Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them
Single-pass membrane receptors contain extracellular domains that respond to external
stimuli and transmit information to intracellular domains through a single transmembrane …
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 …
field of cancer theranostics. Additionally, transformation of the immunologically cold tumor …
A review on targeting nanoparticles for breast cancer
Chemotherapeutic agents have been used extensively in breast cancer remedy. However,
most anticancer drugs cannot differentiate between cancer cells and normal cells, leading to …
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
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 …
pathways with roles in processes such as tissue homeostasis and cancer. EphA2 is known …
Understanding the FRET signatures of interacting membrane proteins
FRET is an indispensable experimental tool for studying membrane proteins. Currently, two
models are available for researchers to determine the oligomerization state of membrane …
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 …
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
Cadherins are essential adhesion proteins that regulate tissue cohesion and paracellular
permeability by assembling dense adhesion plaques at cell-to-cell contacts. Adherens …
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 …
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 …
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 …
and mechanism of ligand-independent phosphorylation of EphA2 at tyrosine 772 (pY772 …