Jie Wu

ORCID: 0000-0002-2864-1606
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Protein Tyrosine Phosphatases
  • Lung Cancer Treatments and Mutations
  • Protein Kinase Regulation and GTPase Signaling
  • Melanoma and MAPK Pathways
  • PI3K/AKT/mTOR signaling in cancer
  • Galectins and Cancer Biology
  • RNA modifications and cancer
  • Cytokine Signaling Pathways and Interactions
  • Chronic Myeloid Leukemia Treatments
  • Chronic Lymphocytic Leukemia Research
  • Ubiquitin and proteasome pathways
  • Cancer Genomics and Diagnostics
  • Advanced biosensing and bioanalysis techniques
  • Sphingolipid Metabolism and Signaling
  • Click Chemistry and Applications
  • Cancer-related Molecular Pathways
  • Cancer, Hypoxia, and Metabolism
  • Signaling Pathways in Disease
  • interferon and immune responses
  • Glycosylation and Glycoproteins Research
  • Cancer Mechanisms and Therapy
  • Radical Photochemical Reactions
  • DNA and Nucleic Acid Chemistry
  • MicroRNA in disease regulation
  • RNA Interference and Gene Delivery

University of Oklahoma Health Sciences Center
2015-2025

Shenzhen University
2024

Xiamen University
2011-2022

Central South University
2014-2022

First Affiliated Hospital of Xi'an Jiaotong University
2022

Hunan Cancer Hospital
2018-2022

Jiangsu University
2022

First People's Hospital of Kunshan
2022

Nanjing Medical University
2022

Jiangsu Province Hospital
2022

Mitogen-activated protein (MAP) kinases p42 mapk and p44 are activated in cells stimulated with epidermal growth factor (EGF) other agents. A principal pathway for MAP kinase (MAPK) activation by EGF consists of sequential activations the guanine nucleotide exchange Sos, guanosine triphosphate binding Ras, Raf-1, MAPK (MKK), MAPK. Because adenosine 3′,5′-monophosphate (cAMP) does not activate has some opposing physiologic effects, effect increasing intracellular concentrations cAMP forskolin...

10.1126/science.7694366 article EN Science 1993-11-12

Mitogen-activated protein kinase (MAPK) cascades are activated by diverse extracellular signals and participate in the regulation of an array cellular programs. In this study, we investigated roles MAPKs induction phase II detoxifying enzymes chemicals. Treatment human hepatoma (HepG2) murine (Hepa1c1c7) cells withtert-butylhydroquinone (tBHQ) or sulforaphane (SUL), two potent enzyme inducers, stimulated activity signal-regulated 2 (ERK2) but not c-Jun N-terminal 1. tBHQ SUL also MAPK...

10.1074/jbc.274.39.27545 article EN cc-by Journal of Biological Chemistry 1999-09-01

Shp2 is a nonreceptor protein tyrosine phosphatase (PTP) encoded by the PTPN11 gene. It involved in growth factorinduced activation of mitogen-activated (MAP) kinases Erk1 and Erk2 (Erk1/2) has been implicated pathogenicity oncogenic bacterium Helicobacter pylori. Moreover, gain-of-function mutations have found childhood leukemias Noonan syndrome. Thus, small molecule PTP inhibitors are much needed reagents for evaluation as therapeutic target chemical biology studies function. By screening...

10.1124/mol.106.025536 article EN Molecular Pharmacology 2006-05-23

Signal transducers and activators of transcription (STATs) are factors that mediate normal biologic responses to cytokines growth factors. However, abnormal activation certain STAT family members, including Stat3, is increasingly associated with oncogenesis. In fibroblasts expressing the Src oncoprotein, Stat3 induces specific gene expression required for cell transformation. Although tyrosine kinase constitutive phosphorylation on tyrosine, Stat3-mediated regulation requires both serine...

10.1128/mcb.19.11.7519 article EN Molecular and Cellular Biology 1999-11-01

Noonan syndrome is a developmental disorder with dysmorphic facies, short stature, cardiac defects, and skeletal anomalies, which can be caused by missense PTPN11 mutations. encodes Src homology 2 domain-containing tyrosine phosphatase (SHP2 or SHP-2), protein that acts in signal transduction downstream to growth factor, hormone, cytokine receptors. We compared the functional effects of three syndrome–causative mutations on SHP2's activity, interaction binding partner, transduction. All SHP2...

10.1002/humu.20005 article EN Human Mutation 2004-01-01

Bif-1, a member of the endophilin B protein family, interacts with Bax and promotes interleukin-3 withdrawal-induced conformational change apoptosis when overexpressed in FL5.12 cells. Here, we provide evidence that Bif-1 plays regulatory role apoptotic activation not only but also Bak appears to be involved suppression tumorigenesis. Inhibition endogenous expression HeLa cells by RNA interference abrogated Bak, cytochrome c release, caspase 3 induced various intrinsic death signals. Similar...

10.1128/mcb.25.21.9369-9382.2005 article EN Molecular and Cellular Biology 2005-10-15

Self-healing polymeric hydrogels have the capability to recover their structures and functionalities upon injury, which are extremely attractive in emerging biomedical applications. This research reports a new kind of self-healing polypeptide based on self-assembly between cholesterol (Chol)-modified triblock poly(L-glutamic acid)-block-poly(ethylene glycol)-block-poly(L-glutamic acid) ((PLGA-b-PEG-b-PLGA)-g-Chol) β-cyclodextrin (β-CD)-modified (PLGA-g-β-CD). The hydrogel formation relied...

10.1021/acs.biomac.5b01287 article EN Biomacromolecules 2015-09-28

Abstract Patients treated with RET protein tyrosine kinase inhibitors (TKIs) selpercatinib or pralsetinib develop TKI resistance by secondary mutations alterative oncogenes, of which oncogenes pose a greater challenge for disease management because multiple potential mechanisms and the unclear tolerability drug combinations. A patient metastatic medullary thyroid carcinoma (MTC) harboring activation loop D898_E901del mutation was selpercatinib. Molecular alterations were monitored tissue...

10.1038/s41698-024-00563-4 article EN cc-by npj Precision Oncology 2024-03-04

Recent evidence suggests that reactive oxygen species (ROS) may function as second messengers in intracellular signal transduction pathways. We explored the possibility ROS were involved lysophosphatidic acid (LPA)-induced mitogen-activated protein (MAP) kinase signaling pathway HeLa cells. Antioxidant N-acetylcysteine inhibited LPA-stimulated MAP activity. Direct exposure of cells to hydrogen peroxide resulted a concentration- and time-dependent activation kinase. Inhibition catalase with...

10.1074/jbc.270.48.28499 article EN cc-by Journal of Biological Chemistry 1995-12-01

Epidermal growth factor (EGF) induces paxillin tyrosine dephosphorylation and Src activation, but the signaling pathways that mediate these responses were largely undefined. We found Gab1, a docking protein for SHP2 protein-tyrosine phosphatase in EGF-stimulated cells, was associated with paxillin. dephosphorylated caused dissociation of Csk, negative regulator Src, from had no effect on paxillin-Src association. A lower level Tyr-530 phosphorylation detected paxillin-associated cells....

10.1074/jbc.m312575200 article EN cc-by Journal of Biological Chemistry 2004-02-01

A major Grb2-associated binder-1 (Gab1) binding partner in epidermal growth factor (EGF)-stimulated cells is protein-tyrosine phosphatase (PTPase) SHP2, which contains tandem SH2 domains. The SHP2 PTPase activity required for activation of the extracellular signal-regulated kinase (ERK) subfamily mitogen-activated protein (MAP) by EGF. To investigate mechanism Gab1 and mediate ERK activation, we characterized Gab1-SHP2 interaction. We found that both Tyr-627 Tyr-659 were to ERK2 Far Western...

10.1074/jbc.m010275200 article EN cc-by Journal of Biological Chemistry 2001-06-01

Gab1-SHP2 association is required for Erk mitogen-activated protein kinase activation by several growth factors. interaction activates SHP2. However, an activated SHP2 still needs to associate with Gab1 mediate activation. It was unclear whether dephosphorylate a negative phosphorylation site on or the pleckstrin homology (PH) domain target it plasma membrane. We found that expression of fusion consisting PH and active (Gab1PH-SHP2DeltaN) induced constitutive Mek1 Erk2 Linking SHP2DeltaN...

10.1074/jbc.m110547200 article EN cc-by Journal of Biological Chemistry 2002-03-01

Preparation of milligram amounts [32P]p42mapk, phosphorylated at Tyr185 or diphosphorylated Tyr185/Thr183, for use as specific protein phosphatase substrates is described. Tyr- but not Thr-phosphorylated p42mapk, accumulates when ATP limiting. Furthermore, Tyr185-phosphorylated p42mapk exhibits an apparent 10-fold decrease in Km (46.6 +/- 6.6 nM) MAP kinase compared to that the dephospho form (approximately 476 nM). We conclude precedes Thr183 phosphorylation, and this prerequisite,...

10.1016/0014-5793(92)80828-5 article EN FEBS Letters 1992-07-13

Mitogen-activated protein (MAP) kinases are serine/threonine activated by dual phosphorylation on threonine and tyrosine residues. A MAP kinase (MKK1 or MEK1) has been identified as a dual-specificity that is sufficient to phosphorylate p42mapk p44mapk the regulatory Because of multiplicity isoforms diverse circumstances agonists leading their activation, we thought it unlikely single MKK could accommodate this complexity. Indeed, two bands with activity have previously after renaturation...

10.1128/mcb.13.8.4539 article EN Molecular and Cellular Biology 1993-08-01
Coming Soon ...