Molecular Genetics and Metabolism Reports最新文献

{"title":"Risk of inadequate protein and micronutrient intakes in patients with PKU with an increased phe-tolerance: Impact of a micronutrient-dense protein substitute","authors":"Carmen Rohde ,&nbsp;Denise Leonne Hofman ,&nbsp;Ira Klawon ,&nbsp;Frank Rutsch ,&nbsp;Iris Rodenburg ,&nbsp;Francjan van Spronsen ,&nbsp;Alena Gerlinde Thiele ,&nbsp;Willie Woestenenk ,&nbsp;Skadi Beblo","doi":"10.1016/j.ymgmr.2025.101264","DOIUrl":"10.1016/j.ymgmr.2025.101264","url":null,"abstract":"<div><h3>Background</h3><div>Patients with phenylketonuria (PKU) with higher phenylalanine (phe)-tolerance may have inadequate diets due to high-quality protein restriction and reduced intakes of nutrient-fortified phe-free, tyrosine (tyr)-enriched protein substitutes (PS).</div></div><div><h3>Methods</h3><div>Open-label, 24-week, multi-centre intervention assessed the impact of a once-daily, micronutrient-dense PS on nutrient intakes in patients with an increased phe-tolerance. Subjects &gt;12 years, consuming 0–25 g protein/day from a regular PS, were recruited. Diet records and fasting blood samples were collected at baseline and study end.</div></div><div><h3>Results</h3><div>11/13 subjects, 15-49y (5 males), with 6/11 taking tetrahydrobiopterin dihydrochloride (BH4) and/or a regular PS, completed the study. At baseline, protein and some essential amino acids (EAA) intakes were below recommendations in 4/11 and 3/11 subjects, respectively. Vitamins A, B2, B12, D, calcium, iron, iodine, zinc and magnesium intakes were below recommendations for 7/11. After the intervention, 2/11 had total protein intakes below recommendations, while 11/11 met EAA recommendations. Micronutrient intakes improved to ≥90 % of recommendations for all subjects except for vitamin B12 (4/11) and phosphorus (1/6). Docosahexaenoic acid (DHA) intakes increased. Blood phe levels remained stable.</div></div><div><h3>Conclusion</h3><div>Patients with PKU who have relaxed their phe-restricted diet are at risk of insufficient nutrient supply, and dietary counselling should be offered. Consuming the study PS increased nutrient intakes closer to dietary recommendations.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101264"},"PeriodicalIF":1.9,"publicationDate":"2025-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145220001","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into ALG3-CDG: A case study combining glycan profiling and genetic analysis","authors":"Rebeka Kodríková ,&nbsp;Zuzana Pakanová ,&nbsp;Maroš Krchňák ,&nbsp;Veronika Krajčovičová ,&nbsp;Anna Šalingová ,&nbsp;Katarína Skalická ,&nbsp;Miriam Kolníková ,&nbsp;Peter Baráth ,&nbsp;Marek Nemčovič","doi":"10.1016/j.ymgmr.2025.101263","DOIUrl":"10.1016/j.ymgmr.2025.101263","url":null,"abstract":"<div><div>Congenital disorders of glycosylation (CDG) are a group of rare metabolic disorders caused by the defects in the glycosylation pathways of biomacromolecules leading to altered glycoprofiles in affected individuals. In this case study, we present a 3-year-old Slovak male patient with developmental delay, hearing impairment, epilepsy, microcephaly, facial dysmorphism, corpus callosum dysgenesis, and cardiac abnormalities. To elucidate the underlying cause, we performed LC-ESI-MS analysis of RapiFluor-labelled <em>N-</em>glycans released from blood serum glycoproteins. The results revealed an abnormal <em>N</em>-glycan profile, characterized by an increased relative abundance of truncated mannosylated structures (Hex3HexNAc2 and Hex4HexNAc2) and a decreased presence of higher-order mannose structures (Hex6-8HexNAc2). A molecular analysis was also conducted. Whole exome sequencing confirmed a diagnosis of ALG3-CDG with compound heterozygous variants: c.165C &gt; T (p.Gly55=) and c.1060C &gt; T (p.Arg354Cys) in the <em>ALG3</em> gene, encoding alpha-1,3-mannosyltransferase in the endoplasmic reticulum. This presented case highlights the importance of glycan profiling and genetic analysis in diagnosing congenital disorders of glycosylation, facilitating early intervention and management.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101263"},"PeriodicalIF":1.9,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219999","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Case report: Lysine improvement in siblings with glutaric acidemia type 1 following reduced medical food intake: Implications for amino acid absorption and reabsorption","authors":"Grace Noh ,&nbsp;Jariya Upadia","doi":"10.1016/j.ymgmr.2025.101262","DOIUrl":"10.1016/j.ymgmr.2025.101262","url":null,"abstract":"<div><div>Glutaric acidemia type 1 (GA1) is a rare metabolic disorder requiring dietary management with lysine (Lys)-free, tryptophan (Trp)-reduced, and arginine (Arg)-fortified medical formulas. This case report describes three siblings with GA1 who exhibited persistently low plasma lysine levels despite meeting age-appropriate dietary protein intake from intact protein sources. Upon reducing medical formula intake while maintaining intact protein consumption, lysine levels normalized, suggesting that excess dietary arginine may inhibit lysine intestinal uptake or reabsorption in the kidneys. These findings highlight the need for further research on amino acid interactions in GA1 dietary management and emphasize careful formula prescription to prevent unintended lysine deficiency.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101262"},"PeriodicalIF":1.9,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145220000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular characterization of a novel synonymous variant in a Mexican patient with Pompe disease","authors":"Carmen Alaez-Verson ,&nbsp;Carlos Alberto González-Domínguez ,&nbsp;Imelda Vergara Sanchez ,&nbsp;Luz María Sanchez Sanchez ,&nbsp;Ivonne Natalia Flores ,&nbsp;Ekaterina Kazakova ,&nbsp;Joaquin Garcia-Solorio ,&nbsp;Carolina Molina-Garay ,&nbsp;Luis Leonardo Flores-Lagunes ,&nbsp;Ivan Martínez Duncker","doi":"10.1016/j.ymgmr.2025.101253","DOIUrl":"10.1016/j.ymgmr.2025.101253","url":null,"abstract":"<div><h3>Introduction</h3><div>Pompe disease (PD) is an autosomal recessive disorder caused by a deficiency of lysosomal acid alpha-1,4-glucosidase (GAA; EC 3.2.1.20), encoded by the GAA gene, leading to progressive neuromuscular deterioration. The mutational spectrum of <em>GAA</em> is expanding, particularly with recognition of splicing-impacting synonymous variants. Here, we report the molecular characterization and reclassification of a novel synonymous <em>GAA</em> variant in a female Mexican patient with enzymatically confirmed infantile-onset PD (IOPD).</div></div><div><h3>Methods</h3><div>DNA and RNA were extracted from peripheral blood. Next-generation sequencing of a clinical exome panel identified variants in the <em>GAA</em> gene. The whole coding sequence of the <em>GAA</em> was amplified from cDNA, subcloned, and analyzed by Sanger sequencing to assess splicing alterations.</div></div><div><h3>Results</h3><div>The pathogenic variant c.1979G &gt; A (p.Arg660His) and a novel VUS c.2799G &gt; A (p.Lys933=) were detected. The variant c.2799G &gt; A is predicted to affect splicing. mRNA analysis revealed three isoforms, one corresponding to c.1979G &gt; A and two others caused by alternative splicing of c.2799G &gt; A (isoforms 1 and 2). The isoform-1 showed c.2799G &gt; A, followed by 61 bp retention of intron 19, predicted to cause a frameshift p.(A934fs). Isoform 2 has a 90 bp deletion in exon 19, resulting in a p.V904_K933del in-frame deletion.</div></div><div><h3>Discussion</h3><div>This study demonstrates that the synonymous variant c.2799G &gt; A is pathogenic due to its impact on RNA splicing. Our findings highlight the importance of transcript analysis for VUS reclassification and stress the clinical relevance of evaluating synonymous variants in genetic diagnostics and patient management.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101253"},"PeriodicalIF":1.9,"publicationDate":"2025-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Case report of neuronopathic mucopolysaccharidosis type II: Early intracerebroventricular enzyme replacement therapy and hematopoietic cell transplantation with developmental outcomes up to 5 years of age","authors":"Azuma Ikari ,&nbsp;Asahito Hama ,&nbsp;Torayuki Okuyama","doi":"10.1016/j.ymgmr.2025.101254","DOIUrl":"10.1016/j.ymgmr.2025.101254","url":null,"abstract":"<div><div>Neuronopathic mucopolysaccharidosis type II (MPS II) is a severe lysosomal storage disorder associated with early-onset developmental regression and a poor prognosis. Although enzyme replacement therapy (ERT) and hematopoietic cell transplantation (HCT) have been employed to address systemic symptoms, they have not demonstrated sufficient efficacy in treating central nervous system (CNS) involvement. The intracerebroventricular administration of idursulfase beta has emerged as a novel approach for targeting CNS manifestations. Here, we report the clinical course of a male patient diagnosed with neuronopathic MPS II at 2 months of age, based on family history and genetic analysis. Intravenous ERT was initiated early, followed by the introduction of intracerebroventricular idursulfase beta at 10 months, and HCT at 23 months. Since then, only intracerebroventricular ERT has been continued. At 5 years of age, the patient exhibited age-appropriate neurodevelopment, stable cognitive function, and normal physical growth without signs of developmental regression. Imaging findings remained stable, and cerebrospinal fluid biomarkers normalized. Notably, the patient harbored a missense variant potentially associated with residual enzymatic activity, which may have contributed to favorable outcomes. To our knowledge, this is the first reported case in which normal development was maintained until 5 years of age in a patient with neuronopathic MPS II. This case highlights the potential benefits of early diagnosis and a multimodal therapeutic strategy, including intracerebroventricular ERT and HCT, for preserving neurodevelopment. It also holds significance as a rare but valuable example, suggesting the efficacy of a novel treatment paradigm for a condition traditionally associated with a poor prognosis.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101254"},"PeriodicalIF":1.9,"publicationDate":"2025-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Real-world experience of switching to taliglucerase among patients with Gaucher disease in Québec: A case series","authors":"Angelo Rizzolo ,&nbsp;Marie-Claude Miron ,&nbsp;Jean-François Delisle ,&nbsp;Nathalie Alos ,&nbsp;Philippe M. Campeau ,&nbsp;François Mercier","doi":"10.1016/j.ymgmr.2025.101257","DOIUrl":"10.1016/j.ymgmr.2025.101257","url":null,"abstract":"<div><div>Enzyme replacement therapy (ERT) for Gaucher disease (GD) effectively prevents skeletal, visceral, and hematologic complications of this inherited, lysosomal storage disorder. Taliglucerase is one of the three commercially available ERT products and became the recommended first-line therapy in Québec, Canada in 2016. Thus, 19 patients were switched from imiglucerase to taliglucerase, but more than a quarter experienced significant side effects. Here, we summarize these patients' clinical course and describe 6 suspected product-related adverse-effects.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101257"},"PeriodicalIF":1.9,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155270","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Serum hepcidin as a biomarker of treatment response in Gaucher disease","authors":"Tiago Koppe ,&nbsp;Franciele C. Pinheiro ,&nbsp;Marina Siebert ,&nbsp;Suelen Basgalupp ,&nbsp;Liane E. Daudt ,&nbsp;Ida Vanessa D. Schwartz","doi":"10.1016/j.ymgmr.2025.101255","DOIUrl":"10.1016/j.ymgmr.2025.101255","url":null,"abstract":"<div><div>Gaucher disease (GD) is a lysosomal disorder associated with hyperferritinemia and altered hepcidin levels. This study evaluated the effect of GD-specific treatment on serum hepcidin and interleukin-6 (IL-6) in seven treatment-naïve Brazilian patients with type 1 GD. Concentrations were measured before and after initiation of treatment. Hepcidin levels significantly decreased and IL-6 showed a downward trend. These results suggest that hepcidin may also exert endocrine effects in GD-related iron metabolism.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101255"},"PeriodicalIF":1.9,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145118390","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Clinical and biochemical characterization of a patient with prolidase deficiency, a rare disorder of collagen metabolism","authors":"Troy K. Coody ,&nbsp;Irene De Biase ,&nbsp;Julie M. Porter ,&nbsp;Marzia Pasquali ,&nbsp;Brian J. Shayota","doi":"10.1016/j.ymgmr.2025.101258","DOIUrl":"10.1016/j.ymgmr.2025.101258","url":null,"abstract":"<div><div>Prolidase deficiency (PD) is an autosomal recessive inborn error of metabolism, with an estimated incidence of 1 per 1.25 million births. Prolidase is critical for the turnover of proline and hydroxyproline-rich proteins, such as collagen. Collagen metabolism is essential for matrix regeneration during cellular proliferation and complex bodily functions such as wound healing and immunological cell differentiation. PD clinical manifestations include persistent skin ulcerations and poor wound healing, hypertelorism, high arched palate, depressed nasal bridge, micrognathia, splenomegaly, intellectual disability, recurring infections, and hematological abnormalities. Biochemically, a diagnosis of PD is supported by increased urinary excretion of glycyl-proline and other proline-containing iminopeptides detected by amino acid analysis. There are no current targeted therapies, but suggested interventions have included topical proline-glycine ointment, manganese supplementation, topical and oral steroids, and immunomodulation with monoclonal antibodies.</div><div>Here, we describe a 30-year-old patient with PD whose clinical course has been characterized by recurrent skin ulcerations/cysts with secondary scarring, recurrent infections, anemia, thrombocytopenia, lymphopenia, elevated liver enzymes, hirsutism, and seemingly unrelated papillary thyroid cancer. Skin manifestations were particularly severe due to the added complication of a diagnosis of hidradenitis suppurativa. Quantitative analysis of amino acids and related compounds revealed markedly elevated glycyl-proline in urine and plasma. To further characterize the biochemical phenotype, untargeted metabolomic analysis was sent on both plasma and urine. An increase was noted in several metabolites from the prolidase-dependent dipeptide recycling pathways. A better understanding of the pathophysiological mechanisms involved in prolidase deficiency may prove useful as different therapeutic approaches are being considered.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101258"},"PeriodicalIF":1.9,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145118391","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Early diagnosis and management in Gaucher disease: A case series emphasizing the critical role of newborn screening","authors":"Éliane Beauregard-Lacroix ,&nbsp;Madeline Steffensen ,&nbsp;Caitlin Menello ,&nbsp;Can Ficicioglu","doi":"10.1016/j.ymgmr.2025.101256","DOIUrl":"10.1016/j.ymgmr.2025.101256","url":null,"abstract":"<div><div>Type 1 Gaucher disease is a lysosomal storage disorder associated with marked phenotypic heterogeneity, including among individuals carrying genotypes historically defined as “mild”. Early diagnosis, workup and follow-up care are crucial to avoid irreversible complications. We present a case series of 5 pediatric patients with type 1 Gaucher disease who had been identified based on newborn screening (NBS), parental carrier status, or clinical presentation. They were followed over time for monitoring of clinical status, hematologic indices, biomarkers including glucopsychosine, and imaging studies. Enzyme replacement therapy (ERT) was started when rising trends of biomarkers and/or new clinical symptoms appeared. Three patients were identified by NBS, one at birth due to parental carrier status, and one after symptomatic presentation with femoral fracture. All patients required initiation of ERT between 9 months and 5 years of age due to evidence of disease progression. Early diagnosis via NBS and proactive monitoring enabled timely ERT initiation in four cases, preventing irreversible organ damage and clinical complications. In contrast, the unscreened case presented with severe skeletal and hematologic involvement at baseline. Rising glucopsychosine was a sensitive early marker of disease activity and MRI was more sensitive at detecting organomegaly than ultrasound. These cases emphasize the vital importance of NBS, regular biomarker surveillance, and early intervention, even in presumed mild cases based on genotype. Early diagnosis via NBS, individualized monitoring and timely treatment are fundamental to optimizing outcomes in Gaucher disease type 1.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101256"},"PeriodicalIF":1.9,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145109136","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improving sapropterin administration efficacy in PKU: Clinical practice case studies","authors":"Martina Tosi ,&nbsp;Anne Daly ,&nbsp;Catherine Ashmore ,&nbsp;Alex Pinto ,&nbsp;Suresh Vijay ,&nbsp;Elvira Verduci ,&nbsp;Sharon Evans ,&nbsp;Anita MacDonald","doi":"10.1016/j.ymgmr.2025.101252","DOIUrl":"10.1016/j.ymgmr.2025.101252","url":null,"abstract":"<div><div>In patients with phenylketonuria (PKU), sapropterin dihydrochloride (sapropterin) lowers blood phenylalanine (Phe) and may enhance Phe tolerance in sapropterin responsive patients. Attention to its administration, particularly the timing, and giving it with food with appropriate macronutrient composition, is important. We describe two boys with PKU who improved their Phe tolerance and metabolic control when they adjusted their method of sapropterin administration. Case 1: aged 7.2<del>5</del> years with mild PKU experienced a 40 % reduction in blood Phe after a 30-day sapropterin trial (20 mg/kg). Initially, he took sapropterin once daily dissolved in water. This increased his protein tolerance from 26 g to 50 g/day and reduced his protein equivalent from protein substitute to 20 g/day. His blood Phe was a median of 230 μmol/L (range: 130–300). After six months, twice-daily dosing further improved his protein tolerance to 60 g/day, with a lower median blood Phe (130 μmol/L, range: 80–220). By age 8 years, he swallowed tablets intact with meals, ate an unrestricted protein intake (∼80 g/day), stopped protein substitute, maintained excellent metabolic control with perceived cognitive improvement. Case 2: a boy who aged 4.9<del>92</del> years with mild PKU had a 33 % reduction in blood Phe after a 30-day sapropterin (20 mg/kg) trial. Initially, he took sapropterin once daily dissolved in water, increasing his protein tolerance from 14 g to 55 g/day, and reducing protein equivalent from protein substitute to 20 g/day. Median blood Phe was 240 μmol/L (range: 120–320). At age 6.9<del>2</del> years, twice-daily dosing and swallowing intact tablets further lowered his blood Phe, to a mean of 130 μmol/L (range: 100–130). He stopped dietary protein restriction and protein substitute intake. These case studies showed clinical and dietary benefits with adjustment of sapropterin administration. It was unclear if the improvements observed were associated with twice daily sapropterin administration, attention to taking it with fat containing meals, swallowing the tablets intact, or a combination of these. Further research to monitor the efficacy and safety of administration change is necessary.</div></div>","PeriodicalId":18814,"journal":{"name":"Molecular Genetics and Metabolism Reports","volume":"45 ","pages":"Article 101252"},"PeriodicalIF":1.9,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145096334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}