AOD-9604

AOD-9604 in brief

AOD-9604 is a synthetic 16-residue peptide, Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe, closed by a Cys7 to Cys14 disulfide: the last fifteen residues of human growth hormone with a tyrosine added in front. Identity is verified across five registries, CAS 221231-10-3, and it is also catalogued as LAT-8881 by a second company. Six randomised, double-blind, placebo-controlled trials were run for obesity and the pooled safety report found no change in serum IGF-1, no adverse effect on an oral glucose tolerance test and no anti-AOD9604 antibodies; the 24-week study that was to show efficacy enrolled 534 subjects, randomised 502, and failed on its primary weight-loss endpoint, after which no approval followed and no phase 3 study was registered. That failure is documented through a later review of sponsor-reported outcomes rather than through a published trial report. It is prohibited at all times in sport, which is why most recent measurement comes from doping-control laboratories. The growth hormone receptor was ruled out as its binding site, no affinity for any target has been published, and most experiments in this family used a neighbouring peptide rather than this one.^{[1,2,3,4,5,6]}

AOD-9604 regulatory status

AOD-9604 holds no marketing authorisation under either of its names: Drugs@FDA, the European Medicines Agency medicines database and the Health Canada Drug Product Database return no record of AOD-9604 or LAT-8881 (all searched November 2026). The registered clinical record reaches phase 2: ClinicalTrials.gov lists completed phase 2 studies of LAT8881 in acute migraine and in neuropathic pain, beside a completed phase 1 study, and no phase 3 study is registered. It is prohibited at all times under the World Anti-Doping Agency 2026 Prohibited List, which names AOD-9604 as an example of a growth hormone fragment in class S2.2.3 and treats the whole of class S2 as non-specified substances. The FDA lists AOD-9604 among bulk drug substances previously in category 2 whose nominations for compounding were withdrawn by the nominators, stating a possible significant risk of immunogenicity and complexities with peptide-related impurities and characterisation, that it has no, or only limited, safety-related information, and that it has identified serious adverse events that may be associated with AOD-9604, though causality is not clear (page current as of 22 April 2026).^{[7,8,9,10,11,6,12]}

AOD-9604 at a glance

• A 16-residue peptide closed by one disulfide, positions 7 to 14, with free termini and no other modification. Positions 2 to 16 are the last fifteen residues of the human growth hormone chain; position 1 is an added tyrosine that appears in no form of the hormone.^[1,2,13]
• Identity is verified across four independent registries that agree on the sequence and the ring: the FDA substance record, PubChem, ChEBI and the hormone sequence record. CAS 221231-10-3.^[1,2,14,13]
• The growth hormone receptor is not its binding site. In cells transfected with that receptor the peptide did not compete with radiolabelled growth hormone and did not drive proliferation, while the intact hormone did both; the later development programme restates the same point.^[5,15]
• The one receptor-level positive is indirect. Both the hormone and this peptide raised beta3-adrenergic receptor RNA in obese mice toward the level seen in lean mice, and the chronic endpoints seen in wild-type mice were absent in beta3-adrenergic receptor knockout mice, while an acute reading persisted there. The authors concluded the actions are not mediated directly through that receptor: one species, one laboratory, an organism-level readout, RNA rather than protein, and no binding measured in either direction.^[16]
• Human evidence exists and is short and negative on efficacy. Six randomised, double-blind, placebo-controlled trials were run, the pooled safety report found nothing distinguishable from placebo on the growth-hormone-associated endpoints it examined, and the 24-week study enrolling 534 subjects failed on its primary weight-loss endpoint. No report of that trial was published, so the efficacy conclusion rests on a later review of sponsor-reported outcomes.^[3,4]
• No 3D structure of this molecule exists, experimental or computed, and no binding affinity for any target has been published. The one target identification in the literature rests on a pulldown using a conjugate of a metabolite rather than the peptide itself.^[2,17,18,19]
• Most experiments in this family used a neighbouring molecule: the bare fifteen-residue 177-191 peptide, the sibling 176-191 fragment, or a six-residue fragment of this one. Each card below names the construct actually used.^{[20,21,22,23]}

What is AOD-9604?

Human growth hormone is a single chain of 191 amino acids. From the 1970s a group in Melbourne asked whether separate stretches of that chain carried separate activities, and synthesised short peptides copying its ends. A 1978 study in rats compared six carboxyl-terminal fragments, hGH 172-191, 176-191, 177-191, 178-191, 179-191 and 180-191: the four longest changed blood glucose and plasma insulin and the two shortest were inert, from which the authors concluded that a minimum stretch of sequence was needed and had to be in the right physical arrangement. Work then settled on the fifteen-residue 177-191 peptide, designated AOD9401.^[24,20,13]

AOD-9604 is that fifteen-residue peptide with a tyrosine added in front of it. The name first appears in the indexed literature in 2000, and AOD stands for anti-obesity drug, as a 2026 review still spells out. A drug profile recorded phase IIa trials as under way by February 2002. Six randomised, double-blind, placebo-controlled trials were run in all, and the programme ended at phase 2: a 24-week study enrolled 534 subjects, randomised 502, and did not show a significant effect on its primary weight-loss endpoint, no approval followed under this name for obesity, and no phase 3 study is registered. The trial itself was never reported in a journal, so that outcome is known from a 2026 review summarising sponsor-reported programme results, which says so explicitly. It is a prohibited substance in sport, which is why most measurement published about it since 2013 comes from doping-control laboratories rather than from pharmacology.^{[25,26,27,3,4,28,29,30,31]}

The same molecule has a second life under a second name. From about 2023 it appears as LAT8881, held by a different company, and the FDA substance record gives LAT-8881 as its preferred display name while ChEBI labels the class lat-8881 with AOD-9604 as a synonym. Under that name it was carried into controlled trials in an unrelated indication, and a 2023 systematic review from outside the sponsor group files it by molecular target as an activator of lanthionine synthetase C-like protein. Papers about AOD-9604 and papers about LAT8881 are papers about one peptide.^[1,14,32,15]

The names in this family do not line up with the molecules, and that is most of what a reader needs to hold on to. This entry is the 16-mer beginning with tyrosine. The separate library entry hGH Fragment 176-191 is a different 16-mer beginning with phenylalanine. AOD9401 and the bare hGH 177-191 are the 15-mer. LAT9997 is a six-residue fragment of this peptide. A 2026 review writes the compound as AOD9604 (hGH 176-191), equating two of those, while a 2026 doping-control method determines them as separate analytes in the same assay.^[4,23,22,33]

AOD-9604 structure and sequence

The molecule is small and almost entirely plain. Sixteen residues, all-L, free amino and carboxyl termini, no cap, no lipid, no polyethylene glycol, no glycan and no metal; the FDA record structural-modifications list is empty. Fifteen stereocentres follow from the residues themselves, fourteen alpha carbons plus the beta carbon of isoleucine 4, the glycines at 12 and 15 contributing none. One feature is not inherited: the tyrosine at position 1, which is the only chemical difference between this peptide and the sibling 176-191 fragment, where that position is a phenylalanine.^[1,2,13]

The one shape-bearing feature is the disulfide. Cys7 and Cys14 are bridged, closing a ring of eight residues at the carboxyl end and leaving the first six residues as a tail. That bond is not an engineered addition: it is the hormone own Cys182 to Cys189 bridge, annotated on the parent sequence record, and all four sources that describe the geometry agree on it, the FDA systematic name giving cyclic (7 to 14), the PubChem isomeric SMILES drawn closed, and the development programme describing a 16-amino-acid cyclic peptide. The ring is also where the molecule survives longest: of six fragments identified after incubation in serum and urine, the one that persisted was the nine-residue CRSVEGSCG, which spans exactly that bridge.^{[1,2,22,13,33]}

There is no 3D view of this peptide to show, and no honest substitute for one. Nothing has been deposited: searches of the Protein Data Bank by name return nothing, and a sequence search returns only crystal structures of the whole hormone, whose chains begin the fragment region one residue later and so do not contain this molecule amino terminus. PubChem holds no computed conformer either. Reference pages elsewhere show a modelled conformer in this space, and none is shown here on purpose: a 16-residue peptide with one disulfide and a six-residue tail has no single conformation in solution, so a force-field minimum drawn for it is a picture of a calculation rather than of the molecule, and on a page whose other numbers are measured it would read as the same kind of fact as they are. The closest measurement is a two-dimensional 1H NMR study of the fifteen-residue sister peptide, which reported type I beta-turns at Ser8-Val9-Glu10-Gly11 and at Ser12-Cys13-Gly14-Phe15 in a water and dimethylsulfoxide mixture, each preceded by loop-like structure, and noted some similarity to the corresponding residues in the hormone crystal structure. That paper numbers its cysteines 6 and 13 because it counts from leucine, so its ring is the same ring, one residue offset.^[17,2,21,33]

The sequence is all-L, inherited unchanged from the human protein apart from the added tyrosine, which the systematic name also gives as the L enantiomer. No source describes a D-residue or any other non-proteinogenic substitution. Two of the sixteen residues are glycine, at positions 12 and 15, so fourteen residues carry an alpha stereocentre, and the isoleucine at position 4 adds a second centre at its beta carbon, giving fifteen in all. The disulfide between Cys7 and Cys14 is the only ring. The reduced state is a real alternative rather than a notational one: the two public records disagree by exactly two hydrogens, PubChem computing C78H123N23O23S2 for the bridged molecule while the FDA record estimates C78H125N23O23S2, which is the open chain.^[2,1]

What studies on AOD-9604 show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

AOD-9604 compared with hGH Fragment 176-191 and Somatropin

Four things about the 3 compounds most often read beside it, on axes that can be checked: what kind of substance it is, its formula and mass, what public records settle about which substance it is, and the strongest three-dimensional evidence that exists for it. Every figure is the one stated on that compound's own page, which is where it is cited, so the two can never disagree. The table compares no effect, no potency and nothing a compound has been reported to do, and these compounds are not alternatives to one another.

What has been ruled out, and the one target that has been proposed

The most solid molecular statement about this peptide is a negative one. In cells transfected with the human growth hormone receptor it did not compete with radiolabelled growth hormone and did not drive proliferation, while the hormone itself did both, so whatever the fragment does it is not acting as a smaller copy of its parent at the parent receptor. The later development programme restates that independence in its own papers. A beta3-adrenergic receptor knockout experiment is sometimes read as naming a receptor, and it does not: it reports that chronic endpoints disappear in the knockout and that receptor RNA expression changes, which is a dependency in a pathway rather than a binding site.^[5,15,16]

One positive target has been proposed, by one research lineage. A photoaffinity conjugate of the peptide active metabolite captured lanthionine synthetase C-like protein 1 from rodent spinal cord, and knocking that protein down in dorsal root ganglion abolished the peptide electrophysiological effects; an earlier paper from the same group had found that siRNA inhibition of the lanthionine synthetase C-like proteins countered its effect on cell viability. The FDA substance record carries the assignment as a formal annotation, naming lanthionine synthetase C-like protein 2 as an activation target, and a 2023 systematic review from outside the sponsor group files the molecule by that mechanism.^[18,15,1,32]

What is missing from that proposal is the measurement that would settle it. The probe that captured the protein was built from a metabolite rather than from the sixteen-residue peptide, so a direct contact between this molecule and that protein is inferred. No dissociation constant, inhibition constant or potency figure for any target was found in any source, ChEMBL holds no bioactivity table, and no structure or model of any complex exists. Nor has a residue-by-residue map of the active part been made on this peptide: the one structure-activity series trimmed a six-residue fragment, and the single named signalling readout, suppression of AKT phosphorylation at serine 473, was measured on that fragment too. A 2026 orthopaedic review nonetheless groups the compound with growth hormone secretagogues and attributes IGF-1 signalling to the whole group, which no experiment on this peptide supports and which the receptor result contradicts.^{[18,19,22,35,36]}

What is still unknown about AOD-9604

The sharpest open problem is not chemical but nominal, and it has consequences for how the literature is read. Four molecules circulate under overlapping names: this 16-mer beginning with tyrosine, the sibling 16-mer beginning with phenylalanine that the library carries as hGH Fragment 176-191, the bare 15-mer called AOD9401 or hGH 177-191, and the six-residue LAT9997. A 2026 review writes the compound as AOD9604 (hGH 176-191), equating the first two, while a 2026 doping-control method determines them as separate analytes in one run. No study was found that compares AOD-9604 with either neighbour in the same experiment, so the consequence of the added tyrosine is unmeasured, which matters because the 1978 series showed that removing residues from that same end, from 178-191 to 179-191, turned an active peptide inert.^[4,23,24,33]

Chemistry is otherwise settled, with two loose ends in the records themselves and one in the catalogues. PubChem and the FDA record disagree by exactly two hydrogens, the first describing the bridged molecule and the second estimating the open chain, so the two public formulas encode different oxidation states. The same PubChem record carries three somatostatin aliases, which are simply wrong: the parent is somatotropin. And the catalogued form is the acetate with its stoichiometry written as an unspecified X, quoted beside the free peptide's formula weight, by a record that also describes a 15-residue peptide while naming sixteen residues; a second supplier record publishes a different standard InChIKey for the same stated formula. Nothing in the indexed literature reports the disulfide state, purity or impurity profile of any supplied preparation, and the one published analysis of preparations of unknown composition containing this peptide, by a national medicines laboratory, could not be read beyond its title, so this page states nothing about what it found.^{[2,1,13,37,38,39]}

The evidence is concentrated in a way that is easy to miss when papers are counted rather than read. Nearly all the metabolic work from 1978 to 2001 comes from one Melbourne and Monash lineage, and nearly all of it used the 15-mer: the enzyme-activity readings, the adipocyte transport measurements, the chronic mouse series and the human-tissue assay. The modern target work comes from a second, sponsor-affiliated lineage and mostly used the metabolite or the hexapeptide. The one study outside both that used AOD-9604 itself scored cartilage histopathology in a rabbit model and bears on no molecular question. Independent corroboration exists for the identity, the analytical behaviour and the development history, and not for the pharmacology. Two 1993 papers also print the fragment sequence with its serine and valine transposed, contradicting both the protein record and the 2000 NMR paper: a typesetting error, but a propagated one.^{[20,40,41,25,18,42,43,44,21]}

Finally, the structural question is wide open rather than answered negatively. There is no deposited structure, no computed conformer, and no coordinates even for the sister peptide whose turns were described in 2000, so nothing can be re-examined. The only persistence data are an in vitro metabolite profile and a stored-specimen stability study, both from doping-control laboratories, and the fragment that survives longest spans the disulfide, which is suggestive about the ring and has not been tested as such. A reader should treat the shape of this molecule, its binding site and its potency at any target as unmeasured.^{[21,17,2,33,23]}

The human record is the part most likely to be misread, in either direction. Six randomised, double-blind, placebo-controlled trials were run and their pooled safety reading is reassuring on the endpoints it examined, but it is a sponsor-affiliated pooled report rather than a trial publication, no participant totals or durations were readable here, and the single study that tested efficacy was never published at all. So the compound simultaneously has more human data than most peptides in this space and no peer-reviewed efficacy trial, and the one efficacy outcome on record, a failure on the primary weight-loss endpoint at 24 weeks in 502 randomised subjects, reaches a reader only through a 2026 review quoting sponsor-reported results. The FDA's bulk-substances record states a possible significant risk of immunogenicity and identified serious adverse events that may be associated with the substance, causality not clear, which stands beside the pooled report's finding of no antibodies in the participants tested and is not cancelled by it.^[3,4,12]

Key papers on AOD-9604

1. Increase of fat oxidation and weight loss in obese mice caused by chronic treatment with human growth hormone or a modified C-terminal fragment.

   Heffernan MA, Thorburn AW, Fam B, Summers R, Conway-Campbell B, Waters MJ, Ng FM (2001), International Journal of Obesity and Related Metabolic Disorders · Radioligand competition binding and proliferation in transfected cells

   The one receptor-level experiment on this peptide, and the reason the growth hormone receptor can be ruled out as its binding site.

2. Safety and Tolerability of the Hexadecapeptide AOD9604 in Humans

   Stier H, Vos E, Kenley D (2013), Journal of Endocrinology and Metabolism · Pooled human safety and tolerability report

   The only peer-reviewed account of the human programme, and the place to see how far it goes: safety endpoints across six placebo-controlled trials, pooled, by authors two of whom are affiliated with the developer.

3. Detection and in vitro metabolism of AOD9604.

   Cox HD, Smeal SJ, Hughes CM, Cox JE, Eichner D (2015), Drug Testing and Analysis · In vitro metabolite identification and method validation

   The clearest independent statement of what the molecule is, with the metabolite profile and the nine-residue fragment that outlasts the parent.

4. Lanthionine synthetase C-like protein 1 (LanCL1): a therapeutic target for neuropathic pain.

   Spanswick DC, Wei H, Zhao FY, Caldeira Borges da Cruz MP, Whyment AD, Campbell-Galland A, O'Sullivan K, Autelitano F, Guillemot M, Kenley D, Gearing AJ, Pickering AE, Imlach WL (2026), Pain · Photoaffinity pulldown with knockdown and electrophysiology

   The only target identification published for the molecule, and the place to see exactly how far the evidence goes: a pulldown using a conjugate of the metabolite.

5. The conformational and biological analysis of a cyclic anti-obesity peptide from the C-terminal domain of human growth hormone.

   Ogru E, Wilson JC, Heffernan M, Jiang WJ, Chalmers DK, Libinaki R, Ng F (2000), Journal of Peptide Research · Two-dimensional 1H NMR solution conformation

   The only conformational measurement in the family. Read it for the turn geometry and for the fact that the construct is the fifteen-residue peptide, not this one.

6. Molecular and cellular actions of a structural domain of human growth hormone (AOD9401) on lipid metabolism in Zucker fatty rats.

   Ng FM, Jiang WJ, Gianello R, Pitt S, Roupas P (2000), Journal of Molecular Endocrinology · Enzyme activity assays in isolated rat adipose tissue

   The only enzyme-activity endpoints anywhere in this family, with the intact hormone measured alongside.

7. Rapid and harmonized analytical workflow for the determination of peptidic and non-peptidic doping agents in dried and liquid blood matrices.

   Mazzarino M, Colpaert T, Deventer K, Van Eenoo P (2026), Analyst · Analytical validation with matrix stability study

   Where AOD-9604 and hGH 176-191 are treated as separate analytes in one assay, which is the cleanest published answer to the naming collision.

8. Hyperglycemic action of synthetic C-terminal fragments of human growth hormone.

   Ng FM, Bornstein J (1978), American Journal of Physiology · In vivo rat study of six synthetic fragments

   The origin of the whole fragment series, and the experiment showing that trimming this fragment amino-terminal end can abolish its activity.

References

1. 1.FDA Global Substance Registration System. Substance record UNII 7UP768IP4M (AOD-9604, display name LAT-8881). GSRS, National Center for Advancing Translational Sciences. source · database record
2. 2.PubChem. Compound Summary: CID 71300630, AOD-9604. PubChem, National Library of Medicine. source · database record
3. 3.Stier H, Vos E, Kenley D. (2013). Safety and Tolerability of the Hexadecapeptide AOD9604 in Humans. Journal of Endocrinology and Metabolism. 3:7-15. doi:10.4021/jem157w · abstract only
4. 4.Dominikowski A, Rękoś Z, Olejarz M, Szczepanek-Parulska E, Domin R, Ruchała M. (2026). The emerging landscape of performance-enhancing peptides modulating GH-IGF1 axis: bridging the gap between clinical evidence and patient self-administration. Frontiers in Endocrinology. 17:1822475. doi:10.3389/fendo.2026.1822475 · abstract only
5. 5.Heffernan MA, Thorburn AW, Fam B, Summers R, Conway-Campbell B, Waters MJ, Ng FM. (2001). Increase of fat oxidation and weight loss in obese mice caused by chronic treatment with human growth hormone or a modified C-terminal fragment. International Journal of Obesity and Related Metabolic Disorders. 25:1442-9. doi:10.1038/sj.ijo.0801740 · abstract only
6. 6.World Anti-Doping Agency. (2026). The 2026 Prohibited List: International Standard. World Anti-Doping Agency. source · full text read
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18. 18.Spanswick DC, Wei H, Zhao FY, Caldeira Borges da Cruz MP, Whyment AD, Campbell-Galland A, O'Sullivan K, Autelitano F, Guillemot M, Kenley D, Gearing AJ, Pickering AE, Imlach WL. (2026). Lanthionine synthetase C-like protein 1 (LanCL1): a therapeutic target for neuropathic pain. Pain. 167:1850-1868. doi:10.1097/j.pain.0000000000004014 · abstract only
19. 19.ChEMBL. Molecule record CHEMBL6068615, AOD-9604. ChEMBL, European Bioinformatics Institute. source · database record
20. 20.Ng FM, Jiang WJ, Gianello R, Pitt S, Roupas P. (2000). Molecular and cellular actions of a structural domain of human growth hormone (AOD9401) on lipid metabolism in Zucker fatty rats. Journal of Molecular Endocrinology. 25:287-98. doi:10.1677/jme.0.0250287 · abstract only
21. 21.Ogru E, Wilson JC, Heffernan M, Jiang WJ, Chalmers DK, Libinaki R, Ng F. (2000). The conformational and biological analysis of a cyclic anti-obesity peptide from the C-terminal domain of human growth hormone. Journal of Peptide Research. 56:388-97. doi:10.1034/j.1399-3011.2000.00771.x · abstract only
22. 22.West AC, Harpur CM, Le Page MA, Lam M, Hodges C, Ely LK, Gearing AJ, Tate MD. (2024). Harnessing Endogenous Peptide Compounds as Potential Therapeutics for Severe Influenza. The Journal of Infectious Diseases. 230:e384-e394. doi:10.1093/infdis/jiad566 · abstract only
23. 23.Mazzarino M, Colpaert T, Deventer K, Van Eenoo P. (2026). Rapid and harmonized analytical workflow for the determination of peptidic and non-peptidic doping agents in dried and liquid blood matrices. Analyst. 151:4398-4413. doi:10.1039/d6an00455e · abstract only
24. 24.Ng FM, Bornstein J. (1978). Hyperglycemic action of synthetic C-terminal fragments of human growth hormone. American Journal of Physiology. 234:E521-6. doi:10.1152/ajpendo.1978.234.5.E521 · abstract only
25. 25.Ng FM, Sun J, Sharma L, Libinaka R, Jiang WJ, Gianello R. (2000). Metabolic studies of a synthetic lipolytic domain (AOD9604) of human growth hormone. Hormone Research. 53:274-8. doi:10.1159/000053183 · abstract only
26. 26.Mendias CL, Awan TM. (2026). Safety and Efficacy of Approved and Unapproved Peptide Therapies for Musculoskeletal Injuries and Athletic Performance. Sports Medicine. 56:1921-1935. doi:10.1007/s40279-026-02437-0 · abstract only
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28. 28.Thevis M, Schänzer W. (2014). Analytical approaches for the detection of emerging therapeutics and non-approved drugs in human doping controls. Journal of Pharmaceutical and Biomedical Analysis. 101:66-83. doi:10.1016/j.jpba.2014.05.020 · abstract only
29. 29.Thevis M, Thomas A, Schänzer W. (2014). Detecting peptidic drugs, drug candidates and analogs in sports doping: current status and future directions. Expert Review of Proteomics. 11:663-73. doi:10.1586/14789450.2014.965159 · abstract only
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32. 32.Huerta MÁ, Garcia MM, García-Parra B, Serrano-Afonso A, Paniagua N. (2023). Investigational Drugs for the Treatment of Postherpetic Neuralgia: Systematic Review of Randomized Controlled Trials. International Journal of Molecular Sciences. 24:12987. doi:10.3390/ijms241612987 · abstract only
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35. 35.West AC, Harpur CM, Lam M, Ambrose RL, Hodges CJ, Mudge S, Kenley D, Gearing AJ, Tate MD. (2026). Short-course intranasal LAT9997 therapy limits post-influenza bacterial pneumonia by recalibrating lung immunity. Mucosal Immunology. 19:1875-1888. doi:10.1016/j.mucimm.2026.01.008 · abstract only
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38. 38.Royal Society of Chemistry. ChemSpider record 57582224, AOD9604. ChemSpider. source · database record
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40. 40.Heffernan MA, Jiang WJ, Thorburn AW, Ng FM. (2000). Effects of oral administration of a synthetic fragment of human growth hormone on lipid metabolism. American Journal of Physiology: Endocrinology and Metabolism. 279:E501-7. doi:10.1152/ajpendo.2000.279.3.E501 · abstract only
41. 41.Natera SH, Jiang WJ, Ng FM. (1994). Reduction of cumulative body weight gain and adipose tissue mass in obese mice: response to chronic treatment with synthetic hGH 177-191 peptide. Biochemistry and Molecular Biology International. 33:1011-21. PMID 7987248 · abstract only
42. 42.Kwon DR, Park GY. (2015). Effect of Intra-articular Injection of AOD9604 with or without Hyaluronic Acid in Rabbit Osteoarthritis Model. Annals of Clinical and Laboratory Science. 45:426-32. PMID 26275694 · abstract only
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