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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: P38958
• Protein Description: RecName: Full=Protein PET100, mitochondrial; Flags: Precursor;
• Gene Information: Name=PET100; OrderedLocusNames=YDR079W; ORFNames=D4441;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the PET100 family. .
• Key Domains: Pet100. (IPR018625); Pet100 (PF09803)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PET100" 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 'PET100' 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 PET100 (gene ID: PET100, UniProt: P38958) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: P38958
• Protein Description: RecName: Full=Protein PET100, mitochondrial; Flags: Precursor;
• Gene Information: Name=PET100; OrderedLocusNames=YDR079W; ORFNames=D4441;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the PET100 family. .
• Key Domains: Pet100. (IPR018625); Pet100 (PF09803)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PET100" 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 'PET100' 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 PET100 (gene ID: PET100, UniProt: P38958) 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: PET100 (YDR079W; UniProt P38958) in Saccharomyces cerevisiae (S288c)

1) Target verification (critical gene/protein identity)

The gene PET100 discussed here is the S. cerevisiae nuclear gene YDR079W, encoding Protein PET100, mitochondrial (precursor) (UniProt P38958). The defining primary study cloned PET100 by complementation of a respiratory-deficient mutant and demonstrated it is required for cytochrome c oxidase (COX; respiratory complex IV) assembly, matching the UniProt description and the PET100 family/domain expectations for a small mitochondrial assembly factor rather than an enzyme or transporter (https://doi.org/10.1074/jbc.271.31.18499; published Aug 1996) (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 8-9).

2) Key concepts and definitions (current understanding)

Cytochrome c oxidase (complex IV) and “assembly factors”

Cytochrome c oxidase (COX; complex IV) is the terminal enzyme of the mitochondrial electron transport chain, catalyzing electron transfer from cytochrome c to oxygen. Because COX contains both mitochondrially encoded catalytic subunits and nuclear-encoded structural subunits, its formation requires many assembly factors—proteins that are not part of the final enzyme but are required for steps such as membrane insertion, cofactor insertion, stabilization of intermediates, and modular joining of assembly “modules” (review context) (https://doi.org/10.3390/ijms25073814; published Mar 2024) (guaragnella2024morethanjust pages 9-11, guaragnella2024morethanjust pages 4-5).

PET100 as a COX-specific assembly factor

In yeast, PET100 is best understood as a COX-specific biogenesis/assembly factor that acts after COX subunits are made and imported into mitochondria—i.e., it is required for late-stage assembly into an active holoenzyme rather than for subunit synthesis or import (https://doi.org/10.1074/jbc.271.31.18499; Aug 1996) (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 2-3).

A 2024 review synthesizing yeast and human literature places PET100 within late COX biogenesis and proposes that PET100 contributes to stabilization of a late intermediate (“S3”) representing joined COX1+COX2 modules before COX3 addition, consistent with a stabilization/coordination role rather than a catalytic function (https://doi.org/10.3390/ijms25073814; Mar 2024) (guaragnella2024morethanjust pages 9-11, guaragnella2024morethanjust pages 4-5).

3) Experimentally supported function, pathway placement, and localization

3.1 Primary function (what PET100 does)

Primary experimentally supported role: PET100 is required for the assembly/biogenesis of cytochrome c oxidase (complex IV) in S. cerevisiae.

Key primary findings from Church et al. (1996, JBC):
- A PET100 null strain lacks cytochrome c oxidase activity and lacks assembled cytochromes a and a3 (spectral signature of COX), while other respiratory cytochromes/carriers remain present—supporting a COX-specific defect rather than global respiratory chain collapse (https://doi.org/10.1074/jbc.271.31.18499; Aug 1996) (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 8-9).
- Mitochondria from the PET100 null strain still contain the individual COX subunit polypeptides, indicating PET100 is not required for COX subunit synthesis or their localization to mitochondria, but is required at a later step for assembly into the active enzyme (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 2-3).

These data support annotating Pet100 as a non-enzymatic assembly/stabilization factor (a “molecular chaperone” in the broad sense of assisting assembly) rather than a metabolic enzyme with substrate specificity (church1996cloningandcharacterization pages 2-3, sampson2012highthroughputdrug pages 88-89).

3.2 Subcellular localization (where PET100 acts)

Direct microscopy/topology was not established in the primary PET100 cloning paper; instead, localization is supported by sequence features:
- Pet100 is predicted to contain an N-terminal mitochondrial targeting sequence (cleavage predicted around residues 13–14) and a hydrophobic segment (residues ~20–38) consistent with membrane association (https://doi.org/10.1074/jbc.271.31.18499; Aug 1996) (church1996cloningandcharacterization pages 5-6, church1996cloningandcharacterization pages 8-9).
- The authors explicitly noted they could not determine whether Pet100 resides in the inner or outer mitochondrial membrane based on their data, so inner-membrane assignment should be treated as inference without additional evidence (church1996cloningandcharacterization pages 8-9).

Given its COX assembly role and predicted membrane segment, the most conservative evidence-based statement is: Pet100 is a mitochondrially targeted, likely membrane-associated protein required for COX assembly, with precise membrane topology unresolved in the cited primary study (church1996cloningandcharacterization pages 5-6, church1996cloningandcharacterization pages 8-9).

3.3 Pathway context (COX assembly modules and intermediates)

A 2024 review of COX deficiencies highlights PET100 in late COX biogenesis and situates it in the COX2-module context, proposing:
- PET100 acts to stabilize the joined COX1+COX2 intermediate (“S3”) prior to addition of the COX3 module (https://doi.org/10.3390/ijms25073814; Mar 2024) (guaragnella2024morethanjust pages 9-11).
- PET100 participates in an interaction network with PET117 and MR-1S; this group is described as associating more strongly with a nascent COX2 intermediate than with the COX1 module, suggesting coordination/stabilization between COX1 and COX2 module intermediates (guaragnella2024morethanjust pages 8-9).
- In yeast literature summarized by the review, PET100 is reported to associate with two COX subassembly complexes: one containing Cox7/Cox8/Cox9, and another containing subunits 5 and 6 (Cox5/Cox6; equivalent to human COX4/COX6) (guaragnella2024morethanjust pages 13-14).

The review emphasizes that the molecular mechanism remains incompletely resolved, highlighting PET100 as a factor with strong genetic/phenotypic evidence but less mechanistic detail than cofactor-handling proteins (guaragnella2024morethanjust pages 13-14).

4) Mutant phenotypes and quantitative data (key statistics)

4.1 Respiratory growth phenotype

PET100 loss causes respiratory deficiency, operationally detected as inability (null) or reduced ability (leaky allele) to grow on non-fermentable carbon sources such as glycerol (YPG) (church1996cloningandcharacterization pages 5-6, church1996cloningandcharacterization pages 3-3).

4.2 Mitochondrial COX activity (quantitative)

Church et al. (1996) measured COX activity in isolated mitochondria, showing a dramatic genotype-dependent loss:
- Wild type (JM43): 74.76 (set to 100%)
- pet100-1 (B9-10D): 13.90 (18.60% of WT)
- pet100 null (pet100::LEU2; JM43GD100): 0.87, reported as ~0.01% of WT (essentially absent) (church1996cloningandcharacterization pages 3-4) (church1996cloningandcharacterization media cab4f922).

Difference spectra further show the aa3 peak is reduced in pet100-1 and absent in the null, consistent with loss of assembled COX (church1996cloningandcharacterization media cab4f922, church1996cloningandcharacterization media 79137f77).

4.3 COX subunit presence vs assembly

Despite the near-complete loss of COX activity, immunoblot evidence indicates COX subunits are still detectable and processed in mutant mitochondria, though steady-state levels of several subunits are partially reduced, consistent with instability/turnover of unassembled intermediates (church1996cloningandcharacterization pages 7-8).

5) Recent developments and latest research (2023–2024 prioritized)

Direct 2023–2024 primary mechanistic studies on yeast Pet100 itself are limited in the retrieved corpus; however, recent authoritative synthesis and adjacent mechanistic advances refine interpretation of PET100’s role:

1. Updated module-based COX assembly model incorporating PET100: The 2024 review integrates yeast genetics and human disease studies and places PET100 in late-stage stabilization of the COX1–COX2 joined intermediate (S3), and in a PET100/PET117/MR-1S interaction network preferentially associated with nascent COX2 intermediates (https://doi.org/10.3390/ijms25073814; Mar 2024) (guaragnella2024morethanjust pages 9-11, guaragnella2024morethanjust pages 8-9).

2. Broader principle: coupling mitochondrial gene expression/translation to assembly: A 2024 review emphasizes that many insights on coordination of translation and OXPHOS assembly derive from yeast, including feedback loops linking COX1 translation to assembly intermediates (via Mss51) (https://doi.org/10.1093/hmg/ddae025; published May 2024) (kremer2024coordinatingmitochondrialtranslation pages 2-3, kremer2024coordinatingmitochondrialtranslation pages 1-2). While not PET100-specific, this framework supports the plausibility of late-stage assembly factors (like PET100) influencing the stability of intermediates that feed back on biogenesis.

3. Respiratory supercomplex plasticity and modular incorporation (yeast systems): A 2024 preprint engineered a tethered yeast III2IV2 supercomplex, supporting robust respiration but selectively altering cytosolic-NADH-driven respiration, illustrating that complex III–IV organization can modulate respiratory physiology (https://doi.org/10.1101/2024.12.19.629262; posted Dec 2024) (eldeeb2024bioengineeredyeasttethered pages 1-4). Although PET100 was not tested, this highlights a contemporary direction where complex IV assembly/stability factors may be examined in relation to supercomplex formation and metabolic plasticity.

4. High-resolution yeast supercomplex structure/function (2023): Work in S. pombe resolved a III2–IV supercomplex structure and quantified activities (e.g., CIV activity measured at 300 ± 30 e−/s under their assay conditions), illustrating modern structural/functional approaches for complex IV-containing assemblies (https://doi.org/10.1073/pnas.2307697120; published Nov 2023) (moe2023structureandfunction pages 2-3). This is organism-adjacent (not S. cerevisiae PET100), but methodologically relevant.

6) Current applications and real-world implementations

6.1 Yeast PET100 as a model for human complex IV deficiency

A key applied use of yeast COX assembly genetics is to interpret and validate human pathogenic variants. The 2024 review explicitly frames yeast as instrumental for identifying COX assembly genes and understanding inherited COX deficiencies in humans, including PET100-associated disease (https://doi.org/10.3390/ijms25073814; Mar 2024) (guaragnella2024morethanjust pages 13-14).

In that clinical genetics context, PET100 is highlighted as a mutational target in severe lactic acidosis/Leigh syndrome presentations (reviewed patient series: eight patients in six families with a start-codon null allele; plus an independent truncating mutation in a consanguineous family) (guaragnella2024morethanjust pages 13-14). While this is not yeast functional annotation per se, it is a major real-world implementation of PET100 knowledge: connecting assembly-factor biology to diagnosis and mechanism.

6.2 PET100 as a tool gene for respiratory-chain perturbation

Because PET100 deletion produces a near-COX-null respiratory phenotype while leaving other respiratory carriers relatively intact, PET100 mutants can serve as experimental tools to isolate the consequences of complex IV loss (COX-specific impairment) from broader mitochondrial disruption (church1996cloningandcharacterization pages 8-9, church1996cloningandcharacterization media cab4f922).

7) Expert opinion and analysis (authoritative sources)

• Church et al. (1996) conclude that PET100 is required at a late step in assembly of the active holoenzyme because COX subunits are present in mutant mitochondria but holoenzyme activity and cytochromes a/a3 are missing; they also emphasize COX specificity and rule out a heme A biosynthetic defect via heme supplementation (https://doi.org/10.1074/jbc.271.31.18499; Aug 1996) (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 7-8).

• Guaragnella et al. (2024) emphasize that PET100’s precise molecular mechanism remains to be elucidated, despite its established necessity for assembly and its association with defined subassemblies and late-stage intermediates (https://doi.org/10.3390/ijms25073814; Mar 2024) (guaragnella2024morethanjust pages 13-14).

8) Evidence summary table (data + interpretations)

The following table consolidates primary experimental evidence and separates it from 2024 review-based mechanistic models:

Table: This table summarizes the strongest primary experimental findings for yeast PET100/YDR079W and separates them from later review-based mechanistic models. It is useful for distinguishing directly demonstrated functions and phenotypes from current assembly-pathway inferences.

9) Visual evidence (figures/tables supporting key claims)

• COX activity measurements (Table II) and cytochrome difference spectra (Figure 7) from Church et al. (1996) provide direct quantitative and qualitative evidence of COX loss in pet100 mutants (church1996cloningandcharacterization media cab4f922, church1996cloningandcharacterization media 79137f77).

10) Limitations and gaps (important for functional annotation)

1. Membrane topology and precise submitochondrial localization: The primary PET100 cloning study provides strong prediction-based mitochondrial targeting evidence but does not definitively place Pet100 in the inner mitochondrial membrane or define its orientation; future work or additional primary literature would be needed for a topology-level annotation (church1996cloningandcharacterization pages 8-9).
2. Molecular mechanism: Even in 2024 synthesis, PET100 is discussed as associating with subassemblies and stabilizing late intermediates, but detailed biochemical mechanism (binding interfaces, kinetics, stoichiometry) remains incompletely resolved (guaragnella2024morethanjust pages 13-14).

Key take-home functional annotation (evidence-weighted)

PET100 (YDR079W; UniProt P38958) encodes a small mitochondrially targeted, likely membrane-associated protein that is essential for assembly/biogenesis of cytochrome c oxidase (complex IV) in S. cerevisiae. Loss of PET100 causes respiratory deficiency, near-complete loss of COX enzymatic activity, and absence of assembled cytochromes a/a3, while COX subunit polypeptides remain present—supporting a late-stage assembly/stabilization role rather than a role in subunit synthesis or heme A biosynthesis (church1996cloningandcharacterization pages 1-2, church1996cloningandcharacterization pages 3-4, church1996cloningandcharacterization pages 7-8, church1996cloningandcharacterization media cab4f922).

References

1. (church1996cloningandcharacterization pages 1-2): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

2. (church1996cloningandcharacterization pages 8-9): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

3. (guaragnella2024morethanjust pages 9-11): Nicoletta Guaragnella, T. Cervelli, Bel é m Sampaio-Marques, Chenelle A. Caron-Godon, Emma Collington, Jessica L. Wolf, Genna Coletta, and D. M. Glerum. More than just bread and wine: using yeast to understand inherited cytochrome oxidase deficiencies in humans. International Journal of Molecular Sciences, 25:3814, Mar 2024. URL: https://doi.org/10.3390/ijms25073814, doi:10.3390/ijms25073814. This article has 5 citations.

4. (guaragnella2024morethanjust pages 4-5): Nicoletta Guaragnella, T. Cervelli, Bel é m Sampaio-Marques, Chenelle A. Caron-Godon, Emma Collington, Jessica L. Wolf, Genna Coletta, and D. M. Glerum. More than just bread and wine: using yeast to understand inherited cytochrome oxidase deficiencies in humans. International Journal of Molecular Sciences, 25:3814, Mar 2024. URL: https://doi.org/10.3390/ijms25073814, doi:10.3390/ijms25073814. This article has 5 citations.

5. (church1996cloningandcharacterization pages 2-3): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

6. (sampson2012highthroughputdrug pages 88-89): Liam D P Sampson. High throughput drug discovery in s. cerevisiae: the characterisation of fc-592 and fc-888. ArXiv, 2012. URL: https://doi.org/10.26686/wgtn.17003443.v1, doi:10.26686/wgtn.17003443.v1. This article has 1 citations.

7. (church1996cloningandcharacterization pages 5-6): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

8. (guaragnella2024morethanjust pages 8-9): Nicoletta Guaragnella, T. Cervelli, Bel é m Sampaio-Marques, Chenelle A. Caron-Godon, Emma Collington, Jessica L. Wolf, Genna Coletta, and D. M. Glerum. More than just bread and wine: using yeast to understand inherited cytochrome oxidase deficiencies in humans. International Journal of Molecular Sciences, 25:3814, Mar 2024. URL: https://doi.org/10.3390/ijms25073814, doi:10.3390/ijms25073814. This article has 5 citations.

9. (guaragnella2024morethanjust pages 13-14): Nicoletta Guaragnella, T. Cervelli, Bel é m Sampaio-Marques, Chenelle A. Caron-Godon, Emma Collington, Jessica L. Wolf, Genna Coletta, and D. M. Glerum. More than just bread and wine: using yeast to understand inherited cytochrome oxidase deficiencies in humans. International Journal of Molecular Sciences, 25:3814, Mar 2024. URL: https://doi.org/10.3390/ijms25073814, doi:10.3390/ijms25073814. This article has 5 citations.

10. (church1996cloningandcharacterization pages 3-3): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

11. (church1996cloningandcharacterization pages 3-4): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

12. (church1996cloningandcharacterization media cab4f922): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

13. (church1996cloningandcharacterization media 79137f77): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

14. (church1996cloningandcharacterization pages 7-8): Cynthia Church, Christine Chapon, and Robert O. Poyton. Cloning and characterization of pet100, a gene required for the assembly of yeast cytochrome c oxidase*. The Journal of Biological Chemistry, 271:18499-18507, Aug 1996. URL: https://doi.org/10.1074/jbc.271.31.18499, doi:10.1074/jbc.271.31.18499. This article has 63 citations.

15. (kremer2024coordinatingmitochondrialtranslation pages 2-3): Laura S Kremer and Peter Rehling. Coordinating mitochondrial translation with assembly of the oxphos complexes. Human Molecular Genetics, 33:R47-R52, May 2024. URL: https://doi.org/10.1093/hmg/ddae025, doi:10.1093/hmg/ddae025. This article has 25 citations and is from a domain leading peer-reviewed journal.

16. (kremer2024coordinatingmitochondrialtranslation pages 1-2): Laura S Kremer and Peter Rehling. Coordinating mitochondrial translation with assembly of the oxphos complexes. Human Molecular Genetics, 33:R47-R52, May 2024. URL: https://doi.org/10.1093/hmg/ddae025, doi:10.1093/hmg/ddae025. This article has 25 citations and is from a domain leading peer-reviewed journal.

17. (eldeeb2024bioengineeredyeasttethered pages 1-4): Mazzen H. Eldeeb, Zoe Cosner, Andreas Carlstrom, Jeffri-Noelle Mays, Gabriella F. Rodriguez, Jens Berndtsson, Martin Ott, and Flavia Fontanesi. Bioengineered yeast tethered respiratory supercomplexes reveal mechanisms governing efficient substrate utilization. bioRxiv, Dec 2024. URL: https://doi.org/10.1101/2024.12.19.629262, doi:10.1101/2024.12.19.629262. This article has 0 citations.

18. (moe2023structureandfunction pages 2-3): Agnes Moe, Anna-Roza Dimogkioka, Doron Rapaport, Linda Näsvik Öjemyr, and Peter Brzezinski. Structure and function of the s. pombe iii–iv–cyt c supercomplex. Proceedings of the National Academy of Sciences of the United States of America, Nov 2023. URL: https://doi.org/10.1073/pnas.2307697120, doi:10.1073/pnas.2307697120. This article has 22 citations and is from a highest quality peer-reviewed journal.

Citations

1. church1996cloningandcharacterization pages 8-9
2. guaragnella2024morethanjust pages 9-11
3. guaragnella2024morethanjust pages 8-9
4. guaragnella2024morethanjust pages 13-14
5. church1996cloningandcharacterization pages 3-4
6. church1996cloningandcharacterization pages 7-8
7. eldeeb2024bioengineeredyeasttethered pages 1-4
8. moe2023structureandfunction pages 2-3
9. church1996cloningandcharacterization pages 1-2
10. guaragnella2024morethanjust pages 4-5
11. church1996cloningandcharacterization pages 2-3
12. sampson2012highthroughputdrug pages 88-89
13. church1996cloningandcharacterization pages 5-6
14. church1996cloningandcharacterization pages 3-3
15. kremer2024coordinatingmitochondrialtranslation pages 2-3
16. kremer2024coordinatingmitochondrialtranslation pages 1-2
17. https://doi.org/10.1074/jbc.271.31.18499;
18. https://doi.org/10.3390/ijms25073814;
19. https://doi.org/10.1093/hmg/ddae025;
20. https://doi.org/10.1101/2024.12.19.629262;
21. https://doi.org/10.1073/pnas.2307697120;
22. https://doi.org/10.1074/jbc.271.31.18499
23. https://doi.org/10.3390/ijms25073814
24. https://doi.org/10.1074/jbc.271.31.18499,
25. https://doi.org/10.3390/ijms25073814,
26. https://doi.org/10.26686/wgtn.17003443.v1,
27. https://doi.org/10.1093/hmg/ddae025,
28. https://doi.org/10.1101/2024.12.19.629262,
29. https://doi.org/10.1073/pnas.2307697120,