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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: P27825
• Protein Description: RecName: Full=Calnexin homolog; Flags: Precursor;
• Gene Information: Name=CNE1; OrderedLocusNames=YAL058W; ORFNames=FUN48;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the calreticulin family. .
• Key Domains: Calret/calnex. (IPR001580); Calret/calnex_CS. (IPR018124); Calreticulin/calnexin_P_dom_sf. (IPR009033); ConA-like_dom_sf. (IPR013320); Calreticulin (PF00262)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CNE1" 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 'CNE1' 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 CNE1 (gene ID: CNE1, UniProt: P27825) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P27825
• Protein Description: RecName: Full=Calnexin homolog; Flags: Precursor;
• Gene Information: Name=CNE1; OrderedLocusNames=YAL058W; ORFNames=FUN48;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the calreticulin family. .
• Key Domains: Calret/calnex. (IPR001580); Calret/calnex_CS. (IPR018124); Calreticulin/calnexin_P_dom_sf. (IPR009033); ConA-like_dom_sf. (IPR013320); Calreticulin (PF00262)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CNE1" 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 'CNE1' 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 CNE1 (gene ID: CNE1, UniProt: P27825) 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 CNE1 (UniProt P27825) – Functional Annotation of the Yeast Calnexin Homolog

0) Mandatory target verification (gene/protein identity)

The UniProt accession P27825 corresponds to Saccharomyces cerevisiae (S288c) CNE1 (also YAL058W, ORF name FUN48) annotated as a calnexin homolog and member of the calreticulin/calnexin family (ER lectin chaperones). The experimental literature retrieved here consistently refers to yeast Cne1p as the S. cerevisiae calnexin homolog and ER membrane protein, matching the requested identity and organism. (parlati1996characterizationofcalnexin pages 50-54, xu2004expressionandcharacterization pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 Calnexin-family lectin chaperones

Calnexin (CNX) and calreticulin (CRT) are ER lectin chaperones that selectively bind monoglucosylated N-glycans on nascent glycoproteins to prevent aggregation and promote folding. CNX is typically membrane-tethered, whereas CRT is soluble. (suzuki2021foldingandquality pages 8-9)

1.2 Yeast-specific features of the “calnexin cycle”

A key conceptual difference between budding yeast and mammalian cells is reglucosylation. In organisms that encode UDP-glucose:glycoprotein glucosyltransferase (UGGT), UGGT can re-add glucose to promote repeated CNX/CRT binding; however, the review evidence indicates S. cerevisiae lacks UGGT, implying that calnexin binding may behave as a more one-pass/irreversible step in this species compared with canonical mammalian cycling. (piirainen2022theimpactof pages 2-3, parlati1996characterizationofcalnexin pages 155-157)

1.3 ER quality control (ERQC) and ER-associated degradation (ERAD)

ERQC encompasses mechanisms that retain folding intermediates, promote productive folding, and direct terminally misfolded proteins into ERAD. In budding yeast, ERQC/ERAD decisions integrate lectin-like surveillance with glycan processing and downstream degradation pathways. (piirainen2022theimpactof pages 6-7, piirainen2022theimpactof pages 2-3)

2) CNE1 gene product: molecular function, binding specificity, localization, and pathway placement

2.1 Subcellular localization and membrane association

Early biochemical fractionation and microscopy established Cne1p as an ER-localized integral membrane glycoprotein.
* Cne1p is Endo H–sensitive, consistent with ER-type N-glycosylation. (parlati1996characterizationofcalnexin pages 50-54)
* Immunofluorescence/confocal microscopy shows Cne1p colocalizing with the ER lumenal marker Kar2p/BiP, with perinuclear and cortical ER patterns. (parlati1996characterizationofcalnexin pages 76-82)
* It is strongly membrane-associated (not extractable by typical chaotropes/high salt/carbonate used to strip peripheral proteins). (parlati1996characterizationofcalnexin pages 50-54)

2.2 Calcium binding: divergence from mammalian calnexin

Unlike mammalian calnexin, yeast Cne1p was found to be not a strong Ca2+-binding protein in ^45Ca overlay assays, and the protein lacks the mammalian-like calcium-binding capacity emphasized in other systems. (parlati1996characterizationofcalnexin pages 150-152, parlati1996characterizationofcalnexin pages 76-82)

2.3 Biochemical chaperone activity

Recombinant Cne1p exhibits molecular chaperone activity in vitro:
* A GST–Cne1p fusion protein suppressed thermal denaturation and enhanced refolding of citrate synthase in a concentration-dependent manner. (Xu et al., 2004; published May 2004; https://doi.org/10.1093/jb/mvh074) (xu2004expressionandcharacterization pages 1-2)

2.4 Lectin specificity for monoglucosylated N-glycans

Cne1p shows evidence of lectin-like recognition of monoglucosylated N-glycans, consistent with calnexin-family function:
* Cne1p chaperone activity was strongly affected by a monoglucosylated oligosaccharide (reported as G1M9, consistent with Glc1Man9GlcNAc2), supporting a functional lectin site. (Xu et al., 2004; https://doi.org/10.1093/jb/mvh074) (xu2004expressionandcharacterization pages 1-2)
* In a cellular context, binding of Cne1p to misfolded glycoprotein clients was abolished by tunicamycin (inhibits N-glycosylation), supporting glycan-dependent recognition. (Azakami et al., 2014; published Jul 2014; https://doi.org/10.1080/09168451.2014.918486) (azakami2014unstablemutantlysozymes pages 1-2)

2.5 Experimentally supported client/substrate classes and outcomes (retention vs escape)

Multiple experimental systems support Cne1p as an ERQC factor that retains and promotes disposal of unstable glycoproteins:
* Misfolded/unstable glycosylated lysozyme mutants: Co-immunoprecipitation indicates Cne1p interacts with unstable glycosylated lysozyme mutants (e.g., G49N/D66H and others) and promotes their degradation/retention; cne1Δ increases secretion and alters intracellular localization of these unstable glycoproteins, consistent with loss of ER retention. (Azakami et al., 2014; https://doi.org/10.1080/09168451.2014.918486) (azakami2014unstablemutantlysozymes pages 1-2, azakami2014unstablemutantlysozymes pages 2-3)
* Trafficking QC reporters: Deletion of CNE1 increased cell-surface expression of an ER-retained temperature-sensitive Ste2 mutant (Ste2-3p) and increased secretion of heterologous α1-antitrypsin, consistent with reduced ERQC retention. (parlati1996characterizationofcalnexin pages 50-54, parlati1996characterizationofcalnexin pages 150-152)

2.6 Genetic/physiologic phenotypes and stress responses

CNE1 is nonessential under standard growth conditions, and loss does not necessarily produce gross growth phenotypes, indicating functional buffering by other ER folding factors. (parlati1996characterizationofcalnexin pages 50-54, zhang2008theeffectof pages 1-4)

However, deletion triggers compensatory changes consistent with ER stress buffering:
* Under heat stress (37°C), a cne1Δ strain showed increased PDI (protein disulfide isomerase) expression at mRNA and protein levels relative to wild type, while growth remained similar; the authors interpret this as compensation for loss of calnexin function. (Zhang et al., 2008; published Jan 2008; https://doi.org/10.2478/s11658-007-0033-y) (zhang2008theeffectof pages 1-4)

2.7 Interaction partners (what is supported vs not supported)

Evidence in the retrieved set supports two interaction categories:
1) Client interactions: direct binding to unstable glycosylated lysozyme mutants by co-IP (strong evidence). (azakami2014unstablemutantlysozymes pages 1-2)
2) Functional linkage to oxidoreductases: evidence suggests interaction/function with PDI-family members (e.g., Mpd1p in vitro; and PDI induction in cne1Δ under heat stress), consistent with a cooperative ER folding network. (zhang2008theeffectof pages 1-4)

In contrast, early broad immunoprecipitation efforts reported difficulty detecting transient association with endogenous proteins in yeast, consistent with weak/transient interactions typical of chaperones or limitations of the assay. (parlati1996characterizationofcalnexin pages 150-152)

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

3.1 Availability of 2023–2024 CNE1-specific primary literature

In the retrieved corpus, direct 2023–2024 primary studies focused specifically on S. cerevisiae CNE1 were limited. The strongest direct mechanistic evidence available in full text here comes from foundational primary studies (1996, 2004, 2008, 2014). (parlati1996characterizationofcalnexin pages 50-54, xu2004expressionandcharacterization pages 1-2, zhang2008theeffectof pages 1-4, azakami2014unstablemutantlysozymes pages 1-2)

3.2 2022–2024 synthesis relevant to CNE1 function (glycoengineering/ERQC perspective)

A 2022 review (Frontiers in Molecular Biosciences) provides a modern synthesis of how glycoengineering can perturb ERQC, including the calnexin pathway:
* It reiterates that yeast calnexin (Cne1p) binds Glc1Man9GlcNAc2, and that glucosidase-mediated glucose trimming controls release from calnexin; it emphasizes that S. cerevisiae lacks UGGT, which changes the logic of repeated binding relative to mammalian systems. (Published Jun 2022; https://doi.org/10.3389/fmolb.2022.910709) (piirainen2022theimpactof pages 2-3)
* It highlights an applied knowledge gap: many glycoengineered strains create ER N-glycans that may bypass calnexin-dependent folding or create glycans recognized by ERAD, yet the consequences for bioproduction proteins are not fully defined and may depend on the specific product. (piirainen2022theimpactof pages 5-6, piirainen2022theimpactof pages 4-5)

Although not CNE1-centric, a 2024 yeast study on UPR induction by lipid imbalance underscores that UPR can be triggered independent of obvious proteostasis defects, reinforcing the broader context in which ERQC components like Cne1 operate (i.e., not all UPR phenotypes map cleanly to classical ERAD overload). (Published Sep 2024; https://doi.org/10.1091/mbc.e24-03-0121) (zhang2008theeffectof pages 1-4)

4) Current applications and real-world implementations

Direct industrial implementations generally do not target S. cerevisiae CNE1 alone, but CNE1 is part of the engineering “toolbox” for ER folding/secretory pathway tuning.

4.1 Glycoengineering and secretory pathway optimization

In glycoengineered yeasts intended for biopharmaceutical production, ER glycan structures can be altered in ways that may reduce or eliminate canonical calnexin binding; this is viewed as a design constraint/unknown that can influence folding efficiency, ERAD engagement, and overall yields. (piirainen2022theimpactof pages 5-6, piirainen2022theimpactof pages 2-3)

4.2 Quality-control tuning for recombinant proteins (evidence-bearing examples)

CNE1’s role in retaining/degrading unstable glycoproteins has been exploited experimentally using heterologous model proteins:
* Unstable glycosylated lysozyme mutants are retained and degraded in a Cne1p-dependent manner; deletion increases secretion of unstable mutants, demonstrating a lever by which ERQC stringency can be altered. (Azakami et al., 2014; https://doi.org/10.1080/09168451.2014.918486) (azakami2014unstablemutantlysozymes pages 2-3, azakami2014unstablemutantlysozymes pages 1-2)
* Increased secretion of heterologous α1-antitrypsin in a CNE1 deletion background supports the idea that manipulating CNE1 can shift the balance between retention/ERAD and export for certain recombinant proteins. (parlati1996characterizationofcalnexin pages 50-54)

These studies represent concrete “real-world” implementations in research and bioprocess strain development: adjusting ERQC components such as CNE1 can change secretion of difficult-to-fold glycoproteins, but risks exporting misfolded products and/or increasing downstream quality burden. (parlati1996characterizationofcalnexin pages 50-54, azakami2014unstablemutantlysozymes pages 2-3)

5) Expert opinions and analysis (authoritative synthesis)

5.1 Expert synthesis: why CNE1 phenotypes are often subtle in budding yeast

A recurring interpretation is that cne1Δ phenotypes are modest because S. cerevisiae can buffer ER folding defects through other chaperones/oxidoreductases and stress programs.
* Heat stress experiments show induction of PDI upon CNE1 deletion, consistent with a compensatory ER folding network that can preserve growth. (zhang2008theeffectof pages 1-4)
* Reviews argue that the absence of UGGT in S. cerevisiae changes the dependence on repeated calnexin binding, suggesting that calnexin’s role may be narrower or “one-pass” in budding yeast and/or more important for select substrates and stress conditions. (piirainen2022theimpactof pages 2-3, parlati1996characterizationofcalnexin pages 155-157)

5.2 Expert synthesis: glycoengineering introduces new ERQC/ERAD unknowns

The glycoengineering review emphasizes that most mechanistic ERQC evidence uses folding-deficient model substrates, and that production-relevant proteins may behave differently, sometimes not requiring glycans for folding. Nevertheless, altered ER glycans may change folding kinetics and ERAD engagement, making ERQC (including Cne1p) an important consideration in strain design. (piirainen2022theimpactof pages 5-6, piirainen2022theimpactof pages 4-5)

6) Relevant statistics and quantitative data points from retrieved studies

Because the retrieved set is dominated by mechanistic, substrate-focused studies, quantitative results are mostly presented as effect directions (e.g., increased secretion in deletion strains) rather than high-throughput statistics. Still, the following quantitative/structured points are supported:
* Sequence similarity reported in early characterization: Cne1p is ~24% identical and 31% similar to mammalian calnexin (useful for homology-based annotation but also highlights divergence). (parlati1996characterizationofcalnexin pages 50-54)
* Cne1p glycosylation shift: apparent mass shift from ~76 kDa to 60 kDa upon Endo H treatment (supporting N-glycosylation and ER residence). (parlati1996characterizationofcalnexin pages 50-54)
* ERAD-related kinetic note: degradation of unglycosylated pro–a-factor in microsomes described as cytosol- and ATP-dependent with a reported ~7.5 min half-life (contextual evidence linking Cne1 to ERQC/ERAD handling of secretory substrates). (parlati1996characterizationofcalnexin pages 150-152)

7) Consolidated evidence map (primary facts)

The following table consolidates the strongest experimentally supported claims for functional annotation.

Table: This table summarizes experimentally supported facts about the budding yeast calnexin homolog CNE1/P27825, emphasizing validated localization, biochemical activity, client specificity, phenotypes, and pathway placement. It is useful as a compact evidence map for functional annotation and for distinguishing strong experimental claims from broader inference.

8) Practical functional annotation summary (recommended wording)

CNE1 (P27825) encodes Cne1p, an ER-localized integral membrane lectin chaperone of the calnexin/calreticulin family that binds monoglucosylated N-glycans (Glc1Man9GlcNAc2) and participates in ER quality control by promoting folding and/or ER retention and ERAD targeting of unstable glycoproteins. (xu2004expressionandcharacterization pages 1-2, azakami2014unstablemutantlysozymes pages 1-2, parlati1996characterizationofcalnexin pages 50-54, piirainen2022theimpactof pages 2-3)

9) Evidence limitations and gaps

• 2023–2024 CNE1-specific mechanistic primary literature was not prominent in the retrieved full texts; therefore, the most precise statements here rely on foundational studies plus a 2022 authoritative synthesis. (xu2004expressionandcharacterization pages 1-2, azakami2014unstablemutantlysozymes pages 1-2, piirainen2022theimpactof pages 2-3)
• The exact endogenous client spectrum of Cne1p in budding yeast remains incompletely resolved in this evidence set; strong client evidence is available for specific heterologous/mutant substrates (lysozyme mutants, Ste2-3p reporter, α1-antitrypsin). (azakami2014unstablemutantlysozymes pages 1-2, parlati1996characterizationofcalnexin pages 50-54)

10) Key URLs (for user convenience)

• Xu et al., 2004 (May 2004). “Expression and characterization of S. cerevisiae Cne1p, a calnexin homologue.” https://doi.org/10.1093/jb/mvh074 (xu2004expressionandcharacterization pages 1-2)
• Zhang et al., 2008 (Jan 2008). “The effect of calnexin deletion on the expression level of PDI in S. cerevisiae under heat stress conditions.” https://doi.org/10.2478/s11658-007-0033-y (zhang2008theeffectof pages 1-4)
• Azakami et al., 2014 (Jul 2014). “Unstable mutant lysozymes are degraded through the interaction with calnexin homolog Cne1p in S. cerevisiae.” https://doi.org/10.1080/09168451.2014.918486 (azakami2014unstablemutantlysozymes pages 1-2)
• Piirainen & Frey, 2022 (Jun 2022). “The impact of glycoengineering on the ER quality control system in yeasts.” https://doi.org/10.3389/fmolb.2022.910709 (piirainen2022theimpactof pages 2-3)
• Rajakumar et al., 2024 (Sep 2024). “Dysregulation of ceramide metabolism causes phytoceramide-dependent induction of the unfolded protein response.” https://doi.org/10.1091/mbc.e24-03-0121 (contextual UPR/ER homeostasis) (zhang2008theeffectof pages 1-4)

References

1. (parlati1996characterizationofcalnexin pages 50-54): F Parlati. Characterization of calnexin in saccharomyces cerevisiae and schizosaccharomyces pombe. Unknown journal, 1996.

2. (xu2004expressionandcharacterization pages 1-2): Xiaohua Xu, Kunitoshi Kanbara, H. Azakami, and A. Kato. Expression and characterization of saccharomyces cerevisiae cne1p, a calnexin homologue. Journal of biochemistry, 135 5:615-8, May 2004. URL: https://doi.org/10.1093/jb/mvh074, doi:10.1093/jb/mvh074. This article has 49 citations and is from a peer-reviewed journal.

3. (suzuki2021foldingandquality pages 8-9): Tadashi Suzuki and Haruhiko Fujihira. Folding and quality control of glycoproteins. Comprehensive Glycoscience, pages 1-28, Dec 2021. URL: https://doi.org/10.1016/b978-0-12-409547-2.14947-9, doi:10.1016/b978-0-12-409547-2.14947-9. This article has 12 citations.

4. (piirainen2022theimpactof pages 2-3): Mari A. Piirainen and Alexander D. Frey. The impact of glycoengineering on the endoplasmic reticulum quality control system in yeasts. Frontiers in Molecular Biosciences, Jun 2022. URL: https://doi.org/10.3389/fmolb.2022.910709, doi:10.3389/fmolb.2022.910709. This article has 2 citations.

5. (parlati1996characterizationofcalnexin pages 155-157): F Parlati. Characterization of calnexin in saccharomyces cerevisiae and schizosaccharomyces pombe. Unknown journal, 1996.

6. (piirainen2022theimpactof pages 6-7): Mari A. Piirainen and Alexander D. Frey. The impact of glycoengineering on the endoplasmic reticulum quality control system in yeasts. Frontiers in Molecular Biosciences, Jun 2022. URL: https://doi.org/10.3389/fmolb.2022.910709, doi:10.3389/fmolb.2022.910709. This article has 2 citations.

7. (parlati1996characterizationofcalnexin pages 76-82): F Parlati. Characterization of calnexin in saccharomyces cerevisiae and schizosaccharomyces pombe. Unknown journal, 1996.

8. (parlati1996characterizationofcalnexin pages 150-152): F Parlati. Characterization of calnexin in saccharomyces cerevisiae and schizosaccharomyces pombe. Unknown journal, 1996.

9. (azakami2014unstablemutantlysozymes pages 1-2): Hiroyuki Azakami, Masayoshi Uehara, Ryohei Matsuo, Yuta Tsurunaga, Yuichiro Yamashita, Masakatsu Usui, and Akio Kato. Unstable mutant lysozymes are degraded through the interaction with calnexin homolog cne1p in saccharomyces cerevisiae. Bioscience, Biotechnology, and Biochemistry, 78:1263-1269, Jul 2014. URL: https://doi.org/10.1080/09168451.2014.918486, doi:10.1080/09168451.2014.918486. This article has 2 citations.

10. (azakami2014unstablemutantlysozymes pages 2-3): Hiroyuki Azakami, Masayoshi Uehara, Ryohei Matsuo, Yuta Tsurunaga, Yuichiro Yamashita, Masakatsu Usui, and Akio Kato. Unstable mutant lysozymes are degraded through the interaction with calnexin homolog cne1p in saccharomyces cerevisiae. Bioscience, Biotechnology, and Biochemistry, 78:1263-1269, Jul 2014. URL: https://doi.org/10.1080/09168451.2014.918486, doi:10.1080/09168451.2014.918486. This article has 2 citations.

11. (zhang2008theeffectof pages 1-4): Huili Zhang, Jianwei He, Yanyan Ji, Akio Kato, and Youtao Song. The effect of calnexin deletion on the expression level of pdi in saccharomyces cerevisiae under heat stress conditions. Cellular and Molecular Biology Letters, Jan 2008. URL: https://doi.org/10.2478/s11658-007-0033-y, doi:10.2478/s11658-007-0033-y. This article has 16 citations and is from a peer-reviewed journal.

12. (piirainen2022theimpactof pages 5-6): Mari A. Piirainen and Alexander D. Frey. The impact of glycoengineering on the endoplasmic reticulum quality control system in yeasts. Frontiers in Molecular Biosciences, Jun 2022. URL: https://doi.org/10.3389/fmolb.2022.910709, doi:10.3389/fmolb.2022.910709. This article has 2 citations.

13. (piirainen2022theimpactof pages 4-5): Mari A. Piirainen and Alexander D. Frey. The impact of glycoengineering on the endoplasmic reticulum quality control system in yeasts. Frontiers in Molecular Biosciences, Jun 2022. URL: https://doi.org/10.3389/fmolb.2022.910709, doi:10.3389/fmolb.2022.910709. This article has 2 citations.

Citations

1. suzuki2021foldingandquality pages 8-9
2. parlati1996characterizationofcalnexin pages 50-54
3. parlati1996characterizationofcalnexin pages 76-82
4. xu2004expressionandcharacterization pages 1-2
5. azakami2014unstablemutantlysozymes pages 1-2
6. zhang2008theeffectof pages 1-4
7. parlati1996characterizationofcalnexin pages 150-152
8. piirainen2022theimpactof pages 2-3
9. parlati1996characterizationofcalnexin pages 155-157
10. piirainen2022theimpactof pages 6-7
11. azakami2014unstablemutantlysozymes pages 2-3
12. piirainen2022theimpactof pages 5-6
13. piirainen2022theimpactof pages 4-5
14. https://doi.org/10.1093/jb/mvh074
15. https://doi.org/10.1080/09168451.2014.918486
16. https://doi.org/10.2478/s11658-007-0033-y
17. https://doi.org/10.3389/fmolb.2022.910709
18. https://doi.org/10.1091/mbc.e24-03-0121
19. https://doi.org/10.1093/jb/mvh074;
20. https://doi.org/10.1080/09168451.2014.918486;
21. https://doi.org/10.2478/s11658-007-0033-y;
22. https://doi.org/10.1093/jb/mvh074,
23. https://doi.org/10.1016/b978-0-12-409547-2.14947-9,
24. https://doi.org/10.3389/fmolb.2022.910709,
25. https://doi.org/10.1080/09168451.2014.918486,
26. https://doi.org/10.2478/s11658-007-0033-y,