Carla Aranda-Vallejo

ORCID: 0009-0007-0402-8042
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About
Contact & Profiles
Research Areas
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Proteoglycans and glycosaminoglycans research
  • PARP inhibition in cancer therapy
  • Biochemical and Molecular Research
  • DNA Repair Mechanisms
  • Vitamin C and Antioxidants Research
  • Pancreatic function and diabetes
  • Biotin and Related Studies
  • Electrochemical sensors and biosensors
  • Cellular transport and secretion

Centre for Genomic Regulation
2023-2024

Heidelberg University
2024

German Cancer Research Center
2024

DKFZ-ZMBH Alliance
2024

Barcelona Institute for Science and Technology
2023

Abstract Currently available genetically encoded H 2 O probes report on the thiol redox state of probe, which means that they reflect balance between probe oxidation and reduction. Here we introduce use engineered heme peroxidase APEX2 as a thiol-independent chemogenetic directly irreversibly converts molecules into either fluorescent or luminescent signals. We demonstrate sensitivity, specificity, ability to quantitate endogenous turnover. show how can be used detect changes in generation...

10.1038/s41467-024-45511-9 article EN cc-by Nature Communications 2024-02-09

Abstract Agonist-mediated stimulated pathway of mucin and insulin release are biphasic in which rapid fusion pre-docked granules is followed by slow docking from the reserve pool. Here, based on a cell-culture system, we show that plasma membrane-located tetraspanin-8 sequesters syntaxin-2 to control release. Tetraspanin-8 affects during second phase The tetraspanin-8/syntaxin-2 complex does not contain VAMP-8, functions with mediate granule fusion. We suggest sequestering syntaxin-2,...

10.1038/s41467-023-39277-9 article EN cc-by Nature Communications 2023-06-22

Nuclear metabolism and DNA damage response are intertwined processes, but the precise molecular links remain elusive. Here, we explore this crosstalk using triple-negative breast cancer (TNBC) as a model, subtype often prone to accumulation. We show that de novo purine synthesis enzyme IMPDH2 is enriched on chromatin in TNBC compared other subtypes. localization dependent, repression leads On chromatin, interacts with modulates PARP1 activity by controlling nuclear availability of NAD

10.1038/s41467-024-53877-z article EN cc-by-nc-nd Nature Communications 2024-11-12
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