T
Teresa Carlomagno
Researcher at Leibniz University of Hanover
Publications - 139
Citations - 4327
Teresa Carlomagno is an academic researcher from Leibniz University of Hanover. The author has contributed to research in topics: RNA & Nuclear magnetic resonance spectroscopy. The author has an hindex of 37, co-authored 132 publications receiving 3787 citations. Previous affiliations of Teresa Carlomagno include Leibniz Institute for Neurobiology & Massachusetts Institute of Technology.
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Journal ArticleDOI
Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity.
Cecilia Ballaré,Martin Lange,Audrone Lapinaite,Glòria Mas Martín,Lluis Morey,Gloria Pascual,Robert Liefke,Bernd Simon,Yang Shi,Or Gozani,Teresa Carlomagno,Salvador Aznar Benitah,Salvador Aznar Benitah,Luciano Di Croce,Luciano Di Croce +14 more
TL;DR: It is shown that direct recognition of methylated histone H3 Lys36 (H3K36me), a mark associated with activation, by thePRC2 subunit Phf19 is required for the full enzymatic activity of the PRC2 complex.
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Argyrin a reveals a critical role for the tumor suppressor protein p27kip1 in mediating antitumor activities in response to proteasome inhibition.
Irina Nickeleit,Steffen Zender,Florenz Sasse,Robert Geffers,Gudrun Brandes,Inga Sörensen,Heinrich Steinmetz,Stefan Kubicka,Teresa Carlomagno,Dirk Menche,Ines Gütgemann,Jan Buer,Achim Gossler,Michael P. Manns,Markus Kalesse,Ronald Frank,Nisar P. Malek +16 more
TL;DR: This work identifies argyrin A, a cyclical peptide derived from the myxobacterium Archangium gephyra, as a potent antitumoral drug and finds that the biological effects of proteasome inhibition per se depend on the expression of p27(kip1).
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The INPHARMA method: protein-mediated interligand NOEs for pharmacophore mapping.
Víctor M. Sánchez-Pedregal,Marcel Reese,Jens Meiler,Marcel J. J. Blommers,Christian Griesinger,Teresa Carlomagno +5 more
TL;DR: The observation of interligandspin-diffusion-mediated transferred-NOE data are reported on, which have the potential to be used for the determination of the relative orientation of two competitive ligands in the receptor binding pocket.
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The structure of the box C/D enzyme reveals regulation of RNA methylation
Audrone Lapinaite,Bernd Simon,Lars Skjærven,Magdalena Rakwalska-Bange,Frank Gabel,Teresa Carlomagno +5 more
TL;DR: A powerful combination of NMR spectroscopy and small-angle neutron scattering is used to solve the structure of the 390 kDa archaeal RNP enzyme bound to substrate RNA and provides a means for differential control of methylation levels at the two sites and at the same time offers an unexpected regulatory mechanism for rRNA folding.
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Molecular mechanism of SHP2 activation by PD-1 stimulation
Michelangelo Marasco,Anna Berteotti,J. Weyershaeuser,Niko Thorausch,Justyna Sikorska,Joern Krausze,H. J. Brandt,John Kirkpatrick,Pablo Rios,Wolfgang W. A. Schamel,Maja Köhn,Teresa Carlomagno +11 more
TL;DR: It is demonstrated that full activation is obtained only upon phosphorylation of both ITIM and ITSM: ITSM binds C-SH2 with strong affinity, recruiting SHP2 to PD-1, while ITIM binds N- SH2, displacing it from the catalytic pocket and activating ShP2.