The Multi-Target Strategy — Part Two
How the autophagy strategy is designed to layer HCQ, AKBA, metabolic pressure, and host support across multiple cancer survival pathways
Part Two of a three-part investigation into autophagy inhibition, metabolic siege, and protecting the host.
Part One established why dormant, treatment-arrested, and chemotherapy-stressed cancer cells can become heavily dependent on autophagy.
That dependence creates a real strategic target.
Part Two maps the strategy itself.
This is not a single-agent idea.
It is a layered siege.
Read the trilogy in order: The Early Window — Part One → The Multi-Target Strategy — Part Two → Protecting the Host — Part Three
Each compound is chosen to do one of four jobs.
deepen autophagy pressure
remove a metabolic escape route
suppress a survival-signalling node
reduce collateral damage to the host
This strategy is mechanistic and preclinical-heavy.
It is not standard of care.
Several components have real interaction, cardiac, retinal, liver, or tolerance considerations.
It only makes sense in supervised use.
The compounds covered here
This part covers the core strategy.
Liposomal AKBA
Hydroxychloroquine
Liposomal curcumin
Liposomal berberine
Urolithin A
EGCG 80%
Glutamine Inhibifour
Glycolysis Inhibithree
The dietary considerations come in Part Three.
Layer one: the autophagy blockade
The foundation is a two-point autophagy strategy.
One layer presses on autophagy signalling upstream.
The other blocks completion downstream.
Together, they are designed to leave stressed cancer cells with rising cargo, poor recycling, and fewer metabolic exits.
Liposomal AKBA — upstream autophagy suppressor and NF‑κB p65 governor
Acetyl‑11‑keto‑β‑boswellic acid (AKBA) is the most pharmacologically active boswellic acid from Boswellia serrata resin.
In this strategy, AKBA attacks cancer cell autophagy from the top of the signalling cascade.
It suppresses ERK/mTOR and p53/mTOR pathways.
Through these, it downregulates core autophagy machinery proteins: ATG5, ATG3, ATG7, ATG12, Beclin‑1, and LC3‑II.
These are the structural proteins that build the autophagosome.
Without them, the cancer cell struggles to even begin the autophagy process it depends on.
Beyond autophagy, AKBA simultaneously suppresses NF‑κB p65.
NF‑κB p65 is a critical pro‑survival and pro‑inflammatory transcription factor.
AKBA also inhibits VEGFR‑2, HIF‑1α, and HIF‑1β.
HIF‑1α and HIF‑1β are master activators of tumour survival under hypoxic conditions and primary drivers of VEGF‑mediated angiogenesis.
By downregulating them, AKBA cuts the tumour’s ability to build new blood vessels and to adapt to a low‑oxygen microenvironment.
AKBA’s role as an NF‑κB p65 suppressor is also the key reason it is indispensable alongside HCQ in this strategy.
HCQ’s blockade of autophagy causes p62/SQSTM1 to accumulate inside cancer cells.
That accumulation is part of the intended mechanism: it traps the cell in a toxic, undegraded‑cargo state.
But if it is left ungoverned, elevated p62 can activate NF‑κB p65 and create a pro‑survival escape signal.
AKBA suppresses this NF‑κB p65 activation.
It denies the cancer cell the survival route that p62 accumulation would otherwise open.
This is the molecular reason why the AKBA + HCQ combination produces effects greater than either agent alone.
Boswellic Acid + Chloroquine in Prostate Cancer Pre-Clinical Study - Great Results
An important finding from prostate cancer research is that combining boswellic acid with the autophagy inhibitor chloroquine (CQ) produced dramatically enhanced results. BA145 (a boswellic acid analogue) plus CQ suppressed tumour growth by 58% in aggressive prostate cancer xenografts — more than double the effect of BA145 alone. CQ potentiated BA145's suppression of VEGFR-2, HIF-1α, and HIF-1β, while boosting pro-apoptotic signals. This suggests a therapeutic strategy where AKBA could be combined with autophagy inhibitors for greater effect. https://pmc.ncbi.nlm.nih.gov/articles/PMC4509694/
Liposomal delivery is not negotiable.
Standard Boswellia extracts have poor oral bioavailability because AKBA is hydrophobic and rapidly cleared in first‑pass metabolism.
Phospholipid‑complexed liposomal formulations dramatically increase AKBA absorption and plasma concentrations, turning a theoretical effect into a realistic tissue‑level exposure.
Visit our Boswellia/AKBA in Oncology hub
Hydroxychloroquine (HCQ) — the downstream lysosomal fusion block
While AKBA suppresses autophagy from above, HCQ attacks it from below.
HCQ is a lysosomotropic agent.
It accumulates in lysosomes throughout the body over weeks and months.
As it builds up, it raises the pH of the lysosomal compartment.
Its primary anti-autophagy mechanism is specific.
It prevents the physical fusion between autophagosomes and lysosomes.
That means autophagosomes can still form, but they cannot deliver their cargo for degradation.
The lysosome remains intact.
It simply never receives the delivery.
This creates a toxic accumulation of undegraded autophagosomes inside the cancer cell.
It becomes a cellular waste crisis.
When the same cell is also being stripped of glycolytic and glutamine fuel sources by the rest of the strategy, that crisis becomes much harder to survive.
HCQ also prevents the lysosomal degradation of pro-apoptotic mediators that cancer cells would otherwise destroy.
That means it may help keep some of the cell’s own death signals alive.
The pharmacokinetic reality of HCQ matters.
It has a long terminal half-life.
It also accumulates extensively in tissue.
That means both therapeutic effect and host burden build gradually over time.
This is one of the main reasons Part Three matters so much.
The more HCQ accumulates in lysosome-rich healthy tissues, including retina, cardiac muscle, and skeletal muscle, the more important careful supervision becomes.
Human Trial Summary: Three months for dormant tumour cells to be reduced by 80% with HCQ alone
The CLEVER trial (NCT03032406) enrolled 51 breast-cancer survivors with bone-marrow disseminated tumour cells.
Patients received hydroxychloroquine, everolimus, or both.
After three month long treatment cycles, more than 80% of participants in each arm had no detectable dormant tumour cells in bone marrow.
Reported DTC reduction was:
HCQ alone: 80%
Everolimus alone: 78%
HCQ + everolimus: 87%
In practical terms, this makes three months the key early checkpoint used in the trial for assessing dormant-cell clearance.
At a median follow-up of 42 months, recurrence-free survival remained high:
HCQ alone: 91.7%
Everolimus alone: 92.9%
HCQ + everolimus: 100%
Clearance also tracked with better outcomes.
That makes the trial important even though it remains early and small.
Primary paper: Targeting dormant tumor cells to prevent recurrent breast cancer
Layer two: inflammation, survival signalling, and chemosensitisation
This layer bridges autophagy pressure with metabolic pressure.
It focuses on NF-κB, HIF-1α, mTOR-related signalling, and treatment adaptation.
Liposomal Curcumin — the inflammatory and metabolic bridge
Curcumin, the primary bioactive polyphenol of Curcuma longa, operates across multiple targets that bridge the autophagy layer and the metabolic siege layer.
Its most important contributions in this strategy are the suppression of NF‑κB, inhibition of mTOR, and direct downregulation of HIF‑1α.
That means it reinforces AKBA’s work from a different molecular angle.
It deepens the inflammatory blockade.
It adds to the upstream autophagy pressure.
And it strengthens the push against hypoxia adaptation.
Curcumin also directly disrupts glutamine metabolism in cancer cells.
It downregulates glutaminase (GLS).
It also suppresses c‑Myc, the transcription factor that drives cancer cells to increase glutamine uptake and utilisation.
That makes curcumin more than an anti-inflammatory compound.
In this strategy, it acts as a bridge between the autophagy blockade and the glutaminolysis inhibition layer.
It connects nutrient sensing to metabolic fuel sourcing.
The combination of AKBA and curcumin has direct evidence of synergy across colorectal cancer cell lines.
Gene expression arrays showed that they regulate distinct but complementary anti-cancer signalling pathways.
Together, they form a dual-compound platform for NF‑κB and HIF‑1α suppression that is broader than either alone.
As with AKBA, liposomal delivery is essential.
Standard curcumin has notoriously poor bioavailability.
Phospholipid-complexed liposomal formulations are the minimum standard if the goal is meaningful plasma and tissue exposure.
Visit our Curcumin in Oncology Hub
Liposomal Berberine — AMPK pressure, glycolytic pressure, and flux loading
Berberine contributes through a different and very important mechanism.
It activates AMPK while simultaneously suppressing mTOR and impairing glycolytic capacity in cancer cells.
That makes it relevant to both energy stress and autophagy pressure.
In glioblastoma models, berberine profoundly altered the metabolic state of cancer cells through the AMPK/mTOR/ULK1 pathway.
It induced autophagy flux.
At the same time, it impaired the cells’ ability to fuel themselves through glycolysis.
This reduced invasive properties and proliferative potential, and it induced apoptotic cell death.
That creates a critical strategic pairing with HCQ.
Berberine can load more autophagosome cargo into the pathway.
HCQ then blocks completion at the fusion gate.
So in this strategy, berberine does not contradict HCQ.
It can intensify the pressure by increasing the load on a pathway that HCQ prevents the cell from clearing.
In ovarian cancer, berberine was also shown to reduce both glycolysis and autophagy levels through the LINC00123/P65/MAPK10 axis.
That inhibited cancer cell proliferation and metastasis.
Its suppression of NF‑κB through inhibition of p65 nuclear translocation adds a third convergent anti-survival action alongside AKBA and curcumin.
Berberine also suppresses VEGF expression, HIF‑1α activity, and the PI3K/Akt signalling pathway.
That deepens the anti-angiogenic and hypoxia-adaptive blockade already established elsewhere in the strategy.
In breast cancer cells, berberine inhibits cancer stem cell self-renewal and downregulates Rb pathway signalling.
That creates cell cycle arrest and amplifies the CDK4/6-induced G1 arrest already relevant to the clinical context described in Part One.
Liposomal delivery significantly improves berberine’s bioavailability and gut tolerability compared with standard berberine HCl formulations.
Visit our Berberine in Oncology hub.
Layer three: host protection and direct anti-cancer pressure
This layer matters because the strategy is not acting only on cancer cells.
Healthy tissue is exposed too.
That is where Urolithin A becomes strategically different.
Urolithin A — the dual-role agent
Urolithin A occupies a unique position in the strategy.
It is both a host-protective agent and a direct anti-cancer compound.
It is produced by gut bacteria from ellagitannins found in pomegranate, berries, and walnuts.
But human production varies widely.
That makes supplementation the most reliable way to achieve consistent levels.
In healthy tissue, Urolithin A’s primary mechanism is activation of PINK1/Parkin-mediated selective mitophagy.
This is the process that identifies and removes damaged mitochondria.
That is fundamentally different from the bulk autophagy pressure created elsewhere in the strategy.
This distinction matters.
HCQ works at the autophagosome-lysosome fusion gate.
Urolithin A works at the initiation and tagging end of selective mitophagy.
It also supports lysosomal quality by restoring cathepsin activity and promoting lysophagy.
In the original Part Two framework, this lysophagy role is linked to p62-Ser403.
That is why Urolithin A and HCQ are not direct duplicates.
They act on different sub-steps of the wider autophagy-lysosome system.
In cancer cells, Urolithin A’s role changes.
AMPK activation by Urolithin A suppresses mTOR.
That adds direct metabolic anti-tumour pressure.
It also complements the mTOR-related pressure already created elsewhere in the strategy.
Direct anti-proliferative effects have been documented in colorectal, breast, and prostate cancer cell lines.
In cancer cells with already-damaged mitochondrial networks and suppressed PINK1/Parkin signalling, Urolithin A’s mitophagy drive may not rescue the cell.
It may instead accelerate cell death, because the cell cannot complete the quality-control process that Urolithin A initiates.
The p62 dimension is especially important here.
Urolithin A uses p62-Ser403 as the lysophagy adaptor in healthy cells.
That is different from the cancer-promoting p62-Ser349 accumulation that HCQ can drive in tumour cells.
With AKBA suppressing the NF-κB p65 arm of p62 signalling, the strategy’s three p62-related agents — HCQ, Urolithin A, and AKBA — are not competing for the same target in the same way.
They are acting through different phosphorylation states and different functional consequences.
That is one of the most important host-protection questions in the whole strategy.
Visit our Urolithin A in Oncology hub
EGCG 80% — glutamine pressure and signalling reinforcement
EGCG 80% — glutaminolysis inhibitor and autophagy modulator
Epigallocatechin gallate, or EGCG, appears in this strategy in two places.
It is used as a standalone 80% standardised extract.
It is also included inside Glutamine Inhibifour.
Its main role here is glutamine-pathway pressure.
EGCG targets glutamine metabolism at the GLUD1 and GLUD2 enzyme level.
It inhibits the conversion of glutamate to α-ketoglutarate.
That is a rate-limiting step in the glutaminolysis pathway.
By suppressing GLUD1 and GLUD2, EGCG reduces the cancer cell’s ability to use glutamine as a TCA cycle substrate and biosynthetic precursor.
That impairs proliferation in neuroblastoma, glioma, and colorectal cancer cells.
EGCG also modulates autophagy through PI3K/Akt/mTOR suppression.
That adds to the upstream autophagy-initiation blockade already maintained by AKBA, berberine, and curcumin.
At the same time, EGCG suppresses HIF‑1α, NF‑κB, and VEGF expression.
That gives it a second role.
It is not only pressing on glutamine metabolism.
It is also reinforcing the broader anti-survival signalling platform already established across the strategy.
The fact that EGCG is present both as a standalone extract and inside Glutamine Inhibifour reflects the strategic importance placed on glutamine pathway disruption.
Visit our EGCG in Oncology hub.
Layer four: the metabolic siege
Cancer cells do not rely on autophagy alone.
They also lean on glycolysis and glutaminolysis.
If autophagy is blocked, those other fuel routes become more important.
That is why the strategy tries to press on all three.
Glutamine Inhibifour — four agents, one pathway
Glutamine is the most abundant circulating amino acid.
For many cancer cells, it is also a major fuel source and a major nitrogen source.
This blend is designed to disrupt that pathway at several different points at once.
Each of its four compounds contributes something distinct.
Ursolic acid
Ursolic acid is the keystone compound in this blend.
Its most important role here is direct inhibition of STAT3 activation.
That matters because glutamine does more than feed the cell.
It can also activate STAT3 and drive proliferation independently of its metabolic role.
Ursolic acid blocks STAT3 phosphorylation at Y705 by suppressing c-Src, JAK1, JAK2, and ERK1/2.
That cuts the glutamine-to-proliferation signalling axis.
Ursolic acid also suppresses PI3K/Akt/mTOR signalling.
It promotes mitochondria-mediated apoptosis in breast cancer cells.
It reverses cisplatin resistance in ovarian cancer stem cells.
It also inhibits metastasis by suppressing MMP‑2 and MMP‑9 expression.
Caffeic acid
Caffeic acid adds both metabolic and inflammatory pressure.
It is a phenylpropanoid found in propolis and plant foods, and it is unrelated to caffeine.
In this framework, it helps reprogram cancer cell glucose handling through the TCA cycle via oxidative decarboxylation.
That increases oxidative stress in cancer cells and sensitises them to metabolic disruption.
Caffeic acid also suppresses HIF‑1α through PDK1 modulation.
It inhibits the Akt/mTOR/SREBP1 pathway.
In breast cancer cells, it has been shown to reverse doxorubicin resistance.
It also synergises with metformin in cervical cancer models.
Its suppression of TNF‑α, IL‑1β, and IL‑6 adds an anti-inflammatory effect that becomes more relevant again in the senescence discussion in Part Three.
Hesperidin
Hesperidin is a support compound rather than the lead driver in this blend.
It contributes documented mTOR inhibition, NF‑κB suppression, and interference with glucose and glutamine metabolic reprogramming in cancer cells.
That means it supports both the anti-inflammatory platform and the broader metabolic disruption strategy.
EGCG
The EGCG fraction adds more pressure on the glutamine pathway.
As described above, it targets GLUD1 and GLUD2 and reduces the glutamate-to-α-ketoglutarate conversion step.
At the same time, it reinforces mTOR, HIF‑1α, and NF‑κB suppression already established elsewhere in the strategy.
Why STAT3 matters here
This is one of the most important ideas in the whole glutamine layer.
Glutamine is not only a fuel.
It is also a signal.
Research has shown that glutamine can activate STAT3 independently of its metabolic role.
That means restricting glutamine substrate alone may not be enough.
The glutamine-STAT3 signalling axis also has to be blocked.
That is why ursolic acid is so important in this blend.
It blocks the signalling arm, not just the fuel arm.
Glycolysis Inhibithree — a triple strike on the Warburg pathway
When autophagy is blocked and glutamine pressure rises, glycolysis becomes the next major escape route.
This blend is designed to make that escape route much harder to use.
It targets three different points in glycolysis.
Phlorizin
Phlorizin targets glucose entry.
It inhibits sodium-glucose cotransporters SGLT1 and SGLT2.
These are among the transport systems cancer cells use to import glucose from the surrounding environment.
Without adequate glucose import, glycolytic flux is starved at the entry point.
This is entry-point pressure.
Tanshinone IIA
Tanshinone IIA targets glycolysis more deeply.
It inhibits hexokinase 2, the first and rate-limiting enzyme of glycolysis.
It also suppresses SIX1-driven expression of HK2, PKM2, and LDHA in NSCLC cells.
That means it is not only hitting one enzyme.
It is suppressing a broader glycolytic programme.
Beyond glycolysis, Tanshinone IIA also inhibits the PI3K/Akt/mTOR axis through EGFR, IGFR, and VEGFR suppression.
It induces ferroptosis in gastric cancer via the p53/SLC7A11 pathway.
It also promotes apoptosis across multiple tumour types.
Its ferroptosis relevance is important because it adds a distinct killing mechanism that the other strategy compounds do not cover.
Shikonin
Shikonin is the most selective glycolytic compound in this layer.
Its main relevance is tumour-specific PKM2 inhibition.
PKM2 is much more strongly linked to cancer cells than PKM1.
It controls the final rate-limiting step of glycolysis, converting phosphoenolpyruvate to pyruvate.
Because shikonin inhibits PKM2 more selectively, it may offer a degree of cancer-cell selectivity that broader glycolytic blockers do not.
Shikonin also inhibits STAT3 signalling.
That creates useful convergence with ursolic acid in the glutaminolysis layer.
Why the glycolysis layer matters
These three compounds do different jobs.
Phlorizin restricts glucose entry.
Tanshinone IIA presses on early glycolytic commitment.
Shikonin presses on the final PKM2 step.
Together, they block the beginning, middle, and end of the glycolytic pathway.
That makes metabolic compensation through glycolysis much harder.
A cancer cell that has autophagy blocked, glutamine signalling suppressed, and glycolysis obstructed at three points has very few mainstream energy routes left.
The strategy as a system — why each layer depends on the others
This strategy is built around convergence.
The goal is to close several escape routes at once.
It is not one “hero” compound.
It is coordinated pressure across recycling, fuel use, and survival signalling.
Pressure point | Main compounds | Intended effect | Why it matters |
|---|---|---|---|
Upstream autophagy initiation | AKBA, berberine, curcumin, EGCG | Press on autophagy signalling before flux completes | Makes recycling harder to start |
Autophagy completion | HCQ | Blocks autophagosome-lysosome fusion | Cargo accumulates instead of clearing |
NF‑κB survival signalling | AKBA, curcumin, berberine, caffeic acid | Suppresses a major stress-survival pathway | Cuts a common escape route |
Hypoxia and angiogenesis | AKBA, curcumin, berberine, EGCG, Tanshinone IIA | Presses on HIF‑1α and VEGF-linked adaptation | Reduces low-oxygen survival and new vessel support |
Glycolysis | Phlorizin, Tanshinone IIA, shikonin, berberine | Restricts glucose entry and glycolytic throughput | Reduces fast fuel access |
Glutamine fuel and STAT3 signalling | EGCG, ursolic acid, caffeic acid, hesperidin, curcumin | Restricts glutamine use and glutamine-linked signalling | Cuts both fuel and growth signalling |
Stemness and resistance | Berberine, ursolic acid, EGCG, curcumin | Presses on stem-like survival and treatment adaptation | Makes resistance harder to maintain |
Host mitochondrial protection | Urolithin A | Supports mitochondrial quality control in healthy tissue | Helps protect the host while pressure rises |
p62 escape governance | AKBA with HCQ | Limits NF‑κB activation from HCQ-related cargo buildup | Helps stop p62 from becoming a survival advantage |
The intended result is simple.
The cancer cell loses recycling.
It loses glycolytic flexibility.
It loses glutamine fuel and glutamine-linked signalling.
It loses hypoxic adaptation.
It loses inflammatory survival signalling.
It loses angiogenic support.
That does not guarantee death in every tumour.
But it does leave the cell with far fewer exits.
What Part Three addresses next
Part Two is the mechanistic map.
Part Three has to deal with the host.
That is the harder problem.
HCQ accumulates in lysosomes throughout the body.
That includes retina, cardiac muscle, and skeletal muscle.
Its long half-life means that early initiation can translate into months of cumulative exposure in healthy tissue.
Berberine, although generally well tolerated, has cytochrome P450 interaction relevance.
EGCG at higher doses has hepatic considerations.
And the question of whether Urolithin A and HCQ truly coexist without reducing each other’s usefulness needs a proper answer.
Part Three addresses those issues directly.
It looks at what HCQ does to healthy cell mitochondria at the molecular level.
It maps the lysosomal sub-targets that help explain why Urolithin A and HCQ are not acting at the same exact site.
It addresses the p62 phosphorylation-state strategy that allows HCQ, Urolithin A, and AKBA to work in parallel without simply cancelling each other out.
It also covers the monitoring framework needed to make this kind of protocol clinically actionable in a supervised setting.
That includes phospho-p62, LC3-II, LAMP1, and cardiac review.
Part Three also returns to the dietary foundation.
That matters for p62 re-synthesis, mitochondrial protection, and glycaemic stability throughout the protocol.
And finally, it introduces the senolytic second strike.
That is the strategy for clearing therapy-induced senescent cancer cells that escape the autophagy blockade by switching survival mode.
Continue with Protecting the Host — Part Three.
For the senolytic follow-up pathway that sits beside this strategy, also see Senescence — The Second Escape Route.
Key references
Anti-cancer properties of boswellic acids: mechanism of action as anti-inflammatory, anti-angiogenic, cytotoxic and chemo-sensitising agents
https://www.frontiersin.org/journals/pharmacology/articles/10.3389/fphar.2023.1187181/fullAcetyl-11-Keto-β-Boswellic Acid Exerts the Anti-Cancer Effects via Autophagy Suppression
https://pmc.ncbi.nlm.nih.gov/articles/PMC6986255/3-O-Acetyl-11-keto-β-boswellic acid ameliorated aberrant metabolic reprogramming and suppressed glioblastoma
https://pmc.ncbi.nlm.nih.gov/articles/PMC7016292/Chloroquine inhibits autophagic flux by decreasing autophagosome-lysosome fusion
https://pmc.ncbi.nlm.nih.gov/articles/PMC6103682/Berberine induces autophagy in glioblastoma by targeting the AMPK/mTOR/ULK1 pathway
https://pmc.ncbi.nlm.nih.gov/articles/PMC5341849/Berberine modulates ovarian cancer autophagy and glycolysis via LINC00123/P65/MAPK10
https://pubmed.ncbi.nlm.nih.gov/39395322/The Anti-Cancer Mechanisms of Berberine: A Review
https://pmc.ncbi.nlm.nih.gov/articles/PMC6996556/Regulation of Cell Signaling Pathways by Berberine in Cancer
https://pmc.ncbi.nlm.nih.gov/articles/PMC6521278/Pharmacological Effects of Urolithin A and Its Role in Muscle Health
https://pmc.ncbi.nlm.nih.gov/articles/PMC10609777/Urolithin A promotes p62-dependent lysophagy to prevent acute liver injury
https://pubmed.ncbi.nlm.nih.gov/38890703/Targeting glutamine metabolism as a therapeutic strategy for cancer
https://www.nature.com/articles/s12276-023-00971-9Glutamine activates STAT3 to control cancer cell proliferation independently of its metabolism
https://pmc.ncbi.nlm.nih.gov/articles/PMC5245769/Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation in multiple myeloma
https://pubmed.ncbi.nlm.nih.gov/17855663/Ursolic Acid Inhibits Breast Cancer Metastasis by Suppressing PI3K/Akt/mTOR
https://www.frontiersin.org/journals/oncology/articles/10.3389/fonc.2021.745584/fullCaffeic Acid Expands Anti-Tumor Effect of Metformin in Human Cervical Carcinoma
https://pmc.ncbi.nlm.nih.gov/articles/PMC5343995/Caffeic acid phenethyl ester reverses doxorubicin resistance in breast cancer via Akt/mTOR/SREBP1
https://pubmed.ncbi.nlm.nih.gov/36960852/The mechanisms of tanshinone in the treatment of tumors
https://pmc.ncbi.nlm.nih.gov/articles/PMC10642231/Tanshinone IIA inhibits cell growth by suppressing SIX1-induced aerobic glycolysis in NSCLC
https://pubmed.ncbi.nlm.nih.gov/35527783/Tanshinone IIA inhibits glucose metabolism leading to apoptosis in cervical cancer
https://pmc.ncbi.nlm.nih.gov/articles/PMC6775814/Shikonin and its analogs inhibit cancer cell glycolysis by targeting tumour PKM2
https://pubmed.ncbi.nlm.nih.gov/21516121/Shikonin Inhibits Tumor Growth of ESCC by suppressing PKM2
https://www.jcancer.org/v12p4830.htmExploiting the Achilles heel of cancer: disrupting glutamine metabolism
https://www.frontiersin.org/journals/pharmacology/articles/10.3389/fphar.2024.1345522/fullInhibition of glutaminolysis in combination with other therapies to curb cancer
https://pmc.ncbi.nlm.nih.gov/articles/PMC8570367/Natural compounds modulate autophagy with potential implication in cancer treatment
https://pmc.ncbi.nlm.nih.gov/articles/PMC8343111/Berberine: An Important Emphasis on Its Anticancer Effects through Modulation of Various Cell Signalling Pathways
https://pmc.ncbi.nlm.nih.gov/articles/PMC9505063/
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