Results 41 to 50 of about 3,688,591 (305)
Molecular Oncology, EarlyView.The novel styrylquinazolinone‐based molecule W1B effectively suppresses glioblastoma by inhibiting IGF1R and EGFR. In high‐glucose microenvironments driving tumor resistance, W1B acts synergistically with the EGFR inhibitor dacomitinib. This combination safely blocks compensatory survival signaling in zebrafish xenograft models. Showcasing promising in
Patryk Rurka +9 more
wiley +1 more source
Identification of the protein kinases Pyk3 and Phg2 as regulators of the STATc-mediated response to hyperosmolarity [PDF]
, 2014 Cellular adaptation to changes in environmental osmolarity is crucial for cell survival. In Dictyostelium, STATc is a key regulator of the transcriptional response to hyperosmotic stress. Its phosphorylation and consequent activation is controlled by two
Christoph S Clemen +23 more
core +1 more source
Molecular Oncology, EarlyView.Breast cancer remains a major cause of cancer death in women, frequently developing endocrine therapy resistance. This study demonstrates that upregulated p21‐activated kinase 1 (PAK1) activity drives resistance to tamoxifen and long‐term estrogen deprivation in ER+ breast cancer models.
Luisa Schwarzmüller +10 more
wiley +1 more source
Protection against gamma-radiation injury by protein tyrosine phosphatase 1B
Redox Biology, 2018 Protein tyrosine phosphatase 1B (PTP1B) is widely expressed in mammalian tissues, in particular in immune cells, and plays a pleiotropic role in dephosphorylating many substrates.
Marina Mojena +10 more
doaj +1 more source
Protein Tyrosine Phosphatase Assays [PDF]
Current Protocols in Immunology, 2011 AbstractTyrosine phosphorylation and dephosphorylation of proteins play a critical role in many processes of the immune system, from early development to fully differentiated effector function. Since the opposing actions of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) determine the steady‐state level of tyrosine ...
openaire +2 more sources
Characterization of the function of a novel protein tyrosine phophatase predicted by the genome sequence of Arabidopsis thaliana [PDF]
, 2003 Covalent modification of proteins by reversible phosphorylation, catalysed by specific protein kinases and phosphatases, is an important mechanism for enzyme activity regulation in metabolism and signalling pathways.
Reignoux, Sabrina Natacha Aurore
core
Molecular Oncology, EarlyView.Single‐cell DNA methylation (scDNAme) profiling maps epimutational clonal evolution, revealing mechanisms of malignancy and therapeutic resistance across diverse cancer types. By providing a high‐resolution landscape of intratumoral heterogeneity, these technologies empower precise patient stratification, guide the development of enhanced ...
Ik Soo Kim
wiley +1 more source
Protein tyrosine phosphatase-1B modulates pancreatic β-cell mass.
PLoS ONE, 2014 Protein tyrosine phosphatase 1B (PTP1B) is a negative regulator of the insulin signalling pathway. It has been demonstrated that PTP1B deletion protects against the development of obesity and Type 2 Diabetes, mainly through its action on peripheral ...
Rebeca Fernandez-Ruiz +3 more
doaj +1 more source
Mutations that impair Eyes absent tyrosine phosphatase activity in vitro reduce robustness of retinal determination gene network output in Drosophila. [PDF]
PLoS ONE, 2017 A limited collection of signaling networks and transcriptional effectors directs the full spectrum of cellular behaviors that comprise development. One mechanism to diversify regulatory potential is to combine multiple biochemical activities into the ...
Trevor L Davis +2 more
doaj +1 more source
Functional characterisation of a predicted chloroplastic plant protein phosphatase [PDF]
, 2009 The phosphatase AtPTPKISI is involved in the control of starch metabolism in Arabidopsis thaliana leaves at night. The SEX4 (Starch Excess 4) mutants, lacking this predicted phosphatase, have strongly reduced rates of starch metabolism.
Seymour, Michael David John
core