BYON4228 is a pan-allelic antagonistic SIRPα antibody that potentiates destruction of antibody-opsonized tumor cells and lacks binding to SIRPγon T cells

Autor: Mary J van Helden, Seline A Zwarthoff, Roel J Arends, Inge M J Reinieren-Beeren, Marc C B C Paradé, Lilian Driessen-Engels, Karin de Laat-Arts, Désirée Damming, Ellen W H Santegoeds-Lenssen, Daphne W J van Kuppeveld, Imke Lodewijks, Hugo Olsman, Hanke L Matlung, Katka Franke, Ellen Mattaar-Hepp, Marloes E M Stokman, Benny de Wit, Dirk H R F Glaudemans, Daniëlle E J W van Wijk, Lonnie Joosten-Stoffels, Jan Schouten, Paul J Boersema, Monique van der Vleuten, Jorien W H Sanderink, Wendela A Kappers, Diels van den Dobbelsteen, Marco Timmers, Ruud Ubink, Gerard J A Rouwendal, Gijs Verheijden, Miranda M C van der Lee, Wim H A Dokter, Timo K van den Berg

Publikováno v: van Helden, M J, Zwarthoff, S A, Arends, R J, Reinieren-Beeren, I M J, Paradé, M C B C, Driessen-Engels, L, de Laat-Arts, K, Damming, D S, Santegoeds-Lenssen, E W H, van Kuppeveld, D W J, Lodewijks, I, Olsman, H, Matlung, H L, Franke, K, Mattaar-Hepp, E, Stokman, M E M, de Wit, B, Glaudemans, D H R F, van Wijk, D E J W, Joosten-Stoffels, L, Schouten, J, Boersema, P J, van der Vleuten, M, Sanderink, J W H, Kappers, W A, van den Dobbelsteen, D, Timmers, M, Ubink, R, Rouwendal, G J A, Verheijden, G, van der Lee, M M C, Dokter, W H A & van den Berg, T K 2023, ' BYON4228 is a pan-allelic antagonistic SIRPα antibody that potentiates destruction of antibody-opsonized tumor cells and lacks binding to SIRPγon T cells ', Journal for Immunotherapy of Cancer, vol. 11, no. 4, jitc-2022-006567 . https://doi.org/10.1136/jitc-2022-006567

BackgroundPreclinical studies have firmly established the CD47-signal-regulatory protein (SIRP)α axis as a myeloid immune checkpoint in cancer, and this is corroborated by available evidence from the first clinical studies with CD47 blockers. Howeve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f6e6308ed606888d418126a12792c8
https://research.vumc.nl/en/publications/67116c0e-064c-4154-86d3-6797beec296d

Structural and functional integrity of the coxsackievirus B3 oriR: spacing between coaxial RNA helices

Autor: Dirk H. R. F. Glaudemans, Willem J. G. Melchers, Frank J. M. van Kuppeveld, Hans A. Heus, Mark J. M. van Ooij

Publikováno v: Journal of General Virology, 87, 689-95
Journal of General Virology, 87, Pt 3, pp. 689-95

The enterovirusoriR is composed of two helices, X and Y, anchored by a kissing (K) interaction. For properoriR function, certain areas of these helices should be specifically oriented towards each other. It was hypothesized that the single-stranded n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7f2d73139344148065a7a517a7d0b10
https://pubmed.ncbi.nlm.nih.gov/16476992

Mutational analysis of different regions in the coxsackievirus 2B protein: requirements for homo-multimerization, membrane permeabilization, subcellular localization, and virus replication

Autor: Arjan S, de Jong, Willem J G, Melchers, Dirk H R F, Glaudemans, Peter H G M, Willems, Frank J M, van Kuppeveld

Publikováno v: The Journal of biological chemistry. 279(19)

The coxsackievirus 2B protein is a small hydrophobic protein (99 amino acids) that increases host cell membrane permeability, possibly by forming homo-multimers that build membrane-integral pores. Previously, we defined the functional role of the two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2a9db631b8bcb4074b1187cee8bf7c46
https://pubmed.ncbi.nlm.nih.gov/14976211