Heterozygous pathogenic CPT2 p.Ser113Leu variant or acquired overload?—recurrent rhabdomyolysis of uncertain attribution: a case report

Introduction

Background

Carnitine palmitoyltransferase II (CPT II) deficiency is an autosomal recessive disorder of long-chain fatty acid oxidation; its myopathic form is an important inherited cause of recurrent exertional rhabdomyolysis, myoglobinuria, and myalgia (1-3). The myopathic form typically presents from adolescence into adulthood, with episodes precipitated by prolonged exercise, fasting, illness, or other metabolic stressors (1-4). The c.338C>T (p.Ser113Leu) variant accounts for approximately 60% of pathogenic alleles in the myopathic form (1). Symptomatic heterozygous carriers of pathogenic CPT2 variants, including p.Ser113Leu, have also been described with exertional attacks and intermediate CPT II enzyme activity, although such monoallelic presentations remain uncommon and incompletely characterized (5,6). Diagnosis can be challenging because supportive findings such as serum creatine kinase (CK) elevation and acylcarnitine abnormalities may be intermittent or nondiagnostic, the clinical definition of rhabdomyolysis itself is heterogeneous, and molecular or enzymatic confirmation is often required when clinical suspicion remains high (1,4,7,8).

Rationale and knowledge gap

Published literature describes CPT II deficiency in athletes and other highly active patients (9,10), and separate case reports identify bodybuilding, anabolic-androgenic steroid (AAS) exposure, and exogenous testosterone as independent precipitants of rhabdomyolysis (11-13). Symptomatic heterozygous CPT2 carriage has also been reported but is uncommon and incompletely characterized (5,6). The retrieved literature did not identify a clearly analogous case combining a heterozygous pathogenic CPT2 variant with frequent exertional stress through both bodybuilding and labor-intensive work, prior AAS use, and continuing supratherapeutic testosterone therapy (5,6,9-13).

Objective

We describe a patient with overlapping inherited and acquired risk factors for recurrent rhabdomyolysis in whom a heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant was identified, illustrating the diagnostic challenge of attribution when acquired precipitants are concurrently plausible and a single heterozygous CPT2 finding is identified in a classically autosomal recessive disorder. We present this article in accordance with the CARE reporting checklist (available at https://jeccm.amegroups.com/article/view/10.21037/jeccm-2026-0031/rc).

Case presentation

All procedures performed in this study were in accordance with the ethical standards of the institutional and/or national research committee(s) and with the Declaration of Helsinki and its subsequent amendments. Written informed consent was obtained from the patient for the publication of this case report. A copy of the written consent is available for review by the editorial office of this journal.

A 49-year-old man with hypertension, chronic kidney disease, prior AAS use, ongoing supratherapeutic exogenous testosterone therapy, and prior alcohol use disorder presented with recurrent rhabdomyolysis later associated with a heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant.

He was an active bodybuilder who trained with weights six times per week while working in a physically demanding role requiring strenuous lifting. He was receiving testosterone therapy at an outside community men’s hormone-optimization clinic, with injectable testosterone cypionate 400 mg administered three times weekly, well in excess of standard physiologic replacement targets and consistent with a wellness- or performance-oriented protocol. Social history included prior alcohol use disorder with abstinence since 2023 and a 20 pack-year smoking history; he had quit smoking 9 years earlier and continued to vape daily. Recurrent episodes of rhabdomyolysis began in 2022, with prior hospitalizations at multiple outside institutions complicated by hyperCKemia, hyperkalemia, and acute kidney injury, and with subsequent chronic kidney disease attributed to this recurrent course. He had previously been evaluated by neurology in 2023, when his presentation was felt to reflect AAS-associated hyperCKemia with renal toxicity; he elected to discontinue boldenone and defer further testing including electromyography (EMG) and muscle biopsy.

During his first two visits to the emergency department (ED) at Mayo Clinic Hospital in Phoenix, Arizona, he established a recurrent pattern of symptomatic rhabdomyolysis managed supportively and initially attributed to heavy exercise and strenuous labor. On his first visit, he reported five to six days of chest pain, diffuse myalgias, and muscle cramps; body mass index (BMI) was 29.7 kg/m², examination was otherwise unremarkable, and electrocardiogram (ECG) was nonischemic. Initial laboratory evaluation showed serum CK 4,092 IU/L, blood urea nitrogen (BUN) 24 mg/dL, creatinine 1.4 mg/dL, mild transaminitis [aspartate aminotransferase (AST) 82 IU/L, alanine aminotransferase (ALT) 66 IU/L], and urinalysis with grade 1 proteinuria and 41–50 red blood cells per high-power field. He received standard supportive care including intravenous fluid resuscitation; CK downtrended to 877 IU/L and he was discharged on hospital day 4. He returned approximately two months later with diffuse cramping and spasms following exercise, despite switching to lighter, high-repetition workouts. Repeat evaluation showed CK 4,028 IU/L with renal function near baseline; he was discharged after CK downtrended to 1,261 IU/L, with counseling to limit exertion to routine activities of daily living (ADLs).

At his third presentation, he again reported substernal chest pressure beginning at work and bilateral lower extremity cramping; his last workout had been three days earlier. Laboratory evaluation showed CK 5,644 IU/L, BUN 26.6 mg/dL, creatinine 1.87 mg/dL, estimated glomerular filtration rate (eGFR) 44 mL/min/1.73 m², AST 120 IU/L, ALT 98 IU/L, and C-reactive protein <3.0 mg/L. Renal ultrasound showed mildly increased parenchymal echogenicity. Cardiac evaluation showed troponin elevation to 41 ng/L with serial downtrend; ECG remained nonischemic. Transthoracic echocardiogram demonstrated a left ventricular ejection fraction of 48% with mild hypokinesis and regional wall motion abnormalities, and coronary angiography demonstrated a 100% discrete occlusion of the first right posterolateral branch, with a small distal segment and collateral filling from the second septal perforator; no intervention was performed. Given the limited territory subtended and the presence of collateral supply, this lesion was not considered a culprit for the observed findings, and no alternative structural cause of the mild systolic dysfunction or troponin elevation was identified. Repeat echocardiography during a subsequent admission demonstrated an ejection fraction of 55% without wall motion abnormalities. CK downtrended to 748 IU/L prior to discharge. Unlike prior admissions, this episode was marked by acute kidney injury and cardiac abnormalities, prompting broader etiologic evaluation.

Following this admission, he was referred to neuromuscular neurology while recurrent presentations continued during the workup. An Invitae genetic panel and metabolic myopathy panel identified a heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant; no other pathogenic or likely pathogenic variants were reported, including in genes associated with glycogen storage disorders, other fatty acid oxidation defects, or RYR1-related disorders. The variant was classified as pathogenic by the testing laboratory using criteria from the American College of Medical Genetics and Genomics/Association for Molecular Pathology (ACMG/AMP), concordant with its classification in ClinVar, where it is reported as pathogenic by multiple submitters (14). In parallel, he was evaluated by a metabolic dietitian and counseled to adopt a high-carbohydrate, low-fat diet, with adjunctive supplementation using medium-chain triglyceride (MCT) oil 10 mL three times daily and L-carnitine 500 mg twice daily, and to avoid prolonged fasting and strenuous exercise.

At neuromuscular evaluation, he reported no weakness and no ocular or bulbar symptoms, and neurologic examination was normal. Baseline aldolase, carnitine, and acylcarnitine levels were obtained: total carnitine 41 nmol/mL, free carnitine 37 nmol/mL, acylcarnitine 4 nmol/mL, and acylcarnitine-to-free carnitine ratio 0.1; all values fell within the laboratory reference range, although the precise interval between specimen collection and the most recent acute episode could not be confirmed and may have influenced interpretation. Through shared decision-making, he declined EMG and muscle biopsy. He was offered, and declined, a work-accommodation letter for a less physically demanding role. He was then referred to clinical genomics for diagnostic clarification.

At clinical genomics evaluation, blood carnitine levels were not significantly reduced, and there was no reported consanguinity or family history of similar disease. Counseling focused on prevention through avoidance of prolonged fasting, prolonged exercise, and other known triggers; adherence to dietary recommendations and supplementation; adequate hydration; use of an emergency care plan during intercurrent illness; and reduction of supraphysiologic testosterone dosing, including discussion of associated cardiovascular and renal risk. Whole genome sequencing subsequently confirmed the heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant; no second pathogenic CPT2 allele was identified, although this finding does not exclude undetected deep intronic or structural variation. Cascade testing of relatives was not pursued in the absence of a family history suggestive of related manifestations, and inheritance of the variant and segregation data therefore remain undetermined.

Despite diagnostic clarification and specialist counseling, recurrent presentations continued with a similar pattern of symptoms, elevated CK, supportive intravenous fluid resuscitation, pain control, and short inpatient stays, as summarized in Table 1. The longitudinal serum CK trend across hospitalizations is shown in Figure 1. Over approximately 1 year, he was hospitalized 13 times at Mayo Clinic Hospital in Phoenix, Arizona, with admission CK ranging from 2,907 to 5,961 IU/L (median 4,648 IU/L) and discharge values remaining above the reference range in every episode (592 to 2,181 IU/L). Episodes recurred at intervals of 14 to 58 days, without discernible change in frequency or CK magnitude, and presentations have continued beyond this reporting period.

Figure 1 Longitudinal trend in serum CK across recurrent hospitalizations for rhabdomyolysis. Serum CK values from 13 inpatient presentations are displayed by days from initial presentation at Mayo Clinic Hospital in Phoenix, Arizona. Each hospitalization appears as a vertical line joining the filled marker (admission CK) at the upper end to the open marker (discharge CK) at the lower end, so the line length represents the in-hospital decline; marker color denotes the diagnostic and management phase, as shown in the key. The dashed line marks the upper limit of normal serum CK (400 IU/L) at the reporting laboratory. Hospital-day 4 and hospital-day 5 measurements during visit 11 overlap on the plot because the successive CK values were nearly identical. CK, creatine kinase; MCT, medium-chain triglyceride.

Patient perspective

The patient consistently described competitive bodybuilding and labor-intensive work as central to his identity, livelihood, and daily routine. He framed his physical conditioning, gym schedule, and on-the-job lifting as personally meaningful and not readily replaceable, and expressed clear reluctance to substantially modify training intensity, accept a less physically demanding role, or step away from his hormone-optimization regimen. He acknowledged that frequent fasting around training, irregular meal timing dictated by his work schedule, and inconsistent dietary adherence were difficult to reconcile with the recommended low-fat, high-carbohydrate, frequent-meal pattern, and indicated that any management plan he could realistically maintain would need to preserve his identity as a bodybuilder and his ability to perform physically demanding work.

Discussion

Key findings

This case describes a 49-year-old man with recurrent rhabdomyolysis, chronic kidney disease, prior AAS use, ongoing supratherapeutic exogenous testosterone therapy, and substantial exertional burden through both bodybuilding and labor-intensive work. His repeated presentations were initially explainable by several plausible acquired precipitants. Genetic evaluation identified a single heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant, and whole genome sequencing did not identify a second pathogenic allele. The biochemical phenotype was nondiagnostic, with carnitine and acylcarnitine values within reference range, and CPT II enzyme activity was not directly assessed because EMG and muscle biopsy were declined. The data are therefore most accurately summarized as a heterozygous pathogenic CPT2 finding in a patient with a clinically compatible exertional rhabdomyolysis phenotype, rather than as a molecularly or enzymatically confirmed CPT II deficiency.

Myopathic CPT II deficiency is classically autosomal recessive and is most often confirmed when biallelic pathogenic CPT2 variants are present, supported by characteristic acylcarnitine abnormalities or reduced enzyme activity (1,4,7,15,16). In our patient, none of these confirmatory features is available, and the phenotype overlaps substantially with disorders driven by AAS exposure, supratherapeutic androgen therapy, exertional injury, and superimposed renal disease (11-13). Existing literature does include symptomatic heterozygous carriers, including p.Ser113Leu-positive athletes with exertional attacks and intermediate CPT II enzyme activity, providing biologic plausibility for a real but partial monoallelic effect; even there, undetected second pathogenic alleles cannot always be excluded (1,5,6). The interpretive frame that best fits the data in our patient is therefore one of a clinically plausible but unconfirmed contribution from a heterozygous CPT2 variant, layered on multiple acquired stressors rather than a fully isolated monogenic explanation.

Strengths and limitations

A major strength of this case is the availability of longitudinal single-site follow-up across approximately 1 year, with broad multidisciplinary involvement spanning emergency medicine, internal medicine, nephrology, cardiology, neuromuscular neurology, metabolic dietetics, and clinical genomics. This perspective allowed recurrent presentations to be interpreted as a pattern, supported escalation from supportive ED management to genetic and metabolic evaluation, and enabled identification of a pathogenic CPT2 finding that might otherwise have gone unrecognized in a setting of episodic symptoms, competing acquired explanations, and nondiagnostic interictal testing (1-4,7,15,16). Diagnostic information was integrated into a multifaceted, evidence-informed prevention framework consistent with published management approaches for myopathic CPT II deficiency (1,15-17).

Several limitations require explicit acknowledgment. First, the molecular finding is a single heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant in a classically autosomal recessive disorder; symptomatic monoallelic disease has been reported but is uncommon, and an occult second pathogenic allele—particularly outside the regions reliably captured by short-read sequencing—cannot be fully excluded (1,5,6). Second, the biochemical phenotype was nondiagnostic, with carnitine and acylcarnitine values within reference range; specimen timing relative to the most recent episode was uncertain and may have reduced sensitivity, but an unrevealing acylcarnitine profile nonetheless weakens rather than supports a confirmed diagnosis (1,4,7). Third, the patient declined EMG and muscle biopsy; CPT II enzyme activity was therefore not assessed, removing the most specific confirmatory step (1,3,7). Recurrent rhabdomyolysis with a single pathogenic CPT2 allele and a nondiagnostic acylcarnitine profile warrants enzyme testing, and a leukocyte- or fibroblast-based assay remains a reasonable alternative to biopsy that is under consideration for our patient (1). Fourth, this is a single-patient report with multiple plausible precipitating factors, which contributes to its descriptive value but prevents definitive attribution of any single recurrence to one isolated trigger or mechanism (3,15,16,18). Fifth, despite diagnostic clarification, counseling, and prevention strategies, the patient has not yet achieved sustained reduction in recurrence; persistent exertional burden, unchanged testosterone dosing, and incomplete dietary adherence likely remain important contributors (1,11-13,15-17). He has nonetheless made meaningful risk-reduction efforts, including discontinuing AAS, abstaining from alcohol, remaining off cigarettes, and reporting adherence to supplementation. Because the behavioral components of the plan have not been consistently implemented, the effectiveness of the multidisciplinary approach cannot be assessed from this case.

Comparison with similar research

Prior reports describe CPT II deficiency in athletes and other highly active individuals with recurrent exertional rhabdomyolysis, while separate reports show that bodybuilding, AAS exposure, and exogenous testosterone can each precipitate rhabdomyolysis without documented CPT II deficiency (1,9-13). Symptomatic heterozygous carriers, including p.Ser113Leu-positive athletes, have been described (1,5,6). A recent series reported two patients with myopathic CPT II deficiency carrying p.Ser113Leu as the sole identified variant, in whom reduced CPT II activity on muscle biopsy or a post-fasting acylcarnitine profile confirmed or supported the diagnosis (19). The heterozygous finding in our patient is therefore not unprecedented, but with CPT II activity unmeasured and a normal interictal acylcarnitine profile, it rests on the clinical phenotype alone. Broader cohort data reinforce this interpretive difficulty: among 23 patients with recurrent rhabdomyolysis, EMG, muscle biopsy, and nuclear DNA testing were largely nondiagnostic, with a definitive genetic cause established in only 1 of 20 patients tested (20). Our case is distinguished less by any single feature than by the coexistence of recurrent rhabdomyolysis, exertional stress through bodybuilding and labor-intensive work, prior AAS use, high-dose testosterone therapy, and a heterozygous pathogenic CPT2 variant within one patient (1,5,6,9-13,15,16).

Explanations of findings

After identification of a pathogenic CPT2 variant, this patient’s recurrent exertional rhabdomyolysis, persistent hyperCKemia, and episodic pattern became clinically compatible with the myopathic phenotype of CPT II deficiency, which is often episodic and may remain underrecognized because routine studies including acylcarnitine testing may be nondiagnostic outside periods of metabolic stress (1,4,7,15,16). The patient’s acquired factors likely amplified expression rather than replaced it as an explanation: repeated heavy exertion, incomplete adherence to dietary modification and fasting avoidance, and his high-dose testosterone regimen plausibly increased catabolic stress and lowered the threshold for recurrent episodes in a patient with underlying metabolic susceptibility (1,11-13,15-17). Admission CK values were consistently lower than those typically reported during crises in CPT II deficiency (19). A single functional allele may confer partial rather than complete deficiency, with reduced long-chain fatty acid oxidation reflecting the intermediate enzyme activity described in symptomatic heterozygotes (5,6). Such a state could plausibly predispose to recurrent episodes of more moderate severity under repeated exertional and metabolic stress. The mild left ventricular dysfunction, regional wall motion abnormalities, and modest troponin elevation observed during the third presentation occurred without obstructive disease in a corresponding territory and are of uncertain etiology. Long-term anabolic and supratherapeutic androgen exposure is associated with reduced left ventricular systolic function and is one plausible contributor (21), although the abnormalities arose during an episode of rhabdomyolysis with acute kidney injury and subsequently resolved, and cardiac magnetic resonance imaging was not obtained.

Implications and actions needed

Recurrent rhabdomyolysis should trigger consideration of an inherited or contributing metabolic myopathy, particularly when severity, recurrence pattern, or persistence is not fully explained by acquired precipitants alone (1,3,4,7,15,16,18). Normal or nondiagnostic screening should not end the workup when clinical suspicion remains high, because myopathic CPT II deficiency can be missed if clinicians rely too heavily on routine testing obtained outside an acute episode (1,4,7,15,16). For the emergency clinician, a recurrent rhabdomyolysis pattern—especially across multiple institutions—warrants explicit handoff to longitudinal subspecialty workup rather than repeated episodic management. Recurrence may persist when occupational, behavioral, and pharmacologic stressors cannot be fully modified (1,5,6,11-13,15-17).

Conclusions

We report a 49-year-old man with recurrent rhabdomyolysis, chronic kidney disease, prior AAS use, continued high-dose testosterone therapy, and substantial exertional burden through bodybuilding and labor-intensive work, in whom a heterozygous pathogenic CPT2 c.338C>T (p.Ser113Leu) variant was identified. The diagnosis is best framed not as an isolated, confirmed CPT II deficiency but as a clinically compatible heterozygous CPT2 finding layered on overlapping acquired precipitants in the absence of biochemical or enzymatic confirmation. Clinicians should maintain a broadened differential for inherited metabolic myopathy when acquired triggers do not fully explain the phenotype, and pair diagnostic evaluation with sustained, patient-centered management of modifiable contributors.

Acknowledgments

None.

Footnote

Reporting Checklist: The authors have completed the CARE reporting checklist. Available at https://jeccm.amegroups.com/article/view/10.21037/jeccm-2026-0031/rc

Peer Review File: Available at https://jeccm.amegroups.com/article/view/10.21037/jeccm-2026-0031/prf

Funding: None.

Conflicts of Interest: All authors have completed the ICMJE uniform disclosure form (available at https://jeccm.amegroups.com/article/view/10.21037/jeccm-2026-0031/coif). The authors have no conflicts of interest to declare.

Ethical Statement: The authors are accountable for all aspects of the work in ensuring that questions related to the accuracy or integrity of any part of the work are appropriately investigated and resolved. All procedures performed in this study were in accordance with the ethical standards of the institutional and/or national research committee(s) and with the Declaration of Helsinki and its subsequent amendments. Written informed consent was obtained from the patient for the publication of this case report. A copy of the written consent is available for review by the editorial office of this journal.

Open Access Statement: This is an Open Access article distributed in accordance with the Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License (CC BY-NC-ND 4.0), which permits the non-commercial replication and distribution of the article with the strict proviso that no changes or edits are made and the original work is properly cited (including links to both the formal publication through the relevant DOI and the license). See: https://creativecommons.org/licenses/by-nc-nd/4.0/.

References

1. LoPiccolo MK, Vockley J. Carnitine palmitoyltransferase II deficiency. In: Adam MP, Bick S, Mirzaa GM, et al., editors. GeneReviews® [Internet]. Seattle (WA): University of Washington, Seattle; 1993-2026. [cited 2026 Apr 22]. Available from: https://www.ncbi.nlm.nih.gov/books/NBK1253/
2. Deschauer M, Wieser T, Zierz S. Muscle carnitine palmitoyltransferase II deficiency: clinical and molecular genetic features and diagnostic aspects. Arch Neurol 2005;62:37-41. [Crossref] [PubMed]
3. Ivin N, Della Torre V, Sanders F, et al. Rhabdomyolysis caused by carnitine palmitoyltransferase 2 deficiency: A case report and systematic review of the literature. J Intensive Care Soc 2020;21:165-73. [Crossref] [PubMed]
4. Yazıcı H, Ak G, Çelik MY, et al. Experience with carnitine palmitoyltransferase II deficiency: diagnostic challenges in the myopathic form. J Pediatr Endocrinol Metab 2024;37:33-41. [Crossref] [PubMed]
5. Joshi PR, Deschauer M, Zierz S. Clinically symptomatic heterozygous carnitine palmitoyltransferase II (CPT II) deficiency. Wien Klin Wochenschr 2012;124:851-4. [Crossref] [PubMed]
6. Ørngreen MC, Dunø M, Ejstrup R, et al. Fuel utilization in subjects with carnitine palmitoyltransferase 2 gene mutations. Ann Neurol 2005;57:60-6. [Crossref] [PubMed]
7. Lu CH, Yang CF, Chen YR, et al. Recurrent rhabdomyolysis caused by palmitoyltransferase II (CPT-2) deficiency but complete normal acylcarnitine profile: A patient presentation and review of the literature. Mol Genet Metab Rep 2024;41:101151. [Crossref] [PubMed]
8. Stahl K, Rastelli E, Schoser B. A systematic review on the definition of rhabdomyolysis. J Neurol 2020;267:877-82. [Crossref] [PubMed]
9. Faigel HC. Carnitine palmitoyltransferase deficiency in a college athlete: a case report and literature review. J Am Coll Health 1995;44:51-4. [Crossref] [PubMed]
10. Krivickas LS. Recurrent rhabdomyolysis in a collegiate athlete: a case report. Med Sci Sports Exerc 2006;38:407-10. [Crossref] [PubMed]
11. Daniels JM, van Westerloo DJ, de Hon OM, et al. Rhabdomyolysis in a bodybuilder using steroids. Ned Tijdschr Geneeskd 2006;150:1077-80. [Article in Dutch]. [PubMed]
12. Braseth NR, Allison EJ Jr, Gough JE. Exertional rhabdomyolysis in a body builder abusing anabolic androgenic steroids. Eur J Emerg Med 2001;8:155-7. [Crossref] [PubMed]
13. Reddy R, Lizama-Hernández S, Port AM. Localized Rhabdomyolysis Associated With Testosterone Enanthate for Gender-Affirming Hormonal Therapy. AACE Clin Case Rep 2022;8:264-6. [Crossref] [PubMed]
14. ClinVar [Internet]. Bethesda (MD): National Center for Biotechnology Information; 2013. Accession VCV000008953, NM_000098.3(CPT2):c.338C>T (p.Ser113Leu). [cited 2026 Aug 23]. Available from: https://www.ncbi.nlm.nih.gov/clinvar/variation/8953/
15. Balasubramanian M, Jenkins TM, Kirk RJ, et al. Recurrent rhabdomyolysis caused by carnitine palmitoyltransferase II deficiency, common but under-recognised: Lessons to be learnt. Mol Genet Metab Rep 2018;15:69-70. [Crossref] [PubMed]
16. Akar HT, Yıldız Y, Mutluay R, et al. Adult-onset carnitine palmitoyl transferase II (CPT II) deficiency presenting with rhabdomyolysis and acute kidney injury. CEN Case Rep 2024;13:81-5. [Crossref] [PubMed]
17. Roe CR, Yang BZ, Brunengraber H, et al. Carnitine palmitoyltransferase II deficiency: successful anaplerotic diet therapy. Neurology 2008;71:260-4. [Crossref] [PubMed]
18. Nance JR, Mammen AL. Diagnostic evaluation of rhabdomyolysis. Muscle Nerve 2015;51:793-810. [Crossref] [PubMed]
19. Politei J, Berardo A, Calabrese E, et al. Long-Chain Fatty Acid Beta-Oxidation Defects: A Case Series and Literature Review. Lipids 2026;61:207-15. [Crossref] [PubMed]
20. Nandakumar D, Bhai S. Evaluating efficacy of clinical tools in determining causes of recurrent rhabdomyolysis. Neuromuscul Disord 2026;60:106333. [Crossref] [PubMed]
21. Baggish AL, Weiner RB, Kanayama G, et al. Cardiovascular Toxicity of Illicit Anabolic-Androgenic Steroid Use. Circulation 2017;135:1991-2002. [Crossref] [PubMed]