Gaetano Calabrese

ORCID: 0000-0002-2212-5280
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • Redox biology and oxidative stress
  • Sulfur Compounds in Biology
  • Enzyme Structure and Function
  • Endoplasmic Reticulum Stress and Disease
  • Genetic Neurodegenerative Diseases
  • Glutathione Transferases and Polymorphisms
  • Ubiquitin and proteasome pathways
  • Advanced Proteomics Techniques and Applications
  • Fungal and yeast genetics research
  • Adipose Tissue and Metabolism
  • Trace Elements in Health
  • Alzheimer's disease research and treatments
  • RNA and protein synthesis mechanisms
  • Heat shock proteins research
  • Metabolomics and Mass Spectrometry Studies
  • Eicosanoids and Hypertension Pharmacology
  • Protein Structure and Dynamics
  • ATP Synthase and ATPases Research

University of British Columbia
2022-2024

Canada's Michael Smith Genome Sciences Centre
2022-2024

University of Cologne
2017-2024

University of Kaiserslautern
2014

Article7 August 2019Open Access Source DataTransparent process Hyperoxidation of mitochondrial peroxiredoxin limits H2O2-induced cell death in yeast Gaetano Calabrese orcid.org/0000-0002-2212-5280 Department for Chemistry, Institute Biochemistry, University Cologne, Germany Search more papers by this author Esra Peker Prince Saforo Amponsah Biology, Cellular Kaiserslautern, the Saarland, Saarbruecken, Michaela Nicole Hoehne Trine Riemer Marie Mai Gerd Patrick Bienert...

10.15252/embj.2019101552 article EN cc-by The EMBO Journal 2019-08-07

The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. main component this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed IMS glutathione pool maintained as reducing cytosol. It thus remained unclear how equilibration protein with prevented in order to allow oxidation-driven import. Here we demonstrate presence...

10.1091/mbc.e14-10-1422 article EN cc-by-nc-sa Molecular Biology of the Cell 2014-11-13

Mutations can disrupt a protein's native function by causing misfolding, which is generally handled an intricate protein quality control network. To better understand the triaging mechanisms of misfolded cytosolic proteins, we screened human mutation library to identify panel unstable mutations. The degradation these mutated proteins largely dependent on ubiquitin proteasome system. Using BioID proximity labelling, found that co-chaperones DNAJA1 and DNAJA2 are key interactors with one...

10.1242/jcs.262019 article EN publisher-specific-oa Journal of Cell Science 2024-12-02

Mitofusins are dynamin-related GTPases that drive mitochondrial fusion by sequential events of oligomerization and GTP hydrolysis, followed their ubiquitylation. Here, we show requires a trilateral salt bridge at hinge point the yeast mitofusin Fzo1, alternatingly forming before after hydrolysis. Mutations causative Charcot-Marie-Tooth disease massively map to this site, underlining relevance bridge. A triple charge swap rescues activity emphasizing close coordination residues with...

10.26508/lsa.201900491 article EN cc-by Life Science Alliance 2019-11-18

Abstract Mutations can result in the loss of a protein’s native function due to protein misfolding, which is generally handled by an intricate quality control network. To better understand triaging mechanisms misfolded cytosolic proteins, we screened human mutation library identify panel unstable mutations. The degradation these mutated proteins largely dependent on ubiquitin proteasome system. Using BioID proximity labelling, found that co-chaperones DNAJA1 and DNAJA2 are key interactors...

10.1101/2024.02.15.580437 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-02-16

Abstract Hydrogen peroxide (H 2 O ) is an important biological molecule, functioning both as a second messenger in cell signaling and, especially at higher concentrations, cause of damage. Cells harbor multiple enzymes that have reducing activity vitro . However, the contribution each these towards scavenging vivo less clear. Therefore, to directly investigate scavenging, we used genetically encoded sensors, roGFP2-Tsa2ΔC R and HyPer7, systematically screen capacity yeast thiol heme...

10.1101/2024.07.03.601836 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-07-03

Some newly translated proteins are more susceptible to misfolding and aggregation upon heat shock in comparison other proteins. To study these thermo-sensitive on a proteomic scale, we present here protocol that combines pulse-SILAC with biochemical fractionation for mass spectrometry analysis, followed by an orthogonal validation selected candidates using the GAL promoter system Saccharomyces cerevisiae. This approach can be further developed stresses specific post-translational...

10.1016/j.xpro.2023.102059 article EN cc-by-nc-nd STAR Protocols 2023-01-25
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