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Jacques Neefjes

Researcher at Leiden University Medical Center

Publications -  352
Citations -  34927

Jacques Neefjes is an academic researcher from Leiden University Medical Center. The author has contributed to research in topics: MHC class I & Antigen presentation. The author has an hindex of 95, co-authored 331 publications receiving 31500 citations. Previous affiliations of Jacques Neefjes include University of Amsterdam & Netherlands Cancer Institute.

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Fluorescent probes for proteolysis: tools for drug discovery.

TL;DR: This work describes various strategies to follow protease activities in cells and organisms and describes progress in the development of fluorescent probes.
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PKA-induced resistance to tamoxifen is associated with an altered orientation of ERα towards co-activator SRC-1

TL;DR: It is demonstrated that phosphorylation of S305 in ERα by PKA leads to an altered orientation between ERα and its coactivator SRC‐1, which renders the transcription complex active in the presence of tamoxifen.
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The EGFR odyssey - from activation to destruction in space and time.

TL;DR: This Review follows the epidermal growth factor (EGF) receptor (EGFR) from ligand engagement, through its voyage on endosomes and, ultimately, to its destruction in the lysosome.
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Spatial Separation of HLA-DM/HLA-DR Interactions within MIIC and Phagosome-Induced Immune Escape

TL;DR: The absence of HLA-DR/DM interactions at the limiting membrane prevents local loading of MHC class II molecules in phagosomes, which may allow these bacteria to successfully evade the immune system.
Journal Article

Phosphorylated peptides can be transported by TAP molecules, presented by class I MHC molecules, and recognized by phosphopeptide-specific CTL.

TL;DR: This study examined the effect of phosphorylation on TAP transport, binding to class I MHC molecules, and recognition by CTL of peptide fragments from known phosphorylated oncogene proteins or virus phosphoproteins, and generated phosphopeptide-specific CTL that discriminate between the phosphorylate and the nonphosphorylated versions of the peptide.