Lukasz Opalinski
University of Wrocław
Binding siteLigand (biochemistry)PhosphorylationTargeted drug deliveryInternalizationFunction (biology)MutantProtein engineeringCell signalingCytotoxic T cellIntegral membrane proteinSortaseVesicular transport proteinReceptorKinaseChemistryFGF1IntegrinIn vitroGrowth factorTyrosine phosphorylationAnisomycinSortase AFibroblastMonomethyl auristatin ETargeted therapyEndocytosisExtracellularIntegrin bindingProtein kinase domainFibroblast growth factor receptor 1Plasma protein bindingBiochemistryMAPK/ERK pathwayCell growthSignal transductionFibroblast growth factorEndocytic cycleFibroblast growth factor receptorCell divisionBiologyCell biologyCancer cell
8Publications
3H-index
21Citations
Publications 8
Newest
#1Natalia Porębska (UWr: University of Wrocław)H-Index: 3
#2Marta Pozniak (UWr: University of Wrocław)H-Index: 1
Last. Lukasz Opalinski (UWr: University of Wrocław)H-Index: 3
view all 10 authors...
Abstract Fibroblast growth factor receptors (FGFRs) are integral membrane proteins involved in various biological processes including proliferation, migration and apoptosis. There are a number of regulatory mechanisms of FGFR signaling, which tightly control the specificity and duration of transmitted signals. The effect of the FGFRs spatial distribution in the plasma membrane on receptor-dependent functions is still largely unknown. We have demonstrated that oligomerization of FGF1 with coiled-...
1 CitationsSource
Cancer is currently the second most common cause of death worldwide. The hallmark of cancer cells is the presence of specific marker proteins such as growth factor receptors on their surface. This feature enables development of highly selective therapeutics, the protein bioconjugates, composed of targeting proteins (antibodies or receptor ligands) connected to highly cytotoxic drugs by a specific linker. Due to very high affinity and selectivity of targeting proteins the bioconjugates recognize ...
Source
#1Martyna SochackaH-Index: 2
#2Lukasz OpalinskiH-Index: 3
Last. Malgorzata ZakrzewskaH-Index: 17
view all 8 authors...
Source
#1Marta Pozniak (UWr: University of Wrocław)H-Index: 1
#2Aleksandra Sokolowska-Wedzina (UWr: University of Wrocław)H-Index: 7
Last. Lukasz Opalinski (UWr: University of Wrocław)H-Index: 3
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Fibroblast growth factor receptor 1 (FGFR1) transmits signals through the plasma membrane regulating essential cellular processes like division, motility, metabolism and death. Overexpression of FGFR1 is observed in numerous tumors and thus constitutes an attractive molecular target for selective cancer treatment. Targeted anti-cancer therapies aim for the precise delivery of drugs into cancer cells, sparing the healthy ones and thus limiting unwanted side effects. One of the key steps in target...
3 CitationsSource
#1Martyna Sochacka (UWr: University of Wrocław)H-Index: 2
#2Lukasz Opalinski (UWr: University of Wrocław)H-Index: 3
Last. Malgorzata Zakrzewska (UWr: University of Wrocław)H-Index: 17
view all 8 authors...
Fibroblast growth factors (FGFs) via their receptors (FGFRs) transduce signals from the extracellular space to the cell interior, modulating pivotal cellular processes such as cell proliferation, motility, metabolism and death. FGF superfamily includes a group of fibroblast growth factor homologous factors (FHFs), proteins whose function is still largely unknown. Since FHFs lack the signal sequence for secretion and are unable to induce FGFR-dependent cell proliferation, these proteins were cons...
6 CitationsSource
#1Anna Szlachcic (UWr: University of Wrocław)H-Index: 10
#2Martyna Sochacka (UWr: University of Wrocław)H-Index: 2
Last. Malgorzata Zakrzewska (UWr: University of Wrocław)H-Index: 17
view all 7 authors...
Fibroblast growth factor 1 (FGF1) has been shown to interact with integrin αvβ3 through a specific binding site, involving Arg35 residue. The FGF1 mutant (R35E) with impaired integrin binding was found to be defective in its proliferative response, although it was still able to interact with FGF receptors (FGFR) and heparin and induce the activation of downstream signaling pathways. Here, we demonstrate that the lack of mitogenic potential of R35E mutant is directly caused by its decreased therm...
4 CitationsSource
#1Malgorzata Zakrzewska (UWr: University of Wrocław)H-Index: 17
#2Lukasz Opalinski (UWr: University of Wrocław)H-Index: 3
Last. Antoni G Wiedlocha (University of Oslo)H-Index: 23
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Mitogen-activated protein kinases (MAPK): Erk1 and Erk2 are key players in negative-feedback regulation of fibroblast growth factor (FGF) signaling. Upon activation, Erk1 and Erk2 directly phosphorylate FGF receptor 1 (FGFR1) at a specific serine residue in the C-terminal part of the receptor, substantially reducing the tyrosine phosphorylation in the receptor kinase domain and its signaling. Similarly, active Erks can also phosphorylate multiple threonine residues in the docking protein FGF rec...
7 CitationsSource
#1Lukasz Opalinski (UWr: University of Wrocław)H-Index: 3
#2Martyna Szczepara (UWr: University of Wrocław)H-Index: 3
Last. Jacek Otlewski (UWr: University of Wrocław)H-Index: 44
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Abstract Fibroblast growth factors (FGFs) and their plasma membrane-localized receptors (FGFRs) transduce signals that regulate developmental processes and metabolism. In numerous cancer types genetic aberrations of FGFR1 lead to its uncontrolled activation. To circumvent the unrestrained signal transduction, several intramolecular inhibitory mechanisms within FGFR1 have evolved. In vitro experiments with receptor truncation have demonstrated that the N-terminal D1 domain of FGFR1 negatively reg...
4 CitationsSource