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gene_info: Name=CHS7; OrderedLocusNames=YHR142W;
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
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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: P38843
• Protein Description: RecName: Full=Chitin synthase export chaperone;
• Gene Information: Name=CHS7; OrderedLocusNames=YHR142W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the CHS7 family. .
• Key Domains: Chs7. (IPR022057); Chs7 (PF12271)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CHS7" 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 'CHS7' 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 CHS7 (gene ID: CHS7, UniProt: P38843) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P38843
• Protein Description: RecName: Full=Chitin synthase export chaperone;
• Gene Information: Name=CHS7; OrderedLocusNames=YHR142W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the CHS7 family. .
• Key Domains: Chs7. (IPR022057); Chs7 (PF12271)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CHS7" 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 'CHS7' 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 CHS7 (gene ID: CHS7, UniProt: P38843) 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 CHS7 (UniProt P38843; YHR142W)

Executive summary

CHS7 (YHR142W; UniProt P38843) encodes Chs7, a small multipass membrane protein that functions primarily as a client-specific export chaperone/escort required for endoplasmic reticulum (ER) exit and productive biogenesis of the major chitin synthase Chs3 (chitin synthase III; CSIII). Loss of CHS7 causes ER retention of Chs3, severe reduction of cell wall chitin and CSIII activity, and associated cell-wall and developmental phenotypes. More recent work (2022–2023) reframes Chs7 as part of a multi-layered proteostasis/quality-control network that prevents Chs3 aggregation and masks cytosolic degrons to avoid ER-associated degradation (ERAD). (trilla1999chs7panew pages 4-5, sanchez2022chitinsynthesisin pages 4-6, sanchez2023multiplequalitycontrol pages 4-6)

1) Key concepts and definitions (current understanding)

1.1 What CHS7 is (gene/protein identity)

Trilla et al. experimentally defined CHS7 as YHR142W and described its product (Chs7p) as a ~316-aa, 6–7 transmembrane protein involved in ER export control specifically tied to chitin synthesis regulation (publication: June 1999, Journal of Cell Biology, https://doi.org/10.1083/jcb.145.6.1153). (trilla1999chs7panew pages 4-5, trilla1999chs7panew pages 5-6)

1.2 What “chitin synthase export chaperone” means in this system

In budding yeast, most chitin in the wall is produced by Chs3/CSIII, a multipass membrane enzyme whose trafficking is highly regulated. Chs7 is “export chaperone” in the sense that Chs3 ER exit depends on Chs7, and without Chs7 Chs3 remains ER-localized despite being synthesized and core-glycosylated. (trilla1999chs7panew pages 5-6, sanchez2022chitinsynthesisin pages 3-4)

A key conceptual update from recent synthesis is that the Chs3/Chs7 system is treated as a paradigm for intracellular trafficking of integral membrane proteins—Chs3 recapitulates many canonical trafficking steps (ER folding, COPII export, Golgi/TGN sorting, endocytosis, recycling, degradation), with Chs7 acting at the earliest “licensing” step. (sanchez2022chitinsynthesisin pages 3-4)

2) Core experimentally supported biology of CHS7

2.1 Primary molecular function: enabling Chs3 ER exit and CSIII output

A central experimental result is that chs7Δ mutants retain Chs3 in the ER (“all the Chs3p-3XHA remained in the ER”), demonstrating Chs7 is required for Chs3 export from the ER. (trilla1999chs7panew pages 6-7, trilla1999chs7panew media afaeb15d)

Chs7 is also a limiting factor for functional CSIII: co-overexpression of CHS3 and CHS7 increased total CSIII almost fourfold, whereas basal activity increased only ~1.3-fold, consistent with increased export/availability of an otherwise ER-limited pool of Chs3. (trilla1999chs7panew pages 7-8)

2.2 Subcellular localization of Chs7

In the original primary study, functional tagged Chs7 showed perinuclear/ER localization and co-localization with the ER marker Sec63p (ER fractionation and imaging). (trilla1999chs7panew pages 5-6, trilla1999chs7panew media 93a4edff)

Later work (thesis-level evidence in the retrieved corpus) argues Chs7 is not exclusively ER-resident: it can exit the ER with Chs3 and co-localize with Chs3 at the bud neck and intracellular puncta, remaining associated and contributing to activity at the surface. While not a 2023–2024 peer-reviewed source in the retrieved set, it provides a mechanistic model consistent with complex persistence noted in the 2022 review. (dharwada2016intracellulartraffickingof pages 40-45, dharwada2016intracellulartraffickingof pages 50-54)

2.3 Pathway placement: CHS7 vs later trafficking factors

A genetic-interaction synthesis explicitly positions CHS7 at the ER step: Chs7 is required for exit of Chs3 from the ER, whereas Chs5/Chs6 are involved in transport of Chs3 from “chitosomes” (TGN pool) to the plasma membrane. (publication: Feb 2005, BMC Genetics, https://doi.org/10.1186/1471-2156-6-8). (lesage2005aninteractionalnetwork pages 1-2)

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

3.1 2022: “Chitin synthesis in yeast: a matter of trafficking” (authoritative review)

Sánchez & Roncero (publication: Oct 2022, Int. J. Mol. Sci., https://doi.org/10.3390/ijms232012251) integrate decades of trafficking work and describe Chs7 as a specific ER chaperone that prevents Chs3 aggregation and promotes ER exit via COPII loading, with Erv14 acting as a cargo receptor; they also note that the Chs3–Chs7 complex can persist along the secretory route, potentially affecting later steps and/or activity. (sanchez2022chitinsynthesisin pages 4-6)

This review further emphasizes that Chs3 folding/assembly is monitored by multiple checkpoints and that trafficking regulation is central to controlling chitin deposition (i.e., chitin output is a trafficking problem as much as an enzymology problem). (sanchez2022chitinsynthesisin pages 3-4)

3.2 2023: Chs7 integrates into ER quality control (ERAD-C masking; multi-pathway QC)

Sanchez et al. (publication: Dec 2023, Molecular Biology of the Cell, https://doi.org/10.1091/mbc.e23-05-0186) provide direct evidence that Chs7 is not merely a passive escort: it masks cytosolic degrons in Chs3, preventing Doa10-mediated ERAD-C targeting when Chs3 is retained in the ER. (sanchez2023multiplequalitycontrol pages 11-13, sanchez2023multiplequalitycontrol pages 9-11)

Key mechanistic points supported in the retrieved excerpts include:
- Chs7 physically interacts with full-length Chs3 and certain truncated Chs3 forms (co-immunoprecipitation). (sanchez2023multiplequalitycontrol pages 11-13)
- In a chs7Δ background, Chs3 constructs can become more ERAD-sensitive; doa10Δ reverses instability for at least some constructs, consistent with Chs7-dependent shielding from ERAD-C. (sanchez2023multiplequalitycontrol pages 11-13, sanchez2023multiplequalitycontrol pages 9-11)
- Chs3 that evades canonical ERAD can redistribute to the inner nuclear membrane (INM) and be degraded by INMAD (Asi complex), framing INMAD as a downstream safeguard for polytopic membrane proteins. (sanchez2023multiplequalitycontrol pages 13-15, sanchez2023multiplequalitycontrol pages 1-2)

Overall, the 2023 study advances the field from “Chs7 is required for export” to “Chs7 is part of a layered ER proteostasis logic that determines whether Chs3 is exported, retained, or degraded.” (sanchez2023multiplequalitycontrol pages 4-6, sanchez2023multiplequalitycontrol pages 11-13)

3.3 2024: status of CHS7-specific primary research in the retrieved corpus

Within the retrieved 2024 corpus for this run, CHS7 is primarily cited as a canonical example of an ER export chaperone for chitin synthases, rather than being the subject of new S. cerevisiae CHS7 experiments. Accordingly, the most direct “latest” primary evidence in the retrieved set is the 2023 MBoC work. (sanchez2023multiplequalitycontrol pages 4-6)

4) Current applications and real-world implementations

4.1 CHS7/Chs7 as a model system for membrane-protein trafficking and ER proteostasis

The Chs3/Chs7 module is widely used as a model polytopic membrane-protein cargo to interrogate principles of ER folding, COPII export, Golgi/TGN sorting, endocytic recycling, and degradation pathways. This is explicit in the 2022 review’s framing of Chs3 as a paradigm cargo whose lifecycle covers most canonical trafficking steps; Chs7 is the dedicated accessory/chaperone controlling the critical ER exit step. (sanchez2022chitinsynthesisin pages 3-4, sanchez2022chitinsynthesisin pages 4-6)

4.2 Indirect relevance to antifungal strategies and fungal cell wall control

Chitin is absent from mammalian cells and is an established antifungal-relevant cell wall component. While CHS7 itself is not an enzyme (and thus not a direct catalytic target), it is essential for productive trafficking of the major chitin synthase and therefore links mechanistically to cell wall robustness. The review emphasizes sustained interest in chitin synthesis regulation as relevant to antifungal approaches. (sanchez2022chitinsynthesisin pages 4-6)

5) Expert opinions and analysis (authoritative synthesis)

5.1 “Chitin synthesis is a matter of trafficking” (conceptual synthesis)

Sánchez & Roncero argue that regulation of chitin deposition (especially by Chs3) is fundamentally a trafficking and localization problem, because activity depends on correct compartmental progression and polarized delivery, not only on catalytic capability. In this framework, Chs7 is a decisive early determinant because it controls whether Chs3 is competent to leave the ER and enter the regulated trafficking itinerary. (sanchez2022chitinsynthesisin pages 3-4, sanchez2022chitinsynthesisin pages 4-6)

5.2 Multi-layer QC perspective (2023)

Sanchez et al. emphasize that several complementary QC mechanisms (N-glycosylation-dependent ERAD-L avoidance, Chs7-dependent ERAD-C degron masking, and INMAD as a late safeguard) together maintain homeostasis for a stable but failure-prone polytopic enzyme. This presents a broader expert-level conclusion: dedicated chaperones like Chs7 can simultaneously function as folding/escort factors and “degron shields” that determine whether a client is trafficked or degraded. (sanchez2023multiplequalitycontrol pages 1-2, sanchez2023multiplequalitycontrol pages 11-13, sanchez2023multiplequalitycontrol pages 13-15)

6) Quantitative data and statistics (recent and classic)

6.1 Direct CHS7-loss phenotypes (classic quantitative results)

In Trilla et al. (1999), chs7Δ mutants exhibit a dramatic reduction in chitin synthesis outputs:
- Cell wall chitin: 13.6% of wild-type (Table II). (trilla1999chs7panew media 93a4edff)
- CSIII activity: 14.6% of wild-type (Table II). (trilla1999chs7panew media 93a4edff)

These quantitative data support the central functional claim that CHS7 is required for normal Chs3/CSIII-dependent chitin deposition. (trilla1999chs7panew pages 4-5)

6.2 Overexpression statistics indicating CHS7 is rate-limiting

Trilla et al. also show that balanced expression matters: co-overexpression of CHS3 and CHS7 increased total CSIII ~4-fold but basal activity only ~1.3-fold, consistent with Chs7 controlling a bottleneck that affects the pool of export-competent Chs3. (trilla1999chs7panew pages 7-8)

6.3 Network-scale statistics for CHS7 functional embedding

Lesage et al. (2005) quantified the genetic interaction landscape:
- Total network: 316 interactions among 163 genes. (lesage2005aninteractionalnetwork pages 1-2)
- CSIII subnetwork: 123 genes / 259 interactions. (lesage2005aninteractionalnetwork pages 2-4)
- CHS7 connectivity in this dataset: 31 genetic connections. (lesage2005aninteractionalnetwork pages 1-2)

These statistics indicate CHS7 is embedded in a dense neighborhood enriched for cell wall assembly and polarized secretion buffering, consistent with its key role in Chs3 trafficking. (lesage2005aninteractionalnetwork pages 1-2, lesage2005aninteractionalnetwork pages 2-4)

7) Localization and pathway evidence (visual and experimental)

Microscopy and biochemical fractionation in Trilla et al. provide direct visual evidence that:
- Chs7 localizes to the ER/nuclear periphery. (trilla1999chs7panew media 93a4edff)
- In chs7Δ mutants, Chs3 is retained in the ER with perinuclear staining. (trilla1999chs7panew media afaeb15d)

These visual panels support the mechanistic model of CHS7 as an ER export factor for Chs3. (trilla1999chs7panew pages 6-7, trilla1999chs7panew pages 5-6)

Summary table artifact

The following table consolidates identity, function, localization, mechanism, interactions, and quantitative phenotypes with DOI URLs.

Table: This table condenses the core experimentally supported knowledge on Saccharomyces cerevisiae CHS7/YHR142W, including identity verification, localization, mechanism, quantitative phenotypes, network context, and recent quality-control insights. It is designed as a citation-ready reference for a gene function report.

References (URLs and publication dates)

• Trilla JA, Durán Á, Roncero C. Chs7p, a New Protein Involved in the Control of Protein Export from the Endoplasmic Reticulum… J Cell Biol. 1999-06. https://doi.org/10.1083/jcb.145.6.1153 (trilla1999chs7panew pages 4-5)
• Sánchez N, Roncero C. Chitin Synthesis in Yeast: A Matter of Trafficking. Int J Mol Sci. 2022-10. https://doi.org/10.3390/ijms232012251 (sanchez2022chitinsynthesisin pages 4-6)
• Sanchez N, de Leon N, Valle R, et al. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Mol Biol Cell. 2023-12. https://doi.org/10.1091/mbc.e23-05-0186 (sanchez2023multiplequalitycontrol pages 4-6)
• Lesage G, Shapiro J, Specht CA, et al. An interactional network of genes involved in chitin synthesis in Saccharomyces cerevisiae. BMC Genet. 2005-02. https://doi.org/10.1186/1471-2156-6-8 (lesage2005aninteractionalnetwork pages 1-2)

Notes on scope and evidence limitations

• The most directly relevant 2023–2024 primary evidence in the retrieved set is the 2023 MBoC study; within this run, no additional 2024 S. cerevisiae CHS7-focused primary papers were retrieved that add new CHS7-specific mechanistic data beyond this framework. (sanchez2023multiplequalitycontrol pages 4-6)
• Some mechanistic claims about Chs7 co-trafficking beyond the ER are supported in the retrieved corpus by thesis-level work and are presented as lower-authority evidence compared with the peer-reviewed primary and review literature. (dharwada2016intracellulartraffickingof pages 40-45, dharwada2016intracellulartraffickingof pages 50-54)

References

1. (trilla1999chs7panew pages 4-5): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

2. (sanchez2022chitinsynthesisin pages 4-6): Noelia Sánchez and César Roncero. Chitin synthesis in yeast: a matter of trafficking. International Journal of Molecular Sciences, 23:12251, Oct 2022. URL: https://doi.org/10.3390/ijms232012251, doi:10.3390/ijms232012251. This article has 21 citations.

3. (sanchez2023multiplequalitycontrol pages 4-6): Noelia Sanchez, Nagore de Leon, Rosario Valle, Jia Jun Fung, Anton Khmelinskii, and Cesar Roncero. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Molecular Biology of the Cell, Dec 2023. URL: https://doi.org/10.1091/mbc.e23-05-0186, doi:10.1091/mbc.e23-05-0186. This article has 3 citations and is from a domain leading peer-reviewed journal.

4. (trilla1999chs7panew pages 5-6): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

5. (sanchez2022chitinsynthesisin pages 3-4): Noelia Sánchez and César Roncero. Chitin synthesis in yeast: a matter of trafficking. International Journal of Molecular Sciences, 23:12251, Oct 2022. URL: https://doi.org/10.3390/ijms232012251, doi:10.3390/ijms232012251. This article has 21 citations.

6. (trilla1999chs7panew pages 6-7): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

7. (trilla1999chs7panew media afaeb15d): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

8. (trilla1999chs7panew pages 7-8): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

9. (trilla1999chs7panew media 93a4edff): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

10. (dharwada2016intracellulartraffickingof pages 40-45): Sai Tejasvi Dharwada. Intracellular trafficking of a model polytopic membrane protein in saccharomyces cerevisiae. ArXiv, Jan 2016. URL: https://doi.org/10.14288/1.0166170, doi:10.14288/1.0166170. This article has 0 citations.

11. (dharwada2016intracellulartraffickingof pages 50-54): Sai Tejasvi Dharwada. Intracellular trafficking of a model polytopic membrane protein in saccharomyces cerevisiae. ArXiv, Jan 2016. URL: https://doi.org/10.14288/1.0166170, doi:10.14288/1.0166170. This article has 0 citations.

12. (lesage2005aninteractionalnetwork pages 1-2): Guillaume Lesage, Jesse Shapiro, Charles A Specht, Anne-Marie Sdicu, Patrice Ménard, Shamiza Hussein, Amy Hin Yan Tong, Charles Boone, and Howard Bussey. An interactional network of genes involved in chitin synthesis in saccharomyces cerevisiae. BMC Genetics, 6:8-8, Feb 2005. URL: https://doi.org/10.1186/1471-2156-6-8, doi:10.1186/1471-2156-6-8. This article has 151 citations.

13. (sanchez2023multiplequalitycontrol pages 11-13): Noelia Sanchez, Nagore de Leon, Rosario Valle, Jia Jun Fung, Anton Khmelinskii, and Cesar Roncero. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Molecular Biology of the Cell, Dec 2023. URL: https://doi.org/10.1091/mbc.e23-05-0186, doi:10.1091/mbc.e23-05-0186. This article has 3 citations and is from a domain leading peer-reviewed journal.

14. (sanchez2023multiplequalitycontrol pages 9-11): Noelia Sanchez, Nagore de Leon, Rosario Valle, Jia Jun Fung, Anton Khmelinskii, and Cesar Roncero. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Molecular Biology of the Cell, Dec 2023. URL: https://doi.org/10.1091/mbc.e23-05-0186, doi:10.1091/mbc.e23-05-0186. This article has 3 citations and is from a domain leading peer-reviewed journal.

15. (sanchez2023multiplequalitycontrol pages 13-15): Noelia Sanchez, Nagore de Leon, Rosario Valle, Jia Jun Fung, Anton Khmelinskii, and Cesar Roncero. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Molecular Biology of the Cell, Dec 2023. URL: https://doi.org/10.1091/mbc.e23-05-0186, doi:10.1091/mbc.e23-05-0186. This article has 3 citations and is from a domain leading peer-reviewed journal.

16. (sanchez2023multiplequalitycontrol pages 1-2): Noelia Sanchez, Nagore de Leon, Rosario Valle, Jia Jun Fung, Anton Khmelinskii, and Cesar Roncero. Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum. Molecular Biology of the Cell, Dec 2023. URL: https://doi.org/10.1091/mbc.e23-05-0186, doi:10.1091/mbc.e23-05-0186. This article has 3 citations and is from a domain leading peer-reviewed journal.

17. (lesage2005aninteractionalnetwork pages 2-4): Guillaume Lesage, Jesse Shapiro, Charles A Specht, Anne-Marie Sdicu, Patrice Ménard, Shamiza Hussein, Amy Hin Yan Tong, Charles Boone, and Howard Bussey. An interactional network of genes involved in chitin synthesis in saccharomyces cerevisiae. BMC Genetics, 6:8-8, Feb 2005. URL: https://doi.org/10.1186/1471-2156-6-8, doi:10.1186/1471-2156-6-8. This article has 151 citations.

18. (trilla1999chs7panew pages 1-2): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

19. (dharwada2016intracellulartraffickingof pages 81-84): Sai Tejasvi Dharwada. Intracellular trafficking of a model polytopic membrane protein in saccharomyces cerevisiae. ArXiv, Jan 2016. URL: https://doi.org/10.14288/1.0166170, doi:10.14288/1.0166170. This article has 0 citations.

20. (trilla1999chs7panew pages 8-10): J. A. Trilla, Á. Durán, and C. Roncero. Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in saccharomyces cerevisiae. The Journal of Cell Biology, 145:1153-1163, Jun 1999. URL: https://doi.org/10.1083/jcb.145.6.1153, doi:10.1083/jcb.145.6.1153. This article has 199 citations.

21. (lesage2005aninteractionalnetwork pages 4-5): Guillaume Lesage, Jesse Shapiro, Charles A Specht, Anne-Marie Sdicu, Patrice Ménard, Shamiza Hussein, Amy Hin Yan Tong, Charles Boone, and Howard Bussey. An interactional network of genes involved in chitin synthesis in saccharomyces cerevisiae. BMC Genetics, 6:8-8, Feb 2005. URL: https://doi.org/10.1186/1471-2156-6-8, doi:10.1186/1471-2156-6-8. This article has 151 citations.

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