Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them

JM Westerfield, FN Barrera - Journal of Biological Chemistry, 2020 - ASBMB
Single-pass membrane receptors contain extracellular domains that respond to external
stimuli and transmit information to intracellular domains through a single transmembrane …

Supramolecular Self‐Assembly‐Facilitated Aggregation of Tumor‐Specific Transmembrane Receptors for Signaling Activation and Converting Immunologically Cold …

J Li, Y Fang, Y Zhang, H Wang, Z Yang… - Advanced …, 2021 - Wiley Online Library
Supramolecular self‐assembling peptide systems are attracting increasing interest in the
field of cancer theranostics. Additionally, transformation of the immunologically cold tumor …

A review on targeting nanoparticles for breast cancer

HGJ Alqaraghuli, S Kashanian… - Current pharmaceutical …, 2019 - ingentaconnect.com
Chemotherapeutic agents have been used extensively in breast cancer remedy. However,
most anticancer drugs cannot differentiate between cancer cells and normal cells, leading to …

The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures

DR Singh, P Kanvinde, C King, EB Pasquale… - Communications …, 2018 - nature.com
The EphA2 receptor tyrosine kinase is capable of activating multiple diverse signaling
pathways with roles in processes such as tissue homeostasis and cancer. EphA2 is known …

Understanding the FRET signatures of interacting membrane proteins

C King, V Raicu, K Hristova - Journal of Biological Chemistry, 2017 - ASBMB
FRET is an indispensable experimental tool for studying membrane proteins. Currently, two
models are available for researchers to determine the oligomerization state of membrane …

The efficacy of receptor tyrosine kinase EphA2 autophosphorylation increases with EphA2 oligomer size

E Zapata-Mercado, G Biener, DM McKenzie… - Journal of Biological …, 2022 - ASBMB
The receptor tyrosine kinase (RTK) EphA2 is expressed in epithelial and endothelial cells
and controls the assembly of cell–cell junctions. EphA2 has also been implicated in many …

[HTML][HTML] P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding

V Vu, T Light, B Sullivan, D Greiner, K Hristova… - Current Biology, 2021 - cell.com
Cadherins are essential adhesion proteins that regulate tissue cohesion and paracellular
permeability by assembling dense adhesion plaques at cell-to-cell contacts. Adherens …

Spatial organization-dependent EphA2 transcriptional responses revealed by ligand nanocalipers

T Verheyen, T Fang, D Lindenhofer… - Nucleic acids …, 2020 - academic.oup.com
Ligand binding induces extensive spatial reorganization and clustering of the EphA2
receptor at the cell membrane. It has previously been shown that the nanoscale spatial …

Dimerization of the Trk receptors in the plasma membrane: effects of their cognate ligands

F Ahmed, K Hristova - Biochemical Journal, 2018 - portlandpress.com
Receptor tyrosine kinases (RTKs) are cell surface receptors which control cell growth and
differentiation, and play important roles in tumorigenesis. Despite decades of RTK research …

Y772 phosphorylation of EphA2 is responsible for EphA2-dependent NPC nasopharyngeal carcinoma growth by Shp2/Erk-1/2 signaling pathway

YP **ang, T **ao, QG Li, SS Lu, W Zhu, YY Liu… - Cell death & …, 2020 - nature.com
EphA2 is an important oncogenic protein and emerging drug target, but the oncogenic role
and mechanism of ligand-independent phosphorylation of EphA2 at tyrosine 772 (pY772 …