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gene_id: GLYCTK
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uniprot_accession: Q8IVS8
protein_description: 'RecName: Full=Glycerate kinase; EC=2.7.1.31 {ECO:0000269|PubMed:16753811,
ECO:0000269|PubMed:20949620}; AltName: Full=HBeAg-binding protein 4;'
gene_info: Name=GLYCTK; Synonyms=HBEBP4; ORFNames=LP5910;
organism_full: Homo sapiens (Human).
protein_family: Belongs to the glycerate kinase type-2 family.
protein_domains: GK-like_C_sf. (IPR037035); GK_N_sf. (IPR038614); MOFRL. (IPR007835);
MOFRL_assoc_dom. (IPR025286); MOFRL_protein. (IPR039760)
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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: Q8IVS8
• Protein Description: RecName: Full=Glycerate kinase; EC=2.7.1.31 {ECO:0000269|PubMed:16753811, ECO:0000269|PubMed:20949620}; AltName: Full=HBeAg-binding protein 4;
• Gene Information: Name=GLYCTK; Synonyms=HBEBP4; ORFNames=LP5910;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the glycerate kinase type-2 family.
• Key Domains: GK-like_C_sf. (IPR037035); GK_N_sf. (IPR038614); MOFRL. (IPR007835); MOFRL_assoc_dom. (IPR025286); MOFRL_protein. (IPR039760)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "GLYCTK" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'GLYCTK' 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 GLYCTK (gene ID: GLYCTK, UniProt: Q8IVS8) in human.

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: Q8IVS8
• Protein Description: RecName: Full=Glycerate kinase; EC=2.7.1.31 {ECO:0000269|PubMed:16753811, ECO:0000269|PubMed:20949620}; AltName: Full=HBeAg-binding protein 4;
• Gene Information: Name=GLYCTK; Synonyms=HBEBP4; ORFNames=LP5910;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the glycerate kinase type-2 family.
• Key Domains: GK-like_C_sf. (IPR037035); GK_N_sf. (IPR038614); MOFRL. (IPR007835); MOFRL_assoc_dom. (IPR025286); MOFRL_protein. (IPR039760)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "GLYCTK" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'GLYCTK' 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 GLYCTK (gene ID: GLYCTK, UniProt: Q8IVS8) in human.

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.

Comprehensive research report: human GLYCTK (UniProt Q8IVS8) — functional annotation

0) Identity verification (critical disambiguation)

The UniProt accession Q8IVS8 corresponds to human GLYCTK (synonyms reported in UniProt include HBEBP4), annotated as glycerate kinase / D-glycerate 2-kinase (EC 2.7.1.31). The primary human genetics and enzymology literature for D-glyceric aciduria explicitly identifies GLYCTK as encoding D-glycerate 2-kinase and establishes causality between GLYCTK loss-of-function variants and disease, confirming the target identity is correct (sass2010d‐glycericaciduriais pages 12-15, zehavi2019severeinfantileepileptic pages 1-2, swanson2017dglycericaciduriadoes pages 1-2).

1) Key concepts and definitions (current understanding)

1.1 Enzymatic function and reaction definition

GLYCTK (D-glycerate 2-kinase; EC 2.7.1.31) catalyzes phosphorylation of D-glycerate to 2-phosphoglycerate (2-PG) (zehavi2019severeinfantileepileptic pages 1-2). This reaction consumes ATP (kinase reaction; ATP consumption is explicitly described in assay coupling approaches and in mechanistic descriptions linking to glycolytic intermediates) and places GLYCTK at a junction between D-glycerate handling and central carbon metabolism (zehavi2019severeinfantileepileptic pages 1-2, sass2010d‐glycericaciduriais pages 12-15).

Pathway placement: D-glycerate is described as an intermediate metabolite of serine and fructose metabolism, and conversion to 2-phosphoglycerate creates a biochemical link into glycolysis/gluconeogenesis via 2-PG (zehavi2019severeinfantileepileptic pages 1-2, guo2006isolationandcharacterization pages 4-5).

1.2 D-glyceric aciduria (DGA) / glycerate kinase deficiency

D-glyceric aciduria (OMIM #220120) is an autosomal recessive inborn error of metabolism caused by mutations in GLYCTK, leading to accumulation of D-glycerate in tissues and massive urinary excretion (zehavi2019severeinfantileepileptic pages 1-2, swanson2017dglycericaciduriadoes pages 1-2). Clinically, DGA is often framed as a disorder linked to serine and fructose metabolism (swanson2017dglycericaciduriadoes pages 1-2, sass2020dglyceratekinasedeficiency pages 1-2).

2) Molecular and biochemical function (evidence-based)

2.1 Substrate specificity (what is known)

The disease and enzymology evidence in the retrieved primary literature specifically centers on D-glycerate as the physiological substrate, with formation of 2-phosphoglycerate as the product (zehavi2019severeinfantileepileptic pages 1-2, sass2010d‐glycericaciduriais pages 12-15). The available extracted evidence does not provide a broader substrate panel; thus, substrate specificity beyond D-glycerate cannot be asserted from the retrieved texts.

2.2 Enzymatic kinetics and activity (quantitative)

A core functional validation study expressed reference human GLYCTK cDNA in HEK293 cells, showing:
- Enzyme activity increased from trace amounts (<0.5 µmol·min⁻¹·g⁻¹ protein) in controls to 30.7 µmol·min⁻¹·g⁻¹ protein after expression of reference GLYCTK (sass2010d‐glycericaciduriais pages 12-15).
- The measured Km for D-glycerate was 0.1 mM (mean of two transfection series) (sass2010d‐glycericaciduriais pages 12-15).
- Patient-derived mutant forms (frameshift or missense) produced no enhanced protein signal and no detectable activity in this expression system (sass2010d‐glycericaciduriais pages 12-15).

Figure-based support for the activity comparison (reference vs mutants) is available as a cropped figure from the paper (sass2010d‐glycericaciduriais media 5f02c9bb).

3) Subcellular localization and isoforms

3.1 Isoform-dependent localization (experimental evidence)

A cloning/characterization study identified two alternatively spliced transcripts, GLYCTK1 and GLYCTK2, and used GFP-fusion experiments in mammalian cells to assess localization:
- Both isoforms were reported as cytosolic (particulate).
- GLYCTK2 was additionally reported to be specifically localized to mitochondria, whereas GLYCTK1 was not (guo2006isolationandcharacterization pages 4-5).

These findings support the concept that GLYCTK function can occur in both cytosolic and mitochondrial compartments, with mitochondrial targeting being isoform-dependent (guo2006isolationandcharacterization pages 4-5).

3.2 Tissue expression

Both transcript variants were detected by RT-PCR across a broad panel of 17 human tissues, indicating widespread expression (guo2006isolationandcharacterization pages 1-4). Mouse in situ hybridization also showed notable expression in neural regions and skeletal muscle (guo2006isolationandcharacterization pages 4-5, guo2006isolationandcharacterization pages 5-6), which has been interpreted as consistent with neurological involvement in severe cases (guo2006isolationandcharacterization pages 5-6).

4) Human disease genetics and phenotype (authoritative primary literature)

4.1 Causality: GLYCTK deficiency causes D-glyceric aciduria

A key human mutation/functional paper reported homozygous exon 5 GLYCTK variants in unrelated DGA patients and functionally demonstrated loss of enzyme activity upon expression of the mutant alleles (sass2010d‐glycericaciduriais pages 12-15). This provides direct experimental support that GLYCTK is the causative gene for DGA in these cases.

4.2 Reported pathogenic variants (examples in retrieved evidence)

Pathogenic GLYCTK variants reported across retrieved studies include:
- c.1448delT (p.Phe483SerfsX2) (sass2010d‐glycericaciduriais pages 12-15, swanson2017dglycericaciduriadoes pages 1-2)
- c.1478T>G (p.Phe493Cys) (sass2010d‐glycericaciduriais pages 12-15)
- c.1558delC (p.Leu520CysfsX108) (sass2010d‐glycericaciduriais pages 12-15)
- c.455T>C (p.Leu152Pro) (zehavi2019severeinfantileepileptic pages 1-2)
- c.517G>T (p.Val173Leu) (sass2020dglyceratekinasedeficiency pages 1-2)

4.3 Quantitative metabolite abnormalities (statistics/data)

In DGA patients with GLYCTK deficiency, quantitative elevations reported include:
- Plasma D-glycerate 1.0–1.3 mM (historical patient A; normal reported as not detectable) (sass2010d‐glycericaciduriais pages 12-15).
- Urinary glycerate reported as 9.32 mol/mol creatinine (patient B) and 11.3, 8.61, 18.6 mol/mol creatinine (three samples from patient C) (sass2010d‐glycericaciduriais pages 12-15).
- Serum glycerate 1 mM (patient C) (sass2010d‐glycericaciduriais pages 12-15).

These values provide concrete biochemical anchors for functional annotation and diagnostic expectations.

4.4 Clinical spectrum and case counts

The phenotype spectrum is repeatedly described as highly variable, ranging from severe progressive infantile encephalopathy to mild/nearly asymptomatic presentations (zehavi2019severeinfantileepileptic pages 1-2, swanson2017dglycericaciduriadoes pages 1-2).

Across case-based summaries in the retrieved literature:
- A review/case report describes 15 previously reported patients plus the current case (total 16) and emphasizes severe neurological impairment in many cases (zehavi2019severeinfantileepileptic pages 1-2).
- Another neuropediatric case report notes that 16 individuals had been described with tentative diagnosis, but only six had prior mutation confirmation, and presents the seventh genetically confirmed case (sass2020dglyceratekinasedeficiency pages 1-2).

Severe neurologic manifestations reported in a progressive case include profound psychomotor retardation, progressive microcephaly, intractable seizures, cortical blindness and deafness, hypotonia progressing to spasticity, progressive brain atrophy on MRI, and death at 9.5 years following status epilepticus (zehavi2019severeinfantileepileptic pages 1-2). A milder neuropediatric case includes severe early hypotonia, hypermobility, tremor, delayed milestones, and diffuse slow EEG background without a specific epileptic syndrome (sass2020dglyceratekinasedeficiency pages 1-2).

5) Recent developments (prioritize 2023–2024)

5.1 State of the retrieved 2023–2024 evidence

Within the tool-retrieved set, no 2023–2024 primary mechanistic papers focused specifically on human GLYCTK enzymology, structure, or cell biology were accessible. The most informative GLYCTK functional/disease evidence available here remains from foundational studies (2006–2020) (sass2010d‐glycericaciduriais pages 12-15, guo2006isolationandcharacterization pages 4-5, zehavi2019severeinfantileepileptic pages 1-2, sass2020dglyceratekinasedeficiency pages 1-2).

Two 2023–2024 papers retrieved are primarily platform/resource contributions rather than GLYCTK biology:
- SpliceProt 2.0 (published 18 Jan 2024) is a proteogenomics repository aimed at cataloging proteoforms; it is relevant indirectly for splice-variant-aware proteomics workflows, but does not provide GLYCTK-specific functional data in the retrieved sections (santos2024spliceprot2.0a pages 1-2, santos2024spliceprot2.0a pages 2-4).
- Metaboverse (published Apr 2023) is a computational tool for metabolic network visualization and pattern discovery; the retrieved excerpt does not provide GLYCTK-specific biology beyond general metabolic-network context (berg2023metaboverseenablesautomated pages 8-9, berg2023metaboverseenablesautomated pages 9-10).

6) Current applications and real-world implementations

6.1 Clinical diagnostics (inborn errors of metabolism)

Real-world implementation of GLYCTK knowledge is primarily in metabolic diagnostics:
- Urine organic acid analysis detects elevated glycerate; subsequent enantioselective analysis can distinguish D- vs L-glycerate to differentiate DGA (GLYCTK deficiency) from primary hyperoxaluria type 2 (L-glycerate) (sass2020dglyceratekinasedeficiency pages 1-2, zehavi2019severeinfantileepileptic pages 1-2).
- Genetic testing (GLYCTK sequencing) provides confirmatory diagnosis and can resolve confounded historical diagnoses (e.g., co-occurring disorders) (swanson2017dglycericaciduriadoes pages 1-2, sass2010d‐glycericaciduriais pages 12-15).

6.2 Functional variant interpretation (experimental implementation)

The HEK293 overexpression assay provides an implemented approach for functional validation of candidate GLYCTK variants, demonstrating that disease-associated alleles can abolish detectable activity/protein (sass2010d‐glycericaciduriais pages 12-15, sass2010d‐glycericaciduriais media 5f02c9bb).

7) Expert opinions and analysis (authoritative interpretation from sources)

7.1 Variant-to-phenotype uncertainty and ascertainment bias

Authors emphasize that clinical expressivity is broad, including families with asymptomatic affected siblings, raising the possibility of ascertainment bias and/or modifying factors (swanson2017dglycericaciduriadoes pages 1-2). This complicates straightforward genotype–phenotype mapping.

7.2 Potential additional roles beyond canonical metabolism

Although GLYCTK is primarily discussed as an enzyme in serine/fructose metabolism, authors have speculated that in higher animals glycerate kinase may have roles in neural systems and cell differentiation (guo2006isolationandcharacterization pages 6-7). A neuropediatric case report explicitly suggests future work should search for additional roles beyond catabolism of serine and fructose (sass2020dglyceratekinasedeficiency pages 1-2). These are hypotheses/opinions rather than demonstrated mechanisms in the extracted evidence.

8) Database corroboration (OpenTargets)

OpenTargets reports a GLYCTK association with D-glyceric aciduria (MONDO_0009070) supported by multiple evidence entries and PubMed links, consistent with the primary literature linking GLYCTK mutations to DGA (sass2010d‐glycericaciduriais pages 12-15).

9) Summary of key evidence (tabulated)

The following table consolidates the key functional annotation points extracted from the retrieved literature.

Table: This table summarizes the key functional annotation evidence for human GLYCTK/Q8IVS8 from the provided literature context, covering enzymatic function, localization, disease association, mutations, phenotype spectrum, and quantitative data.

10) Evidence gaps and recommended next steps (based on retrieved evidence)

1. Substrate specificity beyond D-glycerate: No substrate screening or comparative kinetics were captured in the retrieved texts; targeted enzymology papers would be required.
2. Human-relevant compartment biology: Isoform-dependent mitochondrial localization is supported by GFP-fusion experiments, but further work is needed to define which isoforms predominate by tissue and whether localization changes with physiological state (guo2006isolationandcharacterization pages 4-5).
3. Recent (2023–2024) GLYCTK-focused research: The retrieved dataset did not include recent dedicated GLYCTK studies; further targeted searches (e.g., “GLYCTK structure”, “mitochondrial glycerate kinase”, “D-glyceric aciduria cohort 2024”) may be needed to capture the latest clinical cohort or mechanistic updates.

References

1. (sass2010d‐glycericaciduriais pages 12-15): Jörn Oliver Sass, Kathleen Fischer, Raymond Wang, Ernst Christensen, Sabine Scholl-Bürgi, Richard Chang, Klaus Kapelari, and Melanie Walter. D‐glyceric aciduria is caused by genetic deficiency of d‐glycerate kinase (glyctk). Human Mutation, 31:1280-1285, Dec 2010. URL: https://doi.org/10.1002/humu.21375, doi:10.1002/humu.21375. This article has 36 citations and is from a domain leading peer-reviewed journal.

2. (zehavi2019severeinfantileepileptic pages 1-2): Yoav Zehavi, Hanna Mandel, Ayelet Eran, Sarit Ravid, Muhammad Abu Rashid, Erwin E. W. Jansen, Mirjam M. C. Wamelink, Ann Saada, Avraham Shaag, Orly Elpeleg, and Ronen Spiegel. Severe infantile epileptic encephalopathy associated with d-glyceric aciduria: report of a novel case and review. Metabolic Brain Disease, 34:557-563, Jan 2019. URL: https://doi.org/10.1007/s11011-019-0384-x, doi:10.1007/s11011-019-0384-x. This article has 11 citations and is from a peer-reviewed journal.

3. (swanson2017dglycericaciduriadoes pages 1-2): Michael A. Swanson, Stephanie M. Garcia, Elaine Spector, Kathryn Kronquist, Geralyn Creadon-Swindell, Melanie Walter, Ernst Christensen, Johan L.K. Van Hove, and Jörn Oliver Sass. D-glyceric aciduria does not cause nonketotic hyperglycinemia: a historic co-occurrence. Molecular Genetics and Metabolism, 121:80-82, Jun 2017. URL: https://doi.org/10.1016/j.ymgme.2017.04.009, doi:10.1016/j.ymgme.2017.04.009. This article has 12 citations and is from a peer-reviewed journal.

4. (guo2006isolationandcharacterization pages 4-5): Jin-Hu Guo, Saiyin Hexige, Li Chen, Guang-Jin Zhou, Xiang Wang, Jian-Min Jiang, Ya-Hui Kong, Guo-Qing Ji, Chao-Qun Wu, Shou-Yuan Zhao, and Long Yu. Isolation and characterization of the human d-glyceric acidemia related glycerate kinase gene glyctk1 and its alternatively splicing variant glyctk2. DNA Sequence, 17:1-7, Jan 2006. URL: https://doi.org/10.1080/10425170500476665, doi:10.1080/10425170500476665. This article has 19 citations.

5. (sass2020dglyceratekinasedeficiency pages 1-2): Jörn Oliver Sass, Sidney Behringer, Malkanthi Fernando, Elisabetta Cesaroni, Ida Cursio, Alberto Volpini, and Claudia Till. D-glycerate kinase deficiency in a neuropediatric patient. Brain and Development, 42:226-230, Feb 2020. URL: https://doi.org/10.1016/j.braindev.2019.11.008, doi:10.1016/j.braindev.2019.11.008. This article has 9 citations and is from a peer-reviewed journal.

6. (sass2010d‐glycericaciduriais media 5f02c9bb): Jörn Oliver Sass, Kathleen Fischer, Raymond Wang, Ernst Christensen, Sabine Scholl-Bürgi, Richard Chang, Klaus Kapelari, and Melanie Walter. D‐glyceric aciduria is caused by genetic deficiency of d‐glycerate kinase (glyctk). Human Mutation, 31:1280-1285, Dec 2010. URL: https://doi.org/10.1002/humu.21375, doi:10.1002/humu.21375. This article has 36 citations and is from a domain leading peer-reviewed journal.

7. (guo2006isolationandcharacterization pages 1-4): Jin-Hu Guo, Saiyin Hexige, Li Chen, Guang-Jin Zhou, Xiang Wang, Jian-Min Jiang, Ya-Hui Kong, Guo-Qing Ji, Chao-Qun Wu, Shou-Yuan Zhao, and Long Yu. Isolation and characterization of the human d-glyceric acidemia related glycerate kinase gene glyctk1 and its alternatively splicing variant glyctk2. DNA Sequence, 17:1-7, Jan 2006. URL: https://doi.org/10.1080/10425170500476665, doi:10.1080/10425170500476665. This article has 19 citations.

8. (guo2006isolationandcharacterization pages 5-6): Jin-Hu Guo, Saiyin Hexige, Li Chen, Guang-Jin Zhou, Xiang Wang, Jian-Min Jiang, Ya-Hui Kong, Guo-Qing Ji, Chao-Qun Wu, Shou-Yuan Zhao, and Long Yu. Isolation and characterization of the human d-glyceric acidemia related glycerate kinase gene glyctk1 and its alternatively splicing variant glyctk2. DNA Sequence, 17:1-7, Jan 2006. URL: https://doi.org/10.1080/10425170500476665, doi:10.1080/10425170500476665. This article has 19 citations.

9. (santos2024spliceprot2.0a pages 1-2): Letícia Graziela Costa Santos, Vinícius da Silva Coutinho Parreira, Esdras Matheus Gomes da Silva, Marlon Dias Mariano Santos, Alexander da Franca Fernandes, Ana Gisele da Costa Neves-Ferreira, Paulo Costa Carvalho, Flávia Cristina de Paula Freitas, and Fabio Passetti. Spliceprot 2.0: a sequence repository of human, mouse, and rat proteoforms. International Journal of Molecular Sciences, 25:1183, Jan 2024. URL: https://doi.org/10.3390/ijms25021183, doi:10.3390/ijms25021183. This article has 2 citations.

10. (santos2024spliceprot2.0a pages 2-4): Letícia Graziela Costa Santos, Vinícius da Silva Coutinho Parreira, Esdras Matheus Gomes da Silva, Marlon Dias Mariano Santos, Alexander da Franca Fernandes, Ana Gisele da Costa Neves-Ferreira, Paulo Costa Carvalho, Flávia Cristina de Paula Freitas, and Fabio Passetti. Spliceprot 2.0: a sequence repository of human, mouse, and rat proteoforms. International Journal of Molecular Sciences, 25:1183, Jan 2024. URL: https://doi.org/10.3390/ijms25021183, doi:10.3390/ijms25021183. This article has 2 citations.

11. (berg2023metaboverseenablesautomated pages 8-9): Jordan A. Berg, Youjia Zhou, Yeyun Ouyang, Ahmad A. Cluntun, T. Cameron Waller, Megan E. Conway, Sara M. Nowinski, Tyler Van Ry, Ian George, James E. Cox, Bei Wang, and Jared Rutter. Metaboverse enables automated discovery and visualization of diverse metabolic regulatory patterns. Nature Cell Biology, 25:616-625, Apr 2023. URL: https://doi.org/10.1038/s41556-023-01117-9, doi:10.1038/s41556-023-01117-9. This article has 12 citations and is from a highest quality peer-reviewed journal.

12. (berg2023metaboverseenablesautomated pages 9-10): Jordan A. Berg, Youjia Zhou, Yeyun Ouyang, Ahmad A. Cluntun, T. Cameron Waller, Megan E. Conway, Sara M. Nowinski, Tyler Van Ry, Ian George, James E. Cox, Bei Wang, and Jared Rutter. Metaboverse enables automated discovery and visualization of diverse metabolic regulatory patterns. Nature Cell Biology, 25:616-625, Apr 2023. URL: https://doi.org/10.1038/s41556-023-01117-9, doi:10.1038/s41556-023-01117-9. This article has 12 citations and is from a highest quality peer-reviewed journal.

13. (guo2006isolationandcharacterization pages 6-7): Jin-Hu Guo, Saiyin Hexige, Li Chen, Guang-Jin Zhou, Xiang Wang, Jian-Min Jiang, Ya-Hui Kong, Guo-Qing Ji, Chao-Qun Wu, Shou-Yuan Zhao, and Long Yu. Isolation and characterization of the human d-glyceric acidemia related glycerate kinase gene glyctk1 and its alternatively splicing variant glyctk2. DNA Sequence, 17:1-7, Jan 2006. URL: https://doi.org/10.1080/10425170500476665, doi:10.1080/10425170500476665. This article has 19 citations.

Citations

1. zehavi2019severeinfantileepileptic pages 1-2
2. guo2006isolationandcharacterization pages 4-5
3. guo2006isolationandcharacterization pages 1-4
4. guo2006isolationandcharacterization pages 5-6
5. sass2020dglyceratekinasedeficiency pages 1-2
6. swanson2017dglycericaciduriadoes pages 1-2
7. guo2006isolationandcharacterization pages 6-7
8. berg2023metaboverseenablesautomated pages 8-9
9. berg2023metaboverseenablesautomated pages 9-10
10. https://doi.org/10.1007/s11011-019-0384-x
11. https://doi.org/10.1002/humu.21375
12. https://doi.org/10.1080/10425170500476665
13. https://doi.org/10.1016/j.braindev.2019.11.008
14. https://doi.org/10.1016/j.ymgme.2017.04.009
15. https://doi.org/10.1002/humu.21375,
16. https://doi.org/10.1007/s11011-019-0384-x,
17. https://doi.org/10.1016/j.ymgme.2017.04.009,
18. https://doi.org/10.1080/10425170500476665,
19. https://doi.org/10.1016/j.braindev.2019.11.008,
20. https://doi.org/10.3390/ijms25021183,
21. https://doi.org/10.1038/s41556-023-01117-9,