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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Human TIMM23 (UniProt O14925) — Functional Annotation and Current Evidence (2023–2024 prioritized)

0) Target verification (critical identity check)

The research target is human TIMM23 (gene symbol TIMM23/TIM23), UniProt O14925, annotated as “mitochondrial import inner membrane translocase subunit Tim23” and belonging to the Tim17/Tim22/Tim23 family. A 2024 human-focused structural modeling study explicitly uses hTIMM23 (UniProt O14925) as input for modeling the human core TIM23 translocase, confirming that the literature summarized here concerns the intended protein identity and organism (Homo sapiens). (maruszczak2024structurepredictionanalysis pages 2-3)

1) Key concepts, definitions, and current understanding

1.1 The presequence pathway and the TIM23 (“presequence translocase”) concept

Most mitochondrial proteins are nuclear encoded and must be imported into mitochondria. The TIM23 complex (also called the presequence translocase) is the major inner-membrane translocase for presequence-containing precursor proteins, handling a large fraction of mitochondrial protein biogenesis. Current reviews and primary disease-mechanism work estimate that the TOM–TIM23 route delivers ~60% of the mitochondrial proteome, covering the majority of matrix proteins and many inner membrane proteins (and some IMS proteins). (jain2024hotspotsfordiseasecausing pages 2-4, crameri2024reducedproteinimport pages 1-3, jain2024hotspotsfordiseasecausing pages 1-2)

1.2 TIMM23 molecular role (what TIMM23 “does”)

TIMM23 is a core subunit of the TIM23 inner membrane translocase. It functions in protein translocation/sorting by forming a conserved core with Tim17-family subunits and coordinating with the IMS receptor subunit Tim50 and with accessory modules that determine whether a precursor is:
- fully translocated into the matrix, or
- laterally inserted (stop-transfer) into the inner mitochondrial membrane.
Human TIM23 core composition is typically described as TIMM23 + TIMM17A/B + TIMM50, which dynamically associates with additional factors depending on the substrate and import mode. (crameri2024reducedproteinimport pages 1-3, jain2024hotspotsfordiseasecausing pages 11-12)

1.3 Two operational modes: TIM23MOTOR vs TIM23SORT

Human TIM23 is frequently conceptualized as operating in two functional configurations:
- TIM23MOTOR: coupled to the presequence translocase-associated motor (PAM-like), driving complete translocation into the matrix via ATP-dependent chaperone activity.
- TIM23SORT: enabling lateral release of membrane proteins into the inner membrane.
A 2024 human study of TIM23 dysfunction in TIMM50-associated mitochondrial disease provides a clear, experimentally grounded description of these modules and their component sets. (crameri2024reducedproteinimport pages 1-3, crameri2024reducedproteinimport pages 11-12)

2) Mechanism and pathway placement (best-supported model)

2.1 Core architecture and “channel” concept updated by 2023 structural/mechanistic work

Two 2023 Nature studies in yeast (highly informative for the conserved core mechanism) revise the classical idea that Tim23 alone forms the translocation pore:
- The TIM23 core is supported as a Tim17–Tim23 1:1 heterodimer arranged back-to-back in the idle state, arguing against stable Tim23 homo-oligomeric pore models. (sim2023structuralbasisof pages 1-4)
- Mechanistic mapping of arrested precursors indicates that Tim17 provides the principal lateral transmembrane cavity for presequence translocation; the initiating interaction is driven by conserved negative charges (an acidic patch on the IMS side) that attract positively charged presequences. (fielden2023centralroleof pages 9-11, fielden2023centralroleof pages 11-13, fielden2023centralroleof pages 7-9)

These studies support a model where TIMM23 remains essential but is increasingly interpreted as structural/regulatory within the core, while the primary translocation environment is centered on Tim17-family proteins. (fielden2023centralroleof pages 7-9, sim2023structuralbasisof pages 1-4)

2.2 Human conservation: why yeast data is directly relevant to TIMM23 (O14925)

A 2024 human-focused structure prediction analysis (AlphaFold/ColabFold multimer) models the human core TIM23 using hTIMM23 (O14925) along with TIMM17A or TIMM17B, ROMO1, and TIMM44, and reports that the predicted human core is highly similar to yeast Tim17–Tim23 cryo-EM structures. (maruszczak2024structurepredictionanalysis pages 2-3, maruszczak2024structurepredictionanalysis pages 3-5)

The same work highlights conservation of key functional features implicated by 2023 mechanistic studies (e.g., electrostatic/hydrophobic character of the translocation cavity, including an acidic patch on the IMS side relevant to presequence capture), supporting mechanistic transferability from yeast Tim17/Tim23 to human TIMM17/TIMM23. (maruszczak2024structurepredictionanalysis pages 2-3, maruszczak2024structurepredictionanalysis pages 3-5)

2.3 Key interaction partners for TIMM23 in humans (experiment + expert synthesis)

Recent human disease-mechanism work and a 2024 disease-genetics mini-review converge on the following interacting partners/modules:

Core TIM23 (inner membrane):
- TIMM23 (O14925)
- TIMM17A or TIMM17B (two paralog-based pools)
- TIMM50 (IMS receptor; required for proper complex function)

TIM23MOTOR (matrix translocation):
- TIMM44, HSPA9 (mtHsp70/mortalin), PAM16, GRPEL1/2, and DNAJC co-chaperones (DNAJC19/15) (crameri2024reducedproteinimport pages 1-3, jain2024hotspotsfordiseasecausing pages 2-4)

TIM23SORT (inner membrane insertion):
- TIMM21 and ROMO1 (crameri2024reducedproteinimport pages 1-3)

A key mechanistic point emphasized in expert synthesis is that Tim23–Tim50 interaction is essential for protein translocation, coordinating receptor/channel/motor functions across import steps. (jain2024hotspotsfordiseasecausing pages 11-12)

3) Recent developments (2023–2024) — structures, regulation, and human relevance

3.1 2023: mechanistic “pivot” toward Tim17 as principal translocation cavity

Fielden et al. (Nature, Aug 2023) provide direct evidence that conserved negative charges in Tim17 are essential to initiate translocation; combined mutations strongly impair presequence import while not collapsing membrane potential or TIM22-dependent assembly, supporting a specific TIM23-core functional defect mechanism. (fielden2023centralroleof pages 9-11, fielden2023centralroleof pages 7-9)

Sim et al. (Nature, Jun 2023) support a stable Tim17–Tim23 heterodimer and propose a laterally open Tim17 cavity enclosed by Mgr2 as a plausible translocation route, challenging simplified “aqueous pore by Tim23 alone” models. (sim2023structuralbasisof pages 1-4)

3.2 2024: human core TIM23 architecture and paralog pools (TIMM17A vs TIMM17B)

Maruszczak et al. (FEBS Open Bio, Jun 2024) report two highly similar human core TIM23 populations containing TIMM23 + TIMM17A or TIMM23 + TIMM17B, with high structural similarity to yeast Tim17–Tim23. They propose that functional differences between TIMM17A- and TIMM17B-based translocases likely arise from regulatory factors rather than large structural divergence, and note involvement of ROMO1 as an associated factor in the modeled core. (maruszczak2024structurepredictionanalysis pages 1-2, maruszczak2024structurepredictionanalysis pages 3-5, maruszczak2024structurepredictionanalysis pages 9-11)

3.3 2024: disease genetics focus and mutation “hotspots” in the broader TIM23 system

A 2024 mini-review synthesizing disease-causing variants across the TIM23 system concludes that, among core components, TIMM50 is a prominent hotspot for disease-causing mutations, and that PAM/mortalin (mtHsp70) plus its J-domain regulators are also hotspots. The clinical phenotypes are summarized as predominantly early-age developmental and neurological defects, consistent with essential roles in mitochondrial biogenesis. (jain2024hotspotsfordiseasecausing pages 1-2)

Notably, within the gathered evidence, specific disease-causing variants are emphasized for TIMM50 rather than TIMM23 itself, implying that (as of these sources) TIMM23 may be less frequently reported as a primary Mendelian disease gene compared with TIMM50/PAM components, even though TIMM23 is an essential core subunit. (jain2024hotspotsfordiseasecausing pages 1-2, crameri2024reducedproteinimport pages 1-3)

4) Current applications and real-world implementations

4.1 Translational/clinical implementation: pathway-resolved proteomics + import assays to explain mitochondrial disease

Crameri et al. (Molecular and Cellular Biology, Jun 2024) demonstrate a clinically anchored workflow for mechanistic resolution of mitochondrial disease caused by TIM23-pathway dysfunction:
- patient-derived cells and engineered cell models,
- BN-PAGE assessment of TIM23 complex integrity,
- quantitative proteomics to map proteome vulnerabilities,
- in vitro import assays to separate TIM23MOTOR vs TIM23SORT functional impacts.
This represents a direct real-world implementation of TIM23 biology in mitochondrial disease mechanism discovery. (crameri2024reducedproteinimport pages 1-3, crameri2024reducedproteinimport pages 11-12)

4.2 Structure-guided annotation and hypothesis generation (AlphaFold/ColabFold)

Maruszczak et al. (Jun 2024) exemplify the use of AlphaFold-multimer/ColabFold to model human TIM23 core assemblies with UniProt-defined sequences (including TIMM23 O14925), enabling mapping of conserved functional features and prioritization of regulatory hypotheses for TIMM17A vs TIMM17B-containing complexes. (maruszczak2024structurepredictionanalysis pages 2-3, maruszczak2024structurepredictionanalysis pages 9-11)

5) Quantitative data and statistics (recently reported)

5.1 Proteome fraction handled by TIM23

Recent expert synthesis and primary disease-mechanism work reiterate that the TOM–TIM23 pathway imports ~60% of the mitochondrial proteome, and anchors this estimate to a human mitochondrial proteome of roughly ~1,100–1,500 proteins (13 mtDNA-encoded). (jain2024hotspotsfordiseasecausing pages 1-2, crameri2024reducedproteinimport pages 1-3)

5.2 Module-selective import defects when TIM23 complex integrity is compromised

In TIMM50-associated disease models where TIM23 complex levels/activity are reduced, Crameri et al. quantify in vitro import decreases:
- TIM23MOTOR substrate OTC import reduced to ~82% of control
- TIM23SORT substrates: SURF1 ~67% of control, SCO2 ~62% of control
They also report that TIM22-pathway substrates (n = 58) were largely unchanged, supporting specificity for TIM23 pathway dysfunction. (crameri2024reducedproteinimport pages 11-12)

These measurements provide an experimentally grounded, quantitative view of how disruption of a core TIM23 component (TIMM50) propagates to functional impairment of the TIMM23-containing translocase and reveals substrate-class sensitivity. (crameri2024reducedproteinimport pages 11-12)

6) Expert opinion and integrative analysis (authoritative synthesis)

6.1 Emerging consensus model for TIMM23’s role

Integrating 2023 structure/mechanism papers and 2024 human modeling and disease analyses supports the following interpretation:
1) TIMM23 is essential within the TIM23 presequence translocase core, but Tim17-family proteins appear to provide the dominant translocation cavity driven by conserved electrostatics (negative charges). (fielden2023centralroleof pages 9-11, fielden2023centralroleof pages 7-9, sim2023structuralbasisof pages 1-4)
2) TIMM23 likely plays a structural/regulatory role within the heterodimeric core and in coordinating accessory modules, consistent with the back-to-back heterodimer architecture and the difficulty of reconciling Tim23-only pore models with native structural observations. (sim2023structuralbasisof pages 1-4, fielden2023centralroleof pages 7-9)
3) In humans, the presence of two paralog-based cores (TIMM17A vs TIMM17B) suggests that regulation (stress responsiveness, complex stability, accessory binding) may tune import capacity without major remodeling of TIMM23 itself. (maruszczak2024structurepredictionanalysis pages 3-5, maruszczak2024structurepredictionanalysis pages 9-11)

6.2 Disease perspective: why TIMM23 still matters even when TIMM50 is the “hotspot”

The 2024 review framing TIMM50 as a mutation hotspot, and the 2024 patient-centered TIMM50 study, both emphasize that mutations in one TIM23 component can reduce the steady-state levels/activity of the overall complex (including TIMM23), producing multisystem mitochondrial pathology—thus TIMM23 function is clinically relevant even when TIMM23 is not the primary mutated gene. (jain2024hotspotsfordiseasecausing pages 1-2, crameri2024reducedproteinimport pages 1-3, crameri2024reducedproteinimport pages 11-12)

7) Visual evidence (human core TIM23 figures)

The following figures from the 2024 human modeling study illustrate the subunit set of the human TIM23 complex and structural context for ROMO1 and the TIMM17 paralog variants, providing a visual anchor for TIMM23-centered functional annotation. (maruszczak2024structurepredictionanalysis media e620fbb9, maruszczak2024structurepredictionanalysis media 460c7670, maruszczak2024structurepredictionanalysis media 2ee6cbee)

Summary table (evidence-backed)

Table: This table summarizes the supported functional annotation of human TIMM23 (UniProt O14925), emphasizing localization, molecular role in the TIM23 complex, recent 2023-2024 mechanistic insights, disease relevance, and quantitative findings. It is useful as a concise evidence-backed overview for report writing or annotation review.

Key references (with publication date and URL)

• Sim SI et al. “Structural basis of mitochondrial protein import by the TIM23 complex.” Nature (Jun 2023). https://doi.org/10.1038/s41586-023-06239-6 (sim2023structuralbasisof pages 1-4)
• Fielden LF et al. “Central role of Tim17 in mitochondrial presequence protein translocation.” Nature (Aug 2023). https://doi.org/10.1038/s41586-023-06477-8 (fielden2023centralroleof pages 9-11)
• Maruszczak KK et al. “Structure prediction analysis of human core TIM23 complex reveals conservation of the protein translocation mechanism.” FEBS Open Bio (Jun 2024). https://doi.org/10.1002/2211-5463.13840 (maruszczak2024structurepredictionanalysis pages 2-3)
• Crameri JJ et al. “Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease.” Molecular and Cellular Biology (Jun 2024). https://doi.org/10.1080/10985549.2024.2353652 (crameri2024reducedproteinimport pages 11-12)
• Jain S et al. “Hotspots for Disease-Causing Mutations in the Mitochondrial TIM23 Import Complex.” Genes (Nov 2024). https://doi.org/10.3390/genes15121534 (jain2024hotspotsfordiseasecausing pages 1-2)

References

1. (maruszczak2024structurepredictionanalysis pages 2-3): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

2. (jain2024hotspotsfordiseasecausing pages 2-4): Sahil Jain, Eyal Paz, and Abdussalam Azem. Hotspots for disease-causing mutations in the mitochondrial tim23 import complex. Genes, 15:1534, Nov 2024. URL: https://doi.org/10.3390/genes15121534, doi:10.3390/genes15121534. This article has 1 citations.

3. (crameri2024reducedproteinimport pages 1-3): Jordan J. Crameri, Catherine S. Palmer, Tegan Stait, Thomas D. Jackson, Matthew Lynch, Adriane Sinclair, Leah E. Frajman, Alison G. Compton, David Coman, David R. Thorburn, Ann E. Frazier, and Diana Stojanovski. Reduced protein import via tim23 sort drives disease pathology in timm50-associated mitochondrial disease. Molecular and Cellular Biology, 44:226-244, Jun 2024. URL: https://doi.org/10.1080/10985549.2024.2353652, doi:10.1080/10985549.2024.2353652. This article has 9 citations and is from a domain leading peer-reviewed journal.

4. (jain2024hotspotsfordiseasecausing pages 1-2): Sahil Jain, Eyal Paz, and Abdussalam Azem. Hotspots for disease-causing mutations in the mitochondrial tim23 import complex. Genes, 15:1534, Nov 2024. URL: https://doi.org/10.3390/genes15121534, doi:10.3390/genes15121534. This article has 1 citations.

5. (jain2024hotspotsfordiseasecausing pages 11-12): Sahil Jain, Eyal Paz, and Abdussalam Azem. Hotspots for disease-causing mutations in the mitochondrial tim23 import complex. Genes, 15:1534, Nov 2024. URL: https://doi.org/10.3390/genes15121534, doi:10.3390/genes15121534. This article has 1 citations.

6. (crameri2024reducedproteinimport pages 11-12): Jordan J. Crameri, Catherine S. Palmer, Tegan Stait, Thomas D. Jackson, Matthew Lynch, Adriane Sinclair, Leah E. Frajman, Alison G. Compton, David Coman, David R. Thorburn, Ann E. Frazier, and Diana Stojanovski. Reduced protein import via tim23 sort drives disease pathology in timm50-associated mitochondrial disease. Molecular and Cellular Biology, 44:226-244, Jun 2024. URL: https://doi.org/10.1080/10985549.2024.2353652, doi:10.1080/10985549.2024.2353652. This article has 9 citations and is from a domain leading peer-reviewed journal.

7. (sim2023structuralbasisof pages 1-4): Sue Im Sim, Yuanyuan Chen, Diane L. Lynch, James C. Gumbart, and Eunyong Park. Structural basis of mitochondrial protein import by the tim23 complex. Nature, 621:620-626, Jun 2023. URL: https://doi.org/10.1038/s41586-023-06239-6, doi:10.1038/s41586-023-06239-6. This article has 105 citations and is from a highest quality peer-reviewed journal.

8. (fielden2023centralroleof pages 9-11): Laura F. Fielden, Jakob D. Busch, Sandra G. Merkt, Iniyan Ganesan, Conny Steiert, Hanna B. Hasselblatt, Jon V. Busto, Christophe Wirth, Nicole Zufall, Sibylle Jungbluth, Katja Noll, Julia M. Dung, Ludmila Butenko, Karina von der Malsburg, Hans-Georg Koch, Carola Hunte, Martin van der Laan, and Nils Wiedemann. Central role of tim17 in mitochondrial presequence protein translocation. Nature, 621:627-634, Aug 2023. URL: https://doi.org/10.1038/s41586-023-06477-8, doi:10.1038/s41586-023-06477-8. This article has 64 citations and is from a highest quality peer-reviewed journal.

9. (fielden2023centralroleof pages 11-13): Laura F. Fielden, Jakob D. Busch, Sandra G. Merkt, Iniyan Ganesan, Conny Steiert, Hanna B. Hasselblatt, Jon V. Busto, Christophe Wirth, Nicole Zufall, Sibylle Jungbluth, Katja Noll, Julia M. Dung, Ludmila Butenko, Karina von der Malsburg, Hans-Georg Koch, Carola Hunte, Martin van der Laan, and Nils Wiedemann. Central role of tim17 in mitochondrial presequence protein translocation. Nature, 621:627-634, Aug 2023. URL: https://doi.org/10.1038/s41586-023-06477-8, doi:10.1038/s41586-023-06477-8. This article has 64 citations and is from a highest quality peer-reviewed journal.

10. (fielden2023centralroleof pages 7-9): Laura F. Fielden, Jakob D. Busch, Sandra G. Merkt, Iniyan Ganesan, Conny Steiert, Hanna B. Hasselblatt, Jon V. Busto, Christophe Wirth, Nicole Zufall, Sibylle Jungbluth, Katja Noll, Julia M. Dung, Ludmila Butenko, Karina von der Malsburg, Hans-Georg Koch, Carola Hunte, Martin van der Laan, and Nils Wiedemann. Central role of tim17 in mitochondrial presequence protein translocation. Nature, 621:627-634, Aug 2023. URL: https://doi.org/10.1038/s41586-023-06477-8, doi:10.1038/s41586-023-06477-8. This article has 64 citations and is from a highest quality peer-reviewed journal.

11. (maruszczak2024structurepredictionanalysis pages 3-5): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

12. (maruszczak2024structurepredictionanalysis pages 1-2): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

13. (maruszczak2024structurepredictionanalysis pages 9-11): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

14. (maruszczak2024structurepredictionanalysis media e620fbb9): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

15. (maruszczak2024structurepredictionanalysis media 460c7670): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

16. (maruszczak2024structurepredictionanalysis media 2ee6cbee): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

17. (maruszczak2024structurepredictionanalysis pages 11-12): Klaudia K. Maruszczak, Piotr Draczkowski, Artur Wnorowski, and Agnieszka Chacinska. Structure prediction analysis of human core tim23 complex reveals conservation of the protein translocation mechanism. FEBS Open Bio, 14:1656-1667, Jun 2024. URL: https://doi.org/10.1002/2211-5463.13840, doi:10.1002/2211-5463.13840. This article has 13 citations and is from a peer-reviewed journal.

Citations

1. maruszczak2024structurepredictionanalysis pages 2-3
2. sim2023structuralbasisof pages 1-4
3. crameri2024reducedproteinimport pages 1-3
4. jain2024hotspotsfordiseasecausing pages 11-12
5. jain2024hotspotsfordiseasecausing pages 1-2
6. crameri2024reducedproteinimport pages 11-12
7. fielden2023centralroleof pages 9-11
8. jain2024hotspotsfordiseasecausing pages 2-4
9. fielden2023centralroleof pages 11-13
10. fielden2023centralroleof pages 7-9
11. maruszczak2024structurepredictionanalysis pages 3-5
12. maruszczak2024structurepredictionanalysis pages 1-2
13. maruszczak2024structurepredictionanalysis pages 9-11
14. maruszczak2024structurepredictionanalysis pages 11-12
15. https://doi.org/10.1002/2211-5463.13840;
16. https://doi.org/10.3390/genes15121534
17. https://doi.org/10.3390/genes15121534;
18. https://doi.org/10.1080/10985549.2024.2353652
19. https://doi.org/10.1080/10985549.2024.2353652;
20. https://doi.org/10.1002/2211-5463.13840
21. https://doi.org/10.1038/s41586-023-06239-6;
22. https://doi.org/10.1038/s41586-023-06477-8
23. https://doi.org/10.1038/s41586-023-06239-6
24. https://doi.org/10.1002/2211-5463.13840,
25. https://doi.org/10.3390/genes15121534,
26. https://doi.org/10.1080/10985549.2024.2353652,
27. https://doi.org/10.1038/s41586-023-06239-6,
28. https://doi.org/10.1038/s41586-023-06477-8,