Galloflavin / ROS Cancer Research Results

Gallo, Galloflavin: Click to Expand ⟱

Features:

Galloflavin is a flavonoid compound found in certain plants, such as the Galphimia gracilis. Studies have demonstrated that galloflavin can inhibit the growth of cancer cells and induce apoptosis (cell death) in various types of cancer, including breast, lung, and colon cancer. Galloflavin's anti-cancer effects are thought to be due to its ability to modulate various cellular signaling pathways, including the PI3K/Akt and NF-κB pathways, which are involved in cell survival and proliferation. Additionally, galloflavin has been shown to have antioxidant and anti-inflammatory properties, which may also contribute to its anti-cancer effects.

Galloflavin has been reported to be a lactate dehydrogenase (LDH) inhibitor. LDH is an enzyme that plays a crucial role in the metabolism of cancer cells, particularly in the process of glycolysis, which is the breakdown of glucose to produce energy.
Galloflavin's LDH inhibitory activity has been demonstrated in various studies, which have shown that it can inhibit LDH activity in cancer cells, leading to a decrease in lactate production and an increase in the production of reactive oxygen species (ROS). The increase in ROS can lead to cell death, making galloflavin a potential therapeutic agent for the treatment of cancer.

Galloflavin is unusually clean mechanistically:
-LDH-A inhibition is the primary molecular target
-Everything else (↓ lactate, NAD⁺ stress, ROS, mitochondrial dependence) is downstream
-Apoptosis and tumor suppression are consequences, not drivers
This makes galloflavin one of the best-defined Warburg-effect inhibitors.

Not use if antitumor effect extends to in vivo?

Galloflavin — a synthetic polyphenolic small molecule and non-substrate-competitive inhibitor of human lactate dehydrogenase A and B. It is classified as an experimental metabolic anticancer agent and Warburg-effect inhibitor; the standard abbreviation is GF. Galloflavin, CAS 568-80-9, was originally characterized as an oxidation-derived dimeric product related to gallic acid rather than as a clinically established plant flavonoid. It remains a research compound with no approved therapeutic indication.

Primary mechanisms (ranked):

Direct inhibition of LDH-A and LDH-B, preferentially through binding to the free enzyme.
Suppression of pyruvate-to-lactate conversion, aerobic glycolysis, lactate secretion and glycolysis-dependent ATP production.
Disruption of NADH/NAD⁺ redox recycling and induction of metabolic stress in highly glycolytic cancer cells.
Induction of apoptosis through context-dependent mitochondrial, caspase and survival-signalling changes.
Suppression of MYC-associated metabolic and proliferative signalling in susceptible cancer models.
Reduction of inflammation-associated epithelial–mesenchymal transition, migration and invasive behaviour through decreased lactate production.
Inhibition of noncanonical LDH-A binding to single-stranded DNA and suppression of cellular RNA synthesis.
Context-dependent elevation of ROS, mitochondrial DNA damage and oxidative stress downstream of metabolic disruption.
Context-dependent inhibition of NLRP3-associated inflammatory and malignant signalling in colorectal cancer models.

Bioavailability / PK relevance: No validated human pharmacokinetic, oral-bioavailability or therapeutic-exposure data are available. Galloflavin has been described as having poor physicochemical and drug-development properties, prompting development of galloflavin mimetics and alternative LDH inhibitors. Systemic exposure, metabolic stability, tissue distribution, protein binding and dose-limiting toxicity remain insufficiently characterized.

In-vitro vs systemic exposure relevance: Most anticancer studies use approximately 10–100 µM galloflavin, commonly around 25–50 µM over 24–72 hours. Whether these concentrations can be safely and continuously achieved in human tumors is unknown. Consequently, direct translation of cell-culture efficacy to oral or systemic treatment is not currently justified.

Clinical evidence status: Preclinical only. Evidence consists predominantly of enzyme assays and cultured cancer-cell studies, including breast, lymphoma, endometrial, pancreatic and colorectal models. Some animal or mechanistic studies may exist, but there is no established human cancer trial, approved formulation, clinical dose, demonstrated response rate or regulatory authorization for galloflavin.

Safety and interpretation: Galloflavin inhibits both LDH-A and LDH-B rather than being strictly LDH-A selective. Because LDH is required in normal erythrocytes, skeletal muscle, heart and other tissues during high glycolytic demand, systemic LDH inhibition could produce on-target toxicity. Normal-cell selectivity, hemolytic risk, exercise intolerance, hepatic effects, drug interactions and chronic safety have not been adequately established.

Galloflavin Mechanistic Profile

Rank	Pathway / Axis	Cancer Cells	Normal Cells	TSF	Primary Effect	Notes / Interpretation
1	Lactate dehydrogenase A and B	↓ LDH-A and LDH-B activity	↓ LDH activity expected	P	Direct metabolic enzyme inhibition	Galloflavin preferentially binds the free enzymes without directly competing with pyruvate or NADH. Reported inhibition constants are in the low micromolar range, with greater potency toward LDH-A than LDH-B.
2	Pyruvate to lactate conversion	↓ lactate production ↑ pyruvate	↓ lactate production possible	P–R	Warburg-effect suppression	The most direct cellular consequence of LDH inhibition. Effects are expected to be strongest in tumors that depend heavily on aerobic glycolysis.
3	Glycolysis and ATP production	↓ glycolytic flux ↓ ATP	↓ glycolytic reserve possible	R	Cellular energy stress	Galloflavin may spare mitochondrial respiration initially, but cells unable to compensate through oxidative phosphorylation are particularly vulnerable.
4	NADH and NAD⁺ redox balance	↓ NAD⁺ regeneration ↑ reductive stress	Potential impairment during anaerobic demand	R	Redox and biosynthetic disruption	Reduced LDH-mediated NAD⁺ recycling can constrain glycolysis and indirectly disturb multiple NAD-dependent reactions.
5	MYC metabolic signalling	↓ MYC ↓ proliferation	Insufficient evidence	G	Metabolic and transcriptional growth suppression	Demonstrated particularly in Burkitt lymphoma cells; the direction and magnitude are model-dependent.
6	Mitochondrial apoptosis	↓ BCL-2 ↓ MCL-1 ↑ cleaved caspase-3 ↑ apoptosis	Insufficient selectivity data	G	Programmed cell death	Likely a downstream consequence of prolonged metabolic stress rather than a primary direct molecular target.
7	Reactive oxygen species and mitochondrial damage	↑ ROS ↑ mitochondrial DNA damage	Unknown potential ↑ oxidative injury	R–G	Secondary oxidative cytotoxicity	ROS elevation is not consistently demonstrated across all models and should be considered secondary and context-dependent.
8	Cell-cycle regulation	↑ cell-cycle arrest	Insufficient evidence	G	Reduced proliferation	G2 or other checkpoint changes have been reported depending on the cancer-cell model and exposure duration.
9	Epithelial–mesenchymal transition and migration	↑ E-cadherin ↓ Slug ↓ migration	Insufficient evidence	G	Reduced invasive phenotype	May result partly from reduced extracellular lactate and reversal of inflammation-driven metabolic reprogramming.
10	NLRP3 inflammatory signalling	↓ NLRP3-associated activity ↓ malignant behaviour	Potential ↓ inflammation insufficient evidence	G	Contextual anti-inflammatory and antitumor effect	Reported in colorectal cancer models. It is uncertain whether NLRP3 is directly bound by galloflavin or altered downstream of metabolic effects.
11	LDH-A single-stranded DNA binding and RNA synthesis	↓ LDH-A DNA binding ↓ RNA synthesis	↓ RNA synthesis possible	R–G	Noncanonical transcriptional inhibition	Mechanistically distinct from inhibition of lactate production, but its contribution to selective tumor killing remains uncertain.
12	Chemosensitization and combination metabolic therapy	↑ response to metformin and selected metabolic inhibitors (model-dependent)	Combination toxicity unknown	G	Enhanced metabolic collapse	Combination activity is preclinical and may depend on hypoxia, mitochondrial reserve, glucose availability and tumor genotype.
13	Clinical Translation Constraint	Effective concentrations commonly in the micromolar range	Normal-tissue LDH inhibition and therapeutic window unresolved	G	Limits clinical deployment	Poorly defined PK, formulation limitations, lack of human safety data, dual LDH-A and LDH-B inhibition, metabolic heterogeneity and absence of clinical trials prevent therapeutic interpretation.

P: 0–30 min R: 30 min–3 hr G: >3 hr

ROS, Reactive Oxygen Species: Click to Expand ⟱

Source: HalifaxProj (inhibit)

Type:

Reactive oxygen species (ROS) are highly reactive molecules that contain oxygen and can lead to oxidative stress in cells. They play a dual role in cancer biology, acting as both promoters and suppressors of cancer.
ROS can cause oxidative damage to DNA, leading to mutations that may contribute to cancer initiation and progression. So normally you want to inhibit ROS to prevent cell mutations.
However excessive ROS can induce apoptosis (programmed cell death) in cancer cells, potentially limiting tumor growth. Chemotherapy typically raises ROS.
-mitochondria is the main source of reactive oxygen species (ROS) (and the ETC is heavily related)
ROS Homeostasis in Cancer Cells and Its Potential as a Therapeutic Target

"Reactive oxygen species (ROS) are two electron reduction products of oxygen, including superoxide anion, hydrogen peroxide, hydroxyl radical, lipid peroxides, protein peroxides and peroxides formed in nucleic acids 1. They are maintained in a dynamic balance by a series of reduction-oxidation (redox) reactions in biological systems and act as signaling molecules to drive cellular regulatory pathways."
"During different stages of cancer formation, abnormal ROS levels play paradoxical roles in cell growth and death 8. A physiological concentration of ROS that maintained in equilibrium is necessary for normal cell survival. Ectopic ROS accumulation promotes cell proliferation and consequently induces malignant transformation of normal cells by initiating pathological conversion of physiological signaling networks. Excessive ROS levels lead to cell death by damaging cellular components, including proteins, lipid bilayers, and chromosomes. Therefore, both scavenging abnormally elevated ROS to prevent early neoplasia and facilitating ROS production to specifically kill cancer cells are promising anticancer therapeutic strategies, in spite of their contradictoriness and complexity."
"ROS are the collection of derivatives of molecular oxygen that occur in biology, which can be categorized into two types, free radicals and non-radical species. The non-radical species are hydrogen peroxide (H 2O 2 ), organic hydroperoxides (ROOH), singlet molecular oxygen ( 1 O 2 ), electronically excited carbonyl, ozone (O3 ), hypochlorous acid (HOCl, and hypobromous acid HOBr). Free radical species are super-oxide anion radical (O 2•−), hydroxyl radical (•OH), peroxyl radical (ROO•) and alkoxyl radical (RO•) [130]. Any imbalance of ROS can lead to adverse effects. H2 O 2 and O 2 •− are the main redox signalling agents. The cellular concentration of H2 O 2 is about 10−8 M, which is almost a thousand times more than that of O2 •−".
"Radicals are molecules with an odd number of electrons in the outer shell [393,394]. A pair of radicals can be formed by breaking a chemical bond or electron transfer between two molecules."

Recent investigations have documented that polyphenols with good antioxidant activity may exhibit pro-oxidant activity in the presence of copper ions, which can induce apoptosis in various cancer cell lines but not in normal cells. "We have shown that such cell growth inhibition by polyphenols in cancer cells is reversed by copper-specific sequestering agent neocuproine to a significant extent whereas iron and zinc chelators are relatively ineffective, thus confirming the role of endogenous copper in the cytotoxic action of polyphenols against cancer cells. Therefore, this mechanism of mobilization of endogenous copper." > Ions could be one of the important mechanisms for the cytotoxic action of plant polyphenols against cancer cells and is possibly a common mechanism for all plant polyphenols. In fact, similar results obtained with four different polyphenolic compounds in this study, namely apigenin, luteolin, EGCG, and resveratrol, strengthen this idea.
Interestingly, the normal breast epithelial MCF10A cells have earlier been shown to possess no detectable copper as opposed to breast cancer cells [24], which may explain their resistance to polyphenols apigenin- and luteolin-induced growth inhibition as observed here (Fig. 1). We have earlier proposed [25] that this preferential cytotoxicity of plant polyphenols toward cancer cells is explained by the observation made several years earlier, which showed that copper levels in cancer cells are significantly elevated in various malignancies. Thus, because of higher intracellular copper levels in cancer cells, it may be predicted that the cytotoxic concentrations of polyphenols required would be lower in these cells as compared to normal cells."

Majority of ROS are produced as a by-product of oxidative phosphorylation, high levels of ROS are detected in almost all cancers.
-It is well established that during ER stress, cytosolic calcium released from the ER is taken up by the mitochondrion to stimulate ROS overgeneration and the release of cytochrome c, both of which lead to apoptosis.

Note: Products that may raise ROS can be found using this database, by:
Filtering on the target of ROS, and selecting the Effect Direction of ↑

Targets to raise ROS (to kill cancer cells):
• NADPH oxidases (NOX): NOX enzymes are involved in the production of ROS.
    -Targeting NOX enzymes can increase ROS levels and induce cancer cell death.
    -eNOX2 inhibition leads to a high NADH/NAD⁺ ratio which can lead to increased ROS
• Mitochondrial complex I: Inhibiting can increase ROS production
• P53: Activating p53 can increase ROS levels(by inducing the expression of pro-oxidant genes)
• Nrf2 inhibition: regulates the expression of antioxidant genes. Inhibiting Nrf2 can increase ROS levels
• Glutathione (GSH): an antioxidant. Depleting GSH can increase ROS levels
• Catalase: Catalase converts H2O2 into H2O+O. Inhibiting catalase can increase ROS levels
• SOD1: converts superoxide into hydrogen peroxide. Inhibiting SOD1 can increase ROS levels
• PI3K/AKT pathway: regulates cell survival and metabolism. Inhibiting can increase ROS levels
• HIF-1α inhibition: regulates genes involved in metabolism and angiogenesis. Inhibiting HIF-1α can increase ROS
• Glycolysis: Inhibiting glycolysis can increase ROS levels • Fatty acid oxidation: Cancer cells often rely on fatty acid oxidation for energy production.
-Inhibiting fatty acid oxidation can increase ROS levels
• ER stress: Endoplasmic reticulum (ER) stress can increase ROS levels
• Autophagy: process by which cells recycle damaged organelles and proteins.
-Inhibiting autophagy can increase ROS levels and induce cancer cell death.
• KEAP1/Nrf2 pathway: regulates the expression of antioxidant genes.
    -Inhibiting KEAP1 or activating Nrf2 can increase ROS levels and induce cancer cell death.
• DJ-1: regulates the expression of antioxidant genes. Inhibiting DJ-1 can increase ROS levels
• PARK2: regulates the expression of antioxidant genes. Inhibiting PARK2 can increase ROS levels
• SIRT1 inhibition:regulates the expression of antioxidant genes. Inhibiting SIRT1 can increase ROS levels
• AMPK activation: regulates energy metabolism and can increase ROS levels when activated.
• mTOR inhibition: regulates cell growth and metabolism. Inhibiting mTOR can increase ROS levels
• HSP90 inhibition: regulates protein folding and can increase ROS levels when inhibited.
• Proteasome: degrades damaged proteins. Inhibiting the proteasome can increase ROS levels
• Lipid peroxidation: a process by which lipids are oxidized, leading to the production of ROS.
    -Increasing lipid peroxidation can increase ROS levels
• Ferroptosis: form of cell death that is regulated by iron and lipid peroxidation.
    -Increasing ferroptosis can increase ROS levels
• Mitochondrial permeability transition pore (mPTP): regulates mitochondrial permeability.
    -Opening the mPTP can increase ROS levels
• BCL-2 family proteins: regulate apoptosis and can increase ROS levels when inhibited.
• Caspase-independent cell death: a form of cell death that is regulated by ROS.
    -Increasing caspase-independent cell death can increase ROS levels
• DNA damage response: regulates the repair of DNA damage. Increasing DNA damage can increase ROS
• Epigenetic regulation: process by which gene expression is regulated.
    -Increasing epigenetic regulation can increase ROS levels

-PKM2, but not PKM1, can be inhibited by direct oxidation of cysteine 358 as an adaptive response to increased intracellular reactive oxygen species (ROS)

ProOxidant Strategy:(inhibit the Mevalonate Pathway (likely will also inhibit GPx)
-HydroxyCitrate (HCA) found as supplement online and typically used in a dose of about 1.5g/day or more
-Atorvastatin typically 40-80mg/day, -Dipyridamole typically 200mg 2x/day Combined effect research
-Lycopene typically 100mg/day range (note debatable as it mainly lowers NRF2)

Dual Role of Reactive Oxygen Species and their Application in Cancer Therapy

ROS-Inducing Interventions in Cancer — Canonical + Mechanistic Reference
-generated from AI and Cancer database
ROS rating:  +++ strong | ++ moderate | + weak | ± mixed | 0 none
NRF2:        ↓ suppressed | ↑ activated | ± mixed | 0 none
Conditions:  [D] dose  [Fe] metal  [M] metabolic  [O₂] oxygen
             [L] light [F] formulation [T] tumor-type [C] combination


Item  ROS↑  NRF2  Condition  Mechanism Class  Remarks  

ROS">Piperlongumine
+++  ↓  [D][T]  ROS-dominant
Selective <span class="wphighlight">ROS</span> stressor, Prevents compensatory upregulation of NRF2, ie GSH↓



ROS">Shikonin
+++ ↓/± [D][T] ROS-dominant
<span class="wphighlight">ROS</span> + glycolysis + GPX4 inhibition



ROS">Vitamin K3 (menadione)
+++ ↓ [D] ROS-dominant
Quinone redox cycler; toxicity limits use



ROS">Copper (ionic / nano)
+++ ↓ [Fe][F] ROS-dominant
Fenton-type redox chemistry



ROS">Sodium Selenite
+++ ↓ [D] ROS-dominant
Pro-oxidant, depletes GSH



ROS">Juglone
+++ ↓ [D] ROS-dominant
Strong quinone <span class="wphighlight">ROS</span> chemistry



ROS">Auranofin
+++ ↓ [D] ROS-dominant
TrxR inhibition → redox collapse



ROS">Photodynamic Therapy (PDT)
+++ 0 [L][O₂] ROS-dominant
Singlet oxygen is core cytotoxic mechanism



ROS">Radiotherapy / Radiation
+++ 0 [O₂] ROS-dominant
DNA damage largely via <span class="wphighlight">ROS</span>



ROS">Doxorubicin
+++ ↓ [D] ROS-dominant
Chemo; redox cycling + mitochondrial <span class="wphighlight">ROS</span>



ROS">Cisplatin
++ ↓ [D][T] ROS-dominant
<span class="wphighlight">ROS</span> contributes to DNA/protein damage



ROS">Salinomycin
++ ↓ [D][T] ROS-dominant
<span class="wphighlight">ROS</span>-mediated CSC toxicity



ROS">Artemisinin / DHA
++ ↓ [Fe][T] ROS-dominant
Iron-activated radical generation



ROS">Sulfasalazine
++ ↓ [C][T] ROS-dominant
Ferroptosis; xCT inhibition → lipid <span class="wphighlight">ROS</span>



ROS">FMD / fasting
++ ↓ [M][C][O₂] ROS-dominant
Metabolic stress → mitochondrial <span class="wphighlight">ROS</span>



ROS">Vitamin C (pharmacologic)
++ ↓ [Fe][D] ROS-dominant
Extracellular H₂O₂ at high dose



ROS">Silver nanoparticles
++ ± [F][D] ROS-dominant
<span class="wphighlight">ROS</span> common; selectivity unreliable



ROS">Gambogic acid
++ ↓ [D][T] ROS-dominant
<span class="wphighlight">ROS</span>-mediated apoptosis



ROS">Parthenolide
++ ↓ [D][T] ROS-dominant
<span class="wphighlight">ROS</span> + NF-κB suppression



ROS">Plumbagin
++ ↓ [D] ROS-dominant
Quinone <span class="wphighlight">ROS</span> driver



ROS">Allicin
++ ↓ [D] ROS-dominant
Thiol-reactive oxidative stress



ROS">Ashwagandha (Withaferin A)
++ ↓ [D][T] ROS-dominant
<span class="wphighlight">ROS</span>-mediated apoptosis



ROS">Berberine
++ ↓ [D][M] ROS-dominant
Mitochondrial <span class="wphighlight">ROS</span> induction



ROS">PEITC
++ ↓ [D][C] ROS-dominant
GSH depletion + <span class="wphighlight">ROS</span>



ROS">Methionine restriction
+ ↓ [M][C][T] ROS-secondary
Redox vulnerability increased; <span class="wphighlight">ROS</span> indirect



ROS">DCA
+ ± [M][T] ROS-secondary
<span class="wphighlight">ROS</span> via forced OXPHOS



ROS">Capsaicin
+ ± [D][T] ROS-secondary
Ca²⁺ stress → <span class="wphighlight">ROS</span>



ROS">Galloflavin
+ 0 [D] ROS-secondary
<span class="wphighlight">ROS</span> not primary driver



ROS">Piperine
+ ± [D][F] ROS-secondary
Weak <span class="wphighlight">ROS</span> induction



ROS">Propyl gallate
+ ↓ [D] ROS-secondary
Pro-oxidant at high dose



ROS">Scoulerine
+ ? [D][T] ROS-secondary
Sparse <span class="wphighlight">ROS</span> data



ROS">Thymoquinone
± ± [D][T] Dual redox
Antioxidant ↔ pro-oxidant switch



ROS">Emodin
± ± [D][T] Dual redox
Not cancer-exclusive



ROS">Alpha-lipoic acid (ALA)
± ↑ [D][M] NRF2-dominant
Antioxidant at low dose



ROS">Curcumin
± ↑/↓ [D][F] NRF2-dominant
Hormetic redox behavior



ROS">EGCG
± ↑/↓ [D][O₂] NRF2-dominant
Auto-oxidation artifacts common



ROS">Quercetin
± ↑/↓ [D][Fe] NRF2-dominant
GSH-dependent cycling



ROS">Resveratrol
± ↑ [D][M] NRF2-dominant
<span class="wphighlight">ROS</span> only at high dose



ROS">Sulforaphane
± ↑↑ [D] NRF2-dominant
Strong NRF2 activator



ROS">Lycopene
0 ↑ — Antioxidant
Consistently antioxidant



ROS">Rosmarinic acid
0 ↑ — Antioxidant
Primarily antioxidant



ROS">Citrate
0 0 — Neutral
Metabolic; not a <span class="wphighlight">ROS</span> agent

Scientific Papers found: Click to Expand⟱

935-

Gallo,

Galloflavin, a new lactate dehydrogenase inhibitor, induces the death of human breast cancer cells with different glycolytic attitude by affecting distinct signaling pathways

in-vitro,

BC,

MCF7

in-vitro,

BC,

MDA-MB-231

LDH↓, ROS↑, TumCP↓, Glycolysis↓, ATP↓, ER-α36↓, Apoptosis?,

5205-

Gallo,

Evaluation of the anti-tumor effects of lactate dehydrogenase inhibitor galloflavin in endometrial cancer cells

in-vitro,

Endo,

ISH

25 uM and 43 uM after 72 h

LDH↓, TumCG↓, LDHA↓, Apoptosis↑, cl‑Casp3↑, Mcl-1↓, Bcl-2↓, TumCCA↑, ROS↑, mt-DNAdam↑, GlucoseCon↓, ATP↓, PDH↑, Pyruv↑, Glycolysis↓, TCA↑, cMyc↓, E-cadherin↑, Slug↓,

Showing Research Papers: 1 to 2 of 2

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 2

Pathway results for Effect on Cancer / Diseased Cells:

Clinical Biomarkers(tgid=22) ⓘ

LDH↓, 2,
Total Targets: 23

Pathway results for Effect on Normal Cells:

Total Targets: 0

Scientific Paper Hit Count for: ROS, Reactive Oxygen Species

Query results interpretion may depend on "conditions" listed in the research papers.
Such Conditions may include : 
  -low or high Dose
  -format for product, such as nano of lipid formations
  -different cell line effects
  -synergies with other products 
  -if effect was for normal or cancerous cells

Filter Conditions: Pro/AntiFlg:%  IllCat:%  CanType:%  Cells:%  prod#:177  Target#:275  State#:%  Dir#:%
  wNotes=0  sortOrder:rid,rpid

Galloflavin / ROS Cancer Research Results

Galloflavin Mechanistic Profile

Pathway results for Effect on Cancer / Diseased Cells:

Redox & Oxidative Stress(tgid=1) ⓘ

Mitochondria & Bioenergetics(tgid=3) ⓘ

Core Metabolism/Glycolysis(tgid=4) ⓘ

Cell Death(tgid=5) ⓘ

DNA Damage & Repair(tgid=10) ⓘ

Cell Cycle & Senescence(tgid=11) ⓘ

Proliferation, Differentiation & Cell State(tgid=12) ⓘ

Migration(tgid=13) ⓘ

Clinical Biomarkers(tgid=22) ⓘ

Pathway results for Effect on Normal Cells:

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