about
Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transferPathogenic Cysteine Removal Mutations in FGFR Extracellular Domains Stabilize Receptor Dimers and Perturb the TM Dimer Structure.How IGF-1 activates its receptor.Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation.VEGFR-2 conformational switch in response to ligand binding.FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Uninduced high-yield bacterial expression of fluorescent proteins.The FRET signatures of noninteracting proteins in membranes: simulations and experiments.Intracellular Domain Contacts Contribute to Ecadherin Constitutive Dimerization in the Plasma Membrane.Computational Systems Biochemistry: Beyond the Static Interactome.VEGF-A121a binding to Neuropilins - A concept revisited.Parallels and Distinctions in FGFR, VEGFR, and EGFR Mechanisms of Transmembrane Signaling.A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors.Light scattering artefacts in a funnel phantom using optical CTModelling optical scattering artefacts for varying pathlength in a gel dosimeter phantomA preliminary study of the measurement of slice-width dose profiles (SWDP) on diagnostic x-ray CT scanners using PAGAT polymer gel dosimeters with optical CT read-outTumor and endothelial cells collaborate via transcellular receptor complexesMaintaining confidence in the reporting of scientific outputsPreprints are good for science and good for the publicOn the value of preprints: An early career researcher perspectiveMitigating the impact of conference and travel cancellations on researchers' futuresEvaluating features of scientific conferences: A call for improvementsA survey-based analysis of the academic job market
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sarvenaz Sarabipour
@ast
Sarvenaz Sarabipour
@en
Sarvenaz Sarabipour
@es
Sarvenaz Sarabipour
@nl
Sarvenaz Sarabipour
@sl
type
label
Sarvenaz Sarabipour
@ast
Sarvenaz Sarabipour
@en
Sarvenaz Sarabipour
@es
Sarvenaz Sarabipour
@nl
Sarvenaz Sarabipour
@sl
altLabel
Sarvnaz Sarabi Pour
@en
prefLabel
Sarvenaz Sarabipour
@ast
Sarvenaz Sarabipour
@en
Sarvenaz Sarabipour
@es
Sarvenaz Sarabipour
@nl
Sarvenaz Sarabipour
@sl
P1053
H-2992-2015
P106
P31
P3829
P496
0000-0001-5097-5509