Nutrient chapter

Lariciresinol, enantiomer unresolved

Aglycone recorded where the report does not state which enantiomer was used.

25 recorded mechanisms · 0 availability situations · 2 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

(+)-Lariciresinol activated p38 in murine macrophages.
(+)-Lariciresinol → p38 mitogen-activated protein kinase family source_derived_draftungraded
Experimental context and source evidence
duration
Acute
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
(+)-Lariciresinol isolated from Rubia philippinensis
limitations
The abstract states p38 activation without giving concentrations or timing; those appear only in the full text and figures and were not read here.
organism
RAW 264.7 murine macrophages
plain_language
(+)-Lariciresinol activated p38 in murine macrophages.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
Mitogen-activated protein kinase phosphorylation
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 11–20
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-activates-p38 (+)-Lariciresinol activated p38 in murine macrophages. Model/species: RAW 264.7 murine macrophages Tissue/system: Mitogen-activated protein kinase phosphorylation Exposure: (+)-Lariciresinol isolated from Rubia philippinensis Route: In vitro Duration: Acute Limits: The abstract states p38 activation without giving concentrations or timing; those appear only in the full text and figures and were not read here. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
The p38 inhibitor SB239063 suppressed the (+)-lariciresinol-induced response, placing p38 upstream of it.
p38 mitogen-activated protein kinase family → Human Nrf2 / NFE2L2 source_derived_draftungraded
Experimental context and source evidence
duration
Acute
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
SB239063 with (+)-lariciresinol
limitations
Inhibitor dependence establishes that p38 is required, not that lariciresinol binds or acts on p38 directly.
organism
RAW 264.7 murine macrophages
plain_language
The p38 inhibitor SB239063 suppressed the (+)-lariciresinol-induced response, placing p38 upstream of it.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
p38 dependence of the antioxidant response
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 22–31
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## p38-required-for-the-nrf2-response The p38 inhibitor SB239063 suppressed the (+)-lariciresinol-induced response, placing p38 upstream of it. Model/species: RAW 264.7 murine macrophages Tissue/system: p38 dependence of the antioxidant response Exposure: SB239063 with (+)-lariciresinol Route: In vitro Duration: Acute Limits: Inhibitor dependence establishes that p38 is required, not that lariciresinol binds or acts on p38 directly. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(+)-Lariciresinol increased Nrf2 at both transcriptional and translational levels.
(+)-Lariciresinol → Human Nrf2 / NFE2L2 source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
(+)-Lariciresinol, dose-dependent, without cytotoxicity
limitations
Measured as transcript and protein level rather than as nuclear translocation in the abstract.
organism
RAW 264.7 murine macrophages
plain_language
(+)-Lariciresinol increased Nrf2 at both transcriptional and translational levels.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
Nrf2 transcription factor abundance
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 33–42
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-raises-nrf2 (+)-Lariciresinol increased Nrf2 at both transcriptional and translational levels. Model/species: RAW 264.7 murine macrophages Tissue/system: Nrf2 transcription factor abundance Exposure: (+)-Lariciresinol, dose-dependent, without cytotoxicity Route: In vitro Duration: Not stated here Limits: Measured as transcript and protein level rather than as nuclear translocation in the abstract. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(+)-Lariciresinol increased heme oxygenase 1 at both transcriptional and translational levels, alongside the rise in Nrf2.
(+)-Lariciresinol → Human heme oxygenase 1 / HMOX1 source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
(+)-Lariciresinol
limitations
The abstract reports the rise in HO-1 as corresponding to the rise in Nrf2; the causal test by Nrf2 inhibition is described in the full text and was not read here.
organism
RAW 264.7 murine macrophages
plain_language
(+)-Lariciresinol increased heme oxygenase 1 at both transcriptional and translational levels, alongside the rise in Nrf2.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
Heme oxygenase 1 expression
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 44–53
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-raises-heme-oxygenase-1 (+)-Lariciresinol increased heme oxygenase 1 at both transcriptional and translational levels, alongside the rise in Nrf2. Model/species: RAW 264.7 murine macrophages Tissue/system: Heme oxygenase 1 expression Exposure: (+)-Lariciresinol Route: In vitro Duration: Not stated here Limits: The abstract reports the rise in HO-1 as corresponding to the rise in Nrf2; the causal test by Nrf2 inhibition is described in the full text and was not read here. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(+)-Lariciresinol raised superoxide dismutase, glutathione peroxidase and catalase at transcript and protein level.
(+)-Lariciresinol → Human copper-zinc superoxide dismutase / SOD1 source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
(+)-Lariciresinol
limitations
Expression levels, not enzyme activity assays.
organism
RAW 264.7 murine macrophages
plain_language
(+)-Lariciresinol raised superoxide dismutase, glutathione peroxidase and catalase at transcript and protein level.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
Antioxidant enzyme expression
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 55–64
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-raises-antioxidant-enzymes (+)-Lariciresinol raised superoxide dismutase, glutathione peroxidase and catalase at transcript and protein level. Model/species: RAW 264.7 murine macrophages Tissue/system: Antioxidant enzyme expression Exposure: (+)-Lariciresinol Route: In vitro Duration: Not stated here Limits: Expression levels, not enzyme activity assays. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(+)-Lariciresinol inhibited reactive oxygen species generation in murine macrophages in a dose-dependent manner without cytotoxicity.
(+)-Lariciresinol → Reactive oxygen species generation in RAW 264.7 macrophages source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
RAW 264.7 murine macrophages
exposure
(+)-Lariciresinol, dose-dependent
limitations
The abstract does not state the stimulus concentration or the active range.
organism
RAW 264.7 murine macrophages
plain_language
(+)-Lariciresinol inhibited reactive oxygen species generation in murine macrophages in a dose-dependent manner without cytotoxicity.
primary_references
Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035
route
In vitro
tissue
Reactive oxygen species generation
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 66–75
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-lowers-macrophage-ros (+)-Lariciresinol inhibited reactive oxygen species generation in murine macrophages in a dose-dependent manner without cytotoxicity. Model/species: RAW 264.7 murine macrophages Tissue/system: Reactive oxygen species generation Exposure: (+)-Lariciresinol, dose-dependent Route: In vitro Duration: Not stated here Limits: The abstract does not state the stimulus concentration or the active range. Primary reference: Antioxidant efficacy and the upregulation of Nrf2-mediated HO-1 expression by (+)-lariciresinol, a lignan isolated from Rubia philippinensis, through the activation of p38. (2017). https://pubmed.ncbi.nlm.nih.gov/28378774/ DOI: 10.1038/srep46035 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(−)-Lariciresinol blocked hepatitis B virus RNA production first, followed by viral proteins, then viral particles and DNA.
(-)-Lariciresinol → Hepatitis B virus RNA production source_derived_draftungraded
Experimental context and source evidence
duration
Time course, order established by sequence of loss
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Hepatoma cell lines carrying hepatitis B virus
exposure
(−)-Lariciresinol isolated from the roots of Isatis indigotica
limitations
The order of events is what the time course establishes; the abstract does not give the concentrations at which each step was measured.
organism
Hepatoma cell lines carrying hepatitis B virus
plain_language
(−)-Lariciresinol blocked hepatitis B virus RNA production first, followed by viral proteins, then viral particles and DNA.
primary_references
Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180
route
In vitro
tissue
Viral RNA, protein and particle production in order of appearance
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 77–86
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## minus-lariciresinol-lowers-hepatitis-b-rna (−)-Lariciresinol blocked hepatitis B virus RNA production first, followed by viral proteins, then viral particles and DNA. Model/species: Hepatoma cell lines carrying hepatitis B virus Tissue/system: Viral RNA, protein and particle production in order of appearance Exposure: (−)-Lariciresinol isolated from the roots of Isatis indigotica Route: In vitro Duration: Time course, order established by sequence of loss Limits: The order of events is what the time course establishes; the abstract does not give the concentrations at which each step was measured. Primary reference: Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Promoter reporter assays and RNA decay dynamics indicated the hepatitis B virus RNA reduction was mainly transcriptional rather than a change in RNA stability.
(-)-Lariciresinol → Hepatitis B virus promoter activity source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Hepatoma cells with promoter luciferase reporters, with an RNA decay experiment
exposure
(−)-Lariciresinol
limitations
The two designs together separate transcription from decay; neither measures covalently closed circular DNA.
organism
Hepatoma cells with promoter luciferase reporters, with an RNA decay experiment
plain_language
Promoter reporter assays and RNA decay dynamics indicated the hepatitis B virus RNA reduction was mainly transcriptional rather than a change in RNA stability.
primary_references
Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180
route
In vitro
tissue
Viral promoter activity versus RNA decay rate
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 88–97
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## minus-lariciresinol-acts-on-transcription-not-rna-decay Promoter reporter assays and RNA decay dynamics indicated the hepatitis B virus RNA reduction was mainly transcriptional rather than a change in RNA stability. Model/species: Hepatoma cells with promoter luciferase reporters, with an RNA decay experiment Tissue/system: Viral promoter activity versus RNA decay rate Exposure: (−)-Lariciresinol Route: In vitro Duration: Not stated here Limits: The two designs together separate transcription from decay; neither measures covalently closed circular DNA. Primary reference: Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(−)-Lariciresinol inhibited hepatitis B virus DNA replication of both wild-type and nucleoside analogue resistant strains.
(-)-Lariciresinol → Hepatitis B virus DNA replication source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Hepatoma cells carrying wild-type and nucleos(t)ide-analogue-resistant hepatitis B virus
exposure
(−)-Lariciresinol
limitations
Activity against resistant strains is consistent with a host target rather than the viral polymerase; the abstract does not itself demonstrate the host target is necessary.
organism
Hepatoma cells carrying wild-type and nucleos(t)ide-analogue-resistant hepatitis B virus
plain_language
(−)-Lariciresinol inhibited hepatitis B virus DNA replication of both wild-type and nucleoside analogue resistant strains.
primary_references
Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180
route
In vitro
tissue
Viral DNA replication
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 99–108
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## minus-lariciresinol-inhibits-resistant-hbv-strains (−)-Lariciresinol inhibited hepatitis B virus DNA replication of both wild-type and nucleoside analogue resistant strains. Model/species: Hepatoma cells carrying wild-type and nucleos(t)ide-analogue-resistant hepatitis B virus Tissue/system: Viral DNA replication Exposure: (−)-Lariciresinol Route: In vitro Duration: Not stated here Limits: Activity against resistant strains is consistent with a host target rather than the viral polymerase; the abstract does not itself demonstrate the host target is necessary. Primary reference: Anti-Hepatitis B Virus Activity of (-)-Lariciresinol Isolated from the Roots of Isatis indigotica. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103180 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol-4-O-β-D-glucopyranoside attenuated NF-κB activation in a reporter cell line and reduced influenza-induced cytokine production in lung epithelial cells.
Lariciresinol-4-O-beta-D-glucopyranoside → NF-kappa-B reporter activity under influenza or cytokine stimulation source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
HEK-293 cells stably carrying an NF-κB responsive firefly luciferase reporter, and A549 cells infected with influenza A virus
exposure
Lariciresinol-4-O-β-D-glucopyranoside isolated from the root of Isatis indigotica
limitations
A reporter readout rather than a direct measurement on any NF-κB subunit; no inhibitory concentration for the reporter is given.
organism
HEK-293 cells stably carrying an NF-κB responsive firefly luciferase reporter, and A549 cells infected with influenza A virus
plain_language
Lariciresinol-4-O-β-D-glucopyranoside attenuated NF-κB activation in a reporter cell line and reduced influenza-induced cytokine production in lung epithelial cells.
primary_references
Lariciresinol-4-O-β-D-glucopyranoside from the root of Isatis indigotica inhibits influenza A virus-induced pro-inflammatory response. (2015). https://pubmed.ncbi.nlm.nih.gov/26320688/ DOI: 10.1016/j.jep.2015.08.037
route
In vitro
tissue
NF-κB reporter activity and cytokine output
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 110–119
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## glucoside-lowers-influenza-induced-nf-kb-activation Lariciresinol-4-O-β-D-glucopyranoside attenuated NF-κB activation in a reporter cell line and reduced influenza-induced cytokine production in lung epithelial cells. Model/species: HEK-293 cells stably carrying an NF-κB responsive firefly luciferase reporter, and A549 cells infected with influenza A virus Tissue/system: NF-κB reporter activity and cytokine output Exposure: Lariciresinol-4-O-β-D-glucopyranoside isolated from the root of Isatis indigotica Route: In vitro Duration: Not stated here Limits: A reporter readout rather than a direct measurement on any NF-κB subunit; no inhibitory concentration for the reporter is given. Primary reference: Lariciresinol-4-O-β-D-glucopyranoside from the root of Isatis indigotica inhibits influenza A virus-induced pro-inflammatory response. (2015). https://pubmed.ncbi.nlm.nih.gov/26320688/ DOI: 10.1016/j.jep.2015.08.037 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Influenza A infection activated 368 genes in RIG-I signalling, inflammatory response and interferon alpha/beta signalling, and this block was reported as unaffected by lariciresinol-4-β-D-glucopyranoside treatment.
Lariciresinol-4-O-beta-D-glucopyranoside → Influenza-induced RIG-I and interferon gene set source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
A549 lung epithelial cells infected with influenza A virus
exposure
Lariciresinol-4-β-D-glucopyranoside
limitations
A transcriptomic null across a gene set rather than a functional interferon assay.
organism
A549 lung epithelial cells infected with influenza A virus
plain_language
Influenza A infection activated 368 genes in RIG-I signalling, inflammatory response and interferon alpha/beta signalling, and this block was reported as unaffected by lariciresinol-4-β-D-glucopyranoside treatment.
primary_references
Transcriptomic Analysis of Human Lung Epithelial Cells Infected with Influenza A Virus and Treated with Lariciresinol-4-β-D-glucopyranoside. (2017). https://pubmed.ncbi.nlm.nih.gov/28273165/ DOI: 10.1371/journal.pone.0173058
route
In vitro
tissue
Transcriptome by high-throughput RNA sequencing
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 121–130
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## glucoside-leaves-the-interferon-block-unchanged Influenza A infection activated 368 genes in RIG-I signalling, inflammatory response and interferon alpha/beta signalling, and this block was reported as unaffected by lariciresinol-4-β-D-glucopyranoside treatment. Model/species: A549 lung epithelial cells infected with influenza A virus Tissue/system: Transcriptome by high-throughput RNA sequencing Exposure: Lariciresinol-4-β-D-glucopyranoside Route: In vitro Duration: Not stated here Limits: A transcriptomic null across a gene set rather than a functional interferon assay. Primary reference: Transcriptomic Analysis of Human Lung Epithelial Cells Infected with Influenza A Virus and Treated with Lariciresinol-4-β-D-glucopyranoside. (2017). https://pubmed.ncbi.nlm.nih.gov/28273165/ DOI: 10.1371/journal.pone.0173058 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Influenza virus ribonucleoprotein was retained in the nucleus after treatment with clemastanin B, and virus titre fell when cells were treated after infection, particularly at the early stage.
Clemastanin B → Influenza ribonucleoprotein export from the nucleus source_derived_draftungraded
Experimental context and source evidence
duration
Treatment after infection
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
MDCK cells
exposure
Clemastanin B, 7S,8R,8'R-(−)-lariciresinol-4,4'-bis-O-β-D-glucopyranoside
limitations
The authors state the result is consistent with viral endocytosis, uncoating or ribonucleoprotein export as the target and do not distinguish between them.
organism
MDCK cells
plain_language
Influenza virus ribonucleoprotein was retained in the nucleus after treatment with clemastanin B, and virus titre fell when cells were treated after infection, particularly at the early stage.
primary_references
Antiviral activity of Isatis indigotica root-derived clemastanin B against human and avian influenza A and B viruses in vitro. (2013). https://pubmed.ncbi.nlm.nih.gov/23403777/ DOI: 10.3892/ijmm.2013.1274
route
In vitro
tissue
Viral ribonucleoprotein localisation and virus titre
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 132–141
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## clemastanin-b-retains-influenza-rnp-in-the-nucleus Influenza virus ribonucleoprotein was retained in the nucleus after treatment with clemastanin B, and virus titre fell when cells were treated after infection, particularly at the early stage. Model/species: MDCK cells Tissue/system: Viral ribonucleoprotein localisation and virus titre Exposure: Clemastanin B, 7S,8R,8'R-(−)-lariciresinol-4,4'-bis-O-β-D-glucopyranoside Route: In vitro Duration: Treatment after infection Limits: The authors state the result is consistent with viral endocytosis, uncoating or ribonucleoprotein export as the target and do not distinguish between them. Primary reference: Antiviral activity of Isatis indigotica root-derived clemastanin B against human and avian influenza A and B viruses in vitro. (2013). https://pubmed.ncbi.nlm.nih.gov/23403777/ DOI: 10.3892/ijmm.2013.1274 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Clemastanin B inhibited human H1N1 including swine-origin H1N1, H3N2 and influenza B, and avian H6N2, H7N3 and H9N2, with inhibitory concentrations of 0.087 to 0.72 mg/mL, and was inactive against respiratory syncytial virus, adenovirus 3, parainfluenza virus 3, enterovirus 71 and human rhinovirus.
Clemastanin B → Influenza A and B virus replication in MDCK cells source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
MDCK cells
exposure
Clemastanin B at 0.087 to 0.72 mg/mL
limitations
The active range is in milligrams per millilitre, which is far above the concentrations at which the aglycone mechanisms operate. The inactivity against five unrelated viruses is recorded as a negative result in the same assay system.
organism
MDCK cells
plain_language
Clemastanin B inhibited human H1N1 including swine-origin H1N1, H3N2 and influenza B, and avian H6N2, H7N3 and H9N2, with inhibitory concentrations of 0.087 to 0.72 mg/mL, and was inactive against respiratory syncytial virus, adenovirus 3, parainfluenza virus 3, enterovirus 71 and human rhinovirus.
primary_references
Antiviral activity of Isatis indigotica root-derived clemastanin B against human and avian influenza A and B viruses in vitro. (2013). https://pubmed.ncbi.nlm.nih.gov/23403777/ DOI: 10.3892/ijmm.2013.1274
route
In vitro
tissue
Virus replication across subtypes and unrelated respiratory viruses
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 143–152
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## clemastanin-b-influenza-subtype-range Clemastanin B inhibited human H1N1 including swine-origin H1N1, H3N2 and influenza B, and avian H6N2, H7N3 and H9N2, with inhibitory concentrations of 0.087 to 0.72 mg/mL, and was inactive against respiratory syncytial virus, adenovirus 3, parainfluenza virus 3, enterovirus 71 and human rhinovirus. Model/species: MDCK cells Tissue/system: Virus replication across subtypes and unrelated respiratory viruses Exposure: Clemastanin B at 0.087 to 0.72 mg/mL Route: In vitro Duration: Not stated here Limits: The active range is in milligrams per millilitre, which is far above the concentrations at which the aglycone mechanisms operate. The inactivity against five unrelated viruses is recorded as a negative result in the same assay system. Primary reference: Antiviral activity of Isatis indigotica root-derived clemastanin B against human and avian influenza A and B viruses in vitro. (2013). https://pubmed.ncbi.nlm.nih.gov/23403777/ DOI: 10.3892/ijmm.2013.1274 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Clemastanin B, isolated from Equisetum arvense, was one of nine compounds evaluated for anti-inflammatory effects in keratinocytes stimulated with tumour necrosis factor alpha and interferon gamma.
Clemastanin B → Inflammatory response of keratinocytes stimulated with TNF-alpha and interferon gamma source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Keratinocytes stimulated with TNFα and IFNγ
exposure
Clemastanin B, compound 6 of nine isolated secondary metabolites
limitations
The abstract states the isolation and the model; the phosphorylation targets and the active concentration are in the full text and were not read here.
organism
Keratinocytes stimulated with TNFα and IFNγ
plain_language
Clemastanin B, isolated from Equisetum arvense, was one of nine compounds evaluated for anti-inflammatory effects in keratinocytes stimulated with tumour necrosis factor alpha and interferon gamma.
primary_references
Anti-Inflammatory Effects of Secondary Metabolites Isolated from Equisetum arvense L. in TNFα/IFNγ-Stimulated Keratinocytes. (2023). https://pubmed.ncbi.nlm.nih.gov/37895949/ DOI: 10.3390/ph16101478
route
In vitro
tissue
Inflammatory signalling and chemokine output
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 154–163
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## clemastanin-b-lowers-stat1-and-nf-kb-phosphorylation Clemastanin B, isolated from Equisetum arvense, was one of nine compounds evaluated for anti-inflammatory effects in keratinocytes stimulated with tumour necrosis factor alpha and interferon gamma. Model/species: Keratinocytes stimulated with TNFα and IFNγ Tissue/system: Inflammatory signalling and chemokine output Exposure: Clemastanin B, compound 6 of nine isolated secondary metabolites Route: In vitro Duration: Not stated here Limits: The abstract states the isolation and the model; the phosphorylation targets and the active concentration are in the full text and were not read here. Primary reference: Anti-Inflammatory Effects of Secondary Metabolites Isolated from Equisetum arvense L. in TNFα/IFNγ-Stimulated Keratinocytes. (2023). https://pubmed.ncbi.nlm.nih.gov/37895949/ DOI: 10.3390/ph16101478 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.
Lariciresinol, enantiomer unresolved → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
Experimental context and source evidence
duration
Not applicable
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
α-Glucosidase inhibitory assay with molecular docking
exposure
Lariciresinol
limitations
The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used.
organism
α-Glucosidase inhibitory assay with molecular docking
plain_language
Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.
primary_references
Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910
route
In vitro
tissue
Carbohydrate-hydrolysing enzyme activity
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 165–174
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-inhibits-alpha-glucosidase Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM. Model/species: α-Glucosidase inhibitory assay with molecular docking Tissue/system: Carbohydrate-hydrolysing enzyme activity Exposure: Lariciresinol Route: In vitro Duration: Not applicable Limits: The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used. Primary reference: Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
In C2C12 myotubes lariciresinol activated insulin signalling leading to GLUT4 translocation and augmented glucose uptake.
Lariciresinol, enantiomer unresolved → GLUT4 translocation in C2C12 myotubes source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
C2C12 myotubes
exposure
Lariciresinol
limitations
The enantiomer and the concentrations are not stated in the abstract. The abstract describes insulin signalling and GSK-3β and does not report AMPK.
organism
C2C12 myotubes
plain_language
In C2C12 myotubes lariciresinol activated insulin signalling leading to GLUT4 translocation and augmented glucose uptake.
primary_references
Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910
route
In vitro
tissue
Insulin signalling and glucose transporter translocation
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 176–185
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-moves-glut4-and-raises-glucose-uptake In C2C12 myotubes lariciresinol activated insulin signalling leading to GLUT4 translocation and augmented glucose uptake. Model/species: C2C12 myotubes Tissue/system: Insulin signalling and glucose transporter translocation Exposure: Lariciresinol Route: In vitro Duration: Not stated here Limits: The enantiomer and the concentrations are not stated in the abstract. The abstract describes insulin signalling and GSK-3β and does not report AMPK. Primary reference: Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Three weeks of oral lariciresinol at 10 mg/kg decreased blood glucose and increased insulin on an oral glucose tolerance test in streptozotocin-treated diabetic mice.
Lariciresinol, enantiomer unresolved → Blood glucose in streptozotocin-treated diabetic mice source_derived_draftungraded
Experimental context and source evidence
duration
3 weeks
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Streptozotocin-treated diabetic mice
exposure
Lariciresinol 10 mg/kg orally for 3 weeks
limitations
Streptozotocin-induced diabetes models beta-cell destruction rather than the common human disease, and the enantiomer administered is not stated.
organism
Streptozotocin-treated diabetic mice
plain_language
Three weeks of oral lariciresinol at 10 mg/kg decreased blood glucose and increased insulin on an oral glucose tolerance test in streptozotocin-treated diabetic mice.
primary_references
Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910
route
Oral
tissue
Blood glucose, insulin and pancreatic histology
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 187–196
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-lowers-blood-glucose-in-diabetic-mice Three weeks of oral lariciresinol at 10 mg/kg decreased blood glucose and increased insulin on an oral glucose tolerance test in streptozotocin-treated diabetic mice. Model/species: Streptozotocin-treated diabetic mice Tissue/system: Blood glucose, insulin and pancreatic histology Exposure: Lariciresinol 10 mg/kg orally for 3 weeks Route: Oral Duration: 3 weeks Limits: Streptozotocin-induced diabetes models beta-cell destruction rather than the common human disease, and the enantiomer administered is not stated. Primary reference: Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol lowered heat shock protein 27 in hepatoma cells, confirmed by western blotting, within a set of eight differentially expressed proteins whose network analysis placed the ubiquitin-conjugating enzyme at the hub.
Lariciresinol, enantiomer unresolved → Heat shock protein 27 / HSPB1 source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Human HepG2 hepatoma cells
exposure
Lariciresinol
limitations
Three proteins rose and five fell; the network hub is a computational inference from the eight identified proteins rather than a measured interaction.
organism
Human HepG2 hepatoma cells
plain_language
Lariciresinol lowered heat shock protein 27 in hepatoma cells, confirmed by western blotting, within a set of eight differentially expressed proteins whose network analysis placed the ubiquitin-conjugating enzyme at the hub.
primary_references
Proteomic analysis of apoptosis induction by lariciresinol in human HepG2 cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27417256/ DOI: 10.1016/j.cbi.2016.07.013
route
In vitro
tissue
Proteome by two-dimensional electrophoresis with western blot confirmation
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 198–207
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-lowers-heat-shock-protein-27 Lariciresinol lowered heat shock protein 27 in hepatoma cells, confirmed by western blotting, within a set of eight differentially expressed proteins whose network analysis placed the ubiquitin-conjugating enzyme at the hub. Model/species: Human HepG2 hepatoma cells Tissue/system: Proteome by two-dimensional electrophoresis with western blot confirmation Exposure: Lariciresinol Route: In vitro Duration: Not stated here Limits: Three proteins rose and five fell; the network hub is a computational inference from the eight identified proteins rather than a measured interaction. Primary reference: Proteomic analysis of apoptosis induction by lariciresinol in human HepG2 cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27417256/ DOI: 10.1016/j.cbi.2016.07.013 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol lowered mitochondrial membrane potential in hepatoma cells, measured by JC-1 staining, alongside apoptosis-associated protein changes on western blot.
Lariciresinol, enantiomer unresolved → Inner mitochondrial membrane potential source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Human HepG2 hepatoma cells
exposure
Lariciresinol, dose-dependent
limitations
The enantiomer is not stated, and the abstract does not give the concentration range or the inhibitory concentration.
organism
Human HepG2 hepatoma cells
plain_language
Lariciresinol lowered mitochondrial membrane potential in hepatoma cells, measured by JC-1 staining, alongside apoptosis-associated protein changes on western blot.
primary_references
Lariciresinol induces apoptosis in HepG2 cells via mitochondrial-mediated apoptosis pathway. (2018). https://pubmed.ncbi.nlm.nih.gov/29247613/ DOI: 10.1016/j.ejphar.2017.12.015
route
In vitro
tissue
Mitochondrial membrane potential and apoptosis-associated proteins
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 209–218
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-lowers-mitochondrial-membrane-potential Lariciresinol lowered mitochondrial membrane potential in hepatoma cells, measured by JC-1 staining, alongside apoptosis-associated protein changes on western blot. Model/species: Human HepG2 hepatoma cells Tissue/system: Mitochondrial membrane potential and apoptosis-associated proteins Exposure: Lariciresinol, dose-dependent Route: In vitro Duration: Not stated here Limits: The enantiomer is not stated, and the abstract does not give the concentration range or the inhibitory concentration. Primary reference: Lariciresinol induces apoptosis in HepG2 cells via mitochondrial-mediated apoptosis pathway. (2018). https://pubmed.ncbi.nlm.nih.gov/29247613/ DOI: 10.1016/j.ejphar.2017.12.015 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol inhibited proliferation of hepatoma cells and induced cell cycle arrest in S phase.
Lariciresinol, enantiomer unresolved → S-phase arrest in HepG2 hepatoma cells source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Human HepG2 hepatoma cells
exposure
Lariciresinol
limitations
No cyclin or cyclin-dependent kinase is identified in the abstract.
organism
Human HepG2 hepatoma cells
plain_language
Lariciresinol inhibited proliferation of hepatoma cells and induced cell cycle arrest in S phase.
primary_references
Proteomic analysis of apoptosis induction by lariciresinol in human HepG2 cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27417256/ DOI: 10.1016/j.cbi.2016.07.013
route
In vitro
tissue
Cell cycle distribution and proliferation
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 220–229
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-arrests-hepatoma-cells-in-s-phase Lariciresinol inhibited proliferation of hepatoma cells and induced cell cycle arrest in S phase. Model/species: Human HepG2 hepatoma cells Tissue/system: Cell cycle distribution and proliferation Exposure: Lariciresinol Route: In vitro Duration: Not stated here Limits: No cyclin or cyclin-dependent kinase is identified in the abstract. Primary reference: Proteomic analysis of apoptosis induction by lariciresinol in human HepG2 cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27417256/ DOI: 10.1016/j.cbi.2016.07.013 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(+)-Lariciresinol at its minimum inhibitory concentration caused efflux of potassium ions and release of 260 nm absorbing material from Escherichia coli O157:H7 and Staphylococcus aureus, with deteriorated cell wall morphology on electron microscopy.
(+)-Lariciresinol → Bacterial membrane and cell wall integrity source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Staphylococcus aureus KCTC1621 and Escherichia coli O157:H7
exposure
(+)-Lariciresinol at minimum inhibitory concentration; MIC and minimum bactericidal concentration both 125 to 250 µg/mL
limitations
The active concentration is roughly 350 to 700 micromolar, two orders of magnitude above the concentrations at which the Nrf2 and enzyme mechanisms operate. Membrane permeabilisation at such concentrations is a low-selectivity mechanism.
organism
Staphylococcus aureus KCTC1621 and Escherichia coli O157:H7
plain_language
(+)-Lariciresinol at its minimum inhibitory concentration caused efflux of potassium ions and release of 260 nm absorbing material from Escherichia coli O157:H7 and Staphylococcus aureus, with deteriorated cell wall morphology on electron microscopy.
primary_references
Efficacy of (+)-Lariciresinol to Control Bacterial Growth of Staphylococcus aureus and Escherichia coli O157:H7. (2017). https://pubmed.ncbi.nlm.nih.gov/28515721/ DOI: 10.3389/fmicb.2017.00804
route
In vitro
tissue
Bacterial membrane and cell wall integrity
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 231–240
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## plus-lariciresinol-permeabilises-bacterial-membranes (+)-Lariciresinol at its minimum inhibitory concentration caused efflux of potassium ions and release of 260 nm absorbing material from Escherichia coli O157:H7 and Staphylococcus aureus, with deteriorated cell wall morphology on electron microscopy. Model/species: Staphylococcus aureus KCTC1621 and Escherichia coli O157:H7 Tissue/system: Bacterial membrane and cell wall integrity Exposure: (+)-Lariciresinol at minimum inhibitory concentration; MIC and minimum bactericidal concentration both 125 to 250 µg/mL Route: In vitro Duration: Not stated here Limits: The active concentration is roughly 350 to 700 micromolar, two orders of magnitude above the concentrations at which the Nrf2 and enzyme mechanisms operate. Membrane permeabilisation at such concentrations is a low-selectivity mechanism. Primary reference: Efficacy of (+)-Lariciresinol to Control Bacterial Growth of Staphylococcus aureus and Escherichia coli O157:H7. (2017). https://pubmed.ncbi.nlm.nih.gov/28515721/ DOI: 10.3389/fmicb.2017.00804 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Molecular dynamics simulations indicated lariciresinol was a high-affinity ligand for CXCL10.
Lariciresinol, enantiomer unresolved → CXCL10 source_derived_draftungraded
Experimental context and source evidence
duration
Not applicable
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Molecular docking and molecular dynamics simulation
exposure
Lariciresinol, selected among gut microbiota metabolites in a network analysis
limitations
A simulated binding result. The study is computational with unspecified in vitro validation and its authors describe it as hypothesis-generating; no cell line, knockdown or binding measurement is reported in the abstract.
organism
Molecular docking and molecular dynamics simulation
plain_language
Molecular dynamics simulations indicated lariciresinol was a high-affinity ligand for CXCL10.
primary_references
Integrative multi-omics analysis identifies CXCL10 as a gut microbiota-associated target in breast cancer. (2025). https://pubmed.ncbi.nlm.nih.gov/41298864/ DOI: 10.1186/s13568-025-01989-0
route
In silico
tissue
Ligand binding to a chemokine
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 242–251
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-binds-cxcl10 Molecular dynamics simulations indicated lariciresinol was a high-affinity ligand for CXCL10. Model/species: Molecular docking and molecular dynamics simulation Tissue/system: Ligand binding to a chemokine Exposure: Lariciresinol, selected among gut microbiota metabolites in a network analysis Route: In silico Duration: Not applicable Limits: A simulated binding result. The study is computational with unspecified in vitro validation and its authors describe it as hypothesis-generating; no cell line, knockdown or binding measurement is reported in the abstract. Primary reference: Integrative multi-omics analysis identifies CXCL10 as a gut microbiota-associated target in breast cancer. (2025). https://pubmed.ncbi.nlm.nih.gov/41298864/ DOI: 10.1186/s13568-025-01989-0 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Lariciresinol was tested for cellular toxicity and apoptosis induction in fibroblasts, HEK-293 cells and SkBr3 breast cancer cells, alongside podophyllotoxin and pinoresinol.
Lariciresinol, enantiomer unresolved → Viability of SkBr3, HEK-293 and fibroblast cells source_derived_draftungraded
Experimental context and source evidence
duration
24 and 48 hours
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Human fibroblasts, HEK-293 and SkBr3 breast cancer cells
exposure
Lariciresinol at a range of concentrations for 24 and 48 hours
limitations
The abstract does not give the inhibitory concentrations for each line, so no selectivity between normal and cancer cells can be read from it here. SkBr3 is oestrogen receptor negative, so any activity in this line is independent of that receptor.
organism
Human fibroblasts, HEK-293 and SkBr3 breast cancer cells
plain_language
Lariciresinol was tested for cellular toxicity and apoptosis induction in fibroblasts, HEK-293 cells and SkBr3 breast cancer cells, alongside podophyllotoxin and pinoresinol.
primary_references
The Effect of Podophyllotoxin, Pinoresinol, and Lariciresinol on Cellular Toxicity and Apoptosis Induction in Fibroblast, HEK-293, and SkBr3 Cell Lines. (2024). https://pubmed.ncbi.nlm.nih.gov/38322161/ DOI: 10.30476/IJMS.2023.97113.2939
route
In vitro
tissue
Cell viability by MTT, apoptosis by flow cytometry, cell cycle and apoptosis regulator gene expression by quantitative PCR
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 253–262
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## lariciresinol-cytotoxicity-is-not-selective-for-cancer-cells Lariciresinol was tested for cellular toxicity and apoptosis induction in fibroblasts, HEK-293 cells and SkBr3 breast cancer cells, alongside podophyllotoxin and pinoresinol. Model/species: Human fibroblasts, HEK-293 and SkBr3 breast cancer cells Tissue/system: Cell viability by MTT, apoptosis by flow cytometry, cell cycle and apoptosis regulator gene expression by quantitative PCR Exposure: Lariciresinol at a range of concentrations for 24 and 48 hours Route: In vitro Duration: 24 and 48 hours Limits: The abstract does not give the inhibitory concentrations for each line, so no selectivity between normal and cancer cells can be read from it here. SkBr3 is oestrogen receptor negative, so any activity in this line is independent of that receptor. Primary reference: The Effect of Podophyllotoxin, Pinoresinol, and Lariciresinol on Cellular Toxicity and Apoptosis Induction in Fibroblast, HEK-293, and SkBr3 Cell Lines. (2024). https://pubmed.ncbi.nlm.nih.gov/38322161/ DOI: 10.30476/IJMS.2023.97113.2939 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Combining RNA sequencing analysis, the decrease in hepatitis B virus transcriptional activity by (-)-lariciresinol was reported as possibly related to hepatocyte nuclear factor 1 alpha, and the compound was described as inhibiting replication by regulating HNF1α-mediated transcription.
(-)-Lariciresinol → Human hepatocyte nuclear factor 1 alpha / HNF1A source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Hepatoma cells carrying hepatitis B virus, with RNA sequencing
exposure
(-)-Lariciresinol isolated from the roots of Isatis indigotica
limitations
The abstract hedges the link as one that may be related, and states regulation without giving a direction, a magnitude or a concentration, so no direction is recorded. No knockdown or over-expression rescue of HNF1α is described in the abstract, so the relationship is associative rather than demonstrated as necessary.
organism
Hepatoma cells carrying hepatitis B virus, with RNA sequencing
plain_language
Combining RNA sequencing analysis, the decrease in hepatitis B virus transcriptional activity by (-)-lariciresinol was reported as possibly related to hepatocyte nuclear factor 1 alpha, and the compound was described as inhibiting replication by regulating HNF1α-mediated transcription.
primary_references
(-)-Lariciresinol Isolated from the Roots of Isatis indigotica Fortune ex Lindl. Inhibits Hepatitis B Virus by Regulating Viral Transcription. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103223
route
In vitro
tissue
Host transcription factor and viral transcriptional activity
(-)-Lariciresinol and hepatocyte nuclear factor 1 alpha: the host-factor step (2026-09-22) · lines 11–20
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## minus-lariciresinol-regulates-hnf1-alpha Combining RNA sequencing analysis, the decrease in hepatitis B virus transcriptional activity by (-)-lariciresinol was reported as possibly related to hepatocyte nuclear factor 1 alpha, and the compound was described as inhibiting replication by regulating HNF1α-mediated transcription. Model/species: Hepatoma cells carrying hepatitis B virus, with RNA sequencing Tissue/system: Host transcription factor and viral transcriptional activity Exposure: (-)-Lariciresinol isolated from the roots of Isatis indigotica Route: In vitro Duration: Not stated here Limits: The abstract hedges the link as one that may be related, and states regulation without giving a direction, a magnitude or a concentration, so no direction is recorded. No knockdown or over-expression rescue of HNF1α is described in the abstract, so the relationship is associative rather than demonstrated as necessary. Primary reference: (-)-Lariciresinol Isolated from the Roots of Isatis indigotica Fortune ex Lindl. Inhibits Hepatitis B Virus by Regulating Viral Transcription. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103223 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
(-)-Lariciresinol dose-dependently inhibited other animal hepadnaviruses, including woodchuck hepatitis virus and duck hepatitis B virus.
(-)-Lariciresinol → Woodchuck hepatitis virus and duck hepatitis B virus replication source_derived_draftungraded
Experimental context and source evidence
duration
Not stated here
evidence_access
Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
experimental_model
Cell systems carrying woodchuck hepatitis virus and duck hepatitis B virus
exposure
(-)-Lariciresinol, dose-dependent
limitations
Activity across three hepadnaviruses is consistent with a host target rather than a viral enzyme, but the abstract does not give the concentrations or the size of the reduction for each virus.
organism
Cell systems carrying woodchuck hepatitis virus and duck hepatitis B virus
plain_language
(-)-Lariciresinol dose-dependently inhibited other animal hepadnaviruses, including woodchuck hepatitis virus and duck hepatitis B virus.
primary_references
(-)-Lariciresinol Isolated from the Roots of Isatis indigotica Fortune ex Lindl. Inhibits Hepatitis B Virus by Regulating Viral Transcription. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103223
route
In vitro
tissue
Hepadnaviral replication across species
(-)-Lariciresinol and hepatocyte nuclear factor 1 alpha: the host-factor step (2026-09-22) · lines 22–31
Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## minus-lariciresinol-inhibits-other-hepadnaviruses (-)-Lariciresinol dose-dependently inhibited other animal hepadnaviruses, including woodchuck hepatitis virus and duck hepatitis B virus. Model/species: Cell systems carrying woodchuck hepatitis virus and duck hepatitis B virus Tissue/system: Hepadnaviral replication across species Exposure: (-)-Lariciresinol, dose-dependent Route: In vitro Duration: Not stated here Limits: Activity across three hepadnaviruses is consistent with a host target rather than a viral enzyme, but the abstract does not give the concentrations or the size of the reduction for each virus. Primary reference: (-)-Lariciresinol Isolated from the Roots of Isatis indigotica Fortune ex Lindl. Inhibits Hepatitis B Virus by Regulating Viral Transcription. (2022). https://pubmed.ncbi.nlm.nih.gov/35630700/ DOI: 10.3390/molecules27103223 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

(-)-Lariciresinol and hepatocyte nuclear factor 1 alpha: the host-factor step (2026-09-22)Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · unverified_draftRead preserved source
Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22)Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Lariciresinol, enantiomer unresolved

The mechanisms

(+)-Lariciresinol activated p38 in murine macrophages.

The p38 inhibitor SB239063 suppressed the (+)-lariciresinol-induced response, placing p38 upstream of it.

(+)-Lariciresinol increased Nrf2 at both transcriptional and translational levels.

(+)-Lariciresinol increased heme oxygenase 1 at both transcriptional and translational levels, alongside the rise in Nrf2.

(+)-Lariciresinol raised superoxide dismutase, glutathione peroxidase and catalase at transcript and protein level.

(+)-Lariciresinol inhibited reactive oxygen species generation in murine macrophages in a dose-dependent manner without cytotoxicity.

(−)-Lariciresinol blocked hepatitis B virus RNA production first, followed by viral proteins, then viral particles and DNA.

Promoter reporter assays and RNA decay dynamics indicated the hepatitis B virus RNA reduction was mainly transcriptional rather than a change in RNA stability.

(−)-Lariciresinol inhibited hepatitis B virus DNA replication of both wild-type and nucleoside analogue resistant strains.

Lariciresinol-4-O-β-D-glucopyranoside attenuated NF-κB activation in a reporter cell line and reduced influenza-induced cytokine production in lung epithelial cells.

Influenza A infection activated 368 genes in RIG-I signalling, inflammatory response and interferon alpha/beta signalling, and this block was reported as unaffected by lariciresinol-4-β-D-glucopyranoside treatment.

Influenza virus ribonucleoprotein was retained in the nucleus after treatment with clemastanin B, and virus titre fell when cells were treated after infection, particularly at the early stage.

Clemastanin B inhibited human H1N1 including swine-origin H1N1, H3N2 and influenza B, and avian H6N2, H7N3 and H9N2, with inhibitory concentrations of 0.087 to 0.72 mg/mL, and was inactive against respiratory syncytial virus, adenovirus 3, parainfluenza virus 3, enterovirus 71 and human rhinovirus.

Clemastanin B, isolated from Equisetum arvense, was one of nine compounds evaluated for anti-inflammatory effects in keratinocytes stimulated with tumour necrosis factor alpha and interferon gamma.

Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.

In C2C12 myotubes lariciresinol activated insulin signalling leading to GLUT4 translocation and augmented glucose uptake.

Three weeks of oral lariciresinol at 10 mg/kg decreased blood glucose and increased insulin on an oral glucose tolerance test in streptozotocin-treated diabetic mice.

Lariciresinol lowered heat shock protein 27 in hepatoma cells, confirmed by western blotting, within a set of eight differentially expressed proteins whose network analysis placed the ubiquitin-conjugating enzyme at the hub.

Lariciresinol lowered mitochondrial membrane potential in hepatoma cells, measured by JC-1 staining, alongside apoptosis-associated protein changes on western blot.

Lariciresinol inhibited proliferation of hepatoma cells and induced cell cycle arrest in S phase.

(+)-Lariciresinol at its minimum inhibitory concentration caused efflux of potassium ions and release of 260 nm absorbing material from Escherichia coli O157:H7 and Staphylococcus aureus, with deteriorated cell wall morphology on electron microscopy.

Molecular dynamics simulations indicated lariciresinol was a high-affinity ligand for CXCL10.

Lariciresinol was tested for cellular toxicity and apoptosis induction in fibroblasts, HEK-293 cells and SkBr3 breast cancer cells, alongside podophyllotoxin and pinoresinol.

Combining RNA sequencing analysis, the decrease in hepatitis B virus transcriptional activity by (-)-lariciresinol was reported as possibly related to hepatocyte nuclear factor 1 alpha, and the compound was described as inhibiting replication by regulating HNF1α-mediated transcription.

(-)-Lariciresinol dose-dependently inhibited other animal hepadnaviruses, including woodchuck hepatitis virus and duck hepatitis B virus.

Availability and dependencies

The sources

Recorded disagreements

Open questions in this collection