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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: P53266
• Protein Description: RecName: Full=Cytochrome oxidase assembly protein SHY1; AltName: Full=SURF1 homolog of Yeast; AltName: Full=SURF1-like protein;
• Gene Information: Name=SHY1; OrderedLocusNames=YGR112W; ORFNames=G6150;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the SURF1 family. .
• Key Domains: Surf1/Shy1. (IPR002994); Surf1/Surf4. (IPR045214); SURF1 (PF02104)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SHY1" 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 'SHY1' 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 SHY1 (gene ID: SHY1, UniProt: P53266) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P53266
• Protein Description: RecName: Full=Cytochrome oxidase assembly protein SHY1; AltName: Full=SURF1 homolog of Yeast; AltName: Full=SURF1-like protein;
• Gene Information: Name=SHY1; OrderedLocusNames=YGR112W; ORFNames=G6150;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the SURF1 family. .
• Key Domains: Surf1/Shy1. (IPR002994); Surf1/Surf4. (IPR045214); SURF1 (PF02104)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SHY1" 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 'SHY1' 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 SHY1 (gene ID: SHY1, UniProt: P53266) 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 SHY1 (UniProt P53266; ORF YGR112W) — Functional Annotation

Executive summary

SHY1 (YGR112W) encodes Shy1, a conserved SURF1-family mitochondrial inner membrane protein required for efficient cytochrome c oxidase (Complex IV; COX) biogenesis and respiratory competence in budding yeast. Genetic, biochemical, and complex-isolation studies support a model in which Shy1 acts during early Cox1 maturation/assembly, coordinating cofactor-center maturation (notably heme a3:CuB formation) with assembly intermediates, and coupling assembly status to Cox1 translational regulation via interaction with the Mss51/Cox14 regulatory module. (mick2007shy1couplescox1 pages 1-3, bestwick2010analysisofleigh pages 3-4)

1) Target verification (critical gene/protein identity)

1.1 Gene symbol and protein match

The literature explicitly identifies SHY1 as the yeast homolog of mammalian SURF1, and the gene cloned to complement respiration-deficient pet mutants is identical to ORF YGR112W; the gene was named SHY1 (Surf Homolog of Yeast). (mashkevich1997shy1theyeast pages 1-1)

1.2 Organism verification

The core primary literature establishing and characterizing Shy1 is in budding yeast (Saccharomyces cerevisiae), consistent with the UniProt organism context provided. (mashkevich1997shy1theyeast pages 1-1, mick2007shy1couplescox1 pages 1-1)

1.3 Family/domain/topology consistency

Shy1 is described as a conserved SURF1-family protein with two predicted transmembrane segments (near N- and C-termini) and mitochondrial targeting features, and it behaves as an intrinsic mitochondrial membrane protein in biochemical extraction assays. (mashkevich1997shy1theyeast pages 3-4, mashkevich1997shy1theyeast pages 7-7)

Sub-mitochondrial topology is consistent with an inner mitochondrial membrane (IMM) localization, with much of the polypeptide exposed to the intermembrane space (IMS). (mick2007shy1couplescox1 pages 1-3)

Conclusion: The SHY1 gene/protein studied in the cited literature matches the user-supplied UniProt entry P53266 (cytochrome oxidase assembly protein Shy1; SURF1 family) from S. cerevisiae. (mashkevich1997shy1theyeast pages 1-1, mick2007shy1couplescox1 pages 1-1)

2) Key concepts and definitions (current understanding)

2.1 What is SHY1?

SHY1 encodes an assembly factor (not a catalytic enzyme subunit) required for efficient formation of functional cytochrome c oxidase (COX/Complex IV) in mitochondria. Loss of SHY1 decreases assembled complex IV abundance/activity and impairs respiratory growth. (nijtmans2001shy1poccursin pages 1-2, mick2007shy1couplescox1 pages 1-3)

2.2 What is cytochrome c oxidase (Complex IV) assembly?

Complex IV is the terminal oxidase of the respiratory chain, and its biogenesis requires stepwise assembly of mitochondria-encoded and nuclear-encoded subunits plus cofactor-center maturation (e.g., heme and copper centers). Shy1/SURF1-family proteins are implicated at the stage of Cox1 maturation, where formation of the heme a3:CuB catalytic center is a critical step. (bestwick2010analysisofleigh pages 3-4, stiburek2009theroleof pages 23-26)

2.3 “Coupling translation to assembly” for Cox1

In yeast, Cox1 synthesis is regulated by feedback mechanisms in which the translational activator Mss51 is sequestered in assembly intermediates when downstream assembly is blocked. Shy1 physically associates with Mss51 and Cox14, and thereby is positioned to link Cox1 synthesis regulation to Cox1 maturation/assembly progress. (mick2007shy1couplescox1 pages 1-3, reinhold2011mimickingasurf1 pages 2-3)

3) Molecular function and mechanism (experimental evidence)

3.1 Localization and physical state

• Mitochondrial/IMM localization: Antibody-based localization and biochemical fractionation support Shy1 as a mitochondrial inner membrane protein. (mashkevich1997shy1theyeast pages 1-1, mick2007shy1couplescox1 pages 1-3)
• Integral membrane behavior: Shy1 is not extracted by high-salt and requires detergent, consistent with an integral membrane protein. (mashkevich1997shy1theyeast pages 7-7)
• Higher-order complexes: Shy1 occurs in high-molecular-weight complexes (reported ~250 kDa) consistent with protein–protein interactions relevant to assembly. (nijtmans2001shy1poccursin pages 1-2)

3.2 Role in Complex IV biogenesis and Cox1 maturation

Multiple lines of evidence indicate Shy1 is required for efficient Complex IV assembly:
- Disruption of SHY1 strongly reduces steady-state assembled COX to ~30% of control, yet remaining assembled COX can appear enzymatically normal. (nijtmans2001shy1poccursin pages 1-2)
- Shy1 mediates formation of the heme a3:CuB center in Cox1 (a key catalytic cofactor center), and mutations in Shy1 can cause impaired Cox1 “hemylation” and changes in copper-related phenotypes. (bestwick2010analysisofleigh pages 3-4, bestwick2010analysisofleigh pages 1-2)

Mechanistic proposals (with experimental anchoring):
- Shy1/SURF1 has been proposed to function as a heme insertase or as a chaperone maintaining Cox1 competent for heme insertion; loss of SURF1 leads to accumulation of assembly intermediates. (reinhold2011mimickingasurf1 pages 2-3)
- Comparative evidence summarized in authoritative synthesis suggests bacterial Surf1 homologs can bind heme a in vivo and are implicated in heme insertion/stabilization for terminal oxidase biogenesis, supporting a conserved biochemical theme for the family (but direct heme-binding by yeast Shy1 is not demonstrated in the provided excerpts). (stiburek2009theroleof pages 23-26)

3.3 Coupling to Cox1 translational regulation

Shy1 is not merely a static assembly factor: it participates in regulatory complexes that couple Cox1 synthesis and assembly state.
- Shy1 associates with the Cox1 translational regulators Mss51 and Cox14, forming complexes that connect translational regulation to early assembly. (mick2007shy1couplescox1 pages 1-3)
- Patient-mutation–mimicking Shy1 alleles demonstrate that COX assembly can be uncoupled from translational feedback: e.g., a Shy1 mutant can accumulate in ~200 kDa intermediates and bypass feedback control on Cox1 expression but still block later assembly steps, revealing separable functional contributions. (reinhold2011mimickingasurf1 pages 1-2, reinhold2011mimickingasurf1 pages 10-11)

4) Pathway context: where SHY1 acts

4.1 Biological process / pathway placement

SHY1 functions in the mitochondrial oxidative phosphorylation (OXPHOS) biogenesis pathway, specifically in Complex IV assembly, acting at or near the Cox1 maturation stage and influencing formation of later supercomplexes containing Complex III and IV. (mick2007shy1couplescox1 pages 1-1, mick2007shy1couplescox1 pages 1-3)

4.2 Interaction with respiratory supercomplex formation

Shy1-containing assembly intermediates can associate with other respiratory complexes:
- Purification and complex-association evidence supports Shy1 association with respiratory chain complexes III/IV and transitional supercomplex states. (mick2007shy1couplescox1 pages 1-3, mick2007shy1couplescox1 pages 1-1)
- In a 2024 fission yeast study (see §5), the SURF1 homolog also co-immunoprecipitates with a complex III subunit and BN-PAGE supports links to supercomplex biology, supporting conserved network positioning of SURF1-family proteins. (luo2024characterizationofshy1 pages 11-13, luo2024characterizationofshy1 pages 1-2)

5) Recent developments (prioritizing 2023–2024)

Yeast SHY1 literature is foundational (1997–2011), but 2024 work updates the field with cross-yeast comparative and interaction-network evidence relevant to SURF1-family mechanistic questions.

5.1 2024: Functional characterization of SURF1 homolog in fission yeast (S. pombe)

A 2024 primary study characterized Shy1 in Schizosaccharomyces pombe as a SURF1-domain IMM protein with two transmembrane segments and reported:
- Physical interactions with complex IV subunits and assembly factors; co-immunoprecipitation of a complex III subunit (Rip1) suggested involvement in III–IV supercomplex associations. (luo2024characterizationofshy1 pages 1-2, luo2024characterizationofshy1 pages 11-13)
- BN-PAGE evidence that complex IV abundance is diminished in ∆shy1 strains. (luo2024characterizationofshy1 pages 1-2)
- An interaction network linking Shy1 to Cox1-related factors (including Mss51), copper chaperones, and heme-related factors such as Cox10/Cox11 homologs (interaction scores in their Table 1). (luo2024characterizationofshy1 pages 6-10)

Interpretation for S. cerevisiae SHY1 annotation: While organism-specific compensatory effects exist in S. pombe, these data reinforce that SURF1-family proteins sit at a conserved nexus connecting Cox1 expression/maturation, cofactor insertion pathways, and respiratory complex organization. (luo2024characterizationofshy1 pages 11-13, luo2024characterizationofshy1 pages 6-10)

6) Current applications and real-world implementations

6.1 Yeast as a model for human SURF1 disease variants

Because SURF1 mutations are a frequent cause of Leigh syndrome, yeast SHY1 has been used as an experimentally tractable model to test pathogenic mechanisms of SURF1 alleles.
- Mimicking specific patient alleles in yeast revealed separable roles for SURF1/Shy1 in assembly progression vs translational coupling, and highlighted how variants can cause turnover defects or accumulation in specific assembly intermediates. (reinhold2011mimickingasurf1 pages 1-2, reinhold2011mimickingasurf1 pages 10-11)

6.2 Genetic suppression and pathway probing

SHY1 mutant phenotypes can be modified by nuclear genetic changes or transcriptional activators.
- Nuclear revertants can increase assembled COX by ~4–5× and restore respiration to ~78% of wild type, supporting the concept that upstream expression/biogenesis capacity can buffer COX assembly defects. (barrientos2002shy1pisnecessary pages 1-2, barrientos2002shy1pisnecessary pages 2-3)
- Overexpression of transcriptional activators (HAP-related) can partially rescue respiration and strongly improve generation time on non-fermentable carbon sources (e.g., HAP4 high-copy suppression). (fontanesi2008transcriptionalactivatorshapnfy pages 2-4)

7) Quantitative phenotype summary (statistics/data)

The following table consolidates key quantitative measures from primary studies (COX activities, respiration rates, inhibitor sensitivities, and growth rates).

Table: This table compiles numeric phenotypes reported for Saccharomyces cerevisiae shy1 mutants and suppressors across key studies, including enzyme activities, respiration, COX assembly, inhibitor sensitivity, and growth rates. It is useful for quickly comparing the severity of SHY1 loss and the extent of genetic suppression.

A key visual source for the enzyme activity dataset is the original Table II from Mashkevich et al. (1997). (mashkevich1997shy1theyeast media c0394742)

8) Expert interpretation and current consensus

8.1 Consensus function

Across independent studies, SHY1 is best annotated as a mitochondrial inner membrane Complex IV assembly factor acting during Cox1 maturation/early assembly, with strong evidence for participation in the formation of the heme a3:CuB catalytic center and in coordinating assembly with translation control. (bestwick2010analysisofleigh pages 3-4, mick2007shy1couplescox1 pages 1-3)

8.2 What remains unresolved

Even with strong genetic/biochemical evidence, the precise biochemical action of Shy1 remains incompletely resolved in the provided sources: whether Shy1 directly binds/transfers heme a/a3, acts as a scaffold/chaperone for Cox1 conformational maturation, or mainly regulates/co-localizes cofactor insertion machinery is still under investigation. This uncertainty is explicitly reflected in mechanistic framing and cross-species summaries. (reinhold2011mimickingasurf1 pages 2-3, stiburek2009theroleof pages 23-26)

Appendix: Core sources with publication dates and URLs

• Mashkevich et al., May 1997, J Biol Chem: https://doi.org/10.1074/jbc.272.22.14356 (mashkevich1997shy1theyeast pages 1-1)
• Nijtmans et al., Jun 2001, FEBS Letters: https://doi.org/10.1016/S0014-5793(01)02447-4 (nijtmans2001shy1poccursin pages 1-2)
• Barrientos et al., Jan 2002, EMBO J: https://doi.org/10.1093/emboj/21.1.43 (barrientos2002shy1pisnecessary pages 1-2)
• Mick et al., Oct 2007, EMBO J: https://doi.org/10.1038/sj.emboj.7601862 (mick2007shy1couplescox1 pages 1-3)
• Fontanesi et al., Mar 2008, Hum Mol Genet: https://doi.org/10.1093/hmg/ddm349 (fontanesi2008transcriptionalactivatorshapnfy pages 2-4)
• Bestwick et al., Sep 2010, Mol Cell Biol: https://doi.org/10.1128/MCB.00228-10 (bestwick2010analysisofleigh pages 3-4)
• Reinhold et al., Jun 2011, Hum Mol Genet: https://doi.org/10.1093/hmg/ddr145 (reinhold2011mimickingasurf1 pages 1-2)
• Luo et al., Sep 2024, Scientific Reports (S. pombe Shy1 homolog): https://doi.org/10.1038/s41598-024-72681-9 (luo2024characterizationofshy1 pages 1-2)

References

1. (mick2007shy1couplescox1 pages 1-3): David U Mick, Karina Wagner, Martin van der Laan, Ann E Frazier, Inge Perschil, Magdalena Pawlas, Helmut E Meyer, Bettina Warscheid, and Peter Rehling. Shy1 couples cox1 translational regulation to cytochrome c oxidase assembly. The EMBO Journal, 26:4347-4358, Oct 2007. URL: https://doi.org/10.1038/sj.emboj.7601862, doi:10.1038/sj.emboj.7601862. This article has 173 citations.

2. (bestwick2010analysisofleigh pages 3-4): Megan Bestwick, Mi-Young Jeong, Oleh Khalimonchuk, Hyung Kim, and Dennis R. Winge. Analysis of leigh syndrome mutations in the yeast surf1 homolog reveals a new member of the cytochrome oxidase assembly factor family. Molecular and Cellular Biology, 30:4480-4491, Sep 2010. URL: https://doi.org/10.1128/mcb.00228-10, doi:10.1128/mcb.00228-10. This article has 48 citations and is from a domain leading peer-reviewed journal.

3. (mashkevich1997shy1theyeast pages 1-1): Grigoriy Mashkevich, Barbara Repetto, D. Moira Glerum, Can Jin, and Alexander Tzagoloff. Shy1, the yeast homolog of the mammaliansurf-1 gene, encodes a mitochondrial protein required for respiration*. The Journal of Biological Chemistry, 272:14356-14364, May 1997. URL: https://doi.org/10.1074/jbc.272.22.14356, doi:10.1074/jbc.272.22.14356. This article has 175 citations.

4. (mick2007shy1couplescox1 pages 1-1): David U Mick, Karina Wagner, Martin van der Laan, Ann E Frazier, Inge Perschil, Magdalena Pawlas, Helmut E Meyer, Bettina Warscheid, and Peter Rehling. Shy1 couples cox1 translational regulation to cytochrome c oxidase assembly. The EMBO Journal, 26:4347-4358, Oct 2007. URL: https://doi.org/10.1038/sj.emboj.7601862, doi:10.1038/sj.emboj.7601862. This article has 173 citations.

5. (mashkevich1997shy1theyeast pages 3-4): Grigoriy Mashkevich, Barbara Repetto, D. Moira Glerum, Can Jin, and Alexander Tzagoloff. Shy1, the yeast homolog of the mammaliansurf-1 gene, encodes a mitochondrial protein required for respiration*. The Journal of Biological Chemistry, 272:14356-14364, May 1997. URL: https://doi.org/10.1074/jbc.272.22.14356, doi:10.1074/jbc.272.22.14356. This article has 175 citations.

6. (mashkevich1997shy1theyeast pages 7-7): Grigoriy Mashkevich, Barbara Repetto, D. Moira Glerum, Can Jin, and Alexander Tzagoloff. Shy1, the yeast homolog of the mammaliansurf-1 gene, encodes a mitochondrial protein required for respiration*. The Journal of Biological Chemistry, 272:14356-14364, May 1997. URL: https://doi.org/10.1074/jbc.272.22.14356, doi:10.1074/jbc.272.22.14356. This article has 175 citations.

7. (nijtmans2001shy1poccursin pages 1-2): L.G.J. Nijtmans, M. Artal Sanz, M. Bucko, M.H. Farhoud, M. Feenstra, G.A.J. Hakkaart, M. Zeviani, and L.A. Grivell. Shy1p occurs in a high molecular weight complex and is required for efficient assembly of cytochrome c oxidase in yeast. FEBS Letters, 498:46-51, Jun 2001. URL: https://doi.org/10.1016/s0014-5793(01)02447-4, doi:10.1016/s0014-5793(01)02447-4. This article has 89 citations and is from a peer-reviewed journal.

8. (stiburek2009theroleof pages 23-26): L Stibůrek. The role of human sco1, sco2, surf1 and oxa1l in the biogenesis of the mitochondrial oxidative phosphorylation system. Unknown journal, 2009.

9. (reinhold2011mimickingasurf1 pages 2-3): Robert Reinhold, Bettina Bareth, Martina Balleininger, Mirjam Wissel, Peter Rehling, and David U. Mick. Mimicking a surf1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast. Human molecular genetics, 20 12:2379-93, Jun 2011. URL: https://doi.org/10.1093/hmg/ddr145, doi:10.1093/hmg/ddr145. This article has 28 citations and is from a domain leading peer-reviewed journal.

10. (bestwick2010analysisofleigh pages 1-2): Megan Bestwick, Mi-Young Jeong, Oleh Khalimonchuk, Hyung Kim, and Dennis R. Winge. Analysis of leigh syndrome mutations in the yeast surf1 homolog reveals a new member of the cytochrome oxidase assembly factor family. Molecular and Cellular Biology, 30:4480-4491, Sep 2010. URL: https://doi.org/10.1128/mcb.00228-10, doi:10.1128/mcb.00228-10. This article has 48 citations and is from a domain leading peer-reviewed journal.

11. (reinhold2011mimickingasurf1 pages 1-2): Robert Reinhold, Bettina Bareth, Martina Balleininger, Mirjam Wissel, Peter Rehling, and David U. Mick. Mimicking a surf1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast. Human molecular genetics, 20 12:2379-93, Jun 2011. URL: https://doi.org/10.1093/hmg/ddr145, doi:10.1093/hmg/ddr145. This article has 28 citations and is from a domain leading peer-reviewed journal.

12. (reinhold2011mimickingasurf1 pages 10-11): Robert Reinhold, Bettina Bareth, Martina Balleininger, Mirjam Wissel, Peter Rehling, and David U. Mick. Mimicking a surf1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast. Human molecular genetics, 20 12:2379-93, Jun 2011. URL: https://doi.org/10.1093/hmg/ddr145, doi:10.1093/hmg/ddr145. This article has 28 citations and is from a domain leading peer-reviewed journal.

13. (luo2024characterizationofshy1 pages 11-13): Ying Luo, Yuanqi Xu, Fawad Ahmad, Gang Feng, and Ying Huang. Characterization of shy1, the schizosaccharomyces pombe homolog of human surf1. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72681-9, doi:10.1038/s41598-024-72681-9. This article has 8 citations and is from a peer-reviewed journal.

14. (luo2024characterizationofshy1 pages 1-2): Ying Luo, Yuanqi Xu, Fawad Ahmad, Gang Feng, and Ying Huang. Characterization of shy1, the schizosaccharomyces pombe homolog of human surf1. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72681-9, doi:10.1038/s41598-024-72681-9. This article has 8 citations and is from a peer-reviewed journal.

15. (luo2024characterizationofshy1 pages 6-10): Ying Luo, Yuanqi Xu, Fawad Ahmad, Gang Feng, and Ying Huang. Characterization of shy1, the schizosaccharomyces pombe homolog of human surf1. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72681-9, doi:10.1038/s41598-024-72681-9. This article has 8 citations and is from a peer-reviewed journal.

16. (barrientos2002shy1pisnecessary pages 1-2): A. Barrientos, D. Korr, and A. Tzagoloff. Shy1p is necessary for full expression of mitochondrial cox1 in the yeast model of leigh's syndrome. The EMBO Journal, 21:43-52, Jan 2002. URL: https://doi.org/10.1093/emboj/21.1.43, doi:10.1093/emboj/21.1.43. This article has 210 citations.

17. (barrientos2002shy1pisnecessary pages 2-3): A. Barrientos, D. Korr, and A. Tzagoloff. Shy1p is necessary for full expression of mitochondrial cox1 in the yeast model of leigh's syndrome. The EMBO Journal, 21:43-52, Jan 2002. URL: https://doi.org/10.1093/emboj/21.1.43, doi:10.1093/emboj/21.1.43. This article has 210 citations.

18. (fontanesi2008transcriptionalactivatorshapnfy pages 2-4): Flavia Fontanesi, Can Jin, Alexander Tzagoloff, and Antoni Barrientos. Transcriptional activators hap/nf-y rescue a cytochrome c oxidase defect in yeast and human cells. Human molecular genetics, 17 6:775-88, Mar 2008. URL: https://doi.org/10.1093/hmg/ddm349, doi:10.1093/hmg/ddm349. This article has 67 citations and is from a domain leading peer-reviewed journal.

19. (mashkevich1997shy1theyeast media c0394742): Grigoriy Mashkevich, Barbara Repetto, D. Moira Glerum, Can Jin, and Alexander Tzagoloff. Shy1, the yeast homolog of the mammaliansurf-1 gene, encodes a mitochondrial protein required for respiration*. The Journal of Biological Chemistry, 272:14356-14364, May 1997. URL: https://doi.org/10.1074/jbc.272.22.14356, doi:10.1074/jbc.272.22.14356. This article has 175 citations.

Citations

1. stiburek2009theroleof pages 23-26
2. fontanesi2008transcriptionalactivatorshapnfy pages 2-4
3. bestwick2010analysisofleigh pages 3-4
4. bestwick2010analysisofleigh pages 1-2
5. https://doi.org/10.1074/jbc.272.22.14356
6. https://doi.org/10.1016/S0014-5793(01
7. https://doi.org/10.1093/emboj/21.1.43
8. https://doi.org/10.1038/sj.emboj.7601862
9. https://doi.org/10.1093/hmg/ddm349
10. https://doi.org/10.1128/MCB.00228-10
11. https://doi.org/10.1093/hmg/ddr145
12. https://doi.org/10.1038/s41598-024-72681-9
13. https://doi.org/10.1038/sj.emboj.7601862,
14. https://doi.org/10.1128/mcb.00228-10,
15. https://doi.org/10.1074/jbc.272.22.14356,
16. https://doi.org/10.1016/s0014-5793(01
17. https://doi.org/10.1093/hmg/ddr145,
18. https://doi.org/10.1038/s41598-024-72681-9,
19. https://doi.org/10.1093/emboj/21.1.43,
20. https://doi.org/10.1093/hmg/ddm349,