Xiaomei Qi

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.

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.

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.

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.

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.

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.

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.

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.