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organism: yeast
gene_id: PHO86
gene_symbol: PHO86
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protein_description: 'RecName: Full=Inorganic phosphate transporter PHO86;'
gene_info: Name=PHO86; OrderedLocusNames=YJL117W; ORFNames=J0744;
organism_full: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
protein_family: Not specified in UniProt
protein_domains: Pho86. (IPR024297); Pho86 (PF11124)
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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: P46956
• Protein Description: RecName: Full=Inorganic phosphate transporter PHO86;
• Gene Information: Name=PHO86; OrderedLocusNames=YJL117W; ORFNames=J0744;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Pho86. (IPR024297); Pho86 (PF11124)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PHO86" 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 'PHO86' 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 PHO86 (gene ID: PHO86, UniProt: P46956) 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: P46956
• Protein Description: RecName: Full=Inorganic phosphate transporter PHO86;
• Gene Information: Name=PHO86; OrderedLocusNames=YJL117W; ORFNames=J0744;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Pho86. (IPR024297); Pho86 (PF11124)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PHO86" 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 'PHO86' 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 PHO86 (gene ID: PHO86, UniProt: P46956) 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 PHO86 (YJL117W; UniProt P46956)

0) Target verification (mandatory)

All evidence below refers specifically to Saccharomyces cerevisiae (strain S288c) PHO86 / YJL117W, encoding Pho86p, an endoplasmic-reticulum (ER) resident membrane protein required for ER exit of the high-affinity inorganic phosphate transporter Pho84p (and not to any similarly named proteins in other organisms). Primary evidence explicitly names PHO86/YJL117W and experimentally tests Pho86p localization/function in budding yeast. (lau2000pho86panendoplasmic pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 What Pho86 is (molecular function)

Pho86p is not a phosphate transporter. Instead, it is an ER-resident, cargo-specific trafficking/biogenesis factor that enables Pho84p (a polytopic plasma-membrane phosphate permease) to exit the ER and enter the secretory pathway. The canonical mechanistic description is that Pho86p functions as an ER “outfitter” or accessory factor that promotes COPII-dependent packaging of Pho84p into ER-derived vesicles. (lau2000pho86panendoplasmic pages 1-2, lau2000pho86panendoplasmic pages 4-5)

A useful operational definition supported by cell biology and proteostasis literature is that Pho86 belongs to a class of “specialized membrane-localized chaperones” that prevent aggregation/misfolding of particular polytopic membrane cargos during insertion/folding in the ER membrane, thereby allowing them to become export-competent. (kota2005specializedmembranelocalizedchaperones pages 1-2)

1.2 Biological process context: phosphate homeostasis and the PHO pathway

In budding yeast, phosphate starvation triggers a transcriptional program (the PHO pathway/PHO regulon) that induces high-affinity phosphate acquisition genes. PHO84 and PHO86 are among the genes highly induced upon phosphate starvation, and pho86 loss-of-function mutants phenocopy pho84 mutants in key readouts (defective phosphate uptake and PHO regulon derepression such as constitutive Pho5 acid phosphatase expression), consistent with Pho86 acting upstream by enabling functional Pho84 at the plasma membrane. (lau2000pho86panendoplasmic pages 1-2, howson2003systematicapproachesto pages 149-154)

Importantly, regulation of Pho84 protein localization (plasma membrane in low phosphate; internalization to vacuole after phosphate addition) is post-translational and was shown to be independent of canonical PHO signaling mutants tested in that work; thus Pho86’s core role is best framed as protein trafficking/quality control rather than phosphate sensing per se. (lau2000pho86panendoplasmic pages 3-4)

2) Core experimental evidence for function, localization, and mechanism (primary literature)

2.1 Subcellular localization of Pho86p: ER resident

A functional Pho86p-GFP fusion (low-copy construct that complements pho86Δ phenotypes) localizes to a perinuclear compartment coincident with the ER marker Kar2/BiP, consistent with ER residence. Pho86p-GFP localization was observed in low-phosphate medium and also in high-phosphate medium, indicating Pho86 localization is not itself regulated by extracellular phosphate. (lau2000pho86panendoplasmic pages 3-4, lau2000pho86panendoplasmic media d64c6532)

2.2 Pho86 is required for Pho84 ER exit and plasma-membrane targeting

Pho84p is dynamically regulated: it localizes to the plasma membrane under low-phosphate and is endocytosed and delivered to the vacuole after phosphate addition. In contrast, in pho86Δ cells, Pho84p-GFP is predominantly retained in the ER, co-localizing with Kar2p and other ER markers. This establishes Pho86 as necessary for Pho84 trafficking beyond the ER. (lau2000pho86panendoplasmic pages 1-2, lau2000pho86panendoplasmic pages 3-4, lau2000pho86panendoplasmic media 52ae20e9)

2.3 Mechanism: Pho86-dependent COPII packaging of Pho84 in vitro

A key mechanistic experiment used an in vitro COPII vesicle budding assay from perforated spheroplasts:

• Pho84p-HA is packaged into COPII vesicles from wild-type membranes with ~20% efficiency under reconstituted COPII conditions.
• Omission of Sar1p or coat proteins reduces packaging >3-fold, demonstrating the assay’s dependence on canonical COPII machinery.
• From pho86Δ membranes, Pho84p-HA is not detected above background in the vesicle fraction, showing that Pho86 is required for Pho84 export competence/packaging.
• Pho86p itself is not detected above background in vesicle fractions, supporting a model in which Pho86 acts in the ER but is not co-exported with the cargo.
• Packaging of another cargo (Vph1p) is not affected by pho86Δ in this assay, consistent with cargo specificity.

Together, these experiments are strong evidence that Pho86 is a cargo-specific ER factor required for Pho84 incorporation into COPII vesicles. (lau2000pho86panendoplasmic pages 4-5, lau2000pho86panendoplasmic media 6beb61b8)

2.4 Specificity: Pho86 is not a general secretory factor

pho86Δ cells show normal localization of other plasma-membrane proteins assayed (e.g., Pma1p-HA and Gal2p-GFP), and exhibit normal growth across multiple conditions and normal mating, supporting a specialized role rather than global ER export failure. (lau2000pho86panendoplasmic pages 3-4)

3) Interaction partners and pathway wiring (what is supported vs. what is inferred)

3.1 Pho84 as the primary cognate client cargo

The most directly supported functional relationship is that Pho84 requires Pho86 for ER exit and correct targeting; the requirement is described as specific to Pho84 relative to other hexose-transporter family members tested. (lau2000pho86panendoplasmic pages 1-2, lau2000pho86panendoplasmic pages 4-5)

3.2 Proteostasis framework: specialized ER chaperone class

Pho86 is grouped with other dedicated ER membrane chaperones (e.g., Shr3, Gsf2, Chs7) that prevent aggregation of their cognate multi-pass membrane cargos. In this model, loss of the dedicated factor causes aggregation and ER retention of the client cargo(s), thereby preventing ER export. This provides mechanistic interpretation for Pho86’s role in Pho84 maturation/export, even when direct binding interfaces are not mapped. (kota2005specializedmembranelocalizedchaperones pages 1-2)

3.3 Additional interaction mentioned in recent work (large-scale screen)

A more recent stress-focused study notes that Pho86 was reported to interact with Fet3 in a large-scale screen of membrane protein interactors, raising the possibility that Pho86 overexpression influences iron uptake pathways under arsenate stress; however, this interaction is not presented as a direct, validated biochemical interaction within the retrieved evidence. (isik2022identificationofnovel pages 8-9)

4) Recent developments and latest research (prioritizing 2023–2024 where available)

4.1 Direct PHO86-focused primary studies in 2023–2024

Within the retrieved, accessible literature set, dedicated 2023–2024 primary mechanistic studies centered on PHO86 itself were not identified. The mechanistic foundation still rests primarily on the 2000–2005 cell biology/proteostasis work (ER localization, Pho84 dependence, COPII packaging, specialized chaperone model). (lau2000pho86panendoplasmic pages 4-5, kota2005specializedmembranelocalizedchaperones pages 1-2)

4.2 2022–2024: PHO86 and metalloid stress (arsenate)

A notable recent experimental development is identification of PHO86 overexpression as an arsenate [As(V)] resistance determinant. Key reported findings include:

• PHO86 emerged from an overexpression screen as a gene whose increased dosage confers As(V) resistance (not As(III) resistance). (isik2022identificationofnovel pages 8-8)
• Intracellular arsenic accumulation was assayed after 1 mM As(V) for 1 h (averages from n=6), and the study performed time-course efflux analyses (averaged across n=3 biological replicates). (isik2022identificationofnovel pages 8-8)
• The As(V)-resistance phenotype from PHO86 overexpression requires Pho84, because overexpressing PHO86 in a pho84Δ background did not provide additional As(V) resistance. This is consistent with the known role of Pho86 in increasing Pho84 delivery to the plasma membrane. (isik2022identificationofnovel pages 8-8)
• Proteotoxic damage was assessed via Hsp104-GFP aggregation assays after 2 mM As(V); aggregates were scored by visual inspection of 144–282 cells per condition/timepoint, averaged across n=3 replicates. PHO86-overexpressing cells did not show elevated aggregation despite higher intracellular arsenic, suggesting improved tolerance to intracellular arsenate burden (mechanism unresolved). (isik2022identificationofnovel pages 8-9)

While this 2022 study is slightly outside the user’s preferred 2023–2024 window, it is among the most directly PHO86-relevant recent experimental papers found and provides quantitative assay context. (isik2022identificationofnovel pages 8-8, isik2022identificationofnovel pages 8-9)

5) Current applications and real-world implementations

5.1 Controlling arsenate entry and toxicity through the Pho84/Pho86 axis

Pho84 is a known import route for phosphate analogs such as arsenate; because Pho86 controls Pho84 abundance at the plasma membrane by enabling ER exit, PHO86 perturbation provides an actionable lever for modulating phosphate/arsenate uptake. In practical terms:

• pho86 loss-of-function is associated with arsenate resistance in classical genetic screens (consistent with reduced Pho84 at the surface). (lau2000pho86panendoplasmic pages 1-2)
• Conversely, PHO86 overexpression can increase Pho84 levels and alter arsenate handling and resistance phenotypes in a Pho84-dependent manner. (isik2022identificationofnovel pages 8-8)

This axis can be relevant to (i) engineering yeast strains with altered metalloid uptake/toxicity profiles for screening or bioprocess robustness, and (ii) using yeast as a model to dissect membrane-proteostasis mechanisms for nutrient transporters under stress. (isik2022identificationofnovel pages 8-8, kota2005specializedmembranelocalizedchaperones pages 1-2)

5.2 Broader biotechnology relevance (indirect but mechanistically grounded)

High-affinity phosphate uptake and phosphate homeostasis influence central metabolism and stress responses; therefore, ensuring correct Pho84 biogenesis/trafficking—for which Pho86 is essential—can be a determinant of growth under phosphate limitation and could affect strain performance in phosphate-limited or fluctuating environments. The evidence base supporting this is mechanistic (Pho86→Pho84 trafficking) and physiological (pho86 phenocopies pho84 for phosphate uptake/PHO regulon readouts). (lau2000pho86panendoplasmic pages 1-2, persson2003regulationofphosphate pages 12-13)

6) Quantitative data and statistics (from retrieved studies)

Key quantitative points that can be extracted directly from the retrieved sources are:

• ~20% COPII packaging efficiency for Pho84p-HA from wild-type membranes in vitro under reconstituted COPII conditions; omission of COPII components reduces packaging >3-fold; Pho84 packaging is not detectable above background from pho86Δ membranes. (lau2000pho86panendoplasmic pages 4-5)
• Arsenate stress assays used 1 mM As(V) for 1 h for intracellular arsenic accumulation measurements with n=6; proteotoxicity assays used 2 mM As(V) with aggregation scored in 144–282 cells per condition/timepoint, across n=3 replicates. (isik2022identificationofnovel pages 8-8, isik2022identificationofnovel pages 8-9)

7) Evidence summary table

The following table compiles the principal functional-annotation claims, evidence types, experimental details, and URLs.

Table: This table summarizes core experimental and review-supported evidence for the functional annotation of Saccharomyces cerevisiae Pho86/PHO86. It highlights ER localization, Pho84-specific trafficking, COPII export dependence, phosphate-homeostasis relevance, specialized chaperone/proteostasis roles, and recent stress-related findings.

8) Summary functional annotation (for databases/curation)

Gene/protein: PHO86 / Pho86p (YJL117W; UniProt P46956)

Primary molecular function (experimentally supported): ER-resident membrane factor (“outfitter”/specialized membrane-localized chaperone) required for COPII-dependent ER export of Pho84 high-affinity inorganic phosphate permease; promotes Pho84 acquisition of an export-competent state and/or its selection for COPII packaging. (lau2000pho86panendoplasmic pages 4-5, kota2005specializedmembranelocalizedchaperones pages 1-2)

Biological process: High-affinity phosphate acquisition and phosphate homeostasis (indirectly), via enabling Pho84 delivery to the plasma membrane; impacts PHO regulon outputs (e.g., Pho5 acid phosphatase derepression) primarily through phosphate uptake capacity. (lau2000pho86panendoplasmic pages 1-2, persson2003regulationofphosphate pages 12-13)

Subcellular location: Endoplasmic reticulum (perinuclear ER), phosphate-independent localization. (lau2000pho86panendoplasmic pages 3-4, lau2000pho86panendoplasmic media d64c6532)

Key client cargo: Pho84p (high-affinity phosphate transporter). (lau2000pho86panendoplasmic pages 3-4, lau2000pho86panendoplasmic pages 4-5)

Recent/expanded phenotype space: PHO86 overexpression modulates arsenate [As(V)] stress phenotypes in a Pho84-dependent manner; quantitative assays include arsenic accumulation at 1 mM As(V) and proteotoxicity scoring at 2 mM As(V). (isik2022identificationofnovel pages 8-8, isik2022identificationofnovel pages 8-9)

Key primary sources (with publication dates and URLs)

• Lau W-TW et al. Pho86p… is required for ER exit of the high-affinity phosphate transporter Pho84p. PNAS (Published Feb 2000). https://doi.org/10.1073/pnas.97.3.1107 (lau2000pho86panendoplasmic pages 1-2)
• Kota J & Ljungdahl PO. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J Cell Biol (Jan 2005; published online Dec 28, 2004). https://doi.org/10.1083/jcb.200408106 (kota2005specializedmembranelocalizedchaperones pages 1-2)
• Persson BL et al. Regulation of phosphate acquisition in Saccharomyces cerevisiae. Current Genetics (Jul 2003). https://doi.org/10.1007/s00294-003-0400-9 (persson2003regulationofphosphate pages 12-13)
• Isik E et al. Identification of novel arsenic resistance genes in yeast. MicrobiologyOpen (Apr 2022). https://doi.org/10.1002/mbo3.1284 (isik2022identificationofnovel pages 8-8)

References

1. (lau2000pho86panendoplasmic pages 1-2): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

2. (lau2000pho86panendoplasmic pages 4-5): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

3. (kota2005specializedmembranelocalizedchaperones pages 1-2): Jhansi Kota and Per O. Ljungdahl. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the er. The Journal of Cell Biology, 168:79-88, Jan 2005. URL: https://doi.org/10.1083/jcb.200408106, doi:10.1083/jcb.200408106. This article has 134 citations.

4. (howson2003systematicapproachesto pages 149-154): RW Howson. Systematic approaches to identifying substrates of the budding yeast cyclin dependent kinase pho85. Unknown journal, 2003.

5. (lau2000pho86panendoplasmic pages 3-4): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

6. (lau2000pho86panendoplasmic media d64c6532): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

7. (lau2000pho86panendoplasmic media 52ae20e9): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

8. (lau2000pho86panendoplasmic media 6beb61b8): W.-T. Walter Lau, Russell W. Howson, Per Malkus, Randy Schekman, and Erin K. O'Shea. Pho86p, an endoplasmic reticulum (er) resident protein in saccharomyces cerevisiae, is required for er exit of the high-affinity phosphate transporter pho84p. Proceedings of the National Academy of Sciences of the United States of America, 97 3:1107-12, Feb 2000. URL: https://doi.org/10.1073/pnas.97.3.1107, doi:10.1073/pnas.97.3.1107. This article has 117 citations and is from a highest quality peer-reviewed journal.

9. (isik2022identificationofnovel pages 8-9): Esin Isik, Çiğdem Balkan, Vivien Karl, Hüseyin Çağlar Karakaya, Sansan Hua, Sebastien Rauch, Markus J. Tamás, and Ahmet Koc. Identification of novel arsenic resistance genes in yeast. MicrobiologyOpen, Apr 2022. URL: https://doi.org/10.1002/mbo3.1284, doi:10.1002/mbo3.1284. This article has 5 citations and is from a peer-reviewed journal.

10. (isik2022identificationofnovel pages 8-8): Esin Isik, Çiğdem Balkan, Vivien Karl, Hüseyin Çağlar Karakaya, Sansan Hua, Sebastien Rauch, Markus J. Tamás, and Ahmet Koc. Identification of novel arsenic resistance genes in yeast. MicrobiologyOpen, Apr 2022. URL: https://doi.org/10.1002/mbo3.1284, doi:10.1002/mbo3.1284. This article has 5 citations and is from a peer-reviewed journal.

11. (persson2003regulationofphosphate pages 12-13): Bengt L. Persson, Jens O. Lagerstedt, James R. Pratt, Johanna Pattison-Granberg, Kent Lundh, Soheila Shokrollahzadeh, and Fredrik Lundh. Regulation of phosphate acquisition in saccharomyces cerevisiae. Current Genetics, 43:225-244, Jul 2003. URL: https://doi.org/10.1007/s00294-003-0400-9, doi:10.1007/s00294-003-0400-9. This article has 195 citations and is from a peer-reviewed journal.

12. (isik2022identificationofnovel pages 9-9): Esin Isik, Çiğdem Balkan, Vivien Karl, Hüseyin Çağlar Karakaya, Sansan Hua, Sebastien Rauch, Markus J. Tamás, and Ahmet Koc. Identification of novel arsenic resistance genes in yeast. MicrobiologyOpen, Apr 2022. URL: https://doi.org/10.1002/mbo3.1284, doi:10.1002/mbo3.1284. This article has 5 citations and is from a peer-reviewed journal.

Citations

1. kota2005specializedmembranelocalizedchaperones pages 1-2
2. isik2022identificationofnovel pages 8-9
3. isik2022identificationofnovel pages 8-8
4. persson2003regulationofphosphate pages 12-13
5. howson2003systematicapproachesto pages 149-154
6. isik2022identificationofnovel pages 9-9
7. As(V)
8. https://doi.org/10.1073/pnas.97.3.1107
9. https://doi.org/10.1007/s00294-003-0400-9
10. https://doi.org/10.1083/jcb.200408106
11. https://doi.org/10.1002/mbo3.1284
12. https://doi.org/10.1073/pnas.97.3.1107,
13. https://doi.org/10.1083/jcb.200408106,
14. https://doi.org/10.1002/mbo3.1284,
15. https://doi.org/10.1007/s00294-003-0400-9,