John Foerster

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

Alexander Trockenbacher, Vanessa Suckow, John Foerster et al. · Nature Genetics · 2001 · 289 citations

Genome Instability, Mendelian Disorder, Genetic Disorder +10

Mutation of His-105 in the beta 1 subunit yields a nitric oxide-insensitive form of soluble guanylyl cyclase.

Barbara J. Wedel, P. Humbert, Christian Harteneck et al. · Proceedings of the National Academy of Sciences · 1994 · 250 citations · Full text

Molecular Physiology, Biochemistry, Reactive Nitrogen Specie +14

Optimized production and concentration of lentiviral vectors containing large inserts

Nadya Al‐Yacoub, Małgorzata Romanowska, Natalie Haritonova et al. · The Journal of Gene Medicine · 2007 · 136 citations

Viral Replication, Engineering, Synthetic Virology +16

The Opitz syndrome gene product, MID1, associates with microtubules

Susann Schweiger, John Foerster, Tanja Lehmann et al. · Proceedings of the National Academy of Sciences · 1999 · 136 citations · Full text

Functional Domains of Soluble Guanylyl Cyclase

Barbara J. Wedel, Christian Harteneck, John Foerster et al. · Journal of Biological Chemistry · 1995 · 127 citations · Full text