Guan Chen

发表

Isoform-specific and cell/tissue-dependent effects of p38 MAPKs in regulating inflammation and inflammation-associated oncogenesis.

H. Xin, J. Qin, Xiaomei Qi, 2022, Frontiers in bioscience.

Essential role of p38gamma in K-Ras transformation independent of phosphorylation.

Jiahuai Han, D. Mercola, Jun Tang, 2005, The Journal of biological chemistry.

Oncogenic transformation potentiates apoptosis, S-phase arrest and stress-kinase activation by etoposide

D. Stacey, J. Shu, Guan Chen, 1997, Oncogene.

Influence of Cell Cycle and Oncogene Activity upon Topoisomerase IIα Expression and Drug Toxicity

D. Stacey, M. Hitomi, Guan Chen, 2000, Molecular and Cellular Biology.

Protein-Tyrosine Phosphatase H1 Increases Breast Cancer Sensitivity to Antiestrogens by Dephosphorylating Estrogen Receptor at Tyr537

A. Migliaccio, P. Suresh, Guan Chen, 2013, Molecular Cancer Therapeutics.

Cancer Biology and Signal Transduction Protein-Tyrosine Phosphatase H 1 Increases Breast Cancer Sensitivity to Antiestrogens by Dephosphorylating Estrogen Receptor at Tyr 537

A. Migliaccio, P. Suresh, Guan Chen, 2013 .

p38γ MAPK Is Essential for Aerobic Glycolysis and Pancreatic Tumorigenesis

Liwu Fu, F. Wang, S. Tsai, 2020, Cancer Research.

p38γ Mitogen-activated Protein Kinase Signals through Phosphorylating Its Phosphatase PTPH1 in Regulating Ras Protein Oncogenesis and Stress Response*

Songwang Hou, S. Mirza, P. Suresh, 2012, The Journal of Biological Chemistry.

p38γ Mitogen-activated Protein Kinase (MAPK) Confers Breast Cancer Hormone Sensitivity by Switching Estrogen Receptor (ER) Signaling from Classical to Nonclassical Pathway via Stimulating ER Phosphorylation and c-Jun Transcription*

Z. Basir, C. Myers, Jian Huang, 2012, The Journal of Biological Chemistry.

Kidney-Targeted Epoxyeicosatrienoic Acid Analog, EET-F01, Reduces Inflammation, Oxidative Stress, and Cisplatin-Induced Nephrotoxicity

J. Falck, J. Imig, Guan Chen, 2021, International journal of molecular sciences.

Antisense Oligonucleotides Demonstrate a Dominant Role of c-Ki-RAS Proteins in Regulating the Proliferation of Diploid Human Fibroblasts*

B. Monia, D. Stacey, Guan Chen, 1996, The Journal of Biological Chemistry.

Essential Role of p38γ in K-Ras Transformation Independent of Phosphorylation*

Jiahuai Han, D. Mercola, Jun Tang, 2005, Journal of Biological Chemistry.

PTPH1 dephosphorylates and cooperates with p38gamma MAPK to increase ras oncogenesis through PDZ-mediated interaction.

Rong-shan Li, Songwang Hou, Z. Basir, 2010, Cancer research.

The p38 MAPK stress pathway as a tumor suppressor or more?

Guan Chen, Mathew Loesch, 2008, Frontiers in bioscience : a journal and virtual library.

Identification of a ternary protein-complex as a therapeutic target for K-Ras-dependent colon cancer

Gang Li, Shixiu Wu, Songwang Hou, 2014, Oncotarget.

p38gamma mitogen-activated protein kinase integrates signaling crosstalk between Ras and estrogen receptor to increase breast cancer invasion.

S. Alkan, Jun Tang, Nicole M. Pohl, 2006, Cancer research.

p38 Isoforms Have Opposite Effects on AP-1-dependent Transcription through Regulation of c-Jun

Jiahuai Han, D. Choubey, R. Schultz, 2003, The Journal of Biological Chemistry.

p38 MAPK Activation Selectively Induces Cell Death in K-ras-mutated Human Colon Cancer Cells through Regulation of Vitamin D Receptor*

Jiahuai Han, S. Shirasawa, T. Sasazuki, 2004, Journal of Biological Chemistry.

The K-Ras effector p38γ MAPK confers intrinsic resistance to tyrosine kinase inhibitors by stimulating EGFR transcription and EGFR dephosphorylation

Songwang Hou, N. Yin, C. Myers, 2017, The Journal of Biological Chemistry.

Targeting an oncogenic kinase/phosphatase signaling network for cancer therapy

F. Wang, Xiaomei Qi, Guan Chen, 2018, Acta pharmaceutica Sinica. B.

p38γ MAPK Is a Therapeutic Target for Triple‐Negative Breast Cancer by Stimulation of Cancer Stem‐Like Cell Expansion

N. Yin, M. Dwinell, Jun Tang, 2015, Stem cells.

Ras stimulates DNA topoisomerase IIα through MEK: A link between oncogenic signaling and a therapeutic target

D. Suttle, D. Stacey, D. Templeton, 1999, Oncogene.

p38α Antagonizes p38γ Activity through c-Jun-dependent Ubiquitin-proteasome Pathways in Regulating Ras Transformation and Stress Response*

A. Cuenda, Rongshan Li, Songwang Hou, 2007, Journal of Biological Chemistry.

Estrogen Receptor Inhibits c-Jun-dependent Stress-induced Cell Death by Binding and Modifying c-Jun Activity in Human Breast Cancer Cells*

Jiahuai Han, R. Schultz, S. Borowicz, 2004, Journal of Biological Chemistry.

The p38 and JNK Pathways Cooperate to trans-Activate Vitamin D Receptor via c-Jun/AP-1 and Sensitize Human Breast Cancer Cells to Vitamin D3-induced Growth Inhibition*

Jiahuai Han, H. DeLuca, R. Schultz, 2002, The Journal of Biological Chemistry.

PTPH1 cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization

Rong-shan Li, Songwang Hou, A. Szabo, 2010, Oncogene.

Stress-induced c-Jun-dependent Vitamin D Receptor (VDR) Activation Dissects the Non-classical VDR Pathway from the Classical VDR Activity*

Nicole M. Pohl, R. Pramanik, Xiaomei Qi, 2007, Journal of Biological Chemistry.

Phosphorylation and Stabilization of Topoisomerase IIα Protein by p38γ Mitogen-activated Protein Kinase Sensitize Breast Cancer Cells to Its Poisons*

Z. Lou, Rongshan Li, Songwang Hou, 2011, The Journal of Biological Chemistry.

The p38 Pathway Provides Negative Feedback for Ras Proliferative Signaling*

Jiahuai Han, D. Stacey, M. Hitomi, 2000, The Journal of Biological Chemistry.

p38γ MAPK Cooperates with c-Jun in trans-Activating Matrix Metalloproteinase 9*

T. Iftner, A. Cuenda, Rong-shan Li, 2010, The Journal of Biological Chemistry.

MK2 Regulates Ras Oncogenesis through Stimulating ROS Production.

Yusuke Kobayashi, Xiaomei Qi, Guan Chen, 2012, Genes & cancer.

Tyrosine dephosphorylation enhances the therapeutic target activity of epidermal growth factor receptor (EGFR) by disrupting its interaction with estrogen receptor (ER)

R. Ma, N. Yin, Mei-Jie Zhang, 2015, Oncotarget.

Ras Is Active Throughout the Cell Cycle, but Is Able to Induce Cyclin D1 Only During G2 Phase

Andrew W. Stacey, G. Sa, D. Stacey, 2002, Cell cycle.

p38γ MAPK Inflammatory and Metabolic Signaling in Physiology and Disease

Xiaomei Qi, Guan Chen, 2023, Cells.

p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-proteasome pathways in regulating Ras transformation and stress response.

A. Cuenda, Rongshan Li, Songwang Hou, 2007, The Journal of biological chemistry.

p38γ MAPK is required for inflammation-associated colon tumorigenesis

J. Thomas, Y. Lu, S. Tsai, 2016, Oncogene.

PTPH1 dephosphorylates and cooperates with p38gamma MAPK to increase ras oncogenesis through PDZ-mediated interaction.

Rong-shan Li, Songwang Hou, Z. Basir, 2010, Cancer research.

Cell Cycle 1_1-Inside Pages

D. Stacey, M. Hitomi, J. Harwalkar, 2002 .