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BioAssay: AID 504510

Late stage assay provider results from the probe development effort to identify inhibitors of LYPLA1: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds set 2

Name: Late stage assay provider results from the probe development effort to identify inhibitors of LYPLA1: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds set 2. ..more
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 Tested Compounds
 Tested Compounds
All(2)
 
 
Inactive(2)
 
 
 Tested Substances
 Tested Substances
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Inactive(2)
 
 
 Related BioAssays
 Related BioAssays
AID: 504510
Data Source: The Scripps Research Institute Molecular Screening Center (TCELLCYTOX_INH_ABSORB_4XCC50_SET2)
BioAssay Type: Panel, Confirmatory, Concentration-Response Relationship Observed
Depositor Category: NIH Molecular Libraries Probe Production Network, Assay Provider
BioAssay Version:
Deposit Date: 2011-03-21
Hold-until Date: 2011-10-06
Modify Date: 2011-10-06

Data Table ( Complete ):           All
Tested Compounds:
Depositor Specified Assays
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AIDNameTypeProbeComment
2202Summary of probe development efforts to identify inhibitors of lysophospholipase 1 (LYPLA1).summary2 Summary (LYPLA1 inhibitors)
2203Summary of probe development efforts to identify inhibitors of lysophospholipase 2 (LYPLA2).summary1 Summary (LYPLA2 inhibitors)
2174Counterscreen for PME1 inhibitors: fluorescence polarization-based primary biochemical high throughput screening assay to identify inhibitors of lysophospholipase 1 (LYPLA1).screening Primary screen (LYPLA1 inhibitors in singlicate)
2233Counterscreen for PME1 inhibitors: fluorescence polarization-based biochemical high throughput confirmation assay for inhibitors of lysophospholipase 1 (LYPLA1).screening Confirmation screen (LYPLA1 inhibitors in triplicate)
2177Counterscreen for PME1 inhibitors: fluorescence polarization-based primary biochemical high throughput screening assay to identify inhibitors of lysophospholipase 2 (LYPLA2).screening Primary screen (LYPLA2 inhibitors in singlicate)
2232Counterscreen for PME1 inhibitors: fluorescence polarization-based biochemical high throughput confirmation assay to identify inhibitors of lysophospholipase 2 (LYPLA2).screening Confirmation screen (LYPLA2 inhibitors in triplicate)
493105Assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP inhibition of recombinant and endogenous enzymeother Confirmation screen (LYPLA1 and LYPLA2 inhibitors in singlicate)
493108Late stage assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: fluorescence-based cell-based inhibitionother Late stage screen (LYPLA1 and LYPLA2 inhibitors in singlicate)
493109Late stage assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: LC-MS/MS assay to assess binding of compounds to active siteother Late stage LCMS assay (LYPLA1)
493110Late stage assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: Gel-based Activity-Based Protein Profiling (ABPP) IC50 for LYPLA1 and LYPLA2confirmatory Late stage dose response (LYPLA1 and LYPLA2 inhibitors in triplicate)
493111Late stage assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP inhibition and selectivityother Late stage screen (LYPLA1 and LYPLA2 inhibitors in singlicate)
493154Late stage assay provider results from the probe development effort to identify inhibitors of LYPLA1 and LYPLA2: Gel-based Activity-Based Protein Profiling (ABPP) IC50 for off-target ABHD11confirmatory Late stage dose response counterscreen (ABHD11 inhibitors in triplicate)
493161Late stage assay provider results from the probe development effort to identify dual inhibitors of LYPLA1 and LYPLA2: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compoundsconfirmatory Late stage dose response counterscreen (T-cell cytotoxicity in quadruplicate)
651985Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP evaluation of activity in vivoother
651988Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP inhibition and selectivityother
651991Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compoundsconfirmatory
651978Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1: LCMS-based Activity-Based Protein Profiling (ABPP) SILAC selectivity analysis in vitroother
651998Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1: Substrate-based fluorescence-based biochemical determination of kinetic parametersconfirmatory
652001Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: Substrate-based fluorescence-based biochemical determination of kinetic parametersconfirmatory
652004Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: fluorescence-based biochemical dose-response assayconfirmatory
652030Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: Fluorescence-based biochemical gel-based ABPP inhibition and selectivityother
652018Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1: LCMS-based Activity-Based Protein Profiling (ABPP) SILAC selectivity analysis in vitro, Set 2other
651980Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: LCMS-based cell-based Activity-Based Protein Profiling (ABPP) SILAC selectivity analysis in situother
651986Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP evaluation of activity in situother
651979Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1: LCMS-based cell-based Activity-Based Protein Profiling (ABPP) SILAC selectivity analysis in situother
652003Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1: fluorescence-based biochemical dose-response assayconfirmatory
652029Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: Fluorescence-based biochemical gel-based ABPP inhibitionother
651981Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA2: LCMS-based Activity-Based Protein Profiling (ABPP) SILAC selectivity analysis in vitroother
651987Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical gel-based ABPP gel filtration assay to assess binding modeother
651990Late stage assay provider results from the probe development effort to identify selective inhibitors of LYPLA1 and LYPLA2: Fluorescence-based biochemical dose-response gel-based ABPPconfirmatory
504892Late stage assay provider results from the probe development effort to identify inhibitors of ABHD11: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) inhibition of the human isoform of ABHD11other
743117 On Hold
743118 On Hold
743119 On Hold
743127 On Hold
743132 On Hold
743133 On Hold
743134 On Hold
743137 On Hold
Description:
Source (MLPCN Center Name): The Scripps Research Institute Molecular Screening Center (SRIMSC)
Center Affiliation: The Scripps Research Institute (TSRI)
Assay Provider: Benjamin Cravatt, TSRI
Network: Molecular Libraries Probe Production Centers Network (MLPCN)
Grant Proposal Number: 1 R01 CA132630-01
Grant Proposal PI: Benjamin Cravatt, TSRI
External Assay ID: TCELLCYTOX_INH_ABSORB_4XCC50_SET2

Name: Late stage assay provider results from the probe development effort to identify inhibitors of LYPLA1: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds set 2.

Description:

Protein palmitoylation is an essential post-translational modification necessary for trafficking and localization of regulatory proteins that play key roles in cell growth and signaling. Numerous proteins have been identified as targets of palmitoylation, including cytoskeletal proteins, kinases, receptors, and other proteins involved in various aspects of cellular signaling and homeostasis (1). Using a global chemo-proteomic method for the metabolic incorporation and identification of palmitoylated proteins, we were able to identify hundreds of palmitoylated proteins, revealing palmitoylation as a widespread post-translational modification (PTM) (2). Palmitoylation involves an acyl-thioester linkage to specific cysteines (3,4). Given the labile properties of thioesters, palmitoylation is potentially reversible and may be regulated in a manner analogous to other PTMs (e.g., phosphorylation). As such, identification of proteins responsible for the dynamic modulation of palmitoylation is paramount to understanding its patho/physiological roles. For example, multiple oncogenes, including HRAS and SRC, require palmitoylation for malignant transformation (5), suggesting protein palmitoyl thioesterases may have tumor suppressor activity required to repress aberrant growth signaling. More than a decade ago, the cytosolic serine hydrolase acyl-protein thioesterase 1 (APT1) was identified as an in vitro HRAS palmitoyl thioesterase (6). Initially classified as lysophospholipase 1 (LYPLA1) (7), the enzyme has since been demonstrated to have several hundred-fold higher activity as a protein thioesterase. While the in vitro data (6,8) provided an intriguing clue to its possible role in vivo, prior to our studies, little was known about the in vivo thioesterase activity of LYPLA1. Upon retroviral shRNA knockdown of LYPLA1, we found that HRAS was robustly hyper-palmitoylated, providing the first evidence that the endogenous enzyme is a functional protein palmitoyl thioesterase capable of regulating HRAS palmitoylation in mammalian cells. However, shRNA resulted in only an 80% reduction in LYPLA1 expression (unpublished). LYPLA2 (a.k.a. APT2) is 65% identical to LYPLA1, and also exhibits lysophospholipase activity in vitro, but its potential role as a thioesterase is unknown (9). shRNA knockdown studies of LYPLA2 revealed only partial knockdown of the enzyme, making substrate identification inconclusive (unpublished). A principle goal of post-genomic research is the determination of the molecular and cellular role of uncharacterized enzymes like LYPLA1 and LYPLA2. As such, a dual inhibitor selective for both LYPLA1 and LYPLA2 would greatly aid investigations into the biological function of these related enzymes. Several inhibitors of LYPLA1 have been described (10,11), but none of these agents have proven capable of inhibiting LYPLA1 activity in cells, and no selective inhibitors of LYPLA2 have been reported to date. To comprehensively identify LYPLA1 and LYPLA2 substrates and functionally test the role of these enzymes in dynamic de-palmitoylation and tumorigenesis, development of a high affinity inhibitor, capable of achieving temporal and more complete control over activity, is critical. Alpha/beta hydrolase domain-containing protein 11 (ABHD11) is a poorly characterized serine hydrolase; all that is known about its biology is that it is a mitochondrial enzyme (12) with broad tissue distribution, has little sequence homology to other proteins, and its gene is located in a region of chromosome 7 that is hemizygously deleted in Williams-Beuren syndrome, a rare genetic disease with symptoms that include vascular stenosis, mental retardation, and excessive sociability (13).

References:

1. Smotrys, J.E. and Linder, M.E. PALMITOYLATION OF INTRACELLULAR SIGNALING PROTEINS: Regulation and Function. Annual Review of Biochemistry, 2004. 73: 559-587.
2. Martin, B.R. and Cravatt, B.F. Large-scale profiling of protein palmitoylation in mammalian cells. Nat Methods, 2009. 6: 135-138.
3. Magee, A.I., Koyama, A.H., Malfer, C., Wen, D. and Schlesinger, M. J. Release of fatty acids from virus glycoproteins by hydroxylamine. Biochimica et Biophysica Acta (BBA) - General Subjects, 1984. 798: 156-166.
4. Rose, J.K., Adams, G.A. and Gallione, C.J. The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition. Proc Natl Acad Sci USA, 1984. 81: 2050-2054.
5. Willumsen, B.M., Cox, A.D., Solski, P.A., Der, C.J. and Buss, J.E. Novel determinants of H-Ras plasma membrane localization and transformation. Oncogene, 1996. 13: 1901-1909.
6. Duncan, J.A. and Gilman, A.G. A Cytoplasmic Acyl-Protein Thioesterase That Removes Palmitate from G Protein alpha Subunits and p21RAS. J Biol Chem, 1998. 273: 15830-15837.
7. Sugimoto, H., Hayashi, H. & Yamashita, S. Purification, cDNA cloning, and regulation of lysophospholipase from rat liver. J Biol Chem, 1996. 271: 7705-7711.
8. Hirano, T. et al. Thioesterase activity and subcellular localization of acylprotein thioesterase 1/lysophospholipase 1. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2009. 1791: 797-805.
9. Toyoda, T., Sugimoto, H. and Yamashita, S. Sequence, expression in Escherichia coli, and characterization of lysophospholipase II. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999. 1437: 182-193.
10. Biel, M., Deck, P., Giannis, A. and Waldmann, H. Synthesis and Evaluation of Acyl Protein Thioesterase 1 (APT1) Inhibitors. Chemistry - A European Journal, 2006. 12: 4121-4143.
11. Deck, P. et al. Development and Biological Evaluation of Acyl Protein Thioesterase 1 (APT1) Inhibitors. Angewandte Chemie International Edition, 2005. 44: 4975-4980.
12. Forner, F., et al., Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics, 2006. 5(4): p. 608-19.
13. Schubert, C., The genomic basis of the Williams-Beuren syndrome. Cell. Mol. Life Sci., 2009. 66(7): p. 1178-97.

Keywords:

late stage, late stage AID, assay provider, powders, LYPLA1, lysophospholipase 1, LYPLA2, lysophospholipase 2, APT1, acyl-protein thioesterase 1, APT2, acyl-protein thioesterase 2, palmitoylation, alpha/beta hydrolase domain-containing protein 11, abhydrolase domain-containing protein 11, ABHD11, oncogene, tumor suppressor, serine hydrolase, counterscreen, inhibitor, BW5147, murine T cells, T cells, cytotoxicity, CC50, activity-based protein profiling, ABPP, gel-based ABPP, fluorophosphonate rhodamine, FP-Rh, Scripps, Scripps Research Institute Molecular Screening Center, SRIMSC, Molecular Libraries Probe Production Centers Network, MLPCN
Panel Information
Assays (see Protocol for details)
PID§NameSubstancePanel TargetsDescription
ActiveInactive
1Assay 1: % Surviving cells, serum-free media2
2Assay 2: % Surviving cells, media plus FCS2

§ Panel component ID.
Protocol
Assay Overview:

The purpose of this assay is to determine cytotoxicity of inhibitor compounds belonging to the urea triazole scaffold. In this assay, BW5147-derived murine T-cells in either serum-free media (Assay 1) or media containing FCS (Assay 2) are incubated with test compounds, followed by determination of cell viability. The assay utilizes the WST-1 substrate that is converted into colorimetric formazan dye by the metabolic activity of viable cells. The amount of formed formazan directly correlates to the number of metabolically active cells in the culture. As designed, compounds that reduce cell viability will result in decreased absorbance of the dye. Compounds were tested in quadruplicate in a 7-point 1:5 dilution series starting at a nominal test concentration of 50 uM.

Protocol Summary:

This assay was started by dispensing BW5147-derived murine T cells in RPMI media (100uL, 10E4 cells/well) into a 96-well plate. Both serum-free media (Assay 1) and media supplemented with fetal calf serum (FCS) (Assay 2) were tested. Compound (5 uL of 0-1000 uM in media containing 5% DMSO) was added to each well, giving final compound concentrations of 0-50 uM. Cells were incubated for 48 hours at 37 C in a humidified incubator and cell viability was determined by the WST-1 assay (Roche) according to manufacturer instructions.

The % cell viability for each well was then calculated as follows:

%_Cell_Viability = ( ABS_Test_Compound - MedianABS_Low_Control ) / ( MedianABS_High_Control - MedianABS_Low_Control ) * 100

Where:

Test_Compound is defined as wells containing cells in the presence of test compound.
High_Control is defined as wells containing cells treated with media only (no compound).
Low_Control is defined as wells containing no cells (media only).

For each test compound, percent cell viability was plotted against the log of the compound concentration. The CC50 is reported as ">X uM" (where X = the highest concentration tested for which > 50% cell survival was observed).

PubChem Activity Outcome and Score:

The following applies to each panel in this assay:

Compounds with a CC50 value of less than 5 uM were considered active (cytotoxic). Compounds with a CC50 value greater than or equal to 5 uM were considered inactive (non-cytotoxic).

Activity score was then ranked by the potency of the compounds with fitted curves, with the most potent compounds assigned the highest activity scores.

Assay 1 Score: The PubChem Activity Score range for inactive compounds is 0-0. There are no active compounds.

Assay 2 Score: The PubChem Activity Score range for inactive compounds is 0-0. There are no active compounds.

Overall Outcome and Score:

The overall outcome was active if the compound was active in at least one panel, inactive otherwise.

The overall score is 0 if the compound was inactive, otherwise the score is taken as the fraction of panels where the compound is active, multiplied by 100.

The PubChem Activity Score range for inactive compounds is 0-0. There are no active compounds.

List of Reagents:

BW5147-derived murine T cells (provided by Assay Provider)
RPMI Media (CellGro 10-040-CV)
FCS (Omega Scientific, FB-01)
WST-1 reagent (Roche)
96-well plates (Corning)
Comment
This assay was performed by the assay provider with powder samples of compounds.
Result Definitions
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TIDNameDescriptionPID§Panel TargetsHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Outcome [Assay 1]One of Active, Inactive, or Not Tested1Outcome
2Score [Assay 1]The BioAssay activity ranking score1Integer
3Qualifier [CC50, Assay 1]Activity Qualifier identifies if the resultant data CC50 came from a fitted curve or was determined manually to be less than or greater than its listed CC50 concentration.1String
4CC50 [Assay 1]*The value for concentration at which 50% of surviving cells are observed; CC50 shown in micromolar.1FloatμM
5Cell Viability at 0.0032 uM [1, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate one.1Float%
6Cell Viability at 0.0032 uM [2, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate two.1Float%
7Cell Viability at 0.0032 uM [3, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate three.1Float%
8Cell Viability at 0.0032 uM [4, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate four.1Float%
9Cell Viability at 0.016 uM [1, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate one.1Float%
10Cell Viability at 0.016 uM [2, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate two.1Float%
11Cell Viability at 0.016 uM [3, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate three.1Float%
12Cell Viability at 0.016 uM [4, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate four.1Float%
13Cell Viability at 0.08 uM [1, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate one.1Float%
14Cell Viability at 0.08 uM [2, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate two.1Float%
15Cell Viability at 0.08 uM [3, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate three.1Float%
16Cell Viability at 0.08 uM [4, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate four.1Float%
17Cell Viability at 0.4 uM [1, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate one.1Float%
18Cell Viability at 0.4 uM [2, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate two.1Float%
19Cell Viability at 0.4 uM [3, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate three.1Float%
20Cell Viability at 0.4 uM [4, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate four.1Float%
21Cell Viability at 2 uM [1, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate one.1Float%
22Cell Viability at 2 uM [2, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate two.1Float%
23Cell Viability at 2 uM [3, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate three.1Float%
24Cell Viability at 2 uM [4, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate four.1Float%
25Cell Viability at 10 uM [1, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate one.1Float%
26Cell Viability at 10 uM [2, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate two.1Float%
27Cell Viability at 10 uM [3, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate three.1Float%
28Cell Viability at 10 uM [4, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate four.1Float%
29Cell Viability at 50 uM [1, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate one.1Float%
30Cell Viability at 50 uM [2, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate two.1Float%
31Cell Viability at 50 uM [3, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate three.1Float%
32Cell Viability at 50 uM [4, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate four.1Float%
33Outcome [Assay 2]One of Active, Inactive, or Not Tested2Outcome
34Score [Assay 2]The BioAssay activity ranking score2Integer
35Qualifier [CC50, Assay 2]Activity Qualifier identifies if the resultant data CC50 came from a fitted curve or was determined manually to be less than or greater than its listed CC50 concentration.2String
36CC50 [Assay 2]*The value for concentration at which 50% of surviving cells are observed; CC50 shown in micromolar.2FloatμM
37Cell Viability at 0.0032 uM [1, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate one.2Float%
38Cell Viability at 0.0032 uM [2, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate two.2Float%
39Cell Viability at 0.0032 uM [3, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate three.2Float%
40Cell Viability at 0.0032 uM [4, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate four.2Float%
41Cell Viability at 0.016 uM [1, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate one.2Float%
42Cell Viability at 0.016 uM [2, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate two.2Float%
43Cell Viability at 0.016 uM [3, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate three.2Float%
44Cell Viability at 0.016 uM [4, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate four.2Float%
45Cell Viability at 0.08 uM [1, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate one.2Float%
46Cell Viability at 0.08 uM [2, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate two.2Float%
47Cell Viability at 0.08 uM [3, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate three.2Float%
48Cell Viability at 0.08 uM [4, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate four.2Float%
49Cell Viability at 0.4 uM [1, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate one.2Float%
50Cell Viability at 0.4 uM [2, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate two.2Float%
51Cell Viability at 0.4 uM [3, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate three.2Float%
52Cell Viability at 0.4 uM [4, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate four.2Float%
53Cell Viability at 2 uM [1, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate one.2Float%
54Cell Viability at 2 uM [2, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate two.2Float%
55Cell Viability at 2 uM [3, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate three.2Float%
56Cell Viability at 2 uM [4, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate four.2Float%
57Cell Viability at 10 uM [1, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate one.2Float%
58Cell Viability at 10 uM [2, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate two.2Float%
59Cell Viability at 10 uM [3, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate three.2Float%
60Cell Viability at 10 uM [4, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate four.2Float%
61Cell Viability at 50 uM [1, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate one.2Float%
62Cell Viability at 50 uM [2, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate two.2Float%
63Cell Viability at 50 uM [3, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate three.2Float%
64Cell Viability at 50 uM [4, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate four.2Float%

* Activity Concentration. ** Test Concentration. § Panel component ID.
Additional Information
Grant Number: 1 R01 CA132630-01

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