Tony Luu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Tony Luu has a total of 48 co-authors. Here are the top co-authors by number of shared publications:
- Caius G. Radu
Jonsson Comprehensive Cancer Center, University of California Los Angeles, Los Angeles, USA
48 shared publications - Thuc Le
Department of Molecular and Medical Pharmacology, University of California
48 shared publications - Alykhan Premji
Veterans Health Administration, Greater Los Angeles Healthcare System, Los Angeles, USA
47 shared publications - Amanda Labora
Department of Surgery, University of California, Los Angeles, USA
47 shared publications - Charlotte Chan
Department of Surgery, University of California Los Angeles, Los Angeles, California
47 shared publications - Evan R. Abt
Department of Molecular and Medical Pharmacology, University of California, Los Angeles, CA 90095
47 shared publications
Latest Publications
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 1 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 1 STING agonist diABZI synergizes with MAPK inhibition in PDAC by enhancing apoptosis.
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 1 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 1 STING agonist diABZI synergizes with MAPK inhibition in PDAC by enhancing apoptosis.
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 4 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 4 Immunoblot analysis demonstrating the effect of ± 100 U/ml exogenous IFN on CFPAC-1 and SUIT2 parental cells compared to their respective IFNAR-deficient isogenic cell lines. (B) Immunoblot analysis of CFPAC-1 parental and IFNAR1-KO cells exposed to ± 1 µM diABZI ± 100 nM trametinib for 24 h (C)Immunoblot analysis of the effects of ± 100 U/ml exogenous IFN ± 1 µM diABZI for 24 h.
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 4 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 4 Immunoblot analysis demonstrating the effect of ± 100 U/ml exogenous IFN on CFPAC-1 and SUIT2 parental cells compared to their respective IFNAR-deficient isogenic cell lines. (B) Immunoblot analysis of CFPAC-1 parental and IFNAR1-KO cells exposed to ± 1 µM diABZI ± 100 nM trametinib for 24 h (C)Immunoblot analysis of the effects of ± 100 U/ml exogenous IFN ± 1 µM diABZI for 24 h.
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 2 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 2 Tumor growth is inhibited by STING agonism and MEK inhibition in vivo.
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 2 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 2 Tumor growth is inhibited by STING agonism and MEK inhibition in vivo.
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 3 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 3 MEK inhibition amplifies STING-induced transcription of IFNB1, IL-6, and TNFA in multiple PDAC cell lines.
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 3 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 3 MEK inhibition amplifies STING-induced transcription of IFNB1, IL-6, and TNFA in multiple PDAC cell lines.
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 5 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 5 IL6 is not responsible for the synergistic effects of STING agonism and MEK inhibition.
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 5 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Fig. 5 IL6 is not responsible for the synergistic effects of STING agonism and MEK inhibition.
- Open Access
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Data 1 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Resources and Table
- 25 November 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Data 1 from MEK Inhibition Sensitizes Pancreatic Cancer to STING Agonism by Tumor Cell–intrinsic Amplification of Type I IFN Signaling
Supplementary Resources and Table
- 23 June 2025
- Published by Springer Nature in Nature Nanotechnology
- Vol. 20 (9) , 1-11
Tailoring the adjuvanticity of lipid nanoparticles by PEG lipid ratio and phospholipid modifications
Lipid nanoparticles (LNPs) represent the leading delivery platform for mRNA vaccines with advantageous biocompatibility, scalability, adjuvant activity and often an acceptable safety profile. Here we investigate the physicochemical characteristics and adjuvanticity of four-component LNPs. Previous vaccine studies have demonstrated that altering the ionizable lipid influences the adjuvanticity of an LNP; however, the impact of the polyethylene glycol lipid and phospholipid has received less attention. Our mRNA–LNP vaccine formulations utilized different phospholipids and varying ratios of polyethylene glycol lipid, whereas the ionizable lipid and cholesterol remained approximately constant. We demonstrate that such modifications impact the magnitude and quality of the vaccine-elicited immune responses. We also dissect the underlying mechanisms and show that the biodistribution and cellular uptake of LNPs correlate with the magnitude and quality of the immune responses. These findings support the rational design of novel LNPs to tailor immune responses (cellular or humoral focused) based on the vaccine application.
- 23 June 2025
- Published by Springer Nature in Nature Nanotechnology
- Vol. 20 (9) , 1-11
Tailoring the adjuvanticity of lipid nanoparticles by PEG lipid ratio and phospholipid modifications
Lipid nanoparticles (LNPs) represent the leading delivery platform for mRNA vaccines with advantageous biocompatibility, scalability, adjuvant activity and often an acceptable safety profile. Here we investigate the physicochemical characteristics and adjuvanticity of four-component LNPs. Previous vaccine studies have demonstrated that altering the ionizable lipid influences the adjuvanticity of an LNP; however, the impact of the polyethylene glycol lipid and phospholipid has received less attention. Our mRNA–LNP vaccine formulations utilized different phospholipids and varying ratios of polyethylene glycol lipid, whereas the ionizable lipid and cholesterol remained approximately constant. We demonstrate that such modifications impact the magnitude and quality of the vaccine-elicited immune responses. We also dissect the underlying mechanisms and show that the biodistribution and cellular uptake of LNPs correlate with the magnitude and quality of the immune responses. These findings support the rational design of novel LNPs to tailor immune responses (cellular or humoral focused) based on the vaccine application.
- Open Access
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 3 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 3 MEK inhibition amplifies STING-induced transcription of IFNB1, IL-6, and TNFA in multiple PDAC cell lines.
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 3 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 3 MEK inhibition amplifies STING-induced transcription of IFNB1, IL-6, and TNFA in multiple PDAC cell lines.
- Open Access
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 5 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 5 IL6 is not responsible for the synergistic effects of STING agonism and MEK inhibition.
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 5 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 5 IL6 is not responsible for the synergistic effects of STING agonism and MEK inhibition.
- Open Access
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 4 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 4 Immunoblot analysis demonstrating the effect of ± 100 U/ml exogenous IFN on CFPAC-1 and SUIT2 parental cells compared to their respective IFNAR-deficient isogenic cell lines. (B) Immunoblot analysis of CFPAC-1 parental and IFNAR1-KO cells exposed to ± 1 µM diABZI ± 100 nM trametinib for 24 h (C)Immunoblot analysis of the effects of ± 100 U/ml exogenous IFN ± 1 µM diABZI for 24 h.
- 16 September 2024
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 4 from MEK inhibition sensitizes pancreatic cancer to STING agonism by tumor-cell intrinsic amplification of type I interferon signaling
Supplementary Fig. 4 Immunoblot analysis demonstrating the effect of ± 100 U/ml exogenous IFN on CFPAC-1 and SUIT2 parental cells compared to their respective IFNAR-deficient isogenic cell lines. (B) Immunoblot analysis of CFPAC-1 parental and IFNAR1-KO cells exposed to ± 1 µM diABZI ± 100 nM trametinib for 24 h (C)Immunoblot analysis of the effects of ± 100 U/ml exogenous IFN ± 1 µM diABZI for 24 h.