Deguelin / ROS Cancer Research Results

Deg, Deguelin: Click to Expand ⟱

Features: Insect poisoning, anti-cancer

Deguelin is a natural compound of isoflavonoid-derived rotenoid isolated from several plant species, including Derris trifoliata Lour and Mundulea sericea (Leguminosae) (4)

Deguelin’s ability to modulate multiple signaling pathways—including PI3K/Akt, mTOR, NF-κB, HIF-1α, and MAPK
While preclinical studies have utilized dosages in the approximate range of 4–8 mg/kg in animal models, these figures are specific to the experimental conditions and species used in those studies.

Deguelin is a rotenoid (isoflavonoid-like botanical insecticide class) found in some Lonchocarpus / Derris species. In cancer literature it’s most often described as a mitochondrial Complex I inhibitor with downstream energy stress + survival pathway suppression (Akt/PI3K, NF-κB) and apoptosis/autophagy induction. A major caution is neurotoxicity signal: rotenoids (including deguelin) have been used in Parkinson’s disease animal models via Complex I inhibition.
-

Active identity: Rotenoid (deguelin) — a potent mitochondrial Complex I inhibitor with downstream energy-stress signaling (AMPK/mTOR), survival pathway suppression (Akt, NF-κB), and apoptosis/autophagy induction in cancer models; higher caution category due to rotenoid neurotoxicity signals in animal models.

Deguelin — a naturally occurring rotenoid derived principally from leguminous plants in the Derris, Lonchocarpus, Tephrosia, and related genera. It is a lipophilic isoflavonoid-related botanical insecticide and experimental anticancer small molecule, commonly abbreviated Deg. Its functional identity is dominated by mitochondrial respiratory Complex I inhibition, with secondary suppression of Hsp90-dependent oncogenic proteins and PI3K/AKT, NF-κB, mTOR, HIF-1α, angiogenic, and metastatic signaling. Deguelin is not an approved anticancer drug and has a substantial translational safety concern because systemic exposure can injure dopaminergic neurons and produce Parkinsonism-like pathology in animals.

Primary mechanisms (ranked):

Mitochondrial electron-transport-chain Complex I inhibition, causing reduced oxidative phosphorylation, ATP depletion, energetic stress, and context-dependent ROS accumulation.
Direct or functionally relevant disruption of Hsp90 chaperone activity, destabilizing oncogenic client proteins including AKT, HIF-1α, survivin, and CDK4.
PI3K/AKT survival-axis suppression, contributing to reduced proliferation, survival signaling, invasion, and treatment resistance.
AMPK activation with downstream mTOR and survivin suppression in energy-stressed cancer cells.
Intrinsic mitochondrial apoptosis through mitochondrial membrane dysfunction, cytochrome-c release, caspase activation, and PARP cleavage.
NF-κB pathway suppression through reduced IKK activation and inflammatory or anti-apoptotic transcription.
HIF-1α and VEGF suppression, reducing hypoxic adaptation, angiogenesis, and lymphangiogenesis.
Cell-cycle arrest through reduced cyclins, CDKs, and oncogenic Hsp90 clients, with context-dependent increases in p21 or p27.
Inhibition of migration, epithelial–mesenchymal transition, invasion, and metastasis through context-dependent modulation of c-MET, EGFR, STAT3, MAPK, MMP2, MMP9, and related pathways.
Autophagy induction or modulation, which may be cytotoxic or adaptive depending on tumor type, dose, and treatment duration.

Bioavailability / PK relevance: Deguelin is highly lipophilic and poorly suited to simple aqueous delivery. Rat pharmacokinetic studies found measurable systemic persistence and a relatively long plasma residence time, but human pharmacokinetics, oral bioavailability, therapeutic exposure targets, metabolism, and safe dosing have not been established. Formulation research has therefore focused on analogues, nanoparticles, and other delivery systems intended to improve solubility or tumor exposure. Enhanced delivery could also increase neurological and systemic toxicity.

In-vitro vs systemic exposure relevance: Anticancer effects are frequently reported from low-nanomolar to several-micromolar concentrations, depending on the cell model and endpoint. Some sensitive models respond below 0.1 µM, whereas apoptosis, ROS, autophagy, or broad cytotoxicity studies commonly use approximately 1–20 µM. There is no validated human exposure range demonstrating that these concentrations can be achieved safely. Because mitochondrial Complex I inhibition occurs in normal as well as malignant tissue, systemic exposure cannot be assumed to preserve cancer selectivity.

Clinical evidence status: Preclinical only. Evidence consists primarily of biochemical studies, cancer-cell experiments, xenografts, chemically induced tumor models, and rodent metastasis or chemoprevention studies. No established human anticancer trial evidence, approved indication, clinically validated dose, or accepted adjunct regimen was identified. Neurotoxicity and delivery limitations currently outweigh the strength of the efficacy evidence for clinical translation.

Deguelin Mechanistic Profile

Rank	Pathway / Axis	Cancer Cells	Normal Cells	TSF	Primary Effect	Notes / Interpretation
1	Mitochondrial Complex I and oxidative phosphorylation	Complex I ↓; oxygen consumption ↓; ATP ↓; energetic stress ↑	Complex I ↓; mitochondrial function ↓; neurotoxicity risk ↑	P, R	Bioenergetic inhibition	Central pharmacological action. PTEN-deficient and mitochondrially vulnerable tumors may show increased sensitivity, but inhibition is not tumor-specific.
2	Hsp90 chaperone and oncogenic client stability	Hsp90 function ↓; AKT ↓; survivin ↓; CDK4 ↓; HIF-1α ↓	Protein-homeostasis disruption ↑ (dose-dependent)	R, G	Oncoprotein destabilization	Deguelin has been reported to bind Hsp90 and disrupt client-protein complexes. Structural derivatives have been developed to retain this activity while reducing toxicity.
3	PI3K and AKT survival signaling	PI3K/AKT ↓; p-AKT ↓; proliferation ↓; survival ↓	AKT signaling ↓ (context-dependent)	R, G	Growth and survival suppression	A recurrent mechanism across lung, breast, colon, pancreatic, and other experimental cancer models.
4	AMPK and mTOR energy-sensing axis	AMPK ↑; mTOR ↓; protein synthesis ↓; survivin ↓	AMPK ↑; mTOR ↓ (energy-stress dependent)	R, G	Metabolic growth restriction	Likely downstream in part from mitochondrial ATP depletion and altered AMP-to-ATP balance.
5	Mitochondrial ROS and redox stress	ROS ↑; oxidative damage ↑; apoptosis sensitivity ↑	ROS ↑; oxidative neuronal injury risk ↑	P, R	Redox-mediated cytotoxicity	ROS contribution is model-dependent. Antioxidants such as N-acetylcysteine partially reverse apoptosis in some studies.
6	Intrinsic mitochondrial apoptosis	Mitochondrial membrane potential ↓; cytochrome-c release ↑; caspase-9 ↑; caspase-3 ↑; PARP cleavage ↑	Apoptosis ↑ at toxic exposure	G	Programmed cell death	Common downstream outcome of Complex I inhibition, ROS elevation, Hsp90-client loss, and AKT suppression.
7	NF-κB inflammatory and survival transcription	IKK ↓; IκB degradation ↓; NF-κB activity ↓; anti-apoptotic transcription ↓	Inflammatory signaling ↓ (context-dependent)	R, G	Anti-inflammatory and pro-apoptotic signaling	Reported against constitutive and stimulus-induced NF-κB activation.
8	HIF-1α and angiogenic signaling	HIF-1α ↓; VEGF ↓; hypoxic adaptation ↓; angiogenesis ↓	Physiological hypoxia responses may ↓ at systemic exposure	R, G	Anti-angiogenic activity	May reflect Hsp90-client destabilization, AKT inhibition, and altered mitochondrial oxygen sensing.
9	Cell-cycle regulation	G1 or S-phase arrest ↑; cyclins ↓; CDKs ↓; p21 or p27 ↑	Proliferation ↓ at sufficient exposure	G	Cytostasis	Exact arrest point and regulatory proteins vary among cancer models.
10	Autophagy and stress adaptation	Autophagy ↑ (context-dependent); autophagic death or survival adaptation ↑	Autophagy ↑ (context-dependent)	G	Stress-response modulation	The functional consequence must be experimentally determined; autophagy is not uniformly anticancer.
11	Migration invasion and epithelial–mesenchymal transition	c-MET ↓; EGFR ↓; STAT3 ↓; ERK ↓; MMP2 ↓; MMP9 ↓; EMT ↓; migration ↓	↔ or tissue-repair signaling ↓ (context-dependent)	G	Anti-metastatic activity	Mechanisms differ substantially by cancer lineage and may be secondary to reduced viability or Hsp90-client destabilization.
12	NRF2 antioxidant response	NRF2 ↔ or ↑ (secondary, model-dependent)	NRF2 ↑ may partially compensate for oxidative stress	R, G	Adaptive redox response	NRF2 is not a consistently established primary deguelin target. Direction and therapeutic significance should not be generalized across models.
13	Chemosensitization and radiosensitization	Treatment sensitivity ↑ (model-dependent); survival and HIF-1α signaling ↓	Normal-tissue toxicity may ↑	R, G	Adjunct sensitization	Preclinical reports support sensitization in selected models, but no clinically validated combination or therapeutic window exists.
14	Clinical Translation Constraint	Potential tumor exposure limited by solubility, formulation, heterogeneity, and uncertain therapeutic window	Complex I inhibition; dopaminergic neuron injury; Parkinsonism-like toxicity; possible systemic mitochondrial toxicity	R, G	Major development barrier	No approved formulation, validated human PK, established safe dose, or demonstrated human efficacy. Delivery enhancement does not remove mechanism-based neurotoxicity.

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⟱

6674-

Deg,

Deguelin induces the apoptosis of lung cancer cells through regulating a ROS driven Akt pathway

in-vitro,

Lung,

H1975

ROS↑, eff↓, p‑Akt↓, Casp3↑, Apoptosis↑,

Showing Research Papers: 1 to 1 of 1

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 1

Pathway results for Effect on Cancer / Diseased Cells:

Redox & Oxidative Stress(tgid=1) ⓘ

ROS↑, 1,

Cell Death(tgid=5) ⓘ

p‑Akt↓, 1, Apoptosis↑, 1, Casp3↑, 1,

Drug Metabolism & Resistance(tgid=21) ⓘ

eff↓, 1,
Total Targets: 5

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#:69  Target#:275  State#:%  Dir#:2
  wNotes=0  sortOrder:rid,rpid