Pierre-Henri L. Gaillard

ORCID: 0000-0003-0781-0826
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About
Contact & Profiles
Research Areas
  • DNA Repair Mechanisms
  • CRISPR and Genetic Engineering
  • Genomics and Chromatin Dynamics
  • Genetic factors in colorectal cancer
  • Computational Drug Discovery Methods
  • RNA Research and Splicing
  • DNA and Nucleic Acid Chemistry
  • Fungal and yeast genetics research
  • Free Radicals and Antioxidants
  • Plant Genetic and Mutation Studies
  • Advanced biosensing and bioanalysis techniques
  • PARP inhibition in cancer therapy
  • RNA and protein synthesis mechanisms
  • Genetic Neurodegenerative Diseases
  • Synthesis and Reactivity of Heterocycles
  • Microtubule and mitosis dynamics
  • Genetics and Neurodevelopmental Disorders
  • Synthesis and Characterization of Heterocyclic Compounds
  • Plant biochemistry and biosynthesis
  • Chromosomal and Genetic Variations
  • Synthesis and Biological Evaluation
  • Pleistocene-Era Hominins and Archaeology
  • Molecular Biology Techniques and Applications
  • RNA Interference and Gene Delivery
  • Surfactants and Colloidal Systems

Centre de Recherche en Cancérologie de Marseille
2009-2025

Aix-Marseille Université
2011-2025

Inserm
2013-2025

Centre National de la Recherche Scientifique
2014-2025

Institut Paoli-Calmettes
2017-2023

Institut Pprime
2022

Laboratoire Cognition, Langues, Langage, Ergonomie
2021

Université de Toulouse
2021

Institut National de Recherche en Santé Publique
2017-2019

Scripps Research Institute
2001-2003

Cancer cells acquire unlimited proliferative capacity by either re-expressing telomerase or inducing alternative lengthening of telomeres (ALT), which relies on telomere recombination. Here, we show that ALT recombination requires coordinate regulation the SMX and BTR complexes to ensure appropriate balance resolution dissolution activities at recombining telomeres. Critical this control is SLX4IP, accumulates interacts with SLX4, XPF, BLM. Loss SLX4IP increases ALT-related phenotypes,...

10.1016/j.molcel.2019.07.010 article EN cc-by Molecular Cell 2019-08-22

In most eukaryotes, genes encoding ribosomal RNAs (rDNA) are clustered in long tandem head-to-tail repeats. Studies of Saccharomyces cerevisiae have indicated that rDNA copy number is maintained through recombination events associated with site-specific blockage replication forks (RFs). Here, we describe two Schizosaccharomyces pombe proteins, homologs S. Slx1 and Slx4, as subunits a novel type endonuclease maintains number. The Slx1-Slx4-dependent introduces single-strand cuts duplex DNA on...

10.1091/mbc.e03-08-0586 article EN Molecular Biology of the Cell 2003-10-07

ERCC1-XPF is a structure-specific nuclease with two subunits, ERCC1 and XPF. The enzyme cuts DNA at junctions where single strand moves 5' to 3' away from branch point duplex DNA. This activity has central role in nucleotide excision repair (NER), cross-link recombination. To dissect the activities of it necessary investigate subunits individually, as studies so far have only used heterodimeric complex. We produced recombinant XPF separately Escherichia coli soluble proteins. Activity was...

10.1093/nar/29.4.872 article EN Nucleic Acids Research 2001-02-15

Abstract The Werner Syndrome helicase, WRN, is a promising therapeutic target in cancers with microsatellite instability (MSI). Long‐term MSI leads to the expansion of TA nucleotide repeats proposed form cruciform DNA structures, which turn cause breaks and cell lethality upon WRN downregulation. Here we employed biochemical assays show that helicase can efficiently directly unfold thereby preventing their cleavage by SLX1‐SLX4 structure‐specific endonuclease. are particularly prone...

10.15252/embj.2022111998 article EN cc-by-nc-nd The EMBO Journal 2022-12-21

Abstract While DNA:RNA hybrids contribute to multiple genomic transactions, their unscheduled formation is a recognized source of DNA lesions. Here, through suite systematic screens, we rather observed that wide range yeast mutant situations primarily triggering damage actually leads hybrid accumulation. Focusing on Okazaki fragment processing, establish genic can form as consequence replication-born discontinuities such unprocessed flaps or unligated fragments. Strikingly, “post-lesion”...

10.1038/s41467-025-57588-x article EN cc-by Nature Communications 2025-03-10

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInhibition of Monoamine Oxidase-B by 5H-Indeno[1,2-c]pyridazines: Biological Activities, Quantitative Structure-Activity Relationships (QSARs) and 3D-QSARsSilvia Kneubuehler, Ulrike Thull, Cosimo Altomare, Vincenco Carta, Patrick Gaillard, Pierre-Alain Carrupt, Angelo Carotti, Bernard TestaCite this: J. Med. Chem. 1995, 38, 19, 3874–3883Publication Date (Print):September 1, 1995Publication History Published online1 May 2002Published inissue 1...

10.1021/jm00019a018 article EN Journal of Medicinal Chemistry 1995-09-01

During DNA replication stress, stalled forks need to be stabilized prevent fork collapse and genome instability. The AAA + ATPase WRNIP1 (Werner Helicase Interacting Protein 1) has been implicated in the protection of from nucleolytic degradation, but underlying molecular mechanism remained unclear. Here we show that exerts its protective function downstream reversal. Unexpectedly though, is not part well-studied BRCA2-dependent branch seems protect junction point reversed SLX4-mediated...

10.1016/j.isci.2019.10.010 article EN cc-by-nc-nd iScience 2019-10-08

A prehistoric conch shell converted into a musical instrument makes its first sounds in 18,000 years.

10.1126/sciadv.abe9510 article EN cc-by-nc Science Advances 2021-02-10

Mus81 is a highly conserved endonuclease with homology to the XPF subunit of XPF-ERCC1 complex. In yeast associates second subunit, Eme1 or Mms4, which essential for activity in vitro and vivo function. Human binds homolog fission vivo. We show that recombinant Mus81-Eme1 cleaves replication forks, 3' flap substrates, Holliday junctions vitro. By use differentially tagged versions Eme1, we find Eme1. Thus, complexes containing two more units could function coordinate substrate cleavage...

10.1091/mbc.e03-08-0580 article EN Molecular Biology of the Cell 2003-11-18
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