EUG1

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.

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Research report: EUG1 (YDR518W; UniProt P32474) — Protein disulfide-isomerase family member in Saccharomyces cerevisiae (S288c)

1) Key concepts, definitions, and current understanding

1.1 Protein disulfide isomerase (PDI) family in the ER

Protein disulfide isomerase (PDI) family proteins are thioredoxin-domain oxidoreductases in the endoplasmic reticulum (ER) lumen that catalyze thiol–disulfide exchange reactions during secretory-protein folding, including disulfide bond formation (oxidation), disulfide reduction, and disulfide isomerization (reshuffling of incorrect disulfides) (suzuki2015redoxdiversityin pages 1-2). In budding yeast, Pdi1p is the essential PDI, while several nonessential homologues provide overlapping/auxiliary functions in ER oxidative folding and quality control (xiao2004thecontributionsof pages 2-2, nørgaard2001functionaldifferencesin pages 2-2).

1.2 EUG1 gene/protein identity verification (disambiguation)

Multiple independent sources explicitly place EUG1 (YDR518W) among the PDI1 homologues localized to the yeast ER (MPD1, MPD2, EUG1, EPS1) and among the yeast PDI family members (xiao2004thecontributionsof pages 2-2, suzuki2015redoxdiversityin pages 1-2). In addition, mechanistic evidence refers to “a yeast PDI homologue, Eug1p” and highlights its unusual active-site chemistry (beynonjones2006mutationalanalysisof pages 1-2). These points confirm that the literature summarized here corresponds to the same target as UniProt P32474 (Eug1p in S. cerevisiae), not an unrelated “EUG1” gene from another organism (xiao2004thecontributionsof pages 2-2, beynonjones2006mutationalanalysisof pages 1-2).

2) Molecular features of Eug1p (domains, active sites) and enzymatic mechanism

2.1 Domain architecture and active-site motifs

Eug1p is described as a Pdi1p homologue with two thioredoxin-like domains and two non-canonical redox motifs of the form CXXS (rather than CXXC) (nørgaard2001functionaldifferencesin pages 2-2, nørgaard2001functionaldifferencesin pages 1-2). Active-site positions for the two CxxS motifs were reported as residues 62 and 405 (hacioglu2010therolesof pages 3-4). This “CXXS” configuration is repeatedly emphasized as a key reason for Eug1p’s atypically weak oxidoreductase function relative to canonical PDIs (beynonjones2006mutationalanalysisof pages 1-2, nørgaard2001functionaldifferencesin pages 2-2).

2.2 Catalyzed reaction class and substrate specificity (functional inference + direct substrate assays)

Reaction class: Like other PDI-family oxidoreductases, Eug1p participates in thiol–disulfide exchange, which in principle can catalyze oxidation/reduction/isomerization of disulfide bonds in ER client proteins (suzuki2015redoxdiversityin pages 1-2).

Substrate-level evidence: Several experiments use the secretory pathway substrate procarboxypeptidase Y (proCPY/CPY) to probe PDI-family function in vivo and in vitro. In deletion/overexpression backgrounds, loss of PDI homologues slows CPY maturation (xiao2004thecontributionsof pages 5-7, xiao2004thecontributionsof media f566842d). In biochemical assays, engineered Eug1p variants (see below) catalyze oxidative refolding and disulfide reshuffling of proCPY (nørgaard2001mutationofyeast pages 6-6, nørgaard2001mutationofyeast pages 4-6). These experiments provide the most direct “substrate specificity” evidence available in the retrieved corpus: Eug1p-related activity is demonstrated on a complex secretory cargo (proCPY) rather than a single defined peptide substrate (nørgaard2001mutationofyeast pages 4-6).

2.3 Wild-type Eug1p has weak oxidoreductase/isomerase activity, but detectable chaperone-like activity

Multiple sources converge on the conclusion that wild-type Eug1p is a weak oxidoreductase/isomerase in standard PDI assays:
* A study of yeast PDI family functional differences emphasizes that Eug1p contains CXXS motifs and that Eug1p “alone is unable to carry oxidizing equivalents,” consistent with limited oxidase capacity (nørgaard2001functionaldifferencesin pages 2-2).
* A biochemical study concludes that “wild-type Eug1p is a poor isomerase” and that wild-type Eug1p has only a small signal in an insulin reduction assay and does not improve oxidative refolding of proCPY under the tested conditions (nørgaard2001mutationofyeast pages 4-6).
* A comparative analysis reports that isomerase activities of yeast PDI-family proteins including Eug1p were “extremely low,” while also indicating that (except for Mpd1p) PDI-family proteins retain chaperone activity (kimura2004functionaldifferencesbetween pages 1-2).

In contrast to weak oxidoreductase activity, an ER-quality-control role via binding/anti-aggregation (chaperone-like) function is supported by in vitro chaperone metrics: Eug1p exhibited measurable chaperone activity with a reported parameter KD = 4.21×10^-4 M in the referenced assay context (vala2008characterizationoferv2p pages 58-61).

2.4 Active-site engineering demonstrates causality of the CXXS motif

A key mechanistic demonstration is that converting Eug1p active sites from CXXS → CXXC greatly increases PDI-like function:
* Mutation of Eug1p CXXS active sites to CXXC caused a “dramatic increase” in PDI activity; the engineered form gained oxidase/isomerase activity on proCPY-related substrates (including a GS-proCPY assay where wild-type Eug1p showed no activity) (nørgaard2001mutationofyeast pages 6-6).
* Quantitatively, the engineered Eug1pCXXC-CXXC reached approximately 30–50% of native yeast Pdi1p activity in the study’s assays (nørgaard2001mutationofyeast pages 6-6).
* In proCPY refolding kinetics, the authors reported proCPY has 11 free thiols when fully reduced, decreasing rapidly with a plateau around 1.5–2 thiols per proCPY after ~20–30 minutes; wild-type Eug1p did not affect the refolding rate/yield under those test conditions, while CXXC mutants shortened the lag phase and enhanced folding (nørgaard2001mutationofyeast pages 4-6).

Collectively, these results support the interpretation that Eug1p’s primary physiological contribution is likely not bulk oxidation, and that its atypical active sites may tune it toward noncanonical roles (e.g., assisting folding via binding or specialized redox tasks) rather than being a major disulfide oxidase (nørgaard2001mutationofyeast pages 4-6, nørgaard2001functionaldifferencesin pages 2-2).

3) Cellular localization and pathway context

3.1 ER localization and retention

Eug1p is described as an ER-resident glycoprotein with an N-terminal signal sequence and a C-terminal HDEL ER retention signal, consistent with ER luminal residency (vala2008characterizationoferv2p pages 58-61). This matches broader genetic/functional categorization of EUG1 as one of the yeast ER PDI-family homologues (xiao2004thecontributionsof pages 2-2).

3.2 Role within ER oxidative folding/UPR network

Expression of PDI1 and ER PDI homologues is described as regulated by the unfolded protein response (UPR), and PDI homologues can be upregulated when PDI activity is defective—placing EUG1 within ER stress adaptation/proteostasis circuits (xiao2004thecontributionsof pages 5-7). Functional overlap among ER PDI-family members is also supported by the ability of ER homologues (including EUG1) to rescue a pdi1 mutation when overexpressed (xiao2004thecontributionsof pages 2-2).

4) Genetics, phenotypes, and mechanistic interpretation

4.1 Essentiality and redundancy

In yeast, PDI1 is essential, while EUG1 is nonessential under standard growth conditions (nørgaard2001functionaldifferencesin pages 1-2, vala2008characterizationoferv2p pages 58-61). Nonetheless, EUG1 can participate in partial compensation:
* Overexpressed homologues (EUG1/MPD1/MPD2) can restore viability to a pdi1-deleted strain, but such suppression often requires low endogenous levels of other homologues and is not fully interchangeable (nørgaard2001functionaldifferencesin pages 1-2).
* Specifically, suppression of pdi1 deletion by EUG1 requires endogenous homologues with CXXC motifs, consistent with Eug1p’s inability to provide oxidation alone (nørgaard2001functionaldifferencesin pages 1-2).

4.2 Folding phenotypes: CPY maturation

Across multiple studies, the folding/maturation of secretory cargo is a sensitive readout of PDI-family function:
* In vivo, CPY maturation can become “extremely slow” in backgrounds lacking supportive PDI-homologue activity under certain conditions (xiao2004thecontributionsof pages 5-7).
* A retrieved figure/table from Xiao et al. (2004) provides pulse–chase evidence and half-time quantification for CPY maturation across mutant backgrounds that alter PDI-family capacity (xiao2004thecontributionsof media f566842d, xiao2004thecontributionsof media a580a63e).
* In another report, cells lacking EUG1 were viable but showed a slight vacuolar sorting defect for soluble vacuolar proteins including CPY; overexpression of EUG1 in a pdi1Δ strain permitted growth but did not correct proCPY accumulation, implying incomplete functional overlap with Pdi1p (vala2008characterizationoferv2p pages 58-61).

4.3 ERAD (ER-associated degradation)

Despite strong effects on folding and glycan modification in multiple deletion combinations, one study reports no significant effects on ER-associated degradation (ERAD) across the PDI-deleted strains tested, suggesting that (in that experimental space) PDI-family contributions are more critical for productive folding than for bulk ERAD flux (nørgaard2001functionaldifferencesin pages 1-2).

4.4 Other phenotypes and quantitative data

Beyond secretion/folding readouts:
* Deletion of EUG1 was associated with a reported ~13% decrease in replicative lifespan in one study that surveyed thiol oxidoreductases (hacioglu2010therolesof pages 3-4).

5) Protein–protein interactions (PPIs) and functional networks

5.1 Biochemical interaction evidence

In vitro binding evidence supports interaction between Eug1p and other ER PDI-like proteins:
* Eug1p binds Eps1p with reported KD = 6.06×10^-6 M (vala2008characterizationoferv2p pages 58-61).
* Functional cooperation was suggested by an observation that mixtures of Eps1p + Eug1p enhanced reductive activity in the cited assay context (reported as 122% in the excerpt) (vala2008characterizationoferv2p pages 58-61).

5.2 Recent development (2024): in situ ER PPI mapping (YST-PPI)

A 2024 bioRxiv preprint introduces YST-PPI, an in situ ER-resident PPI mapping approach using split-fast TEV protease, ER retention signals, and a surface-display cleavage readout quantified by flow cytometry (fan2024characterizinginteractionsof pages 1-4, fan2024characterizinginteractionsof pages 13-17). The authors tested 15 ER resident proteins (including Eug1p) and report a network with >74 interacting pairs above a >10% normalized interaction score threshold, with overall score ranges roughly 1–93% (fan2024characterizinginteractionsof pages 1-4, fan2024characterizinginteractionsof pages 7-10).

Within the subset of interactions validated against BioGRID/STRING, the study lists multiple Eug1p interaction partners, including Sil1p, Yos9p, Scj1p, Cpr5p, Mpd1p, Mpd2p, Kre5p, and interactions among PDI-family members (e.g., Pdi1p–Eug1p) (fan2024characterizinginteractionsof pages 10-13). A specifically mentioned Eug1p interaction score example is Eug1p–Scj1p = 5% (fan2024characterizinginteractionsof pages 10-13). This 2024 dataset contributes an updated view of Eug1p’s ER interaction neighborhood, though it is preprint (not yet peer reviewed) and provides limited mechanistic detail per edge in the extracted snippets (fan2024characterizinginteractionsof pages 10-13).

6) Current applications and real-world implementations

Direct “EUG1-specific” engineering examples were limited in the retrieved evidence. However, authoritative yeast biomanufacturing literature strongly supports manipulating ER folding and disulfide-handling capacity (PDI/chaperones/oxidases) as a practical strategy to improve recombinant secretion in S. cerevisiae—a context in which EUG1 is part of the endogenous ER folding-factor repertoire.

A highly cited review on metabolic engineering of secretion reports:
* Overexpression of ER chaperones and folding catalysts such as Kar2p and PDI often improves secretion of heterologous proteins, and Kar2p/PDI cooperativity can increase secretion for some clients (e.g., scFv and β-glucosidase examples described) (hou2012metabolicengineeringof pages 10-11).
* Maintaining/engineering disulfide bonds can substantially affect yields: removal of IGF1 cysteines reduced expression by about one-third, and loss of a core disulfide in CD47 reduced expression level and affinity by ~30% (hou2012metabolicengineeringof pages 9-10).
* Broader strain and pathway engineering (including screens connected to ER oxidation/folding machinery) can yield large improvements, including reported ~15-fold and up to ~70-fold secretion improvements in selected/engineered contexts (hou2012metabolicengineeringof pages 11-12).

These real-world findings imply that, while Pdi1p is the primary essential ER oxidoreductase, the broader PDI-family system (including homologues like Eug1p that may contribute binding/isomerase-like capacity or specialized functions) is a relevant target space when tuning ER proteostasis for production (hou2012metabolicengineeringof pages 10-11, xiao2004thecontributionsof pages 2-2).

7) Expert analysis and synthesis

7.1 What is Eug1p’s “primary function” given the evidence?

The strongest, most Eug1p-specific mechanistic conclusion supported by the retrieved literature is:
* Wild-type Eug1p is an ER luminal PDI-family protein whose unusual CXXS active sites severely limit classical PDI oxidase/isomerase activity, and therefore Eug1p is unlikely to be a major provider of oxidizing equivalents for bulk disulfide formation in yeast (nørgaard2001functionaldifferencesin pages 2-2, nørgaard2001mutationofyeast pages 4-6).
* Eug1p instead appears to contribute through auxiliary ER folding functions, potentially including substrate binding/chaperone activity and/or specialized redox roles that do not require a canonical CXXC active site, consistent with measurable chaperone activity and weak oxidoreductase activity (vala2008characterizationoferv2p pages 58-61, kimura2004functionaldifferencesbetween pages 1-2).
* The fact that CXXS→CXXC engineering converts Eug1p into a much more active PDI strongly argues that Eug1p’s native motif is a functional “design choice” rather than an annotation artifact, and that its physiological role may be tuned away from strong oxidase chemistry (nørgaard2001mutationofyeast pages 6-6, nørgaard2001mutationofyeast pages 4-6).

7.2 Relationship to UPR/quality control and interactions

EUG1 is embedded in ER proteostasis through UPR co-regulation with other PDI homologues (xiao2004thecontributionsof pages 5-7), genetic redundancy/conditional suppression behavior with other PDI homologues (nørgaard2001functionaldifferencesin pages 1-2), and a growing interaction network that includes ER chaperones/cochaperones and quality-control proteins (e.g., Sil1p, Yos9p, Scj1p) observed in the 2024 YST-PPI mapping (fan2024characterizinginteractionsof pages 10-13, fan2024characterizinginteractionsof pages 1-4). This supports the view that Eug1p’s contribution may be best interpreted at the level of ER network function rather than a single high-turnover enzymatic role.

8) Limitations and recency

The retrieval yielded one clear 2024 Eug1p-relevant source (Fan et al., 2024 bioRxiv) that contributes novel interaction mapping methodology and an ER PPI neighborhood including Eug1p (fan2024characterizinginteractionsof pages 10-13, fan2024characterizinginteractionsof pages 1-4). However, peer-reviewed 2023–2024 Eug1p-specific primary literature was not retrieved in this run, so “latest research” emphasis is necessarily weighted toward (i) foundational functional genetics/biochemistry (2001–2004), (ii) mechanistic review context (2015), and (iii) a 2024 preprint for interaction mapping (nørgaard2001functionaldifferencesin pages 1-2, nørgaard2001mutationofyeast pages 4-6, suzuki2015redoxdiversityin pages 1-2, fan2024characterizinginteractionsof pages 10-13).

Evidence summary table

Table: This table summarizes identity, biochemical function, localization, genetics, phenotypes, and interaction evidence for Saccharomyces cerevisiae EUG1/Eug1p using only evidence retrieved in the conversation. It is useful as a compact evidence map linking each major claim to specific context IDs and source citations.

Key figure/table evidence (visual)

Xiao et al. (2004) Table I and Figure 5 provide visual evidence for growth phenotypes across PDI-family deletion backgrounds and CPY maturation pulse–chase/half-time quantification (xiao2004thecontributionsof media f566842d, xiao2004thecontributionsof media a580a63e).

Selected bibliography (with URLs and publication dates)

• Fan X. et al. Characterizing interactions of ER resident proteins in situ through the YST-PPI method. bioRxiv (posted May 21, 2024). https://doi.org/10.1101/2024.05.21.594841 (fan2024characterizinginteractionsof pages 1-4, fan2024characterizinginteractionsof pages 10-13)
• Xiao R. et al. The Contributions of Protein Disulfide Isomerase and Its Homologues to Oxidative Protein Folding in the Yeast Endoplasmic Reticulum. J Biol Chem (Nov 2004). https://doi.org/10.1074/jbc.m409210200 (xiao2004thecontributionsof pages 1-2, xiao2004thecontributionsof pages 5-7)
• Nørgaard P. et al. Functional Differences in Yeast Protein Disulfide Isomerases. J Cell Biol (Feb 2001). https://doi.org/10.1083/jcb.152.3.553 (nørgaard2001functionaldifferencesin pages 1-2, nørgaard2001functionaldifferencesin pages 2-2)
• Nørgaard P., Winther J.R. Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J (Aug 2001). https://doi.org/10.1042/bj3580269 (nørgaard2001mutationofyeast pages 6-6, nørgaard2001mutationofyeast pages 4-6)
• Kimura T. et al. Functional differences between human and yeast protein disulfide isomerase family proteins. BBRC (Jul 2004). https://doi.org/10.1016/j.bbrc.2004.05.178 (kimura2004functionaldifferencesbetween pages 1-2)
• Suzuki Y., Schmitt M.J. Redox diversity in ERAD-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle. Biological Chemistry (May 2015). https://doi.org/10.1515/hsz-2014-0299 (suzuki2015redoxdiversityin pages 1-2)
• Hou J. et al. Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae. FEMS Yeast Research (Aug 2012). https://doi.org/10.1111/j.1567-1364.2012.00810.x (hou2012metabolicengineeringof pages 9-10, hou2012metabolicengineeringof pages 10-11, hou2012metabolicengineeringof pages 11-12)

References

1. (suzuki2015redoxdiversityin pages 1-2): Yutaka Suzuki and Manfred J. Schmitt. Redox diversity in erad-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle. Biological Chemistry, 396:539-554, May 2015. URL: https://doi.org/10.1515/hsz-2014-0299, doi:10.1515/hsz-2014-0299. This article has 11 citations and is from a peer-reviewed journal.

2. (xiao2004thecontributionsof pages 2-2): Ruoyu Xiao, Bonney Wilkinson, Anton Solovyov, Jakob R. Winther, Arne Holmgren, Johanna Lundström-Ljung, and Hiram F. Gilbert. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum*. Journal of Biological Chemistry, 279:49780-49786, Nov 2004. URL: https://doi.org/10.1074/jbc.m409210200, doi:10.1074/jbc.m409210200. This article has 87 citations and is from a domain leading peer-reviewed journal.

3. (nørgaard2001functionaldifferencesin pages 2-2): Per Nørgaard, Vibeke Westphal, Christine Tachibana, Lene Alsøe, Bjørn Holst, and Jakob R. Winther. Functional differences in yeast protein disulfide isomerases. The Journal of Cell Biology, 152:553-562, Feb 2001. URL: https://doi.org/10.1083/jcb.152.3.553, doi:10.1083/jcb.152.3.553. This article has 171 citations.

4. (beynonjones2006mutationalanalysisof pages 1-2): Siân M. Beynon-Jones, Antony N. Antoniou, and Simon J. Powis. Mutational analysis of the oxidoreductase erp57 reveals the importance of the two central residues in the redox motif. FEBS Letters, 580:1897-1902, Mar 2006. URL: https://doi.org/10.1016/j.febslet.2006.02.055, doi:10.1016/j.febslet.2006.02.055. This article has 14 citations and is from a peer-reviewed journal.

5. (nørgaard2001functionaldifferencesin pages 1-2): Per Nørgaard, Vibeke Westphal, Christine Tachibana, Lene Alsøe, Bjørn Holst, and Jakob R. Winther. Functional differences in yeast protein disulfide isomerases. The Journal of Cell Biology, 152:553-562, Feb 2001. URL: https://doi.org/10.1083/jcb.152.3.553, doi:10.1083/jcb.152.3.553. This article has 171 citations.

6. (hacioglu2010therolesof pages 3-4): Elise Hacioglu, Isil Esmer, Dmitri E. Fomenko, Vadim N. Gladyshev, and Ahmet Koc. The roles of thiol oxidoreductases in yeast replicative aging. Mechanisms of Ageing and Development, 131:692-699, Nov 2010. URL: https://doi.org/10.1016/j.mad.2010.09.006, doi:10.1016/j.mad.2010.09.006. This article has 15 citations and is from a peer-reviewed journal.

7. (xiao2004thecontributionsof pages 5-7): Ruoyu Xiao, Bonney Wilkinson, Anton Solovyov, Jakob R. Winther, Arne Holmgren, Johanna Lundström-Ljung, and Hiram F. Gilbert. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum*. Journal of Biological Chemistry, 279:49780-49786, Nov 2004. URL: https://doi.org/10.1074/jbc.m409210200, doi:10.1074/jbc.m409210200. This article has 87 citations and is from a domain leading peer-reviewed journal.

8. (xiao2004thecontributionsof media f566842d): Ruoyu Xiao, Bonney Wilkinson, Anton Solovyov, Jakob R. Winther, Arne Holmgren, Johanna Lundström-Ljung, and Hiram F. Gilbert. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum*. Journal of Biological Chemistry, 279:49780-49786, Nov 2004. URL: https://doi.org/10.1074/jbc.m409210200, doi:10.1074/jbc.m409210200. This article has 87 citations and is from a domain leading peer-reviewed journal.

9. (nørgaard2001mutationofyeast pages 6-6): Per NØRGAARD and Jakob R. WINTHER. Mutation of yeast eug1p cxxs active sites to cxxc results in a dramatic increase in protein disulphide isomerase activity. The Biochemical journal, 358 Pt 1:269-74, Aug 2001. URL: https://doi.org/10.1042/bj3580269, doi:10.1042/bj3580269. This article has 47 citations.

10. (nørgaard2001mutationofyeast pages 4-6): Per NØRGAARD and Jakob R. WINTHER. Mutation of yeast eug1p cxxs active sites to cxxc results in a dramatic increase in protein disulphide isomerase activity. The Biochemical journal, 358 Pt 1:269-74, Aug 2001. URL: https://doi.org/10.1042/bj3580269, doi:10.1042/bj3580269. This article has 47 citations.

11. (kimura2004functionaldifferencesbetween pages 1-2): Taiji Kimura, Yasuhiro Hosoda, Yukiko Kitamura, Hideshi Nakamura, Tomohisa Horibe, and Masakazu Kikuchi. Functional differences between human and yeast protein disulfide isomerase family proteins. Biochemical and biophysical research communications, 320 2:359-65, Jul 2004. URL: https://doi.org/10.1016/j.bbrc.2004.05.178, doi:10.1016/j.bbrc.2004.05.178. This article has 30 citations and is from a peer-reviewed journal.

12. (vala2008characterizationoferv2p pages 58-61): ALL Vala. Characterization of erv2p and pdi1p, two thiol oxidoreductases involved in protein disulfide bond formation in the endoplasmic reticulum of saccharomyces cerevisiae. Unknown journal, 2008.

13. (xiao2004thecontributionsof media a580a63e): Ruoyu Xiao, Bonney Wilkinson, Anton Solovyov, Jakob R. Winther, Arne Holmgren, Johanna Lundström-Ljung, and Hiram F. Gilbert. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum*. Journal of Biological Chemistry, 279:49780-49786, Nov 2004. URL: https://doi.org/10.1074/jbc.m409210200, doi:10.1074/jbc.m409210200. This article has 87 citations and is from a domain leading peer-reviewed journal.

14. (fan2024characterizinginteractionsof pages 1-4): Xian Fan, Huahua He, Ting Wang, Pan Xu, Faying Zhang, Shantong Hu, Yueli Yun, Meng Mei, Guimin Zhang, and Li Yi. Characterizing interactions of er resident proteins in situ through the yst-ppi method. bioRxiv, May 2024. URL: https://doi.org/10.1101/2024.05.21.594841, doi:10.1101/2024.05.21.594841. This article has 0 citations.

15. (fan2024characterizinginteractionsof pages 13-17): Xian Fan, Huahua He, Ting Wang, Pan Xu, Faying Zhang, Shantong Hu, Yueli Yun, Meng Mei, Guimin Zhang, and Li Yi. Characterizing interactions of er resident proteins in situ through the yst-ppi method. bioRxiv, May 2024. URL: https://doi.org/10.1101/2024.05.21.594841, doi:10.1101/2024.05.21.594841. This article has 0 citations.

16. (fan2024characterizinginteractionsof pages 7-10): Xian Fan, Huahua He, Ting Wang, Pan Xu, Faying Zhang, Shantong Hu, Yueli Yun, Meng Mei, Guimin Zhang, and Li Yi. Characterizing interactions of er resident proteins in situ through the yst-ppi method. bioRxiv, May 2024. URL: https://doi.org/10.1101/2024.05.21.594841, doi:10.1101/2024.05.21.594841. This article has 0 citations.

17. (fan2024characterizinginteractionsof pages 10-13): Xian Fan, Huahua He, Ting Wang, Pan Xu, Faying Zhang, Shantong Hu, Yueli Yun, Meng Mei, Guimin Zhang, and Li Yi. Characterizing interactions of er resident proteins in situ through the yst-ppi method. bioRxiv, May 2024. URL: https://doi.org/10.1101/2024.05.21.594841, doi:10.1101/2024.05.21.594841. This article has 0 citations.

18. (hou2012metabolicengineeringof pages 10-11): Jin Hou, Keith E.J. Tyo, Zihe Liu, Dina Petranovic, and Jens Nielsen. Metabolic engineering of recombinant protein secretion by saccharomyces cerevisiae. FEMS yeast research, 12 5:491-510, Aug 2012. URL: https://doi.org/10.1111/j.1567-1364.2012.00810.x, doi:10.1111/j.1567-1364.2012.00810.x. This article has 292 citations and is from a peer-reviewed journal.

19. (hou2012metabolicengineeringof pages 9-10): Jin Hou, Keith E.J. Tyo, Zihe Liu, Dina Petranovic, and Jens Nielsen. Metabolic engineering of recombinant protein secretion by saccharomyces cerevisiae. FEMS yeast research, 12 5:491-510, Aug 2012. URL: https://doi.org/10.1111/j.1567-1364.2012.00810.x, doi:10.1111/j.1567-1364.2012.00810.x. This article has 292 citations and is from a peer-reviewed journal.

20. (hou2012metabolicengineeringof pages 11-12): Jin Hou, Keith E.J. Tyo, Zihe Liu, Dina Petranovic, and Jens Nielsen. Metabolic engineering of recombinant protein secretion by saccharomyces cerevisiae. FEMS yeast research, 12 5:491-510, Aug 2012. URL: https://doi.org/10.1111/j.1567-1364.2012.00810.x, doi:10.1111/j.1567-1364.2012.00810.x. This article has 292 citations and is from a peer-reviewed journal.

21. (xiao2004thecontributionsof pages 1-2): Ruoyu Xiao, Bonney Wilkinson, Anton Solovyov, Jakob R. Winther, Arne Holmgren, Johanna Lundström-Ljung, and Hiram F. Gilbert. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum*. Journal of Biological Chemistry, 279:49780-49786, Nov 2004. URL: https://doi.org/10.1074/jbc.m409210200, doi:10.1074/jbc.m409210200. This article has 87 citations and is from a domain leading peer-reviewed journal.

Citations

1. suzuki2015redoxdiversityin pages 1-2
2. beynonjones2006mutationalanalysisof pages 1-2
3. hacioglu2010therolesof pages 3-4
4. kimura2004functionaldifferencesbetween pages 1-2
5. xiao2004thecontributionsof pages 2-2
6. xiao2004thecontributionsof pages 5-7
7. fan2024characterizinginteractionsof pages 10-13
8. hou2012metabolicengineeringof pages 10-11
9. hou2012metabolicengineeringof pages 9-10
10. hou2012metabolicengineeringof pages 11-12
11. xiao2004thecontributionsof pages 1-2
12. fan2024characterizinginteractionsof pages 1-4
13. fan2024characterizinginteractionsof pages 13-17
14. fan2024characterizinginteractionsof pages 7-10
15. https://doi.org/10.1083/jcb.152.3.553
16. https://doi.org/10.1074/jbc.m409210200
17. https://doi.org/10.1016/j.febslet.2006.02.055
18. https://doi.org/10.1016/j.mad.2010.09.006
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