(Q24319831)

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Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family

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scholarly article

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Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family (English)

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epidermal growth factor receptor

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GOA release 2020-03-11

Erb-b2 receptor tyrosine kinase 2

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GOA release 2020-03-11

identical protein binding

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GOA release 2020-03-11

3

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5

object named as

Ola Söderberg

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Karl-Johan Leuchowius

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object named as

Karl-Johan Leuchowius

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Irene Weibrecht

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object named as

Irene Weibrecht

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author name string

Lars Gedda

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language of work or name

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publication date

October 2009

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Cytometry Part A

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75

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833-9

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10

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A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor

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The EGF receptor family as targets for cancer therapy

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The ErbB receptors and their role in cancer progression.

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ERBB2 oncogene in human breast cancer and its clinical significance

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The EGFR family and its ligands in human cancer. signalling mechanisms and therapeutic opportunities

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ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling

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ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors.

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Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy

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Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding.

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Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements.

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In situ detection of phosphorylated platelet-derived growth factor receptor beta using a generalized proximity ligation method.

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Direct observation of individual endogenous protein complexes in situ by proximity ligation

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The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation

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Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth

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Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor

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Ligand-induced, receptor-mediated dimerization and activation of EGF receptor

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The EGF receptor family: spearheading a merger of signaling and therapeutics

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All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells.

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Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis

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Quantitative multiplexed analysis of ErbB family coexpression for primary breast cancer prognosis in a large retrospective cohort

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Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis

1 reference

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Two-sided fluorescence resonance energy transfer for assessing molecular interactions of up to three distinct species in confocal microscopy

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Identifiers

10.1002/CYTO.A.20771

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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