Thinking Trace

I begin with the InterPro architecture. Three overlapping family signatures—IPR016435 (Diphthamide synthesis DPH1/DPH2 family, residues 2–490), IPR010014 (Diphthamide synthesis DHP2 family, residues 20–485), and IPR016435 (DPH1/DPH2 family, residues 29–484)—span essentially the full polypeptide, indicating a conserved, non-enzymatic adaptor specialized for the diphthamide pathway. Within this scaffold, two homologous-superfamily modules are resolved: IPR042263 (DPH1/DPH2, domain 1, residues 35–126) and IPR042265 (DPH1/DPH2, domain 3, residues 264–366). Additional family-level matches (IPR016435 [54–377]) reinforce that the central body of the protein is devoted to this adaptor role rather than catalysis. The absence of catalytic domain signatures and the dominance of DPH1/DPH2-family scaffolding motifs argue that this protein’s primary molecular function is to bind other proteins and organize a redox-coupled transfer reaction rather than to perform the chemistry itself.

This domain layout causes a specific molecular function: it creates a multivalent platform that binds the radical-SAM enzyme DPH1 and the electron-delivery component DPH3, and positions the histidine target on eEF2. Such scaffolding necessarily entails GO:0005515 protein binding as a core activity. The DPH1/DPH2 adaptor stabilizes the DPH1 active site, aligns the [4Fe–4S]-dependent radical generation with the eEF2 histidine, and couples electron flow from NADH via cytosolic ferredoxin and ferredoxin reductase to the DPH1 radical chemistry. Because the adaptor does not house the catalytic iron–sulfur cluster or the radical chemistry, its contribution is to protein–protein recognition and spatial organization of the electron-transfer chain.

From this molecular function, the biological process follows. By enabling the first step of diphthamide formation on eEF2—removal of the 3-amino-3-deoxy ribose on His1a and creation of a 3-(3-amino-3-carboxypropyl)histidine—the adaptor initiates a post-translational modification that tunes translation elongation fidelity and modulates susceptibility to ADP-ribosylating toxins. This places the protein in the diphthamide biosynthetic process (inferred as GO:0017183). In vertebrates, proper eEF2 modification influences tissue morphogenesis and extracellular matrix production; perturbation of this pathway can manifest as defects in skeletal and cartilage development, which rationalizes involvement in GO:0051216 cartilage development.

The cellular component is dictated by where eEF2 resides and where ferredoxin-coupled redox partners operate. The adaptor must access cytosolic eEF2 and the cytosolic ferredoxin/reductase chain, supporting localization to the GO:0005737 cytoplasm. A nuclear pool is also plausible because eEF2 shuttles and certain assembly or quality-control steps can occur near chromatin-associated translation factors; the scaffold’s solubility and lack of transmembrane features are consistent with a nucleocytoplasmic distribution, including the GO:0005634 nucleus.

Mechanistically, the adaptor forms a ternary complex with DPH1 and DPH3, recruits reduced ferredoxin generated by ferredoxin reductase (NADH-dependent), and docks eEF2 so that DPH1’s radical chemistry can proceed on His1a. Downstream enzymes—DPH5, DPH6, DPH7, and the amidoligase (Dph8/DnaJ family in some systems)—complete the maturation to diphthamide. The listed partners align with this model: DPH3 (electron carrier), DPH5/DPH6/DPH7 (later pathway enzymes), and diphthine–ammonia ligase (Dph8) for the final ligation/processing steps. Multiple eEF2 paralogs (eukaryotic translation elongation factor 2 and its like/tandem-duplicate variants) are the direct substrates that the adaptor presents to the radical machinery. A DnaJ/Hsp40 homolog likely assists folding or assembly of the complex, stabilizing the iron–sulfur enzyme and its scaffold during electron transfer cycles. Together, this architecture and partner set produce a controlled, redox-driven modification of eEF2 that impacts translational fidelity and, secondarily, developmental programs such as cartilage formation.

## Functional Summary

A nucleocytoplasmic adaptor that organizes the first step of the diphthamide modification on the histidine of translation elongation factor 2. It binds the radical-generating enzyme and the ferredoxin-based electron-delivery system, aligns eEF2 for precise chemistry, and thereby enables formation of the amino–aldehyde side chain on the target histidine. By ensuring efficient eEF2 modification, it supports accurate translation and influences developmental programs, including cartilage formation.

## UniProt Summary

Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 together assist the reaction catalyzed by DPH1, which transfers a 3-amino-3-deoxy sugar from eEF2 to an active site histidine residue, forming a 3-(3-amino-3-carboxypropyl)histidine residue. DPH1 is a radical-SAM protein and its catalytic cycle is dependent on electron transfer from NADH via FDXR (ferredoxin reductase) and FDX1 (ferredoxin). DPH2 is not a radical-SAM protein but is required for the reaction and probably acts by binding to DPH1 and eEF2 to facilitate the reaction (By similarity).

## InterPro Domains

    - IPR016435: Diphthamide synthesis DPH1/DPH2 (family) [2-490]
- IPR010014: Diphthamide synthesis DHP2 (family) [20-485]
- IPR016435: Diphthamide synthesis DPH1/DPH2 (family) [29-484]
- IPR016435: Diphthamide synthesis DPH1/DPH2 (family) [33-366]
- IPR042263: Diphthamide synthesis DPH1/DPH2, domain 1 (homologous_superfamily) [35-126]
- IPR016435: Diphthamide synthesis DPH1/DPH2 (family) [54-377]
- IPR042265: Diphthamide synthesis DPH1/DPH2, domain 3 (homologous_superfamily) [264-366]

## GO Term Predictions

### Molecular Function


### Biological Process


### Cellular Component

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: dph2 / DPH2 (Danio rerio; UniProt A4QN59) — functional annotation via conserved diphthamide biosynthesis biology

0) Target verification and scope control (critical)

The user-specified zebrafish protein DPH2 (UniProt A4QN59; gene dph2; ORFName zgc:162269) is annotated as “2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 / diphthamide biosynthesis protein 2”, belonging to the DPH1/DPH2 family (DPH2 subfamily). Within the retrieved scientific corpus, I did not find zebrafish-specific primary studies explicitly naming UniProt A4QN59 or zgc:162269; therefore, organism-specific phenotypes or expression patterns for zebrafish are not asserted here. Functional statements are based on highly conserved, mechanistically characterized eukaryotic/archaeal DPH2 homologs, which is appropriate given the strong conservation of the diphthamide biosynthesis pathway from archaea to humans. (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4)

1) Key concepts and definitions (current understanding)

1.1 Diphthamide (the modified residue)

Diphthamide is a post-translationally modified histidine that occurs exclusively on eukaryotic translation elongation factor 2 (eEF2) and is the molecular target of diphtheria toxin–family ADP-ribosylating toxins. Cells lacking diphthamide are toxin-resistant because the toxin substrate is absent. (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4)

1.2 DPH2 as a core enzyme in diphthamide biosynthesis

DPH2 (together with DPH1) functions in the first committed step of diphthamide biosynthesis: transfer of a 3-amino-3-carboxypropyl (ACP) group derived from S-adenosylmethionine (SAM/AdoMet) onto the C2 of the imidazole ring of a conserved eEF2 histidine. This ACP addition generates an early diphthamide-pathway intermediate on eEF2. (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4, utkur2023dph1anddph2 pages 1-2)

1.3 Pathway overview (DPH1–DPH7)

A foundational pathway outline (originally developed through yeast genetics and conserved across eukaryotes) is: (i) ACP transfer to eEF2 histidine; (ii) trimethylation to form diphthine; (iii) final amidation to yield mature diphthamide. (liu2004identificationofthe pages 1-2) More recent pathway summaries add defined roles for DPH6/DPH7 in the final maturation steps. (zhao2024lossofdiphthamide pages 1-2, utkur2023dph1anddph2 pages 1-2)

Table: This table summarizes the diphthamide biosynthesis pathway with emphasis on the DPH2-containing first step, the enzymes involved across DPH1-7, the reaction chemistry and cofactors, and key recent and foundational citations. It is useful as a compact reference for functional annotation of DPH2 and its pathway context.

2) Primary function of DPH2: reaction, substrate specificity, and mechanism

2.1 Chemical reaction catalyzed (first step)

The DPH2-containing enzyme system catalyzes ACP transfer from SAM to eEF2 histidine, initiating diphthamide formation. This is described explicitly as transfer of the 3-amino-3-carboxypropyl group of SAM/AdoMet to the imidazole C2 of the precursor histidine residue in eEF2. (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4, utkur2023dph1anddph2 pages 1-2)

Substrates (core): SAM/AdoMet and eEF2 (target histidine). (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4)

Key products/byproducts (mechanistic signatures): In archaeal Dph2 biochemistry, SAM cleavage yields 5′-deoxy-5′-methylthioadenosine (MTA) plus an ACP radical, rather than the 5′-deoxyadenosyl radical typical of canonical radical-SAM enzymes. (su2013thebiosynthesisand pages 3-4, su2013thediscoveryand pages 16-21)

2.2 Enzyme class and cofactors: noncanonical radical-SAM-like Fe–S chemistry

Mechanistic work (reviewing archaeal biochemistry and mapping to eukaryotes) supports that DPH2 functions as part of an iron–sulfur (Fe–S) enzyme system that generates an organic radical required for C–C bond formation in the ACP transfer reaction. (su2013thebiosynthesisand pages 10-14, su2013thebiosynthesisand pages 3-4)

A key modern framing is that the Dph1•Dph2 catalytic module constitutes a non-canonical radical SAM enzyme: it uses Fe–S clusters but does not rely on the canonical CX3CX2C motif and does not generate the classical 5′-deoxyadenosyl radical; instead it generates an ACP radical from SAM cleavage that is then used to functionalize eEF2 histidine. (su2013thebiosynthesisand pages 3-4, utkur2024functionalintegrityof pages 1-2)

2.3 Protein partners and complex architecture

In eukaryotes, DPH2 is functionally coupled to DPH1 (forming a heterodimeric core) and requires accessory proteins for efficient catalysis.

• DPH1–DPH2 partnership: Dph1 and Dph2 are homologous and are thought to form a heterodimer that is functionally analogous to archaeal homodimeric Dph2. (su2013thebiosynthesisand pages 3-4)
• DPH3 as electron donor: Dph3 can interact with the Dph1–Dph2 complex and is suggested to mediate electron transfer needed for catalysis. (su2013thebiosynthesisand pages 3-4)
• DPH4 and additional machinery: Modern pathway summaries indicate the initial step is catalyzed by an Fe–S DPH1/DPH2 heterodimer, with involvement of DPH3/DPH4 in supporting the reaction. (utkur2023dph1anddph2 pages 1-2, zhao2024lossofdiphthamide pages 1-2)

3) Subcellular localization and where DPH2 acts

Direct localization evidence in zebrafish was not retrieved. However, diphthamide is a modification on the cytosolic translation factor eEF2, so the pathway is expected to act in the cytosol.

Experimental evidence from plants supports this expectation: Arabidopsis DPH2 localizes to the cytosol and physically interacts with DPH1, consistent with a cytosolic biosynthetic complex acting on cytosolic eEF2. (zhang2025diphthamideformationin pages 1-4)

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

4.1 2024: Motif-level and cofactor-binding advances in DPH2-containing Dph1•Dph2

A 2024 study identified conserved tandem cysteine motifs (TCMs) adjacent to the noncanonical Fe–S binding motifs in Dph1 and Dph2, and showed these cysteines are required for full enzymatic activity and dimer stability. Combined substitution of adjacent cysteines in Dph2 (e.g., double substitution in the Dph2 TCM) nearly abolishes activity, and replacing key cysteine ligands accelerates degradation of both subunits—supporting a tight linkage between cofactor integrity and complex stability. (utkur2024functionalintegrityof pages 1-2, utkur2024functionalintegrityof pages 2-4)

These data refine current understanding of how DPH2 (within Dph1•Dph2) binds and maintains Fe–S cofactors in a noncanonical radical-SAM-like context. (utkur2024functionalintegrityof pages 1-2)

4.2 2023: Human DPH2 variant functionalization and disease susceptibility alleles

A 2023 Disease Models & Mechanisms paper functionally tested DPH1/DPH2 missense alleles and identified two human DPH2 variants (H105P, C341Y) with reduced function in diphthamide synthesis assays, supporting their classification as deficiency-susceptibility alleles. This provides contemporary genotype-to-biochemistry mapping and illustrates which conserved residues in DPH2 are particularly critical for activity. (utkur2023dph1anddph2 pages 1-2, utkur2023dph1anddph2 pages 4-5)

4.3 2024: New cellular roles—translation fidelity linked to replication stress via frameshifting

A 2024 ACS Central Science study connected diphthamide deficiency to DNA replication stress by showing that diphthamide modulates translation of RRM1 via −1 frameshifting, and that dysregulated RRM1 translation is causally linked to elevated replication stress in diphthamide-deficient mammalian cells. The paper emphasizes diphthamide’s role in restraining spurious frameshifting and maintaining translational fidelity, expanding the functional consequences of the DPH2-controlled pathway beyond toxin susceptibility. (zhao2024lossofdiphthamide pages 1-2)

5) Current applications and real-world implementations

5.1 Toxin biology and engineered toxins (conceptual/biomedical relevance)

Because diphthamide on eEF2 is the substrate for diphtheria toxin–like ADP-ribosylating toxins, DPH2 pathway status is directly relevant to toxin susceptibility/resistance at the cellular level. This principle underlies experimental systems in which loss of diphthamide biosynthesis confers resistance to toxins and can be used as a selection readout for pathway integrity. (liu2004identificationofthe pages 1-2, utkur2024functionalintegrityof pages 1-2)

5.2 Human genetics and diagnostic interpretation

Functional assays that quantify diphthamide synthesis (or toxin sensitivity) are used to interpret whether human DPH2 variants are likely pathogenic or hypomorphic, informing clinical genetics of diphthamide deficiency syndrome and related ribosomopathies. (utkur2023dph1anddph2 pages 1-2, utkur2023dph1anddph2 pages 4-5)

6) Expert opinions and authoritative synthesis (reviews and consensus framing)

A widely cited 2013 Critical Reviews in Biochemistry and Molecular Biology review frames DPH2 (via archaeal Dph2 biochemistry) as an unusual radical-SAM-type Fe–S enzyme that generates an ACP radical (rather than 5′-dAdo•) to drive the first step of diphthamide biosynthesis, and emphasizes outstanding mechanistic questions that continued to motivate subsequent structural and biochemical work. (su2013thebiosynthesisand pages 3-4, su2013thebiosynthesisand pages 10-14)

7) Relevant statistics and data (from recent studies)

• Human variant counts with reduced function (2023): The 2023 study identified 2 DPH2 missense variants (H105P and C341Y) with strongly/significantly reduced diphthamide synthase activity in cell/yeast assays. (utkur2023dph1anddph2 pages 1-2, utkur2023dph1anddph2 pages 4-5)
• Qualitative effect sizes (2024 motif study): Combined substitutions in Dph2 tandem cysteines “almost entirely” inactivate Dph1•Dph2 activity and accelerate subunit decay (qualitative, not a numeric metric in the retrieved excerpt). (utkur2024functionalintegrityof pages 2-4)
• Replication-stress connection (2024): The 2024 ACS Central Science paper reports a mechanistic link between diphthamide loss, −1 frameshifting, altered RRM1 translation, and elevated replication stress, but numeric values (e.g., frameshift frequency changes or quantitative replication stress markers) are not present in the retrieved excerpt and would require deeper extraction from the full text. (zhao2024lossofdiphthamide pages 1-2)

8) Summary functional annotation for zebrafish dph2 (A4QN59)

Most supported primary molecular function (high-confidence by homology): zebrafish Dph2 is expected to be a Fe–S-dependent, noncanonical radical-SAM-like enzyme subunit that—together with Dph1—catalyzes the first committed step of diphthamide biosynthesis on eEF2: ACP transfer from SAM to the conserved eEF2 histidine. (liu2004identificationofthe pages 1-2, su2013thebiosynthesisand pages 3-4, utkur2024functionalintegrityof pages 1-2)

Likely cellular compartment: cytosol, consistent with cytosolic eEF2 as substrate and supported by experimental cytosolic localization of plant DPH2. (zhang2025diphthamideformationin pages 1-4)

Likely pathway membership: DPH1–DPH7 diphthamide biosynthesis pathway, supporting translational fidelity (frameshift suppression) and influencing downstream cellular stress phenotypes when perturbed. (zhao2024lossofdiphthamide pages 1-2, utkur2023dph1anddph2 pages 9-10)

Key cited sources (with publication dates and URLs)

• Liu et al. “Identification of the proteins required for biosynthesis of diphthamide…” Molecular and Cellular Biology (Published 2004-11). https://doi.org/10.1128/mcb.24.21.9487-9497.2004 (liu2004identificationofthe pages 1-2)
• Su et al. “The biosynthesis and biological function of diphthamide” Critical Reviews in Biochemistry and Molecular Biology (Published 2013-11). https://doi.org/10.3109/10409238.2013.831023 (su2013thebiosynthesisand pages 3-4, su2013thebiosynthesisand pages 10-14)
• Ütkür et al. “DPH1 and DPH2 variants…” Disease Models & Mechanisms (Published 2023-09). https://doi.org/10.1242/dmm.050207 (utkur2023dph1anddph2 pages 1-2, utkur2023dph1anddph2 pages 4-5)
• Ütkür et al. “Functional Integrity of Radical SAM Enzyme Dph1•Dph2…” Biomolecules (Published 2024-04). https://doi.org/10.3390/biom14040470 (utkur2024functionalintegrityof pages 1-2, utkur2024functionalintegrityof pages 2-4)
• Zhao et al. “Loss of Diphthamide Increases DNA Replication Stress…” ACS Central Science (Published 2024-09). https://doi.org/10.1021/acscentsci.4c00967 (zhao2024lossofdiphthamide pages 1-2)

References

1. (liu2004identificationofthe pages 1-2): Shihui Liu, G. Todd Milne, Jeffrey G. Kuremsky, Gerald R. Fink, and Stephen H. Leppla. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial adp-ribosylating toxins on translation elongation factor 2. Molecular and Cellular Biology, 24:9487-9497, Nov 2004. URL: https://doi.org/10.1128/mcb.24.21.9487-9497.2004, doi:10.1128/mcb.24.21.9487-9497.2004. This article has 204 citations and is from a domain leading peer-reviewed journal.

2. (su2013thebiosynthesisand pages 3-4): Xiaoyang Su, Zhewang Lin, and Hening Lin. The biosynthesis and biological function of diphthamide. Critical Reviews in Biochemistry and Molecular Biology, 48:515-521, Nov 2013. URL: https://doi.org/10.3109/10409238.2013.831023, doi:10.3109/10409238.2013.831023. This article has 94 citations and is from a peer-reviewed journal.

3. (utkur2023dph1anddph2 pages 1-2): Koray Ütkür, Klaus Mayer, Maliha Khan, Thirishika Manivannan, Raffael Schaffrath, and Ulrich Brinkmann. Dph1 and dph2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models. Disease Models & Mechanisms, Sep 2023. URL: https://doi.org/10.1242/dmm.050207, doi:10.1242/dmm.050207. This article has 9 citations and is from a domain leading peer-reviewed journal.

4. (zhao2024lossofdiphthamide pages 1-2): Jiaqi Zhao, Byunghyun Ahn, and Hening Lin. Loss of diphthamide increases dna replication stress in mammalian cells by modulating the translation of rrm1. ACS Central Science, 10:1835-1847, Sep 2024. URL: https://doi.org/10.1021/acscentsci.4c00967, doi:10.1021/acscentsci.4c00967. This article has 5 citations and is from a highest quality peer-reviewed journal.

5. (su2013thediscoveryand pages 16-21): X Su. The discovery and functional studies of two diphthamide biosynthetic genes. Unknown journal, 2013.

6. (su2013thediscoveryand pages 108-116): X Su. The discovery and functional studies of two diphthamide biosynthetic genes. Unknown journal, 2013.

7. (utkur2024functionalintegrityof pages 1-2): Koray Ütkür, Klaus Mayer, Shihui Liu, Ulrich Brinkmann, and Raffael Schaffrath. Functional integrity of radical sam enzyme dph1•dph2 requires non-canonical cofactor motifs with tandem cysteines. Biomolecules, Apr 2024. URL: https://doi.org/10.3390/biom14040470, doi:10.3390/biom14040470. This article has 1 citations.

8. (utkur2024functionalintegrityof pages 2-4): Koray Ütkür, Klaus Mayer, Shihui Liu, Ulrich Brinkmann, and Raffael Schaffrath. Functional integrity of radical sam enzyme dph1•dph2 requires non-canonical cofactor motifs with tandem cysteines. Biomolecules, Apr 2024. URL: https://doi.org/10.3390/biom14040470, doi:10.3390/biom14040470. This article has 1 citations.

9. (utkur2023dph1anddph2 pages 9-10): Koray Ütkür, Klaus Mayer, Maliha Khan, Thirishika Manivannan, Raffael Schaffrath, and Ulrich Brinkmann. Dph1 and dph2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models. Disease Models & Mechanisms, Sep 2023. URL: https://doi.org/10.1242/dmm.050207, doi:10.1242/dmm.050207. This article has 9 citations and is from a domain leading peer-reviewed journal.

10. (su2013thebiosynthesisand pages 10-14): Xiaoyang Su, Zhewang Lin, and Hening Lin. The biosynthesis and biological function of diphthamide. Critical Reviews in Biochemistry and Molecular Biology, 48:515-521, Nov 2013. URL: https://doi.org/10.3109/10409238.2013.831023, doi:10.3109/10409238.2013.831023. This article has 94 citations and is from a peer-reviewed journal.

11. (zhang2025diphthamideformationin pages 1-4): Hongliang Zhang, Nadežda Janina, Koray Ütkür, Thirishika Manivannan, Lei Zhang, Lizhen Wang, Christopher Grefen, Raffael Schaffrath, and Ute Krämer. Diphthamide formation in arabidopsis requires dph1-interacting dph2 for light and oxidative stress resistance. Sep 2025. URL: https://doi.org/10.1101/2024.09.16.613322, doi:10.1101/2024.09.16.613322. This article has 2 citations.

12. (utkur2023dph1anddph2 pages 4-5): Koray Ütkür, Klaus Mayer, Maliha Khan, Thirishika Manivannan, Raffael Schaffrath, and Ulrich Brinkmann. Dph1 and dph2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models. Disease Models & Mechanisms, Sep 2023. URL: https://doi.org/10.1242/dmm.050207, doi:10.1242/dmm.050207. This article has 9 citations and is from a domain leading peer-reviewed journal.

Artifacts

• Edison artifact artifact-00

Citations

1. liu2004identificationofthe pages 1-2
2. su2013thebiosynthesisand pages 3-4
3. zhang2025diphthamideformationin pages 1-4
4. utkur2024functionalintegrityof pages 1-2
5. zhao2024lossofdiphthamide pages 1-2
6. utkur2024functionalintegrityof pages 2-4
7. su2013thediscoveryand pages 16-21
8. su2013thediscoveryand pages 108-116
9. su2013thebiosynthesisand pages 10-14
10. https://doi.org/10.1128/mcb.24.21.9487-9497.2004;
11. https://doi.org/10.3109/10409238.2013.831023;
12. https://doi.org/10.1242/dmm.050207
13. https://doi.org/10.3109/10409238.2013.831023
14. https://doi.org/10.3390/biom14040470
15. https://doi.org/10.1242/dmm.050207;
16. https://doi.org/10.1021/acscentsci.4c00967
17. https://doi.org/10.1021/acscentsci.4c00967;
18. https://doi.org/10.1128/mcb.24.21.9487-9497.2004
19. https://doi.org/10.1128/mcb.24.21.9487-9497.2004,
20. https://doi.org/10.3109/10409238.2013.831023,
21. https://doi.org/10.1242/dmm.050207,
22. https://doi.org/10.1021/acscentsci.4c00967,
23. https://doi.org/10.3390/biom14040470,
24. https://doi.org/10.1101/2024.09.16.613322,