst4-mediated H3K56 deacetylation within DSB repair chromatin architecture and highlights checkpoint-linked Hst3 regulation in the literature base (https://doi.org/10.3390/ijms24043248) (frigerio2023thechromatinlandscape pages 23-24).
• mRNA homeostasis review (Feb 2023): places Hst3 in a transcriptional homeostasis network via cited interactions with the RNA exosome (https://doi.org/10.1080/21541264.2023.2183684) (bryll2023thecircularlogic pages 8-9).
• Proteome-wide DDR/ubiquitylation study (Jan 2024): experimentally supports MMS-linked Hst3 degradation dependence on nuclear proteasome functionality and uses HST3 overexpression phenotypes as an internal benchmark (https://doi.org/10.1016/j.mcpro.2023.100695) (blaszczak2024dissectingubiquitylationand pages 7-9).

10) Evidence summary table

The following table compiles the key functional-annotation points (identity, reaction, substrate specificity, regulation, phenotypes, and recent literature).

Table: This table summarizes identity, enzymatic function, substrate specificity, regulation, phenotypes, and recent literature for Saccharomyces cerevisiae HST3 using only evidence gathered in this run. It is useful as a compact, citation-backed functional annotation artifact for downstream report writing.

11) Key takeaways (functional annotation)

1. Primary molecular function: Hst3 is an NAD+-dependent sirtuin deacetylase whose major demonstrated physiological substrate is histone H3K56ac (maas2006cellcycleand pages 1-2, delgoshaie2013studyofhistone pages 39-44).
2. Pathway role: Hst3-driven removal of H3K56ac is essential for properly timed chromatin maturation and contributes to replication-associated genome stability and DNA damage tolerance (delgoshaie2013studyofhistone pages 75-79, maas2006cellcycleand pages 8-9).
3. Regulatory logic: During replication stress, checkpoint signaling (Mec1/Rad53-dependent) represses HST3 to maintain H3K56ac; forcing Hst3 activity under damage conditions is deleterious (maas2006cellcycleand pages 2-3, maas2006cellcycleand pages 5-6).
4. Quantitative anchors: WT H3K56ac is ~20% of H3 in log phase; loss of Hst3/Hst4 produces >4-fold hyperacetylation and can approach ~98–100% stoichiometry, correlating with severe genome instability phenotypes (maas2006cellcycleand pages 8-9, delgoshaie2013studyofhistone pages 51-56).

12) Limitations of this evidence set

This run did not retrieve a primary localization experiment explicitly stating Hst3’s subcellular localization; nuclear/chromatin action is inferred from substrate and pathway context within the extracted text (gershon2021theamazingacrobat pages 4-5). Additionally, no 2023–2024 primary paper in this run directly provided new biochemical kinetics for Hst3; recent papers primarily provide systems-level DDR/proteostasis context (blaszczak2024dissectingubiquitylationand pages 7-9, frigerio2023thechromatinlandscape pages 23-24).

References

1. (maas2006cellcycleand pages 8-9): Nancy L. Maas, Kyle M. Miller, Lisa G. DeFazio, and David P. Toczyski. Cell cycle and checkpoint regulation of histone h3 k56 acetylation by hst3 and hst4. Molecular cell, 23 1:109-19, Jul 2006. URL: https://doi.org/10.1016/j.molcel.2006.06.006, doi:10.1016/j.molcel.2006.06.006. This article has 307 citations and is from a highest quality peer-reviewed journal.

2. (maas2006cellcycleand pages 2-3): Nancy L. Maas, Kyle M. Miller, Lisa G. DeFazio, and David P. Toczyski. Cell cycle and checkpoint regulation of histone h3 k56 acetylation by hst3 and hst4. Molecular cell, 23 1:109-19, Jul 2006. URL: https://doi.org/10.1016/j.molcel.2006.06.006, doi:10.1016/j.molcel.2006.06.006. This article has 307 citations and is from a highest quality peer-reviewed journal.

3. (maas2006cellcycleand pages 5-6): Nancy L. Maas, Kyle M. Miller, Lisa G. DeFazio, and David P. Toczyski. Cell cycle and checkpoint regulation of histone h3 k56 acetylation by hst3 and hst4. Molecular cell, 23 1:109-19, Jul 2006. URL: https://doi.org/10.1016/j.molcel.2006.06.006, doi:10.1016/j.molcel.2006.06.006. This article has 307 citations and is from a highest quality peer-reviewed journal.

4. (delgoshaie2013studyofhistone pages 39-44): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

5. (maas2006cellcycleand pages 1-2): Nancy L. Maas, Kyle M. Miller, Lisa G. DeFazio, and David P. Toczyski. Cell cycle and checkpoint regulation of histone h3 k56 acetylation by hst3 and hst4. Molecular cell, 23 1:109-19, Jul 2006. URL: https://doi.org/10.1016/j.molcel.2006.06.006, doi:10.1016/j.molcel.2006.06.006. This article has 307 citations and is from a highest quality peer-reviewed journal.

6. (gershon2021theamazingacrobat pages 4-5): Lihi Gershon and Martin Kupiec. The amazing acrobat: yeast’s histone h3k56 juggles several important roles while maintaining perfect balance. Genes, 12:342, Feb 2021. URL: https://doi.org/10.3390/genes12030342, doi:10.3390/genes12030342. This article has 14 citations.

7. (delgoshaie2013studyofhistone pages 51-56): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

8. (delgoshaie2013studyofhistone pages 79-83): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

9. (delgoshaie2013studyofhistone pages 75-79): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

10. (maas2006cellcycleand pages 6-8): Nancy L. Maas, Kyle M. Miller, Lisa G. DeFazio, and David P. Toczyski. Cell cycle and checkpoint regulation of histone h3 k56 acetylation by hst3 and hst4. Molecular cell, 23 1:109-19, Jul 2006. URL: https://doi.org/10.1016/j.molcel.2006.06.006, doi:10.1016/j.molcel.2006.06.006. This article has 307 citations and is from a highest quality peer-reviewed journal.

11. (frigerio2023thechromatinlandscape pages 23-24): Chiara Frigerio, Elena Di Nisio, Michela Galli, Chiara Vittoria Colombo, Rodolfo Negri, and Michela Clerici. The chromatin landscape around dna double-strand breaks in yeast and its influence on dna repair pathway choice. International Journal of Molecular Sciences, 24:3248, Feb 2023. URL: https://doi.org/10.3390/ijms24043248, doi:10.3390/ijms24043248. This article has 32 citations.

12. (bryll2023thecircularlogic pages 8-9): Alysia R. Bryll and Craig L. Peterson. The circular logic of mrna homeostasis. Transcription, 14:18-26, Feb 2023. URL: https://doi.org/10.1080/21541264.2023.2183684, doi:10.1080/21541264.2023.2183684. This article has 14 citations and is from a peer-reviewed journal.

13. (blaszczak2024dissectingubiquitylationand pages 7-9): Ewa Blaszczak, Emeline Pasquier, Gaëlle Le Dez, Adrian Odrzywolski, Natalia Lazarewicz, Audrey Brossard, Emilia Fornal, Piotr Moskalek, Robert Wysocki, and Gwenaël Rabut. Dissecting ubiquitylation and dna damage response pathways in the yeast saccharomyces cerevisiae using a proteome-wide approach. Molecular & Cellular Proteomics, 23:100695, Jan 2024. URL: https://doi.org/10.1016/j.mcpro.2023.100695, doi:10.1016/j.mcpro.2023.100695. This article has 3 citations and is from a domain leading peer-reviewed journal.

14. (delgoshaie2013studyofhistone pages 44-48): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

15. (delgoshaie2013studyofhistone pages 113-118): N Delgoshaie. Study of histone h3 lysine 56 deacetylation in saccharomyces cerevisiae. Unknown journal, 2013.

Citations

1. delgoshaie2013studyofhistone pages 39-44
2. maas2006cellcycleand pages 8-9
3. gershon2021theamazingacrobat pages 4-5
4. delgoshaie2013studyofhistone pages 79-83
5. maas2006cellcycleand pages 2-3
6. frigerio2023thechromatinlandscape pages 23-24
7. bryll2023thecircularlogic pages 8-9
8. maas2006cellcycleand pages 5-6
9. blaszczak2024dissectingubiquitylationand pages 7-9
10. maas2006cellcycleand pages 1-2
11. delgoshaie2013studyofhistone pages 51-56
12. delgoshaie2013studyofhistone pages 75-79
13. maas2006cellcycleand pages 6-8
14. delgoshaie2013studyofhistone pages 44-48
15. delgoshaie2013studyofhistone pages 113-118
16. https://doi.org/10.1016/j.molcel.2006.06.006
17. https://doi.org/10.3390/ijms24043248
18. https://doi.org/10.1080/21541264.2023.2183684
19. https://doi.org/10.3390/genes12030342
20. https://doi.org/10.1016/j.mcpro.2023.100695
21. https://doi.org/10.1016/j.molcel.2006.06.006;
22. https://doi.org/10.3390/ijms24043248;
23. https://doi.org/10.3390/genes12030342;
24. https://doi.org/10.1080/21541264.2023.2183684;
25. https://doi.org/10.1016/j.molcel.2006.06.006,
26. https://doi.org/10.3390/genes12030342,
27. https://doi.org/10.3390/ijms24043248,
28. https://doi.org/10.1080/21541264.2023.2183684,
29. https://doi.org/10.1016/j.mcpro.2023.100695,