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Showing 1–19 of 19 results
Advanced filters: Author: Wolfgang Peti Clear advanced filters

  • Blocking peptidoglycan synthesis kills bacteria. The authors show that the E. faecium PBP5 peptidoglycan binding site is distal to the active site, which could be the focus of antibiotic strategies that hinder substrate recruitment.

    • Yamanappa Hunashal
    • Matthieu Fonvielle
    • Wolfgang Peti
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • De novo Calcineurin (CN) variants cause DEE91, with E282K being the most common. E282K alters CN’s acidic substrate binding pocket to basic, thus shifting substrate preference and dephosphorylation signaling, subsequently impacting neurodevelopment.

    • Karina T. Shirakawa
    • Tvesha Parikh
    • Wolfgang Peti
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-14

    • Wolfgang Peti
    • Rebecca Page
    Amendments and Corrections
    Nature Chemical Biology
    Volume: 10, P: 164

  • Penicillin Binding Proteins (PBPs) are the main targets of β-lactam antibiotics. Here the authors use NMR spectroscopy, crystallography and microbiology to define the dynamics of E. faecium PBP5 in solution and show that increased acyl-enzyme hydrolysis correlates with increased resistance.

    • Yamanappa Hunashal
    • Ganesan Senthil Kumar
    • Wolfgang Peti
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • Padi and Godek et al. solve cryo-electron microscopy structures of protein phosphatase 2A (PP2A):B55 bound to p107 and Eya3, which, together with nuclear magnetic resonance dephosphorylation experiments, show how PP2A:B55 recruits specific substrates and how it achieves efficient dephosphorylation of phosphosites with high cellular fidelity.

    • Sathish K. R. Padi
    • Rachel J. Godek
    • Rebecca Page
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1373-1382

  • TCPTP is a non-receptor type protein tyrosine phosphatase involved in various signalling pathways. Here, the authors provide structural insights into TCPTP activation, showing that TCPTP is inhibited by its C-terminal tail, which can be displaced by the cytosolic tail of integrin-α1, leading to activation.

    • Jai Prakash Singh
    • Yang Li
    • Tzu-Ching Meng
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • Cryo-electron microscopy structures of the PP2A:B55 holoenzyme bound to its inhibitors ARPP19 and FAM122A show distinct binding modes of the two inhibitors.

    • Sathish K. R. Padi
    • Margaret R. Vos
    • Wolfgang Peti
    ResearchOpen Access
    Nature
    Volume: 625, P: 195-203

  • Protein phosphatase specificity is usually achieved via interaction with regulatory partners, which can control their subcellular localization and/or enzymatic specificity. Now structural and functional work on spinophilin reveals its extensive interactions with PP1, which differentially restrict the phosphatase's ability to bind different substrates.

    • Michael J Ragusa
    • Barbara Dancheck
    • Wolfgang Peti
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 459-464

  • Serine/threonine phosphatases such as PP1 associate with a large array of subunit proteins, such as ASPP (apoptosis-stimulating protein of p53) to achieve selective targeting. Here authors solved the crystal structure of the human ASPP2/PP1 complex and explain how ASPP2 can distinguish between PP1 isoforms.

    • M. Teresa Bertran
    • Stéphane Mouilleron
    • Nicolas Tapon
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-19

  • NMR and ITC are used to define essential features of a p38α phosphatase interface that extend beyond the classic KIM binding site, and SAXS analysis software, incorporating NMR chemical shift data, are developed and applied to build a model of the p38α-HePTP complex.

    • Dana M Francis
    • Bartosz Różycki
    • Wolfgang Peti
    Research
    Nature Chemical Biology
    Volume: 7, P: 916-924

  • The Doc-Phd pair forms a bacterial toxin-antitoxin system, but the mechanism by which the Fic-family member Doc causes toxicity is not fully defined. New research shows that Doc unexpectedly functions as a kinase to phosphorylate elongation factor TU, thus inhibiting translation and leading to Doc-mediated growth arrest.

    • Wolfgang Peti
    • Rebecca Page
    News & Views
    Nature Chemical Biology
    Volume: 9, P: 756-757

  • The ATF2 transcription factor is phosphorylated by different mitogen-activated protein (MAP) kinases. Here, the authors show that the functionally distinct MAP kinases JNK and p38 control ATF2 through different binding sites and differential phosphorylation, thereby modulating ATF2’s sensitivity to the JNK and p38 pathways.

    • Klára Kirsch
    • András Zeke
    • Attila Reményi
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-15

  • The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.

    • Ruth Hendus-Altenburger
    • Xinru Wang
    • Wolfgang Peti
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13

  • The toxin-antitoxin pair MqsR and MqsA are linked to biofilm formation, quorum sensing and motility, but their specific role in these and other cellular processes is unclear. The demonstration that MqsA directly represses transcription of rpoS, encoding the master regulator of the stress response, provides a unifying explanation.

    • Xiaoxue Wang
    • Younghoon Kim
    • Thomas K Wood
    Research
    Nature Chemical Biology
    Volume: 7, P: 359-366

  • Expanding the bacterial toxin-antitoxin system classes to a fifth class, GhoST was found to be involved in maintenance of persister cells, dormant cells that are tolerant of antibiotics. GhoS is the antitoxin, an endoribonuclease that cleaves the toxin mRNA ghoT, whose gene product is a membrane-lytic protein.

    • Xiaoxue Wang
    • Dana M Lord
    • Thomas K Wood
    Research
    Nature Chemical Biology
    Volume: 8, P: 855-861

  • This Review article highlights bacterial toxin-antitoxin system components, their function and the mechanisms they use to affect diverse physiological functions and conditions, including dormancy and entry and exit from the persistent state defined by a high tolerance to antibiotics.

    • Rebecca Page
    • Wolfgang Peti
    Reviews
    Nature Chemical Biology
    Volume: 12, P: 208-214

  • The allosteric binding of MSI-1436 to the intrinsically disordered C-terminal region of PTP1B promotes a conformational change to generate a compact inactive structure, validating the use of MSI-1436 to inhibit HER2-mediated tumorigenesis.

    • Navasona Krishnan
    • Dorothy Koveal
    • Nicholas K Tonks
    Research
    Nature Chemical Biology
    Volume: 10, P: 558-566