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Profil bibliographique

Catia L. Pierotti

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

8Publications signalées
681Citations signalées
3Affiliations récentes

Les institutions déclarées

Les domaines associés

Cell death mechanisms and regulationProtein Tyrosine PhosphatasesPhagocytosis and Immune RegulationProtein Kinase Regulation and GTPase SignalingHippo pathway signaling and YAP/TAZ

Les publications récentes

Accès ouvert 2026 article OpenAlex

Shifting paradigms: phosphatases from basic biology to druggable targets

Catia L. Pierotti, Marian Brenner, Yamini Chand, Fabrice Krier et autres

The EMBO Workshop 'Phosphatases: from basic research to translation' (27 to 31 July 2025, Würzburg, Germany) brought together researchers from academia and industry for a deep dive into the rapidly evolving world of phosphatase biology. Over five days, participants explored the interplay …

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0 citations Biology Open
Accès ouvert 2026 article OpenAlex

Regulation and activity of the phosphatase SHP2: SH2 domains, dephosphorylation activity, and beyond

Catia L. Pierotti, Maja Köhn

Src homology 2 (SH2) domain-containing phosphatase-2 (SHP2, PTPN11) is implicated in diseases such as cancer and RASopathies, where it is often mutated. It has gained strong attention due to promising new drug development strategies, with drug candidates currently in clinical trials. SHP2 …

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3 citations Biochemical Society Transactions
Accès ouvert 2025 article OpenAlex

Development of a Peptide Inhibitor Targeting the C‐SH2 Domain of the SHP2 Phosphatase

Azin Kiani, Catia L. Pierotti, Franziska Schedel, Thomas Kokot et autres

Src homology 2 (SH2) domain‐containing phosphatase 2 (SHP2) mediates important signal transduction upon cell surface receptor stimulation, regulating multiple cellular functions. In addition to the catalytically active phosphotyrosine (pTyr) phosphatase domain, SHP2 contains two regulatory pTyr‐binding domains: the N‐SH2 and C‐SH2 domains. …

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2 citations ChemBioChem
Accès ouvert 2023 article OpenAlex

The VEGFR/PDGFR tyrosine kinase inhibitor, ABT-869, blocks necroptosis by targeting RIPK1 kinase

Catia L. Pierotti, Annette V. Jacobsen, Christoph Grohmann, Ruby K. Dempsey et autres

Necroptosis is a mode of programmed, lytic cell death that is executed by the mixed lineage kinase domain-like (MLKL) pseudokinase following activation by the upstream kinases, receptor-interacting serine/threonine protein kinase (RIPK)-1 and RIPK3. Dysregulated necroptosis has been implicated in the pathophysiology of …

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13 citations Biochemical Journal
Accès ouvert 2022 article OpenAlex

The Lck inhibitor, AMG-47a, blocks necroptosis and implicates RIPK1 in signalling downstream of MLKL

Annette V. Jacobsen, Catia L. Pierotti, Kym N. Lowes, Amanda E. Au et autres

Necroptosis is a form of caspase-independent programmed cell death that arises from disruption of cell membranes by the mixed lineage kinase domain-like (MLKL) pseudokinase after its activation by the upstream kinases, receptor interacting protein kinase (RIPK)-1 and RIPK3, within a complex known …

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22 citations Cell Death and Disease
2022 article OpenAlex

Necroptosis in chronic obstructive pulmonary disease, a smoking gun?

Catia L. Pierotti, John Silke

Recent studies, reviewed here, using a cigarette smoke exposure model for chronic obstructive pulmonary disease (COPD) in Ripk3 and Mlkl knock-out mice, and correlation with patient samples, suggest necroptosis plays a pathophysiological role in COPD by promoting inflammation, airway remodeling and emphysema.

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3 citations Immunology and Cell Biology
2020 article OpenAlex

Potent Inhibition of Necroptosis by Simultaneously Targeting Multiple Effectors of the Pathway

Catia L. Pierotti, Maria C. Tanzer, Annette V. Jacobsen, Joanne M. Hildebrand et autres

Necroptosis is an inflammatory form of programmed cell death that has been implicated in various human diseases. Compound 2 is a more potent analogue of the published compound 1 and inhibits necroptosis in human and murine cells at nanomolar concentrations. Several target …

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30 citations ACS Chemical Biology
Accès ouvert 2014 article OpenAlex

Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death

Joanne M. Hildebrand, Maria C. Tanzer, Isabelle S. Lucet, Samuel N. Young et autres

Necroptosis is considered to be complementary to the classical caspase-dependent programmed cell death pathway, apoptosis. The pseudokinase Mixed Lineage Kinase Domain-Like (MLKL) is an essential effector protein in the necroptotic cell death pathway downstream of the protein kinase Receptor Interacting Protein Kinase-3 …

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609 citations Proceedings of the National Academy of Sciences

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