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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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MHC class II molecules on the move for successful antigen presentation

TL;DR: The mechanisms regulating loading and intracellular trafficking of MHC II are discussed and a unique and complex series of reactions are discussed.
Journal Article

Quantifying exosome secretion from single cells reveals a modulatory role for GPCR signaling (vol 217, pg 1129, 2018)

TL;DR: This study designs tetraspanin-based pH-sensitive optical reporters that detect MVB–PM fusion using live total internal reflection fluorescence and dynamic correlative light–electron microscopy and highlights the modulatory dynamics of MVB exocytosis that will help to increase the understanding of exosome physiology and identify druggable targets in exosomal pathologies.
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Moving and positioning the endolysosomal system

TL;DR: The dynamics of endolysosomal organelles should no longer be studied in isolation, but in the context of the whole endomembrane system.
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Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling.

TL;DR: This work shows that the bulk of the translocated peptides are rapidly released from the ER by a mechanism that requires adenosine triphosphate (ATP) and that could not be inhibited by GTP gamma S, and suggests that peptides that are too long for binding to class I molecules in the ER can be trimmed further in theER lumen or transported back to the cytosol.
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Translocation of long peptides by transporters associated with antigen processing (TAP)

TL;DR: TAP binds and preferentially translocates peptides with a length suitable for binding to MHC class I molecules, but peptides that are considerably longer may also be substrates.