Article

Altering the bilayer motif in ERBB2 HER2 TMD and in ErbB HER TMD dimer causing in vitro and in vivo tumor suppression

2020-03-05

Abstract excerpt

Human ERBB2 is a transmembrane signaling tyrosine kinase receptor, which seems an ideal target of human WNT16B, the secreted growth factor possibly causes transmembrane domain (TMD) mutations. There is a strong relationship between the chemical nature of the TMD mutations and the potency with which they activate HER2. In silico , we modeled the possible docking conformation of human WNT16B and human ERBB2 TMD hom...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: b614cc91-2473-50c8-a3c0-a2496d4f22fc
DOI: 10.1101/2020.03.05.978080

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Altering the bilayer motif in ERBB2 HER2 TMD and in ErbB HER TMD dimer causing in vitro and in vivo tumor suppressionDOI 10.1101/2020.03.05.978080Read

Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.Semantic proximity Read

Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association.Semantic proximity Read

Engineered bivalent ligands to bias ErbB receptor-mediated signaling and phenotypes.Semantic proximity Read

A putative molecular-activation switch in the transmembrane domain of erbB2.Semantic proximity Read

A systematic analysis of the resistance and sensitivity of HER2YVMA receptor tyrosine kinase mutant to tyrosine kinase inhibitors in HER2-positive lung cancer.Semantic proximity Read

Rational design of heterodimeric receptors capable of activating target signaling molecules.Semantic proximity Read

Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors.Semantic proximity Read

Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain.Semantic proximity Read

Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.Semantic proximity Read

In silico molecular docking study of natural compounds on wild and mutated epidermal growth factor receptorSemantic proximity Read

Binding of human recombinant mutant soluble ectodomain of FGFR2IIIc to c subtype of FGFRs: implications for anticancer activity.Semantic proximity Read

Synergy between trastuzumab and pertuzumab for human epidermal growth factor 2 (Her2) from colocalization: an in silicobased mechanismSemantic proximity Read