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Showing 1–7 of 7 results
Advanced filters: Author: Markel Martínez-Carranza Clear advanced filters

  • The single stranded DNA binding protein RPA plays a pivotal role in DNA replication. The archaeal RPA hosts a WH domain that interacts with the DNA primase and the replicative polymerase PolD. Here the authors provide a molecular understanding of the regulatory activity of archaeal RPA.

    • Markel Martínez-Carranza
    • Léa Vialle
    • Ludovic Sauguet
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • Ribonucleotide reductase (RNR) is an essential enzyme that catalyzes the synthesis of DNA building blocks. Here, the authors present the cryo-EM structure and mechanism of action of NrdR, the RNR-specific repressor, that controls transcription of RNR genes in bacteria.

    • Inna Rozman Grinberg
    • Markel Martínez-Carranza
    • Pål Stenmark
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Epitope tags are widely used in various applications, but often lack versatility. Here, the authors introduce a small, alpha helical tag, which is recognized by a high affinity nanobody and can be used in a range of different applications, from protein purification to super-resolution imaging and in vivo detection of proteins.

    • Hansjörg Götzke
    • Markus Kilisch
    • Steffen Frey
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • Family D replicative DNA polymerases (PolD) contain a unique proofreading active site. Here, the authors present structures of PolD and enzymatic studies, revealing an unanticipated correction mechanism that extends the repertoire of protein domains known to be involved in DNA proofreading.

    • Leonardo Betancurt-Anzola
    • Markel Martínez-Carranza
    • Ludovic Sauguet
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • Here the authors present the structure of Replication Protein A (RPA) in Archaea. The RPA structure from P. abyssi has been determined in presence and absence of DNA, providing insights into the evolution of this replication factor in eukaryotes

    • Clément Madru
    • Markel Martínez-Carranza
    • Ludovic Sauguet
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • There are seven well-established types of Botulinum neurotoxins (BoNTs). Here the authors report the identification and characterization of a new type of BoNT—BoNT/X—which cleaves a different site on canonical BoNTs substrates and targets SNARE family members not cleaved by known BoNTs.

    • Sicai Zhang
    • Geoffrey Masuyer
    • Pål Stenmark
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10

  • Botulinum neurotoxins (BoNTs) are a family of protein toxins produced by clostridial bacteria that cause muscle paralysis, and exhibit structural and functional diversity within the BoNTs family. Here, the authors report the cryo-EM structure complex of a newly identified serotype BoNT/X with their partner protein NTNH/X and reveal the complex’s pH-dependent stability and receptor-binding properties.

    • Markel Martínez-Carranza
    • Jana Škerlová
    • Pål Stenmark
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-15