Parthasarathy Seshacharyulu
YOU?
Author Swipe
View article: Novel EC914 Targeting the LIFR/DDX21/Fibrillarin Axis Is a Potential Therapeutic Strategy To Overcome Adaptive Chemo-Persistence in Prostate Cancer
Novel EC914 Targeting the LIFR/DDX21/Fibrillarin Axis Is a Potential Therapeutic Strategy To Overcome Adaptive Chemo-Persistence in Prostate Cancer Open
View article: Rac1 GTPase Regulates the βTrCP-Mediated Proteolysis of YAP Independently of the LATS1/2 Kinases
Rac1 GTPase Regulates the βTrCP-Mediated Proteolysis of YAP Independently of the LATS1/2 Kinases Open
Background: Oncogenic mutations in the KRAS gene are detected in >90% of pancreatic cancers (PC). In genetically engineered mouse models of PC, oncogenic KRAS drives the formation of precursor lesions and their progression to invasive PC. …
View article: Understanding the role of Pax5 in development of taxane-resistant neuroendocrine like prostate cancers
Understanding the role of Pax5 in development of taxane-resistant neuroendocrine like prostate cancers Open
View article: Supplementary Revised Figure S1 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S1 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
MUC16 incidence in lung cancer. A, MUC16 is overexpressed in a greater proportion of lung adenocarcinoma compared to other histological subtypes. B, Data from TCGA also shows that MUC16 is highly expressed in adenocarcinoma tissues than sq…
View article: Supplementary Revised Figure S3 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S3 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Chemoresistance properties of MUC16 and effect of cisplatin on apoptosis of MUC16 knockdown cells. A & B, MUC16 knockdown (H1975-shMUC16 seq1 and 2) cells were highly sensitive to cisplatin (A) and gemcitabine (B). C, The percentage of apo…
View article: Supplementary Revised Figure S2 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S2 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Pharmacological inhibition of phospho JAK1/2 in lung cancer cells. A, Upon JAK1/2 inhibition by ruxolitinib, we observed decreased phosphorylation of STAT3 (Y705) but no change in STAT3 expression. B, Similar effect was also observed in MU…
View article: Supplementary Figure legends from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Figure legends from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Supplementary Figure legends
View article: Supplementary Figure legends from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Figure legends from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Supplementary Figure legends
View article: Data from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Data from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Purpose: MUC16, a tumor biomarker and cell surface–associated mucin, is overexpressed in various cancers; however, its role in lung cancer pathogenesis is unknown. Here, we have explored the mechanistic role of MUC16 in lung cancer.…
View article: Supplementary Revised Figure S3 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S3 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Chemoresistance properties of MUC16 and effect of cisplatin on apoptosis of MUC16 knockdown cells. A & B, MUC16 knockdown (H1975-shMUC16 seq1 and 2) cells were highly sensitive to cisplatin (A) and gemcitabine (B). C, The percentage of apo…
View article: Supplementary Revised Figure S1 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S1 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
MUC16 incidence in lung cancer. A, MUC16 is overexpressed in a greater proportion of lung adenocarcinoma compared to other histological subtypes. B, Data from TCGA also shows that MUC16 is highly expressed in adenocarcinoma tissues than sq…
View article: Data from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Data from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Purpose: MUC16, a tumor biomarker and cell surface–associated mucin, is overexpressed in various cancers; however, its role in lung cancer pathogenesis is unknown. Here, we have explored the mechanistic role of MUC16 in lung cancer.…
View article: Supplementary Revised Figure S2 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S2 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Pharmacological inhibition of phospho JAK1/2 in lung cancer cells. A, Upon JAK1/2 inhibition by ruxolitinib, we observed decreased phosphorylation of STAT3 (Y705) but no change in STAT3 expression. B, Similar effect was also observed in MU…
View article: Supplementary Revised Figure S4 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S4 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Stable knockdown of TSPYL5 in lung cancer cells. A, MUC16 expression was significantly elevated in cisplatin resistant cell line. To determine the TSPYL5 role in lung cancer, we stably knocked down TSPYL5 in H292 cells. B, Upon TSPYL5 knoc…
View article: Supplementary Revised Figure S4 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53
Supplementary Revised Figure S4 from MUC16 Regulates TSPYL5 for Lung Cancer Cell Growth and Chemoresistance by Suppressing p53 Open
Stable knockdown of TSPYL5 in lung cancer cells. A, MUC16 expression was significantly elevated in cisplatin resistant cell line. To determine the TSPYL5 role in lung cancer, we stably knocked down TSPYL5 in H292 cells. B, Upon TSPYL5 knoc…
View article: Supplementary Figure S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on BAD and β-catenin
View article: Supplementary Table S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Table S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Clinical characteristics of the PDAC specimens used for the study of PR55α expression by IHC
View article: Data from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Data from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
The protein phosphatase 2 (PP2A) holoenzyme consists of a catalytic subunit, a scaffold subunit, and a regulatory subunit. Based on loss-of-function analysis using PP2A catalytic inhibitors or inhibition via tumor viral antigens, limited s…
View article: Supplementary Figure S4 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S4 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Decrease of PR55α expression in pancreatic cancer cells inhibits tumor growth.
View article: Supplemental Figure Legends from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplemental Figure Legends from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Legends for Supplementary Figures S1-S4
View article: Supplementary Table S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Table S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Clinical characteristics of the PDAC specimens used for the study of PR55α expression by IHC
View article: Data from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Data from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
The protein phosphatase 2 (PP2A) holoenzyme consists of a catalytic subunit, a scaffold subunit, and a regulatory subunit. Based on loss-of-function analysis using PP2A catalytic inhibitors or inhibition via tumor viral antigens, limited s…
View article: Supplementary Figure S3 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S3 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on mobility of pancreatic cancer cells.
View article: Supplemental Materials and Methods from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplemental Materials and Methods from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Description of additional details of materials and methodologies used in this study
View article: Supplementary Figure S2 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S2 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on clonogenicity of pancreatic cancer cells
View article: Supplementary Figure S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S1 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on BAD and β-catenin
View article: Supplemental Figure Legends from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplemental Figure Legends from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Legends for Supplementary Figures S1-S4
View article: Supplementary Figure S3 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S3 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on mobility of pancreatic cancer cells.
View article: Supplementary Figure S2 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplementary Figure S2 from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Effect of PR55α expression on clonogenicity of pancreatic cancer cells
View article: Supplemental Materials and Methods from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling
Supplemental Materials and Methods from PR55α Subunit of Protein Phosphatase 2A Supports the Tumorigenic and Metastatic Potential of Pancreatic Cancer Cells by Sustaining Hyperactive Oncogenic Signaling Open
Description of additional details of materials and methodologies used in this study