BCAAs
The branched-chain amino acids — leucine, isoleucine and valine — grouped and sold as a sports supplement for muscle growth and recovery. Leucine is the key mTOR trigger.
BCAAs at a Glance
The branched-chain amino acids are three of the nine essential amino acids — leucine, isoleucine and valine — named for the branching carbon side chain they share. All three must come from dietary protein, and together they account for roughly 35% of the essential amino acids in muscle protein.
What makes them unusual is where they are handled. Most amino acids are processed first in the liver; BCAAs largely bypass it and are taken up and metabolised directly in skeletal muscle. That muscle-centric metabolism is why they are marketed so heavily for sport.
Of the three, leucine is the pharmacologically interesting one — the primary amino-acid trigger of the mTORC1 pathway that switches on muscle protein synthesis. Isoleucine and valine are much weaker anabolic signals on their own.
The central evidence problem is that BCAAs are building blocks you already get from any complete protein. So the question is rarely “do they do something” but “do they add anything on top of adequate protein” — and for most healthy people eating enough protein, the honest answer is little.
The strongest human evidence for BCAAs is not in the gym at all. It is in liver disease, where they work as a targeted nutritional therapy correcting a disease-driven amino-acid imbalance.
The Three BCAAs
Each branched-chain amino acid has its own page:
| Amino acid | Role | Page |
|---|---|---|
| Leucine | The main mTOR trigger for muscle protein synthesis | L-Leucine |
| Isoleucine | Glucose uptake and energy metabolism | L-Isoleucine |
| Valine | Muscle energy metabolism and tissue repair | L-Valine |
What They’re Used For
- Hepatic encephalopathy — the strongest evidence base BCAAs have, and it has nothing to do with sport.
- Muscle soreness & damage — real but modest, and heterogeneous.
- Muscle protein synthesis — a genuine rise, but sub-maximal compared with whey or a full EAA blend.
- Cirrhosis nutritional support — specialist clinical nutrition, not a consumer use.
- Elderly muscle mass — conditional on adequate protein and resistance training.
- Exercise performance — heavily marketed, weakly supported.
- Tardive dyskinesia — a small, unreplicated niche.
The honest picture on the flagship claim. Leucine can flip the anabolic switch, but sustained muscle protein synthesis needs the full set of essential amino acids as raw material. When total protein intake is already adequate, a complete protein source or a full EAA blend generally does the same job or better. BCAAs are best understood as a convenience format, not a uniquely powerful one.
How It Works
BCAAs are the amino acids the liver mostly ignores. Hepatic branched-chain aminotransferase activity is low, so they pass into systemic circulation and are oxidised in skeletal muscle — the anatomical fact behind their entire sports reputation.
Leucine does the signalling. It is sensed directly and permits mTORC1 activation, which initiates the translation machinery of muscle protein synthesis. Isoleucine and valine do not meaningfully share that property.
But signalling is not substrate. Building protein needs all nine essential amino acids. Taking the three signalling ones in isolation flips the switch without supplying the material — which is precisely why isolated BCAAs produce a smaller synthesis response than an equivalent dose of whey.
Two other mechanisms matter away from the gym. In cirrhosis, circulating BCAAs fall while aromatic amino acids rise; restoring the ratio supports ammonia detoxification through glutamine synthesis and reduces false-neurotransmitter effects on the brain. And because BCAAs compete with aromatic amino acids for the large-neutral-amino-acid transporter at the blood–brain barrier, a BCAA load transiently lowers brain tryptophan uptake — the basis of both the central-fatigue hypothesis and the tardive-dyskinesia work.
The full trial record is in Pharmacology & Research below.
What It's Used For
The branched-chain amino acids (BCAAs) — leucine, isoleucine and valine — are three of the nine essential amino acids, named for their branched carbon side chains and unusual in that they are metabolised largely in skeletal muscle rather than the liver. Their reputation as a sports supplement rests almost entirely on leucine, the primary amino-acid trigger of the mTORC1 pathway that switches on muscle protein synthesis. The central evidence problem is that BCAAs are building blocks the body already gets from any complete protein, so the decision-relevant question is rarely “do they do something” but “do they add anything on top of adequate protein intake” — and for most healthy people who eat enough protein, the honest answer is little. The strongest human evidence for BCAAs is not in the gym at all but in liver disease, where they behave as a targeted nutritional therapy. Throughout, watch two caveats: much sports data is small and industry-adjacent, and taking three amino acids in isolation cannot sustain protein synthesis without the full essential-amino-acid set as raw material.
Support is an experimental score I’m building — a composite weighted by study type (human > animal > in vitro > review) and study volume, then tempered for consistency, form and whether the effect depends on an underlying deficiency or disease state. It’s a beta: a fast way to rank strength of evidence at a glance, not a validated metric. Each application links down to its write-up.
This is the strongest evidence base BCAAs have, and it has nothing to do with sport. A 2017 Cochrane systematic review and meta-analysis pooled 16 randomized trials (827 participants) and found that oral BCAA supplementation improved hepatic encephalopathy — a neuropsychiatric complication of liver failure — compared with control, with no effect on mortality, quality of life or nutritional parameters 1Reference 1Meta-analysisBranched-chain amino acids for people with hepatic encephalopathy — systematic review / meta-analysisView study →.
The mechanism is plausible: in cirrhosis, circulating BCAAs fall while aromatic amino acids rise, and correcting that ratio is thought to reduce ammonia-driven and false-neurotransmitter effects on the brain. The Cochrane authors judged the evidence for the symptom benefit to be of moderate quality.
Gap: the benefit is a correction of a disease-driven amino-acid imbalance, not a general nootropic or cognitive effect — it does not transfer to healthy people, and it did not improve survival.
Several meta-analyses of randomized trials show BCAAs modestly reduce delayed-onset muscle soreness and blunt the rise in muscle-damage biomarkers (creatine kinase, LDH) after strenuous or eccentric exercise 2,
A 2019 meta-analysis found a significant reduction in perceived soreness 2Reference 2Meta-analysisEffect of branched-chain amino acid supplementation on muscle soreness following exercise: a meta-analysisView study →.
A 2017 meta-analysis of RCTs reported lower creatine kinase and soreness with supplementation 3Reference 3Meta-analysisBranched-chain amino acid supplementation and exercise-induced muscle damage in exercise recovery: a meta-analysis of randomized clinical trialsView study →.
A 2024 systematic review with meta-regression concluded the effect is real but depends heavily on dose, timing (loading before the bout) and the degree of muscle damage, with substantial between-study heterogeneity 4Reference 4Meta-analysisAttenuating muscle damage biomarkers and muscle soreness after exercise-induced muscle damage with BCAA supplementation — systematic review and meta-analysis with meta-regressionView study →.
Typical protocols used around 10–20 g/day, often started days before the exercise challenge.
Gap: effect sizes are small-to-moderate and the literature is heterogeneous and often industry-funded; the practical difference in recovery for a typical trainee eating enough protein is modest.
Leucine is a genuine anabolic signal: a 2017 crossover RCT showed that 5.6 g of BCAAs after resistance exercise raised myofibrillar muscle protein synthesis by about 22% versus placebo 5Reference 5RCTBranched-chain amino acid ingestion stimulates muscle myofibrillar protein synthesis following resistance exercise in humans — randomized crossover trialView study →.
But — and this is the load-bearing caveat — that rise was substantially lower than what an equivalent dose of whey protein or a complete essential-amino-acid mixture produces, because sustained synthesis needs all nine essential amino acids as substrate, not just the three signalling ones 6Reference 6ReviewBranched-chain amino acids and muscle protein synthesis in humans: myth or reality? — reviewView study →.
A widely-cited 2017 review framed BCAAs-for-muscle as “myth or reality” and concluded that BCAAs alone cannot support a maximal or sustained anabolic response in humans 6Reference 6ReviewBranched-chain amino acids and muscle protein synthesis in humans: myth or reality? — reviewView study →.
Co-ingestion with carbohydrate does raise the response somewhat 18Reference 18Co-ingestion of branched-chain amino acids and carbohydrate stimulates myofibrillar protein synthesis following resistance exercise in trained young menView study →.
Gap: leucine flips the switch, but the other EAAs are the raw material; in anyone eating adequate protein, isolated BCAAs are a convenience format, not a superior one.
Beyond acute encephalopathy, BCAAs have been tested as long-term nutritional therapy in cirrhosis. A 2003 double-blind, multicentre RCT (174 patients over one year) found that oral BCAA supplements improved event-free survival, nutritional status and self-rated health compared with iso-nitrogenous or iso-caloric controls — although adherence was a challenge because of palatability 7Reference 7RCTNutritional supplementation with branched-chain amino acids in advanced cirrhosis: a double-blind, randomized trialView study →.
The rationale is the same amino-acid imbalance seen in liver failure, plus the BCAAs’ role in supporting muscle mass and ammonia detoxification.
Gap: endpoints are relatively soft (composite event-free survival, nutritional indices) and adherence to the unpalatable formulas was poor; this is specialist clinical nutrition, not a consumer use.
In older adults, the anabolic resistance of ageing muscle makes leucine of particular interest. A 2015 systematic review and meta-analysis found leucine supplementation significantly improved muscle protein synthesis and, in some analyses, lean body mass in older people 8Reference 8Meta-analysisThe effectiveness of leucine on muscle protein synthesis, lean body mass and leg lean mass accretion in older people: a systematic review and meta-analysisView study →.
However, a 2021 umbrella review of systematic reviews on nutritional interventions for muscle in older adults concluded that amino-acid and leucine supplements show benefit mainly when combined with adequate total protein and resistance exercise, and that isolated supplementation has limited stand-alone effect 9Reference 9Meta-analysisNutritional interventions to improve muscle mass, muscle strength, and physical performance in older people: an umbrella review of systematic reviews and meta-analysesView study →.
Gap: benefit is largely conditional on being combined with protein and training, and is strongest in those with low baseline intake — closer to correcting a shortfall than adding a bonus.
Despite heavy marketing, BCAAs do not reliably improve athletic performance. A 2022 systematic review of oral BCAA supplementation in athletes found inconsistent effects on performance outcomes despite frequent changes in blood markers 10Reference 10Systematic reviewOral branched-chain amino acids supplementation in athletes: a systematic reviewView study →, and a 2026 systematic review specifically on endurance performance concluded that biochemical markers — reduced ammonia, altered tryptophan ratios — often move while actual clinical performance endpoints rarely do 11Reference 11Systematic reviewBranched-chain amino acid supplementation and endurance performance: reporting guidelines and systematic review of biochemical vs clinical evidenceView study →.
The “central fatigue” hypothesis, that BCAAs compete with tryptophan for brain uptake and delay perceived fatigue, is mechanistically coherent 15Reference 15ReviewBranched-chain amino acids and central fatigue — reviewView study → but has not translated into robust performance gains.
Gap: the field repeatedly reports biochemical changes as if they were performance benefits; head-to-head, clinical endpoints such as time-trial and power output usually show no meaningful improvement.
A small niche use: randomized trials suggested BCAAs reduced the involuntary movements of tardive dyskinesia — a drug-induced movement disorder — with a 2003 RCT in men reporting significant symptom reduction over 3 weeks 12Reference 12RCTEfficacy of the branched-chain amino acids in the treatment of tardive dyskinesia in men — randomized controlled trialView study →. The proposed mechanism involves lowering aromatic-amino-acid availability and altering brain neurotransmitter synthesis.
Gap: trials are small, mostly in men, and have not been replicated at scale or translated into guideline-level recommendations; newer VMAT2 inhibitors are the evidence-based therapy.
Mechanisms
| Target / pathway | Effect | Relevant to |
|---|---|---|
| mTORC1 (via leucine) | ↑ initiation of muscle protein synthesis | Muscle protein synthesiselderly muscle mass |
| Skeletal-muscle BCAA transaminase / BCKDH | Direct muscle uptake and oxidation, bypassing the liver | Exercise energymuscle metabolism |
| Ammonia detoxification (glutamine synthesis) | ↓ circulating ammonia; corrects the BCAA:AAA ratio | Hepatic encephalopathycirrhosis |
| Large-neutral-amino-acid transporter at the blood–brain barrier | ↓ brain tryptophan and aromatic-AA uptake → altered serotonin/dopamine synthesis | Central fatiguetardive dyskinesia |
| Branched-chain keto acid / insulin signalling | Elevated BCAAs associate with insulin resistance | Metabolic-safety caveat |
Pharmacokinetics
BCAAs are absorbed rapidly from the small intestine and, unusually, escape first-pass hepatic metabolism — the liver has low branched-chain aminotransferase activity, so BCAAs pass into the systemic circulation and are taken up and oxidised primarily in skeletal muscle. Plasma leucine peaks within roughly 30 minutes to an hour of an oral dose, and free amino acids have short circulating half-lives because they are rapidly partitioned into tissue pools or oxidised.
Co-ingestion with carbohydrate raises insulin and can further stimulate the myofibrillar protein-synthesis response 18Reference 18Co-ingestion of branched-chain amino acids and carbohydrate stimulates myofibrillar protein synthesis following resistance exercise in trained young menView study →. Because they compete with aromatic amino acids for the same blood–brain-barrier transporter, a BCAA load transiently lowers brain uptake of tryptophan — the basis of the central-fatigue and tardive-dyskinesia hypotheses. There is no meaningful tissue “loading”: excess intake is oxidised.
Clinical trials
BCAAs are off-patent, cheap and widely available, so most trials are investigator-initiated — sports-nutrition and hepatology groups — rather than industry-registered drug programmes. The clinical-trial literature is largest in liver disease and exercise recovery, with dozens of completed small RCTs and comparatively little late-phase registered activity.
| Completed | Planned | Terminated | Preclinical |
|---|---|---|---|
| ~50+(mostly small RCTs) | Several | 1notable (ALS, halted for excess mortality) | Hundreds |
Last checked: August 2026.
Dietary Sources
BCAAs are not exotic: they are a normal fraction of the protein in nearly every food, making up roughly 15–25% of the amino acids in typical dietary protein and about 35% of the essential amino acids in muscle tissue. Anyone eating adequate protein is already consuming several grams a day without a supplement.
| Food (typical serving) | Approx. total BCAAs |
|---|---|
| Whey protein (1 scoop, ~25 g) | ~5–6 g |
| Chicken breast (100 g) | ~4–5 g |
| Beef (100 g) | ~4–5 g |
| Canned tuna (100 g) | ~4–5 g |
| Eggs (2 large) | ~2.5–3 g |
| Greek yogurt (200 g) | ~2.5–3 g |
| Cooked lentils / beans (1 cup) | ~2.5–3 g |
| Milk (1 cup) | ~1.5–2 g |
Animal proteins are richer in leucine and provide all three in a favourable ratio; plant proteins supply BCAAs too, but at somewhat lower leucine density — which is why plant-based diets sometimes emphasise total protein volume or leucine-rich additions.
The comparison that matters: a single serving of whey or a chicken breast delivers roughly the same BCAA quantity as a typical supplement scoop — plus the other six essential amino acids. Whole protein is the more complete way to get them.
Dosage
These are ranges from the research literature, not a personal recommendation.
There is no single Recommended Dietary Allowance for “BCAAs” as a group; requirements are set for each amino acid individually — approximately 42 mg/kg/day leucine, 19 mg/kg/day isoleucine and 24 mg/kg/day valine for healthy adults (IOM 2005), all easily met by a normal protein intake. No Tolerable Upper Intake Level has been established.
- Commercial products: typically 5–10 g per serving, often around training, usually formulated in a 2:1:1 leucine:isoleucine:valine ratio — which places leucine at roughly 2–3 g per dose, near the “leucine threshold” often cited for a maximal muscle-protein-synthesis response.
- Soreness and muscle-damage trials used higher intakes, around 10–20 g/day, frequently loaded for several days before an exercise challenge 4Reference 4Meta-analysisAttenuating muscle damage biomarkers and muscle soreness after exercise-induced muscle damage with BCAA supplementation — systematic review and meta-analysis with meta-regressionView study →.
- Clinical liver-disease protocols use larger daily amounts of specialised BCAA formulas under
supervision — on the order of 0.25 g/kg/day in hepatic-encephalopathy trials, roughly 17 g/day
for a 70 kg adult 1,
7Reference 1Meta-analysisBranched-chain amino acids for people with hepatic encephalopathy — systematic review / meta-analysisView study →Reference 7RCTNutritional supplementation with branched-chain amino acids in advanced cirrhosis: a double-blind, randomized trialView study → .
A practical caveat: because BCAAs are essential nutrients already present in dietary protein, most people meeting their protein needs from food are covering their baseline requirement regardless of whether they supplement — and a complete protein or full EAA blend provides the same signalling amino acids with the full substrate set.
Safety
BCAAs are essential nutrients found in everyday dietary protein and are well tolerated in healthy adults at food-level and typical supplemental intakes. Reported side effects at supplement doses are mild and mostly gastrointestinal.
- Well tolerated in healthy adults. Side effects at supplement doses are mild and mostly gastrointestinal — nausea, bloating.
- An unresolved ALS signal. An early randomized trial in amyotrophic lateral sclerosis was stopped for excess mortality in the BCAA arm 16Reference 16RCTBranched-chain amino acids and amyotrophic lateral sclerosis: a treatment failure? — randomized controlled trialView study →, and a Cochrane review found no benefit from amino acids in ALS 17Reference 17Systematic reviewAmino acids for amyotrophic lateral sclerosis / motor neuron disease — Cochrane systematic reviewView study →. Do not self-prescribe high doses in neurodegenerative disease.
- Insulin resistance. Chronically elevated circulating BCAAs are a consistent biomarker of insulin resistance and type-2 diabetes 13Reference 13A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistanceView study → — though the causal direction appears to run the other way 14Reference 14Genetic evidence of a causal effect of insulin resistance on branched-chain amino acid levels — Mendelian randomizationView study →. Do not assume extra BCAAs help metabolic disease.
- Kidney and liver disease. High amino-acid intakes are a nitrogen load; in liver disease BCAAs are used therapeutically but only under supervision.
- Competes with levodopa. BCAAs share the large-neutral-amino-acid transporter — separate the timing in Parkinson’s disease.
- No upper limit is set. Absence of a UL does not imply unlimited intake is safe.
Full Safety & Interactions Detail
Three points deserve honest mention.
- Insulin resistance and metabolic disease. Chronically elevated circulating BCAAs are a consistent biomarker of insulin resistance and type-2 diabetes 13Reference 13A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistanceView study →. The causal direction is contested — Mendelian-randomization evidence suggests insulin resistance raises BCAA levels rather than the reverse 14Reference 14Genetic evidence of a causal effect of insulin resistance on branched-chain amino acid levels — Mendelian randomizationView study → — but people with metabolic disease should not assume that adding BCAAs is beneficial, and may reasonably avoid high supplemental doses.
- Neurodegenerative disease. An early randomized trial in amyotrophic lateral sclerosis was stopped for excess mortality in the BCAA arm 16Reference 16RCTBranched-chain amino acids and amyotrophic lateral sclerosis: a treatment failure? — randomized controlled trialView study →, and a Cochrane review of amino acids for ALS found no evidence of benefit 17Reference 17Systematic reviewAmino acids for amyotrophic lateral sclerosis / motor neuron disease — Cochrane systematic reviewView study →. This remains an unresolved signal rather than a settled harm, but it is a clear reason not to self-prescribe high doses in neurodegenerative disease.
- Kidney and liver disease. As a nitrogen load, high supplemental amino-acid intakes warrant caution in renal impairment. In liver disease BCAAs are used therapeutically, but only under clinical supervision.
Interactions: BCAAs can theoretically compete with medications that use the large-neutral-amino-acid transporter — notably levodopa in Parkinson’s disease, where separating the timing is prudent — and may modestly influence blood glucose, which is relevant to anyone on antidiabetic drugs. These are prudence-level cautions rather than well-documented clinically significant interactions.
Scope disclosure. Interactions were assessed partially — the levodopa transporter competition and the blood-glucose consideration were reviewed; no comprehensive drug-interaction screen was performed. Pregnancy and lactation were assessed at a high level: dietary intake is necessary and appropriate, supplemental high doses are not established. No Upper Limit has been set, and absence of one does not imply unlimited intake is safe. Where something was not studied, it is marked “not assessed,” not “safe.”
Not recommended as a supplement without clinician guidance. Adequate dietary BCAAs are a normal, necessary part of protein nutrition in pregnancy and lactation, but the safety of high supplemental doses has not been established. Default to obtaining them from food.
References
- Gluud LL, Dam G, Les I, et al. (2017). Branched-chain amino acids for people with hepatic encephalopathy — systematic review / meta-analysis. Cochrane Database of Systematic Reviews. https://pubmed.ncbi.nlm.nih.gov/28518283/
- Fedewa MV, Spencer SO, Williams TD, et al. (2019). Effect of branched-chain amino acid supplementation on muscle soreness following exercise: a meta-analysis. International Journal for Vitamin and Nutrition Research. https://pubmed.ncbi.nlm.nih.gov/30938579/
- Rahimi MH, Shab-Bidar S, Mollahosseini M, Djafarian K (2017). Branched-chain amino acid supplementation and exercise-induced muscle damage in exercise recovery: a meta-analysis of randomized clinical trials. Nutrition. https://pubmed.ncbi.nlm.nih.gov/28870476/
- Salem A, Trabelsi K, Jahrami H, et al. (2024). Attenuating muscle damage biomarkers and muscle soreness after exercise-induced muscle damage with BCAA supplementation — systematic review and meta-analysis with meta-regression. Sports Medicine – Open. https://pubmed.ncbi.nlm.nih.gov/38625669/
- Jackman SR, Witard OC, Philp A, et al. (2017). Branched-chain amino acid ingestion stimulates muscle myofibrillar protein synthesis following resistance exercise in humans — randomized crossover trial. Frontiers in Physiology. https://pubmed.ncbi.nlm.nih.gov/28638350/
- Wolfe RR (2017). Branched-chain amino acids and muscle protein synthesis in humans: myth or reality? — review. Journal of the International Society of Sports Nutrition. https://pubmed.ncbi.nlm.nih.gov/28852372/
- Marchesini G, Bianchi G, Merli M, et al. (2003). Nutritional supplementation with branched-chain amino acids in advanced cirrhosis: a double-blind, randomized trial. Gastroenterology. https://pubmed.ncbi.nlm.nih.gov/12806613/
- Xu ZR, Tan ZJ, Zhang Q, et al. (2015). The effectiveness of leucine on muscle protein synthesis, lean body mass and leg lean mass accretion in older people: a systematic review and meta-analysis. British Journal of Nutrition. https://pubmed.ncbi.nlm.nih.gov/25234223/
- Gielen E, Beckwée D, Delaere A, et al. (2021). Nutritional interventions to improve muscle mass, muscle strength, and physical performance in older people: an umbrella review of systematic reviews and meta-analyses. Nutrition Reviews. https://pubmed.ncbi.nlm.nih.gov/32483625/
- Martinho DV, Nobari H, Faria A, et al. (2022). Oral branched-chain amino acids supplementation in athletes: a systematic review. Nutrients. https://pubmed.ncbi.nlm.nih.gov/36235655/
- Del Guerra GC, et al. (2026). Branched-chain amino acid supplementation and endurance performance: reporting guidelines and systematic review of biochemical vs clinical evidence. The Physician and Sportsmedicine. https://pubmed.ncbi.nlm.nih.gov/41655197/
- Richardson MA, Bevans ML, Read LL, et al. (2003). Efficacy of the branched-chain amino acids in the treatment of tardive dyskinesia in men — randomized controlled trial. American Journal of Psychiatry. https://pubmed.ncbi.nlm.nih.gov/12777270/
- Newgard CB, An J, Bain JR, et al. (2009). A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistance. Cell Metabolism. https://pubmed.ncbi.nlm.nih.gov/19356713/
- Mahendran Y, Jonsson A, Have CT, et al. (2017). Genetic evidence of a causal effect of insulin resistance on branched-chain amino acid levels — Mendelian randomization. Diabetologia. https://pubmed.ncbi.nlm.nih.gov/28184960/
- Newsholme EA, Blomstrand E (2006). Branched-chain amino acids and central fatigue — review. The Journal of Nutrition. https://pubmed.ncbi.nlm.nih.gov/16365097/
- The Italian ALS Study Group (1993). Branched-chain amino acids and amyotrophic lateral sclerosis: a treatment failure? — randomized controlled trial. Neurology. https://pubmed.ncbi.nlm.nih.gov/8255440/
- Parton M, Mitsumoto H, Leigh PN (2003). Amino acids for amyotrophic lateral sclerosis / motor neuron disease — Cochrane systematic review. Cochrane Database of Systematic Reviews. https://pubmed.ncbi.nlm.nih.gov/14583978/
- Jackman SR, Wallis GA, Yu J, et al. (2023). Co-ingestion of branched-chain amino acids and carbohydrate stimulates myofibrillar protein synthesis following resistance exercise in trained young men. International Journal of Sport Nutrition and Exercise Metabolism. https://pubmed.ncbi.nlm.nih.gov/37225168/
