Search

Your search keyword '"Carpy, Alejandro"' showing total 26 results
Start Over Author "Carpy, Alejandro"
26 results on '"Carpy, Alejandro"'

1. The physiological interactome of TCR-like antibody therapeutics in human tissues

Author

Marrer-Berger, Estelle, Nicastri, Annalisa, Augustin, Angelique, Kramar, Vesna, Liao, Hanqing, Hanisch, Lydia Jasmin, Carpy, Alejandro, Weinzierl, Tina, Durr, Evelyne, Schaub, Nathalie, Nudischer, Ramona, Ortiz-Franyuti, Daniela, Breous-Nystrom, Ekaterina, Stucki, Janick, Hobi, Nina, Raggi, Giulia, Cabon, Lauriane, Lezan, Emmanuelle, Umaña, Pablo, Woodhouse, Isaac, Bujotzek, Alexander, Klein, Christian, and Ternette, Nicola

Published
2024
Full Text
View/download PDF

2. Forimtamig, a novel GPRC5D-targeting T-cell bispecific antibody with a 2+1 format, for the treatment of multiple myeloma

Author

Eckmann, Jan, Fauti, Tanja, Biehl, Marlene, Zabaleta, Aintzane, Blanco, Laura, Lelios, Iva, Gottwald, Stefan, Rae, Richard, Lechner, Stefanie, Bayer, Christa, Dekempe, Quincy, Osl, Franz, Carrié, Nadege, Kassem, Sahar, Lorenz, Stefan, Christopeit, Tony, Carpy, Alejandro, Bujotzek, Alexander, Bröske, Ann-Marie, Dekhtiarenko, Iryna, Attig, Jan, Kunz, Leo, Cremasco, Floriana, Adelfio, Roberto, Fertig, Georg, Dengl, Stefan, Gassner, Christian, Bormann, Felix, Kirstenpfad, Claudia, Kraft, Thomas, Diggelmann, Sarah, Knobloch, Melanie, Hage, Carina, Feddersen, Romi, Heidkamp, Gordon, Pöschinger, Thomas, Mayoux, Maud, Bernasconi, Luise, Prosper, Felipe, Dumontet, Charles, Martinet, Ludovic, Leclair, Stéphane, Xu, Wei, Paiva, Bruno, Klein, Christian, and Umaña, Pablo

Published
2025
Full Text
View/download PDF

3. Targeting intracellular WT1 in AML with a novel RMF-peptide-MHC-specific T-cell bispecific antibody

Author

Augsberger, Christian, Hänel, Gerulf, Xu, Wei, Pulko, Vesna, Hanisch, Lydia Jasmin, Augustin, Angelique, Challier, John, Hunt, Katharina, Vick, Binje, Rovatti, Pier Eduardo, Krupka, Christina, Rothe, Maurine, Schönle, Anne, Sam, Johannes, Lezan, Emmanuelle, Ducret, Axel, Ortiz-Franyuti, Daniela, Walz, Antje-Christine, Benz, Jörg, Bujotzek, Alexander, Lichtenegger, Felix S., Gassner, Christian, Carpy, Alejandro, Lyamichev, Victor, Patel, Jigar, Konstandin, Nikola, Tunger, Antje, Schmitz, Marc, von Bergwelt-Baildon, Michael, Spiekermann, Karsten, Vago, Luca, Jeremias, Irmela, Marrer-Berger, Estelle, Umaña, Pablo, Klein, Christian, and Subklewe, Marion

Published
2021
Full Text
View/download PDF

4. The physiological interactome of TCR-like antibody therapeutics in human tissues

Author

Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Marrer-Berger, Estelle, Nicastri, Annalisa, Augustin, Angelique, Kramar, Vesna, Liao, Hanqing, Hanisch, Lydia Jasmin, Carpy, Alejandro, Weinzierl, Tina, Durr, Evelyne, Schaub, Nathalie, Nudischer, Ramona, Ortiz-Franyuti, Daniela, Breous-Nystrom, Ekaterina, Stucki, Janick, Hobi, Nina, Raggi, Giulia, Cabon, Lauriane, Lezan, Emmanuelle, Umaña, Pablo, Woodhouse, Isaac, Bujotzek, Alexander, Klein, Christian, Ternette, Nicola, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Marrer-Berger, Estelle, Nicastri, Annalisa, Augustin, Angelique, Kramar, Vesna, Liao, Hanqing, Hanisch, Lydia Jasmin, Carpy, Alejandro, Weinzierl, Tina, Durr, Evelyne, Schaub, Nathalie, Nudischer, Ramona, Ortiz-Franyuti, Daniela, Breous-Nystrom, Ekaterina, Stucki, Janick, Hobi, Nina, Raggi, Giulia, Cabon, Lauriane, Lezan, Emmanuelle, Umaña, Pablo, Woodhouse, Isaac, Bujotzek, Alexander, Klein, Christian, and Ternette, Nicola

Published
2024

5. Immune-infiltrated kidney organoid-on-chip model for assessing T cell bispecific antibodies

Author

Kroll, Katharina T., primary, Mata, Mariana M., additional, Homan, Kimberly A., additional, Micallef, Virginie, additional, Carpy, Alejandro, additional, Hiratsuka, Ken, additional, Morizane, Ryuji, additional, Moisan, Annie, additional, Gubler, Marcel, additional, Walz, Antje-Christine, additional, Marrer-Berger, Estelle, additional, and Lewis, Jennifer A., additional

Published
2023
Full Text
View/download PDF

8. RG6234: A Novel 2:1 GPRC5D T Cell Bispecific Antibody Exhibits Best in Class Potential for the Treatment of Multiple Myeloma As a Monotherapy and in Combination

Author

Eckmann, Jan, primary, Fauti, Tanja, additional, Zabaleta, Aintzane, additional, Blanco, Laura, additional, Kassem, Sahar, additional, Carrié, Nadege, additional, Lorenz, Stefan, additional, Carpy, Alejandro, additional, Christopeit, Tony, additional, Fertig, Georg, additional, Bernasconi, Luise, additional, Biehl, Marlene, additional, Diggelmann, Sarah, additional, Knobloch, Melanie, additional, Mayoux, Maud, additional, Dumontet, Charles, additional, Paiva, Bruno, additional, Martinet, Ludovic, additional, Leclair, Stéphane, additional, Xu, Wei, additional, Klein, Christian, additional, and Umaña, Pablo, additional

Published
2022
Full Text
View/download PDF

13. Proteomic analysis of Rac1 signaling regulation by guanine nucleotide exchange factors

Author

Marei, Hadir, Carpy, Alejandro, Macek, Boris, and Malliri, Angeliki

Subjects
Proteomics, rac1 GTP-Binding Protein, P-Rex1, Small GTPases, Tandem Affinity Purification (TAP), Cell Communication, Stable Isotope Labeling by Amino acids in Cell culture (SILAC), TMOD3, Mice, IQGAP1, Cell Movement, Cell Line, Tumor, Protein Interaction Mapping, Tiam1, Animals, Guanine Nucleotide Exchange Factors, Humans, Extra Views, Ingenuity Integrated Pathway Analysis (IPA), Guanine nucleotide Exchange Factors (GEFs), ras GTPase-Activating Proteins, Isotope Labeling, NIH 3T3 Cells, Rac1, Protein Binding, Signal Transduction
Abstract

The small GTPase Rac1 is implicated in various cellular processes that are essential for normal cell function. Deregulation of Rac1 signaling has also been linked to a number of diseases, including cancer. The diversity of Rac1 functioning in cells is mainly attributed to its ability to bind to a multitude of downstream effectors following activation by Guanine nucleotide Exchange Factors (GEFs). Despite the identification of a large number of Rac1 binding partners, factors influencing downstream specificity are poorly defined, thus hindering the detailed understanding of both Rac1's normal and pathological functions. In a recent study, we demonstrated a role for 2 Rac-specific GEFs, Tiam1 and P-Rex1, in mediating Rac1 anti- versus pro-migratory effects, respectively. Importantly, via conducting a quantitative proteomic screen, we identified distinct changes in the Rac1 interactome following activation by either GEF, indicating that these opposing effects are mediated through GEF modulation of the Rac1 interactome. Here, we present the full list of identified Rac1 interactors together with functional annotation of the differentially regulated Rac1 binding partners. In light of this data, we also provide additional insights into known and novel signaling cascades that might account for the GEF-mediated Rac1-driven cellular effects.

Published
2016

14. Targeting Intracellular WT1 in AML Utilizing a T Cell Bispecific Antibody Construct: Augmenting Efficacy through Combination with Lenalidomide

Author

Klein, Christian, primary, Augsberger, Christian, additional, Xu, Wei, additional, Heitmüller, Christina, additional, Hanisch, Lydia, additional, Sam, Johannes, additional, Pulko, Vesna, additional, Schönle, Anne, additional, Challier, John, additional, Carpy, Alejandro, additional, Konstandin, Nikola, additional, Rothe, Maurine, additional, Hänel, Gerulf, additional, Bücklein, Veit, additional, Lichtenegger, Felix S., additional, Tunger, Antje, additional, Schmitz, Marc, additional, von Bergwelt, Michael, additional, Spiekermann, Karsten, additional, Umana, Pablo, additional, and Subklewe, Marion, additional

Published
2019
Full Text
View/download PDF

15. Ubiquitin-dependent regulation of Cdc42 by XIAP

Author

Murali, Arun, primary, Shin, Jaeyoung, additional, Yurugi, Hajime, additional, Krishnan, Aswini, additional, Akutsu, Masato, additional, Carpy, Alejandro, additional, Macek, Boris, additional, and Rajalingam, Krishnaraj, additional

Published
2017
Full Text
View/download PDF

19. Ubiquitin-dependent regulation of Cdc42 by XIAP

Author

Melino, G., Murali, Arun, Shin, Jaeyoung, Yurugi, Hajime, Krishnan, Aswini, Akutsu, Masato, Carpy, Alejandro, Maček, Boris, Rajalingam, Krishnaraj, Melino, G., Murali, Arun, Shin, Jaeyoung, Yurugi, Hajime, Krishnan, Aswini, Akutsu, Masato, Carpy, Alejandro, Maček, Boris, and Rajalingam, Krishnaraj

Abstract

Rho GTPases control fundamental cellular processes and Cdc42 is a well-studied member of the family that controls filopodia formation and cell migration. Although the regulation of Cdc42 activity by nucleotide binding is well documented, the mechanisms driving its proteostasis are not clear. Here, we demonstrate that the highly conserved, RING domain containing E3 ubiquitin ligase XIAP controls the protein stability of Cdc42. XIAP binds to Cdc42 and directly conjugates poly ubiquitin chains to the Lysine 166 of Cdc42 targeting it for proteasomal degradation. Depletion of XIAP led to an increased protein stability and activity of Cdc42 in normal and tumor cells. Consistently, loss of XIAP enhances filopodia formation in a Cdc42-dependent manner and this phenomenon phenocopies EGF stimulation. Further, XIAP depletion promotes lung colonization of tumor cells in mice in a Cdc42-dependent manner. These observations shed molecular insights into ubiquitin-dependent regulation of Cdc42 and that of actin cytoskeleton.

Published
2017

20. Ubiquitin-dependent regulation of MEKK2/3-MEK5-ERK5 signaling module by XIAP and cIAP1

Author

Takeda, Armelle-Natsuo, Oberoi-Khanuja, Tripat Kaur, Glatz, Gabor, Schulenburg, Katharina, Scholz, Rolf-Peter, Carpy, Alejandro, Macek, Boris, Remenyi, Attila, and Rajalingam, Krishnaraj

Subjects
Ubiquitin, Humans, X-Linked Inhibitor of Apoptosis Protein, Articles, MAP Kinase Kinase Kinase 3, MAP Kinase Kinase 5, MAP Kinase Kinase Kinase 2, MAP Kinase Kinase Kinases, Mitogen-Activated Protein Kinase 7, Inhibitor of Apoptosis Proteins
Abstract

Mitogen-activated protein kinases (MAPKs) are highly conserved protein kinase modules, and they control fundamental cellular processes. While the activation of MAPKs has been well studied, little is known on the mechanisms driving their inactivation. Here we uncover a role for ubiquitination in the inactivation of a MAPK module. Extracellular-signal-regulated kinase 5 (ERK5) is a unique, conserved member of the MAPK family and is activated in response to various stimuli through a three-tier cascade constituting MEK5 and MEKK2/3. We reveal an unexpected role for Inhibitors of Apoptosis Proteins (IAPs) in the inactivation of ERK5 pathway in a bimodal manner involving direct interaction and ubiquitination. XIAP directly interacts with MEKK2/3 and competes with PB1 domain-mediated binding to MEK5. XIAP and cIAP1 conjugate predominantly K63-linked ubiquitin chains to MEKK2 and MEKK3 which directly impede MEK5–ERK5 interaction in a trimeric complex leading to ERK5 inactivation. Consistently, loss of XIAP or cIAP1 by various strategies leads to hyperactivation of ERK5 in normal and tumorigenic cells. Loss of XIAP promotes differentiation of human primary skeletal myoblasts to myocytes in a MEKK2/3-ERK5-dependent manner. Our results reveal a novel, obligatory role for IAPs and ubiquitination in the physical and functional disassembly of ERK5-MAPK module and human muscle cell differentiation.

Published
2014

24. IAPs regulate the plasticity of cell migration by directly targeting Rac1 for degradation

Author

Oberoi, Tripat Kaur, primary, Dogan, Taner, additional, Hocking, Jennifer C, additional, Scholz, Rolf-Peter, additional, Mooz, Juliane, additional, Anderson, Carrie L, additional, Karreman, Christiaan, additional, Meyer zu Heringdorf, Dagmar, additional, Schmidt, Gudula, additional, Ruonala, Mika, additional, Namikawa, Kazuhiko, additional, Harms, Gregory S, additional, Carpy, Alejandro, additional, Macek, Boris, additional, Köster, Reinhard W, additional, and Rajalingam, Krishnaraj, additional

Published
2011
Full Text
View/download PDF

25. Absolute Proteome and Phosphoproteome Dynamics during the Cell Cycle of Schizosaccharomyces pombe(Fission Yeast)*

Author

Carpy, Alejandro, Krug, Karsten, Graf, Sabine, Koch, André, Popic, Sasa, Hauf, Silke, and Macek, Boris

Abstract

To quantify cell cycle-dependent fluctuations on a proteome-wide scale, we performed integrative analysis of the proteome and phosphoproteome during the four major phases of the cell cycle in Schizosaccharomyces pombe. In highly synchronized cells, we identified 3753 proteins and 3682 phosphorylation events and relatively quantified 65% of the data across all phases. Quantitative changes during the cell cycle were infrequent and weak in the proteome but prominent in the phosphoproteome. Protein phosphorylation peaked in mitosis, where the median phosphorylation site occupancy was 44%, about 2-fold higher than in other phases. We measured copy numbers of 3178 proteins, which together with phosphorylation site stoichiometry enabled us to estimate the absolute amount of protein-bound phosphate, as well as its change across the cell cycle. Our results indicate that 23% of the average intracellular ATP is utilized by protein kinases to phosphorylate their substrates to drive regulatory processes during cell division. Accordingly, we observe that phosphate transporters and phosphate-metabolizing enzymes are phosphorylated and therefore likely to be regulated in mitosis.

Published
2014
Full Text
View/download PDF

26. Deep Coverage of the Escherichia coliProteome Enables the Assessment of False Discovery Rates in Simple Proteogenomic Experiments*

Author

Krug, Karsten, Carpy, Alejandro, Behrends, Gesa, Matic, Katarina, Soares, Nelson C., and Macek, Boris

Abstract

Recent advances in mass spectrometry (MS) have led to increased applications of shotgun proteomics to the refinement of genome annotation. The typical “proteo-genomic” workflows rely on the mapping of peptide MS/MS spectra onto databases derived via six-frame translation of the genome sequence. These databases contain a large proportion of spurious protein sequences which make the statistical confidence of the resulting peptide spectrum matches difficult to assess. Here we performed a comprehensive analysis of the Escherichia coliproteome using LTQ-Orbitrap MS and mapped the corresponding MS/MS spectra onto a six-frame translation of the E. coligenome. We hypothesized that the protein-coding part of the E. coligenome approaches complete annotation and that the majority of six frame-specific (novel) peptide spectrum matches can be considered as false positive identifications. We confirm our hypothesis by showing that the posterior error probability distribution of novel hits is almost identical to that of reversed (decoy) hits; this enables us to estimate the sensitivity, specificity, accuracy, and false discovery rate in a typical bacterial proteo-genomic dataset. We use two complementary computational frameworks for processing and statistical assessment of MS/MS data: MaxQuant and Trans-Proteomic Pipeline. We show that MaxQuant achieves a more sensitive six-frame database search with an acceptable false discovery rate and is therefore well suited for global genome reannotation applications, whereas the Trans-Proteomic Pipeline achieves higher specificity and is well suited for high-confidence validation. The use of a small and well-annotated bacterial genome enables us to address genome coverage achieved in state-of-the-art bacterial proteomics: identified peptide sequences mapped to all expressed E. coliproteins but covered 31.7% of the protein-coding genome sequence. Our results show that false discovery rates can be substantially underestimated even in “simple” proteo-genomic experiments obtained by means of high-accuracy MS and point to the necessity of further improvements concerning the coverage of peptide sequences by MS-based methods.

Published
2013
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results