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Joseph Schlessinger

Researcher at Max Planck Society

Publications -  59
Citations -  8274

Joseph Schlessinger is an academic researcher from Max Planck Society. The author has contributed to research in topics: Receptor & Epidermal growth factor. The author has an hindex of 39, co-authored 59 publications receiving 8197 citations. Previous affiliations of Joseph Schlessinger include National Institutes of Health & Research Triangle Park.

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EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling.

TL;DR: EGF-induced tyrosine phosphorylation of PLC-II may be a regulatory event linking the tyrosinesine kinase activity of EGF receptor to the PIP2 hydrolysis signaling pathway.
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Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors.

TL;DR: The complete cDNA cloning of two human genes previously designated flg and bek is reported, indicating that bek and flg bind either aFGF or bFGF with dissociation constants of (2‐15) x 10(‐11) M.
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Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing.

TL;DR: A single amino acid substitution rendered a "down-regulated" receptor into a receptor that can recycle from cytoplasmic compartment back to the cell surface, suggesting that degradation of normal EGF receptors after endocytosis is due to the kinase activity endogenous to this receptor.
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Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body

TL;DR: It is concluded that sorting of internalized receptor for degradation or recycling can occur through spatial segregation within the MVB, and sorting of EGF-R is controlled by tyrosine kinase activity.
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Signal Transduction Due to HIV-1 Envelope Interactions with Chemokine Receptors CXCR4 or CCR5

TL;DR: The results presented here provide the first evidence for activation of an intracellular signaling event that can initiate multiple signaling pathways as a consequence of contact between HIV-1 and chemokine receptors.