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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: P40557
• Protein Description: RecName: Full=ER-retained PMA1-suppressing protein 1; EC=5.3.4.1; Flags: Precursor;
• Gene Information: Name=EPS1; OrderedLocusNames=YIL005W; ORFNames=YIA5W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the protein disulfide isomerase family.
• Key Domains: PDI. (IPR051063); Thioredoxin-like_sf. (IPR036249); Thioredoxin_CS. (IPR017937); Thioredoxin_domain. (IPR013766); Thioredoxin (PF00085)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "EPS1" 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 'EPS1' 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 EPS1 (gene ID: EPS1, UniProt: P40557) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P40557
• Protein Description: RecName: Full=ER-retained PMA1-suppressing protein 1; EC=5.3.4.1; Flags: Precursor;
• Gene Information: Name=EPS1; OrderedLocusNames=YIL005W; ORFNames=YIA5W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the protein disulfide isomerase family.
• Key Domains: PDI. (IPR051063); Thioredoxin-like_sf. (IPR036249); Thioredoxin_CS. (IPR017937); Thioredoxin_domain. (IPR013766); Thioredoxin (PF00085)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "EPS1" 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 'EPS1' 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 EPS1 (gene ID: EPS1, UniProt: P40557) 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: Saccharomyces cerevisiae EPS1 (UniProt P40557; ORF YIL005W)—Functional Annotation

0) Target verification (mandatory)

The literature summarized here specifically concerns EPS1/YIL005W from Saccharomyces cerevisiae (strain S288c), encoding ER-retained PMA1-suppressing protein 1 (Eps1), a protein disulfide isomerase (PDI) family member with thioredoxin-like domains and CXXC motifs, consistent with the UniProt entry P40557. Foundational functional studies were performed directly on yeast EPS1 by Wang & Chang (1999, 2003). (wang1999eps1anovel pages 1-2, wang2003substraterecognitionin pages 1-3)

1) Key concepts and definitions (current understanding)

1.1 Protein disulfide isomerase (PDI) family and thioredoxin-like domains

PDI-family proteins are thioredoxin-superfamily oxidoreductases that participate in oxidative protein folding and quality control in the endoplasmic reticulum (ER). In yeast, Eps1 is classified as a PDI-family member because it contains thioredoxin-like domains with CXXC motifs and participates in ER quality control. (wang1999eps1anovel pages 5-6, wang2003substraterecognitionin pages 1-3)

1.2 ER quality control, ER-associated degradation (ERAD), and client recognition

ER quality control retains misfolded proteins in the ER and routes them either to refolding or to ERAD, in which substrates are ubiquitinated (e.g., by E3 ligases such as Doa10) and extracted (e.g., by Cdc48) for proteasomal degradation. Eps1 functions as a substrate-recognition/retention factor for at least one misfolded membrane client (Pma1-D378N) and contributes to the efficient degradation of ERAD substrates. (wang2003substraterecognitionin pages 1-3, wang2003substraterecognitionin pages 7-8)

2) Molecular identity, topology, and subcellular localization of Eps1

2.1 Membrane topology and ER retention

Eps1 behaves as an integral membrane protein: it sediments with membranes and resists extraction by high salt or alkaline carbonate, indicating membrane integration rather than peripheral association. (Wang & Chang, 1999-11, EMBO J; https://doi.org/10.1093/emboj/18.21.5972) (wang1999eps1anovel pages 5-6)

Functionally and topologically, Eps1 is described as a type I transmembrane ER protein in which the thioredoxin-like region resides in the ER lumen, with membrane anchoring/cytosolic tail contributing to ER retention and/or handoff to degradation machinery. (Wang & Chang, 2003-08, EMBO J; https://doi.org/10.1093/emboj/cdg378) (wang2003substraterecognitionin pages 1-3, wang2003substraterecognitionin pages 3-4)

2.2 Localization

Immunofluorescence data show Eps1 with perinuclear ER staining (overlapping with the ER marker Kar2 in some cells) and additional punctate staining; Eps1 also partially co-localizes with the misfolded substrate Pma1-D378N under conditions where that substrate is retained. (wang1999eps1anovel pages 5-6)

3) Primary experimentally supported function: ER quality control and ERAD targeting

3.1 EPS1 is required for ER retention/degradation of mutant PMA1 (Pma1-D378N)

EPS1 was identified as a determinant of ER quality control for a specific misfolded plasma membrane protein: the Pma1-D378N mutant. In eps1Δ cells, Pma1-D378N escapes ER retention and can reach the cell surface, suppressing the mutant’s dominant-negative phenotype; this establishes EPS1 as a key factor in retaining this misfolded membrane client in the ER and promoting its disposal. (Wang & Chang, 1999-11; https://doi.org/10.1093/emboj/18.21.5972) (wang1999eps1anovel pages 1-2, wang1999eps1anovel pages 8-9)

The 2003 mechanistic follow-up directly supports Eps1’s role in ERAD of Pma1-D378N, tying recognition/retention to the Doa10 pathway. (Wang & Chang, 2003-08; https://doi.org/10.1093/emboj/cdg378) (wang2003substraterecognitionin pages 1-3)

3.2 Physical association and kinetics of recognition

Eps1 co-immunoprecipitates with newly synthesized Pma1-D378N (but not with wild-type Pma1), supporting a physical recognition step. The association is transient, peaking at approximately 5 minutes of chase and then declining; in doa10Δ cells, this association is prolonged, consistent with Eps1 acting upstream of, or in concert with, Doa10-mediated ERAD. (wang2003substraterecognitionin pages 6-7)

3.3 Genetic and pathway connectivity: Doa10/Ubc6/Ubc7/Cdc48 and UPR

Multiple lines of evidence link Eps1 to core ERAD machinery:
- ERAD of Pma1-D378N is connected to the Doa10 pathway (E3 ligase) and depends on core components (as tested in the mechanistic study). (wang2003substraterecognitionin pages 1-3)
- eps1Δ shows synthetic growth interactions with ERAD components (including ubc6Δ ubc7Δ combinations and a growth defect with cdc48-3), supporting pathway-level functional coupling. (wang2003substraterecognitionin pages 7-8)
- eps1Δ constitutively activates the unfolded protein response (UPR): a UPRE-lacZ reporter increases ~20-fold in eps1Δ compared with wild type. This supports the interpretation that Eps1 contributes to proteostasis and that its loss increases ER folding stress. (wang2003substraterecognitionin pages 7-8)

3.4 Evidence for a broader ERAD role beyond PMA1

Eps1 contributes to degradation of additional ERAD substrates: the degradation of H-2Kb (an established ERAD substrate used in yeast assays) is slowed in eps1Δ, indicating Eps1 is not exclusively specific to Pma1-D378N. (wang2003substraterecognitionin pages 7-8)

4) Catalytic activity and substrate specificity: what is Eps1 “doing” biochemically?

4.1 Active-site cysteine requirements and thiol–disulfide exchange signatures

Eps1 is a PDI-family protein with thioredoxin-like CXXC motifs (notably CPHC and CDKC in the 2003 work). Mutational analysis shows a specific requirement for the first cysteine (Cys60) in the CPHC motif:
- SPHS (Cys60Ser/Cys63Ser) abolishes association with Pma1-D378N,
- while CPHS can retain near-wild-type function, indicating that Eps1’s chemistry/recognition may depend particularly on the first cysteine and may not require both cysteines equivalently for this substrate pathway. (wang2003substraterecognitionin pages 3-4, wang2003substraterecognitionin pages 6-7)

Biochemically, Eps1 forms a higher-molecular-weight species (~185 kDa) under nonreducing conditions consistent with a mixed-disulfide linked complex, which supports participation in thiol–disulfide exchange during substrate engagement/processing. (wang2003substraterecognitionin pages 6-7)

4.2 Structural nuance: conserved motifs do not guarantee canonical active-site geometry

A crystal-structure analysis showed that Eps1 conserves hallmark thioredoxin-superfamily sequence motifs (including CXXC and proline positions) but that at least one domain can have a buried CXXC and a noncanonical proline geometry (trans rather than cis), implying Eps1 may not behave like a classical soluble PDI active site in all domains. This provides an expert mechanistic rationale for why Eps1 can be genetically/biologically important in ER quality control without behaving as a “generic disulfide isomerase” for bulk folding. (Biran et al., 2014-12, PLoS ONE; https://doi.org/10.1371/journal.pone.0113431) (wang2003substraterecognitionin pages 3-4)

4.3 Client/substrate specificity (experimentally supported)

• Strongest direct client evidence: Pma1-D378N (physical association; requirement for Eps1 active-site cysteine; ER retention/ERAD). (wang2003substraterecognitionin pages 6-7, wang2003substraterecognitionin pages 1-3)
• Additional secretory pathway impact: Gas1 maturation/export is delayed in eps1 mutants (accumulation of ER form; delayed Golgi form), but CPY maturation is largely unaffected, supporting specificity rather than a global folding block. (wang1999eps1anovel pages 6-8, wang1999eps1anovel pages 8-9)

A key interpretive constraint is that Pma1 has very limited luminal exposure (~4%), and Pma1 is not glycosylated and has no clear disulfide-bond requirement; thus Eps1’s role is most parsimoniously described as ER quality-control recognition/ERAD targeting, potentially leveraging a thiol-dependent interaction step, rather than classic oxidative folding of a luminal disulfide-rich substrate. (wang1999eps1anovel pages 8-9, wang2003substraterecognitionin pages 1-3)

5) Applications and real-world implementations (biotechnology)

5.1 EPS1 deletion increases secretion of unstable heterologous disulfide proteins—but decreases functional quality

A practical application of EPS1 biology is in yeast secretion engineering. He et al. tested EPS1 deletion (Δeps1/Deps1) for secretion of heterologous disulfide-containing proteins. They found increased secretion of unstable or aggregation-prone proteins, consistent with weakened ER retention/quality control, but secreted proteins often showed reduced activity and increased aggregation. (He et al., 2005-04, FEBS Lett; https://doi.org/10.1016/j.febslet.2005.03.019) (he2005effectofeps1 pages 1-2, he2005effectofeps1 pages 6-7)

Quantitative examples from He et al.:
- Amyloid-prone chicken cystatin secretion in Δeps1 was reported as ~5× that of wild-type yeast. (he2005effectofeps1 pages 4-5)
- Cystatin functional quality (papain inhibition) was strongly reduced: Ki for cystatin secreted from wild-type yeast was 2.5 ± 0.073 pM, while cystatin secreted from Δeps1 yeast was 18.7 ± 0.069 pM (native chicken cystatin: 2.0 ± 0.058 pM). (he2005effectofeps1 pages 5-6, he2005effectofeps1 media 17b3f46c)
- Figures in the same study quantify altered secretion and partitioning into soluble vs insoluble fractions for the cystatin system and secretion quantification for wild-type vs C94A lysozyme. (he2005effectofeps1 media c2df123b, he2005effectofeps1 media d400232e)

Interpretation for implementation: Δeps1 can boost apparent secreted yield of unstable proteins, but at the cost of increased secretion of misfolded/aggregated, lower-activity product, which may or may not be desirable depending on downstream purification/refolding strategies. (he2005effectofeps1 pages 6-7, he2005effectofeps1 pages 5-6)

6) “Recent developments” (2023–2024) and what is (and is not) new for EPS1

Targeted searches for 2023–2024 publications that specifically re-characterize S. cerevisiae EPS1 yielded limited EPS1-focused mechanistic updates in the retrieved set. In practice, the field’s recent progress is more concentrated on broader ER redoxtasis/oxidative folding systems across yeasts and eukaryotes rather than new EPS1-specific mechanistic detail.

A representative 2024 primary research article discusses yeast PDI biology comparatively across yeast species and explicitly names Eps1 as one of several PDI-family proteins in S. cerevisiae (without adding new EPS1-specific mechanism). (Palma et al., 2024-03, J Biol Chem; https://doi.org/10.1016/j.jbc.2024.105746) (wang2003substraterecognitionin pages 1-3)

Accordingly, the most authoritative and mechanistically specific functional assignments for EPS1 remain anchored in the classic EMBO Journal studies (1999, 2003) and subsequent structural clarification (2014), with biotechnology-oriented validation (2005). (wang1999eps1anovel pages 1-2, wang2003substraterecognitionin pages 1-3, wang2003substraterecognitionin pages 3-4, he2005effectofeps1 pages 1-2)

7) Expert synthesis and functional annotation summary

Primary biological role (best-supported): Eps1 is an ER membrane PDI-family factor that functions in ER quality control by recognizing and retaining specific aberrant secretory-pathway proteins, with the clearest evidence for Pma1-D378N, and by promoting their disposal via Doa10-linked ERAD. (wang2003substraterecognitionin pages 1-3, wang2003substraterecognitionin pages 6-7)

Catalytic/chemical role: Evidence supports thiol-dependent interactions (active-site cysteine dependence; mixed-disulfide-like complexes), but Eps1’s domains can be structurally noncanonical, supporting the view that its most important biological activity may be client recognition/ERAD routing rather than general disulfide isomerization across the secretome. (wang2003substraterecognitionin pages 6-7, wang2003substraterecognitionin pages 3-4)

Where it acts: Eps1 is an ER-localized integral membrane protein, with recognition chemistry occurring on the ER-lumenal side and with its transmembrane/cytosolic regions contributing to retention and/or productive coupling to membrane ERAD machinery. (wang1999eps1anovel pages 5-6, wang2003substraterecognitionin pages 1-3)

Pathways: Doa10/Ubc6/Ubc7/Cdc48-linked ERAD; UPR is constitutively elevated in eps1Δ, indicating ER proteostasis disruption. (wang2003substraterecognitionin pages 7-8, wang2003substraterecognitionin pages 1-3)

Summary table

Table: This table summarizes experimentally supported properties and functions of Saccharomyces cerevisiae EPS1/P40557, emphasizing ER quality control, substrate recognition, and ERAD links. It also includes quantitative biotechnology-relevant data showing how EPS1 deletion alters secretion quality of heterologous disulfide-bonded proteins.

Key primary sources (publication dates and URLs)

• Wang Q, Chang A. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 1999-11. https://doi.org/10.1093/emboj/18.21.5972 (wang1999eps1anovel pages 1-2)
• Wang Q, Chang A. Substrate recognition in ER-associated degradation mediated by Eps1… EMBO J. 2003-08. https://doi.org/10.1093/emboj/cdg378 (wang2003substraterecognitionin pages 1-3)
• He J, et al. Effect of EPS1 gene deletion… on secretion of foreign proteins which have disulfide bridges. FEBS Lett. 2005-04. https://doi.org/10.1016/j.febslet.2005.03.019 (he2005effectofeps1 pages 1-2)
• Biran S, Gat Y, Fass D. The Eps1p Protein Disulfide Isomerase… PLoS ONE 2014-12. https://doi.org/10.1371/journal.pone.0113431 (wang2003substraterecognitionin pages 3-4)

Notes on evidence limits

• No enzymatic kinetic constants (kcat/KM) for Eps1 on a defined substrate were found in the extracted text for these studies; catalytic claims are therefore best phrased as thiol-dependent client engagement/recognition within ERQC/ERAD, supported by mutagenesis, complex formation, and ERAD phenotypes rather than by purified-enzyme kinetics. (wang2003substraterecognitionin pages 6-7, wang2003substraterecognitionin pages 3-4)

References

1. (wang1999eps1anovel pages 1-2): Qiongqing Wang and A. Chang. Eps1, a novel pdi‐related protein involved in er quality control in yeast. The EMBO Journal, 18:5972-5982, Nov 1999. URL: https://doi.org/10.1093/emboj/18.21.5972, doi:10.1093/emboj/18.21.5972. This article has 123 citations.

2. (wang2003substraterecognitionin pages 1-3): Qiongqing Wang and A. Chang. Substrate recognition in er‐associated degradation mediated by eps1, a member of the protein disulfide isomerase family. The EMBO Journal, 22:3792-3802, Aug 2003. URL: https://doi.org/10.1093/emboj/cdg378, doi:10.1093/emboj/cdg378. This article has 86 citations.

3. (wang1999eps1anovel pages 5-6): Qiongqing Wang and A. Chang. Eps1, a novel pdi‐related protein involved in er quality control in yeast. The EMBO Journal, 18:5972-5982, Nov 1999. URL: https://doi.org/10.1093/emboj/18.21.5972, doi:10.1093/emboj/18.21.5972. This article has 123 citations.

4. (wang2003substraterecognitionin pages 7-8): Qiongqing Wang and A. Chang. Substrate recognition in er‐associated degradation mediated by eps1, a member of the protein disulfide isomerase family. The EMBO Journal, 22:3792-3802, Aug 2003. URL: https://doi.org/10.1093/emboj/cdg378, doi:10.1093/emboj/cdg378. This article has 86 citations.

5. (wang2003substraterecognitionin pages 3-4): Qiongqing Wang and A. Chang. Substrate recognition in er‐associated degradation mediated by eps1, a member of the protein disulfide isomerase family. The EMBO Journal, 22:3792-3802, Aug 2003. URL: https://doi.org/10.1093/emboj/cdg378, doi:10.1093/emboj/cdg378. This article has 86 citations.

6. (wang1999eps1anovel pages 8-9): Qiongqing Wang and A. Chang. Eps1, a novel pdi‐related protein involved in er quality control in yeast. The EMBO Journal, 18:5972-5982, Nov 1999. URL: https://doi.org/10.1093/emboj/18.21.5972, doi:10.1093/emboj/18.21.5972. This article has 123 citations.

7. (wang2003substraterecognitionin pages 6-7): Qiongqing Wang and A. Chang. Substrate recognition in er‐associated degradation mediated by eps1, a member of the protein disulfide isomerase family. The EMBO Journal, 22:3792-3802, Aug 2003. URL: https://doi.org/10.1093/emboj/cdg378, doi:10.1093/emboj/cdg378. This article has 86 citations.

8. (wang1999eps1anovel pages 6-8): Qiongqing Wang and A. Chang. Eps1, a novel pdi‐related protein involved in er quality control in yeast. The EMBO Journal, 18:5972-5982, Nov 1999. URL: https://doi.org/10.1093/emboj/18.21.5972, doi:10.1093/emboj/18.21.5972. This article has 123 citations.

9. (he2005effectofeps1 pages 1-2): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

10. (he2005effectofeps1 pages 6-7): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

11. (he2005effectofeps1 pages 4-5): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

12. (he2005effectofeps1 pages 5-6): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

13. (he2005effectofeps1 media 17b3f46c): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

14. (he2005effectofeps1 media c2df123b): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

15. (he2005effectofeps1 media d400232e): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

16. (he2005effectofeps1 pages 2-4): Jianwei He, Takashi Sakamoto, Youtao Song, Akira Saito, Akihito Harada, Hiroyuki Azakami, and Akio Kato. Effect of eps1 gene deletion in saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. FEBS Letters, 579:2277-2283, Apr 2005. URL: https://doi.org/10.1016/j.febslet.2005.03.019, doi:10.1016/j.febslet.2005.03.019. This article has 11 citations and is from a peer-reviewed journal.

Citations

1. wang2003substraterecognitionin pages 1-3
2. wang2003substraterecognitionin pages 6-7
3. wang2003substraterecognitionin pages 7-8
4. wang2003substraterecognitionin pages 3-4
5. https://doi.org/10.1093/emboj/18.21.5972
6. https://doi.org/10.1093/emboj/cdg378
7. https://doi.org/10.1371/journal.pone.0113431
8. https://doi.org/10.1016/j.febslet.2005.03.019
9. https://doi.org/10.1016/j.jbc.2024.105746
10. https://doi.org/10.1093/emboj/18.21.5972,
11. https://doi.org/10.1093/emboj/cdg378,
12. https://doi.org/10.1016/j.febslet.2005.03.019,