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Montserrat Camps

Researcher at Merck Serono

Publications -  73
Citations -  8670

Montserrat Camps is an academic researcher from Merck Serono. The author has contributed to research in topics: Mitogen-activated protein kinase & MAP2K7. The author has an hindex of 37, co-authored 73 publications receiving 8263 citations. Previous affiliations of Montserrat Camps include University of Barcelona & Merck KGaA.

Papers
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Journal ArticleDOI

Dopamine D1 and D2 receptors visualized in MPTP treated C57 mice by in vitro autoradiography: lack of evidence of receptor modifications in parkinsonian mice.

TL;DR: A compensatory mechanism of the surviving dopaminergic neurones as well as the participation of spare receptors is suggested to explain the lack of receptor modification after the lesion obtained as seen by the striatal reduction of dopamine and metabolites content, after MPTP administration.
Patent

Novel scintillation proximity assays for aminoglycoside binding molecules (abms)

TL;DR: In this article, the scintillation proximity effect is exploited to identify and quantify Aminoglycoside Binding Molecules (ABMs), enzymes modifying such molecules, and compounds modulating the interaction between ABMs and either enzymes or aminoglycosides.
Journal ArticleDOI

Effect of age and cinnarizine treatment on brain dopamine receptors.

TL;DR: Chronic treatment with cinnarizine alters both D1 and D2 receptor densities, with a higher sensitivity of the D1 subtype, which could indicate that the interactions between dopamine receptor subtypes may be necessary for the full expression of behavioral events mediated by the D2 receptors.
Journal ArticleDOI

THU0275 Pharmacodynamic Modeling of BTK Occupancy versus Efficacy in RA and SLE Models Using The Novel Specific BTK Inhibitor M2951

TL;DR: In mouse models of RA and SLE, M2951 displayed robust efficacy as demonstrated by a marked reduction of disease severity, and may inform rational dose decisions as M29 51 is advanced for development in rheumatologic diseases.
Patent

Pharmaceutically active sulfonamide derivatives bearing both lipophilic and ionisable moieties as inhibitors of Protein Jun-kinases

TL;DR: In this paper, the authors have proposed sulfonamide derivatives having a lipophilic moiety and which are substantially soluble under physiological conditions for use as pharmaceutically active compounds.