M
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.
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Journal ArticleDOI
Dual specificity phosphatases: a gene family for control of MAP kinase function
TL;DR: Dual specificity phosphatases are an emerging subclass of the protein tyrosine phosphatase (PTP) gene superfam‐ily, which appears to be selective for dephosphorylating the critical phosphothreonine and phosphoty‐rosine residues within MAP kinases.
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Blockade of PI3Kgamma suppresses joint inflammation and damage in mouse models of rheumatoid arthritis
Montserrat Camps,Thomas Rückle,Hong Ji,Vittoria Ardissone,Felix Rintelen,Jeffrey P. Shaw,Chiara Ferrandi,Christian Chabert,Corine Gillieron,Bernard Françon,Thierry Martin,Denise Gretener,Dominique Perrin,Didier Leroy,Pierre-Alain Vitte,Emilio Hirsch,Matthias P. Wymann,Rocco Cirillo,Matthias Schwarz,Christian Rommel +19 more
TL;DR: It is shown that Pik3cg−/− mice are largely protected in mouse models of rheumatoid arthritis; this protection correlates with defective neutrophil migration, further validating PI3Kγ as a therapeutic target.
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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase
Montserrat Camps,Anthony Nichols,Corine Gillieron,Bruno Antonsson,Marco Muda,Christian Chabert,Ursula Boschert,Steve Arkinstall +7 more
TL;DR: Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases and was resistant to enzymatic inactivation by MKP.
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Targeting dual-specificity phosphatases: manipulating MAP kinase signalling and immune responses
TL;DR: From a drug discovery perspective, DUSP family members are promising drug targets for manipulating MAPK-dependent immune responses in a cell-type and disease-context-dependent manner, to either boost or subdueimmune responses in cancers, infectious diseases or inflammatory disorders.
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Bcl-2 Undergoes Phosphorylation by c-Jun N-terminal Kinase/Stress-activated Protein Kinases in the Presence of the Constitutively Active GTP-binding Protein Rac1
Kinsey Maundrell,Bruno Antonsson,Edith Magnenat,Montserrat Camps,Marco Muda,Christian Chabert,Corine Gillieron,Ursula Boschert,Elizabeth Vial-Knecht,Jean-Claude Martinou,Steve Arkinstall +10 more
TL;DR: This is the first report of Bcl-2 phosphorylation by the JNK/SAPK class of MAP kinases and could indicate a key modification allowing control of B cl-2 function by cell surface receptors, Rho family GTPases, and/or cellular stresses.