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Ribitol
Ribitol
Ribitol
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Ribitol
Names
IUPAC name
D-Ribitol[1]
Systematic IUPAC name
(2R,3S,4S)-Pentane-1,2,3,4,5-pentol
Other names
(2R,3S,4S)-Pentane-1,2,3,4,5-pentaol (not recommended)
Adonit
Adonite
Adonitol
Adonitrol
Pentitol
1,2,3,4,5-Pentanepentol
1,2,3,4,5-Pentanol
Pentane-1,2,3,4,5-pentol
Identifiers
3D model (JSmol)
1720524
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.006.987 Edit this at Wikidata
EC Number
  • 207-685-7
82894
KEGG
UNII
  • InChI=1S/C5H12O5/c6-1-3(8)5(10)4(9)2-7/h3-10H,1-2H2/t3-,4+,5- checkY
    Key: HEBKCHPVOIAQTA-ZXFHETKHSA-N checkY
  • InChI=1/C5H12O5/c6-1-3(8)5(10)4(9)2-7/h3-10H,1-2H2/t3-,4+,5-
  • O[C@H](CO)[C@@H](O)[C@@H](O)CO
Properties
C5H12O5
Molar mass 152.146 g·mol−1
Melting point 102 °C (216 °F; 375 K)
−91.30·10−6 cm3/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
checkY verify (what is checkY☒N ?)

Ribitol, or adonitol, is a crystalline pentose alcohol (C5H12O5) formed by the reduction of ribose. It occurs naturally in the plant Adonis vernalis[2] as well as in the cell walls of some Gram-positive bacteria, in the form of ribitol phosphate, in teichoic acids.[3] It also forms part of the chemical structure of riboflavin and flavin mononucleotide (FMN), which is a nucleotide coenzyme used by many enzymes, the so-called flavoproteins.[4]

Ribitol is one of four stereoisomers having the formula C5H12O5:

References

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Ribitol

View on Grokipedia
from Grokipedia
Ribitol, also known as adonitol, is a sugar (C₅H₁₂O₅) formed by the reduction of the group of to a , resulting in a straight-chain with five hydroxyl groups. It appears as a white, crystalline solid with a of 102–105 °C and high in (up to 936 mg/mL at 25 °C). Chemically, ribitol is a due to its symmetric structure, lacking optical activity, and has a molecular weight of 152.15 g/mol. In biochemistry, ribitol plays a crucial role as a structural component of riboflavin (vitamin B₂), where it forms the side chain attached to the isoalloxazine ring, essential for the vitamin's function in flavin coenzymes like FMN and . It is also biosynthesized via the in vivo and serves as a precursor for CDP-ribitol, which is incorporated into the cell walls of as part of ribitol teichoic acids—polymers of ribitol phosphate units linked by phosphodiester bonds and often substituted with sugars or D-alanine. These teichoic acids contribute to bacterial cell wall integrity, ion regulation, and pathogenicity in species like Staphylococcus aureus and Bacillus subtilis. Ribitol occurs naturally in certain plants, such as , from which it was originally isolated, and is a normal in human and erythrocytes, though its levels can elevate in metabolic disorders like transaldolase deficiency. In , it supports growth in some bacterial species and is used in settings to study cell wall biosynthesis inhibitors targeting teichoic acid pathways. Its role in both eukaryotic vitamins and prokaryotic structures highlights ribitol's evolutionary significance in across kingdoms.

Chemical characteristics

Molecular structure

Ribitol is a straight-chain pentitol with the C₅H₁₂O₅ and a molecular weight of 152.146 g/mol. Its systematic IUPAC name is (2R,3S,4S)-pentane-1,2,3,4,5-pentaol, reflecting the specific stereochemical configuration at its three chiral carbon atoms. As a , ribitol is produced by the reduction of , in which the of the is converted to a , yielding a fully saturated polyhydroxy chain incapable of forming cyclic structures. The of ribitol features an configuration at C2, an S configuration at C3, and an S configuration at C4, resulting in a with a plane of passing through C3 and its attached hydroxyl group. This imparts optical inactivity despite the presence of chiral centers. In the convention, ribitol is represented with the carbon chain vertically oriented, hydroxyl groups pointing to the right at C2 and C4, and to the left at C3:

CH₂OH H−C−OH HO−C−H H−C−OH CH₂OH

CH₂OH H−C−OH HO−C−H H−C−OH CH₂OH

This projection highlights the internal mirror plane at C3. In three-dimensional conformation, ribitol typically adopts an extended zig-zag chain in the solid state and solution, stabilized by intramolecular hydrogen bonding between adjacent hydroxyl groups, though flexible gauche rotations allow conformational variability. Compared to other polyols, ribitol shares the five-carbon chain and five hydroxyl groups characteristic of pentitols like , which differs in stereochemistry at C3 and lacks the meso symmetry, whereas , a hexitol, features an additional carbon and hydroxyl group, enabling distinct metabolic roles.

Physical properties

Ribitol appears as a white crystalline solid. It has a of 102–105 °C. The compound decomposes before reaching its boiling point, with an estimated value of approximately 495 °C at standard pressure. Ribitol exhibits high solubility in water, up to 936 g/L at 25 °C, owing to its structure; it is slightly soluble in (approximately 5 g/L) and insoluble in non-polar solvents such as . The of ribitol is 1.53 g/cm³. As a , it shows no optical activity, with a specific rotation [α]D = 0°. Ribitol is hygroscopic and remains stable under neutral conditions, though it is sensitive to degradation by strong acids or bases.

Chemical reactivity

Ribitol is synthesized through the catalytic of , where the group of is reduced to a using hydrogen gas and catalysts such as or . This transformation is represented by the : C5H10O5 (ribose)+H2→C5H12O5 (ribitol)\text{C}_5\text{H}_{10}\text{O}_5 \text{ (ribose)} + \text{H}_2 \rightarrow \text{C}_5\text{H}_{12}\text{O}_5 \text{ (ribitol)} The reaction proceeds under mild conditions, typically in aqueous or alcoholic media, yielding ribitol as a stable polyol. The five hydroxyl groups in ribitol's linear structure enable diverse reactivity, including esterification with carboxylic acids or anhydrides, etherification with alkyl halides under basic conditions, and phosphorylation using phosphorylating agents like phosphorus oxychloride. A representative example is the selective phosphorylation at the 5-position to form ribitol-5-phosphate, achieved through regioselective chemical methods involving protected intermediates. These reactions highlight ribitol's utility as a building block in organic synthesis, where the hydroxyl groups can be functionalized sequentially due to their primary and secondary nature. As a lacking a free or group, ribitol is non-reducing and thus does not engage in the with amines under thermal conditions, nor does it undergo facile oxidation to aldaric acids via reagents like , behaviors characteristic of reducing sugars such as . This non-reducing property stems from its fully reduced structure, which prevents the formation of reactive carbonyl intermediates. Ribitol demonstrates relative stability to oxidation compared to aldoses, consuming 4 moles of per mole to cleave vicinal linkages while generating 2 moles of and 2 moles of as byproducts, without the rapid ring-opening oxidation seen in cyclic sugars. This controlled reactivity allows to serve as a tool for of ribitol-containing polymers. Common derivatives include peracetylated ribitol, formed via treatment with , and tosylates prepared with tosyl chloride, both employed as activated intermediates for nucleophilic substitutions in synthetic routes.

Sources and production

Natural sources

Ribitol, a pentitol derived from the reduction of , is primarily found in certain , where it serves as a compatible solute. In the plant (pheasant's eye), ribitol accumulates in leaves at concentrations ranging from 0.9% to 5.3% of dry weight, varying by and environmental conditions. This accumulation helps maintain cellular osmotic balance under abiotic stresses such as . Ribitol has also been detected in other , including the roots of Bupleurum falcatum and the beans of , though at lower levels. In microbial sources, ribitol is a key structural component in . For instance, in Bacillus subtilis strain W23, it forms the repeating ribitol-5-phosphate units in wall teichoic acids, which constitute a major anionic polymer in the cell envelope. These teichoic acids link to via a bridge and play roles in integrity. Ribitol is also present as a in some , such as Escherichia coli C strains, where it can be catabolized via the rtl operon for energy utilization, though it is absent in standard K-12 and B strains. Additionally, ribitol appears in the capsular of pathogens like Proteus mirabilis and Vibrio parahaemolyticus. Trace amounts of ribitol occur in mammalian tissues, primarily as a moiety within (vitamin B2), which is distributed via the bloodstream bound to proteins like . , containing the ribitol backbone, is essential for cofactors (FMN and ) involved in energy metabolism across tissues, with ribitol itself detectable in human urine and serum under normal conditions but elevated in disorders like transaldolase deficiency. It is produced endogenously in fibroblasts and erythrocytes through reduction but is not a major free solute. Environmentally, ribitol functions as an in halotolerant and facing salt or stress. In like ( lycopersicum), ribitol levels increase alongside in leaves under NaCl or conditions, stabilizing proteins and membranes without disrupting cellular functions. Similarly, in , its incorporation into polymers aids adaptation to osmotic challenges in saline habitats. Ribitol in plant extracts is commonly identified and quantified using analytical techniques such as gas chromatography-mass spectrometry (GC-MS) or (NMR) . In GC-MS protocols, ribitol serves as an for due to its stability, allowing detection of polyols in derivatized samples from stressed tissues. NMR provides structural confirmation without derivatization, revealing its meso-configuration in complex extracts.

Biosynthetic pathways

In , ribitol is biosynthesized primarily as ribitol-5-phosphate through the reduction of D-ribulose-5-phosphate, an intermediate in the , by the enzyme ribitol-5-phosphate 2-dehydrogenase (EC 1.1.1.405, also known as TarJ), which utilizes NADPH as a cofactor. This step is followed by activation of ribitol-5-phosphate to CDP-ribitol by the cytidylyltransferase TarI (EC 2.7.7.40), integrating the product into synthesis in such as and . The overall reduction can be represented as: D-ribulose-5-phosphate+NADPH+H+→D-ribitol-5-phosphate+NADP+\text{D-ribulose-5-phosphate} + \text{NADPH} + \text{H}^+ \rightarrow \text{D-ribitol-5-phosphate} + \text{NADP}^+ In , ribitol biosynthesis occurs via the reduction of D-ribose-5-phosphate to D-ribitol-5-phosphate, catalyzed by D-ribose-5-phosphate reductase using NADPH; this enzyme has been partially purified from L. leaves and exhibits specificity for the phosphorylated substrate. This pathway is upregulated under abiotic stresses, such as , leading to increased ribitol accumulation as an in species like , where levels rise in response to water deficit. In mammals, direct biosynthesis of ribitol is limited, with ribitol-5-phosphate likely formed indirectly through multiple routes, including the reduction of D-ribose-5-phosphate or phosphorylation of exogenous ribitol, though the specific reductase remains unidentified. Recent studies as of 2024 have detected endogenous reductase activities in mammalian cells capable of generating ribitol-5-phosphate from substrates like ribulose-5-phosphate, though the specific primary enzyme remains to be confirmed. CDP-ribitol, the activated form, is then synthesized from ribitol-5-phosphate and CTP by the enzyme isoprenoid synthase domain-containing protein (ISPD), a CDP-ribitol synthase essential for O-mannosylation of proteins like α-dystroglycan. While ribitol is a component of dietary riboflavin (vitamin B2), mammals rely on this exogenous source rather than de novo synthesis for riboflavin-derived ribitol. Microbial pathways, including bacterial ribitol synthesis, are subject to regulation via feedback inhibition by ribitol or downstream products to maintain cellular homeostasis, though specific mechanisms for eukaryotic systems are less characterized.

Synthetic preparation

Ribitol is commonly synthesized in the laboratory through the chemical reduction of D-ribose, primarily via catalytic . This method exploits the reactivity of the group in ribose to form the corresponding alcohol. The process typically employs as the catalyst in a solvent such as 75% , with hydrogen gas at pressures of 40-100 atm and temperatures of 50-80 °C for 3 hours, achieving yields exceeding 90%. Alternative catalysts like (Pd/C) can also be used under similar high-pressure conditions to facilitate the stereospecific reduction. Microbial represents another key synthetic route, utilizing engineered microorganisms to convert glucose into ribitol through overexpressed reductase enzymes. For instance, the yeast Trichosporonoides oedocephalis ATCC 16958, optimized in a two-phase fed-batch process with initial glucose at 50 g/L followed by infusion of 150 g/L, produces up to 65 g/L ribitol after 120 hours, with a volumetric of 0.322 g/L/h. Similarly, metabolically engineered strains, modified with genes such as XYL2 for xylitol dehydrogenase and DOG1 for sugar phosphate phosphatase, yield ribitol titers of 0.56 g/L from 20 g/L glucose in batch fermentation, though these are lower than optimized bacterial systems. Fed-batch processes with engineered overexpressing reductases can reach 50-100 g/L, emphasizing scalability for research applications. A less common approach involves selective oxidation and reduction starting from , a stereoisomer of ribitol, but this method faces challenges due to the need for precise control to avoid unwanted epimerization and stereoisomer mixtures. Purification of synthetic ribitol typically involves to remove catalysts or cells, followed by from aqueous solutions, which achieves purities greater than 99%. The resulting crystals are washed with and dried. Overall, ribitol production remains primarily at the scale for and pharmaceutical purposes, with no widespread industrial due to limited commercial .

Biological significance

Role in bacterial cell walls

Ribitol serves as a key building block in the cell walls of , where it is incorporated into wall teichoic acids (WTAs) as repeating units of ribitol phosphate (RboP). These polymers typically consist of 20–50 ribitol phosphate units linked via phosphodiester bonds, alternating with phosphate groups and often substituted with sugars such as (GlcNAc) at the 4-position of ribitol, which contributes to the anionic nature and structural diversity of the WTA. The biosynthetic incorporation of ribitol into WTAs begins with the formation of CDP-ribitol, a activated precursor derived from 5-phosphate, which is then polymerized onto a lipid-linked linkage unit. Enzymes such as TagA (also known as TarA in some species like ) catalyze the initial addition of GlcNAc-1-phosphate to the linkage unit, followed by the transfer of ribitol phosphate units by polymerases like TarL, building the ribitol-based backbone that anchors to the layer. WTAs containing ribitol play essential roles in maintaining bacterial cell envelope integrity, including regulation of cell shape, division, and autolysin activity through interactions with . They facilitate cation binding, particularly Mg²⁺, which supports homeostasis and cofactor availability, while sugar modifications on ribitol units confer resistance to bacteriophage adsorption by altering surface charge and accessibility. In Staphylococcus aureus, ribitol-based WTAs are critical for formation, promoting initial adhesion to host surfaces and intercellular cohesion during community development. Mutations disrupting ribitol incorporation, such as deletions in tarA or tarIJ genes, result in truncated or absent WTAs, leading to increased negative charge due to unmasked carboxyl groups, enhanced sensitivity to β-lactam antibiotics, and impaired in infection models.

Involvement in vitamin B2

Ribitol serves as the essential side chain in , also known as vitamin B2, where it is attached at the N-10 position of the isoalloxazine ring to form 7,8-dimethyl-10-ribitylisoalloxazine. In the coenzymes (FMN) and (FAD), ribitol links the isoalloxazine moiety to a group at its 5' hydroxyl position in FMN, and further to an ADP moiety in FAD, facilitating their incorporation into flavoproteins. This structural integration was first elucidated in 1935 by and colleagues, who determined riboflavin's composition including the ribityl chain. In the biosynthesis of , which occurs in , fungi, and plants but not in mammals, the ribityl is derived from the moiety of GTP through reduction by enzymes such as RibD, following the initial formation of a ribosyl-pyrimidine by RibA (GTP cyclohydrolase II). Ribulose-5-phosphate from the is converted by RibB (3,4-dihydroxy-2-butanone-4-phosphate ) to a four-carbon precursor. Subsequently, 6,7-dimethyl-8-ribityllumazine (RibH) assembles this with the ribityl-pyrimidine to form 6,7-dimethyl-8-ribityllumazine, which riboflavin (RibE) cyclizes to yield , completing the attachment of the ribitol chain. The ribitol moiety in FMN and enhances the of these coenzymes in aqueous environments and mediates their binding to apoproteins in flavoproteins, where the isoalloxazine ring performs reactions such as in metabolic pathways including the tricarboxylic acid cycle and oxidation. This binding often involves hydrogen bonding and hydrophobic interactions along the ribitol chain, stabilizing the cofactor during catalytic cycles in enzymes like and dehydrogenases. Riboflavin deficiency impairs the formation of FMN and , disrupting ribitol-containing coenzymes and leading to metabolic disorders such as ariboflavinosis, characterized by impaired energy production and symptoms including oral lesions and , as well as riboflavin-responsive multiple deficiency (RR-MADD), where faulty function causes accumulation and . Supplementation with can restore coenzyme activity in these conditions by replenishing the ribitol-linked flavins essential for mitochondrial electron transport.

Function in mammalian glycosylation

In mammalian cells, ribitol plays a critical role in the post-translational O-mannosylation of α-dystroglycan (α-DG), a key that links the to the . This modification involves the incorporation of ribitol-5-phosphate (Rbo5P) units into the glycan structure, forming a that serves as a scaffold for further and binding. The process begins with the synthesis of CDP-ribitol, catalyzed by the enzyme isoprenoid synthase domain-containing protein (ISPD), which acts as a CDP-ribitol pyrophosphorylase using CTP and ribitol-5-phosphate as substrates. Subsequently, fukutin (FKTN) transfers the first Rbo5P unit from CDP-ribitol to the 3-position of (GalNAc) linked to O-mannose on α-DG, while fukutin-related protein (FKRP) adds a second Rbo5P unit to the first, creating the characteristic tandem structure essential for functional . This ribitol-based glycosylation is vital for α-DG's ability to bind proteins such as , agrin, and , thereby maintaining muscle cell integrity and facilitating neuronal migration during development. Defects in this pathway, arising from mutations in ISPD, FKTN, or FKRP, severely impair α-DG glycosylation, leading to α-dystroglycanopathies, a group of congenital muscular dystrophies including the severe Walker-Warburg characterized by , malformations, and ocular abnormalities. The modification is predominantly expressed in tissues requiring strong cell-matrix interactions, with high levels observed in , , heart, and nerves.

Therapeutic potential

Treatment of dystroglycanopathies

Ribitol has emerged as a promising therapeutic agent for dystroglycanopathies, particularly those caused by mutations in the fukutin-related protein (FKRP) gene, such as limb-girdle muscular dystrophy type 2I (LGMD2I/R9). The mechanism involves oral administration of ribitol, which elevates intracellular pools of cytidine diphosphate (CDP)-ribitol, the substrate for FKRP. This supplementation enhances FKRP-mediated glycosylation of α-dystroglycan in patient-derived cells by compensating for the reduced enzymatic activity of mutant FKRP, thereby restoring functional matriglycan structures essential for muscle integrity. Preclinical studies in FKRP-mutant models have demonstrated ribitol's efficacy in ameliorating phenotypes. In a 2018 study, oral ribitol administered via (5-10% concentration) restored functional of α-dystroglycan in skeletal and cardiac muscles to up to 26% of wild-type levels, reduced in the diaphragm to 11-18%, and improved respiratory muscle function, including maximum velocity and endurance. These effects were observed after 1-6 months of treatment without adverse impacts on body weight, organ histology, or serum markers. Clinical translation has progressed through trials sponsored by BridgeBio Pharma. The Phase 1/2 study (NCT04800874, initiated 2020) evaluated escalating oral doses of BBP-418 (ribitol) in patients with LGMD2I/R9, establishing and tolerability up to approximately 24 g/day (adjusted for body weight, equivalent to ~300-400 mg/kg/day in adults), with common mild side effects like gastrointestinal discomfort but no serious adverse events. Treatment led to improved biomarkers, including a ~2-fold increase in glycosylated α-dystroglycan levels at 3 months, sustained over 21 months, and reductions in serum as a marker of muscle damage. assays on patient fibroblasts showed dose-dependent enhancement of α-dystroglycan binding to . As of 2025, the Phase 3 FORTIFY (NCT05775848, initiated 2023) confirmed ribitol's therapeutic potential, reporting a 1.8-fold increase in glycosylated α-dystroglycan and an 82% reduction in muscle damage markers after one year of oral dosing. In November 2025, BridgeBio announced plans to pursue FDA submission using these results for accelerated approval pathways. Ribitol's oral supplement form offers a low-toxicity profile, with no evidence of or long-term organ damage in preclinical models or human trials to date.

Other biomedical applications

In , ribitol has shown potential to reprogram central carbon in cells. A 2022 metabolomics and transcriptomics study on and MDA-MB-231 cell lines demonstrated that ribitol supplementation enhances by upregulating glycolytic enzymes such as HK2 and PFKL, while also increasing levels of intermediates like lactate and pyruvate. Furthermore, ribitol synergizes with like , expanding the therapeutic window by selectively inhibiting cell growth and migration in models and promoting through downregulation of anti-apoptotic genes such as BCL2. Ribitol's role in bacterial cell walls, where it forms a key component of s, has inspired antimicrobial strategies targeting its incorporation. Inhibitors of wall biosynthesis, such as , disrupt ribitol phosphate polymerization and sensitize like vancomycin-intermediate Staphylococcus aureus (VISA) to , reducing the minimum inhibitory concentration by up to 4-fold . This approach leverages ribitol's essential function in maintaining integrity, potentially restoring efficacy against resistant strains without directly affecting mammalian cells. In metabolic studies, ribitol supplementation alters key pathways in cell models, including and synthesis. Transcriptomic analysis reveals upregulation of PCK2, leading to elevated glucogenic like and aspartate, alongside decreased . pools expand significantly, with increases in AICAR (∼2.3-fold), AMP (∼1.8-fold), and orotate (∼1.8-fold), suggesting ribitol's influence on and . As a pentitol related to the , ribitol holds exploratory potential in research for modulating dehydrogenase activity and balance, though clinical evidence remains limited. Ribitol phosphate oligomers have been investigated as synthetic mimics of wall teichoic acids for development. A 2018 synthesis of tetrameric ribitol phosphate fragments demonstrated potent immunostimulatory activity, inducing elevated levels (e.g., IL-6 and TNF-α) in a subcutaneous air pouch model, outperforming shorter oligomers and supporting their use as adjuvants or antigens in glycoconjugate vaccines against staphylococcal infections. Regarding safety, ribitol exhibits a favorable profile at low doses, with no GRAS designation but recognition as a naturally occurring . In ongoing clinical trials for neuromuscular applications up to , including Phase 3 studies (NCT05775848), ribitol has shown no major adverse effects, remaining well-tolerated at doses up to ~400 mg/kg/day (weight-adjusted) with only mild, transient gastrointestinal symptoms reported.

References

  1. https://hmdb.ca/metabolites/HMDB0000508
  2. https://pubchem.ncbi.nlm.nih.gov/compound/d-Ribitol
  3. https://journals.asm.org/doi/10.1128/jb.01120-08
  4. https://www.sciencedirect.com/topics/medicine-and-dentistry/teichoic-acid
  5. https://www.nature.com/articles/ja2013100
  6. https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/ribitol
  7. https://pubchem.ncbi.nlm.nih.gov/compound/Ribitol
  8. https://www.medchemexpress.com/Ribitol.html
  9. https://www.sciencedirect.com/topics/chemistry/ribitol
  10. https://ursula.chem.yale.edu/~chem220/chem220js/STUDYAIDS/isomers/RS14272/RSrs.html
  11. https://webbook.nist.gov/cgi/cbook.cgi?ID=C488813&Mask=200
  12. https://patents.google.com/patent/US20220227692A1/en
  13. https://homework.study.com/explanation/on-reaction-with-hydrogen-gas-by-a-platinum-catalyst-ribose-is-converted-into-ribitol-is-ribitol-optically-active-or-inactive-explain.html
  14. https://etheses.whiterose.ac.uk/id/eprint/32709/1/Huxley_201021241_ThesisFinal.pdf
  15. https://www.sciencedirect.com/topics/chemistry/ribitol-phosphate
  16. https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/sugar-alcohol
  17. https://cdnsciencepub.com/doi/pdf/10.1139/v58-248
  18. https://www.sciencedirect.com/topics/neuroscience/ribitol
  19. https://www.sciencedirect.com/science/article/pii/S1074552110003509
  20. https://pubmed.ncbi.nlm.nih.gov/1097416/
  21. https://www.sigmaaldrich.com/US/en/technical-documents/technical-article/cell-culture-and-cell-culture-analysis/mammalian-cell-culture/riboflavin
  22. https://pubmed.ncbi.nlm.nih.gov/33099326/
  23. https://www.researchgate.net/post/Can_we_use_ribitol_as_an_internal_standard_for_the_untargeted_GCMS_metabolomics_for_phytochemical_analysis
  24. https://journals.biologists.com/bio/article/5/6/829/1270/Metabolomics-reveals-significant-variations-in
  25. https://salmonella.biocyc.org/pathway?orgid=META&id=PWY-8416
  26. https://pmc.ncbi.nlm.nih.gov/articles/PMC2631998/
  27. https://academic.oup.com/plphys/article/78/4/758/6080302
  28. https://pmc.ncbi.nlm.nih.gov/articles/PMC5247636/
  29. https://pubmed.ncbi.nlm.nih.gov/38140954/
  30. https://www.nature.com/articles/ncomms11534
  31. https://pubmed.ncbi.nlm.nih.gov/28711406/
  32. https://www.nature.com/articles/s41564-024-01603-2
  33. https://patents.google.com/patent/CN1194262A/en
  34. https://link.springer.com/article/10.1007/s12257-011-0359-1
  35. https://pmc.ncbi.nlm.nih.gov/articles/PMC2042063/
  36. https://patents.google.com/patent/WO1998023766A1/en
  37. https://patents.google.com/patent/EP0136805A2/en
  38. https://doi.org/10.1146/annurev-micro-092412-155620
  39. https://www.sciencedirect.com/topics/medicine-and-dentistry/ribitol
  40. https://karger.com/anm/article/61/3/224/40401/The-Discovery-and-Characterization-of-Riboflavin
  41. https://pmc.ncbi.nlm.nih.gov/articles/PMC3122625/
  42. https://nutritionandmetabolism.biomedcentral.com/articles/10.1186/s12986-023-00764-x
  43. https://www.cell.com/cell-reports/fulltext/S2211-1247(16)30103-6
  44. https://pmc.ncbi.nlm.nih.gov/articles/PMC3378661/
  45. https://www.sciencedirect.com/science/article/abs/pii/S0304416517302143
  46. https://pmc.ncbi.nlm.nih.gov/articles/PMC6395781/
  47. https://www.nature.com/articles/s41467-018-05990-z
  48. https://clinicaltrials.gov/study/NCT04800874
  49. https://bridgebio.com/news/bridgebio-pharma-shares-positive-long-term-data-from-an-ongoing-phase-2-study-which-support-the-potential-use-of-glycosylated-alpha-dystroglycan-%25E2%258D%25BAdg-levels-as-a-surrogate-endpoint-in-limb-girdle-muscular-dystrophy-type-2i-lgmd2i/
  50. https://clinicaltrials.gov/study/NCT05775848
  51. https://www.neurologylive.com/view/bridgebio-pursues-fda-submission-bbp-418-lgmd2i-r9-after-positive-topline-phase-3-results
  52. https://trial.medpath.com/news/13790d3499b3a893/bridgebio-reports-positive-phase-3-results-for-bbp-418-in-rare-muscular-dystrophy
  53. https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0278711
  54. https://pmc.ncbi.nlm.nih.gov/articles/PMC10486979/
  55. https://journals.asm.org/doi/10.1128/aac.05938-11
  56. https://pubs.acs.org/doi/10.1021/acs.orglett.8b01725
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