Cyclic trans-phosphorylation in a homodimer as the predominant mechanism of EGFRvIII action and regulation.

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Cyclic trans-phosphorylation in a homodimer as the predominant mechanism of EGFRvIII action and regulation.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

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Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@nl

type

Item

label

Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@en

Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@nl

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Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@en

Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@nl

P1476

Cyclic trans-phosphorylation i ...... GFRvIII action and regulation.

@en

P2093

Anna Lenart

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Cezary Treda

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Ewelina Stoczynska-Fidelus

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Kamila Rosiak

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Maciej Smolarz

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Wojciech Stec

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P2860

In situ analysis of mutant EGFRs prevalent in glioblastoma multiforme reveals aberrant dimerization, activation, and differential response to anti-EGFR targeted therapy

EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment

EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma

The epidermal growth factor receptor variant III (EGFRvIII): where wild things are altered

Inhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR Signaling

Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain

Glycosylation-induced conformational modification positively regulates receptor-receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells.

EGFR Activation Leads to Cell Death Independent of PI3K/AKT/mTOR in an AD293 Cell Line

A small molecule-kinase interaction map for clinical kinase inhibitors

Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization

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8560-8572

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scholarly article

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10.18632/ONCOTARGET.24058

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P407

English

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P478

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P577

2018-01-06T00:00:00Z

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P698

29492217

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P921

phosphorylation

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5823601

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