Mass spectrometry articles within Nature

Featured

  • Article
    | Open Access

    A protein interaction network constructed with data from high-throughput affinity enrichment coupled to mass spectrometry provides a highly saturated yeast interactome with 31,004 interactions, including low-abundance complexes, membrane protein complexes and non-taggable protein complexes.

    • André C. Michaelis
    • , Andreas-David Brunner
    •  & Matthias Mann

  • Article |

    HLA peptidomic analysis identifies recurrent intracellular bacteria-derived peptides presented on HLA-I and HLA-II molecules in melanoma tumours, revealing how bacteria can modulate immune functions and responses to cancer therapies.

    • Shelly Kalaora
    • , Adi Nagler
    •  & Yardena Samuels

  • Article |

    A method termed ac4C-seq is introduced for the transcriptome-wide mapping of the RNA modification N4-acetylcytidine, revealing widespread temperature-dependent acetylation that facilitates thermoadaptation in hyperthermophilic archaea.

    • Aldema Sas-Chen
    • , Justin M. Thomas
    •  & Schraga Schwartz

  • Article |

    An advanced proteomics workflow is used to identify 340,000 proteins from 100 taxonomically diverse species, providing a comparative view of proteomes across the evolutionary range.

    • Johannes B. Müller
    • , Philipp E. Geyer
    •  & Matthias Mann

  • Article |

    The structure of the multiprotein Fanconi anaemia core complex, determined using cryo-electron microscopy and mass spectrometry, shows that the complex adopts an extended asymmetric structure and highlights the structural and functional asymmetry of the RING finger domains.

    • Shabih Shakeel
    • , Eeson Rajendra
    •  & Lori A. Passmore

  • Letter |

    Enzymatic cleavage within ubiquitin molecules followed by quantitative mass-spectrometry simplifies complex ubiquitin chains and enables mapping of polyubiquitin architectures.

    • Kirby N. Swatek
    • , Joanne L. Usher
    •  & David Komander

  • Letter |

    Structural mass spectrometry of full-length human parkin and a structure of the activated parkin core reveal large-scale domain rearrangements involved in activation of parkin by PINK1.

    • Christina Gladkova
    • , Sarah L. Maslen
    •  & David Komander

  • Letter |

    Isochron burial dating with cosmogenic nuclides 26Al and 10Be shows that the skeleton of the australopithecine individual known as ‘Little Foot’ is around 3.67 million years old, coeval with early Australopithecus from East Africa; a manuport dated to 2.18 million years ago from the Oldowan tool assemblage conforms with the oldest age previously suggested by fauna.

    • Darryl E. Granger
    • , Ryan J. Gibbon
    •  & Marc W. Caffee

  • Letter |

    The structure of the 39S large mitoribosome subunit is solved by cryo-electron microscopy at an impressive 3.4 Å resolution, revealing the location of 50 ribosomal proteins, the peptidyl transferase centre, the tRNAs within this active site, and the nascent peptide chain within the exit tunnel.

    • Basil J. Greber
    • , Daniel Boehringer
    •  & Nenad Ban

  • Article |

    Cryo-electron microscopy combined with chemical crosslinking and mass spectrometry is used to determine the structure of the large subunit of the mammalian mitoribosome; this structure provides detailed structural insight, particularly of the molecular architecture of the polypeptide exit site, which has been structurally remodelled during evolution, presumably to help facilitate the membrane insertion of the highly hydrophobic proteins encoded by the mitochondrial genome.

    • Basil J. Greber
    • , Daniel Boehringer
    •  & Nenad Ban

  • Letter |

    During normal ageing a low rate of division of pre-existing cardiomyocytes, rather than progenitor cells, is responsible for cardiomyocyte genesis; this process is increased fourfold during myocardial infarction.

    • Samuel E. Senyo
    • , Matthew L. Steinhauser
    •  & Richard T. Lee

  • Obituary |

    Chemist who enabled mass spectrometry to weigh up biology.

    • Carol V. Robinson

  • News & Views |

    Labelling molecules by fast oxidation allows mass spectrometry to study protein folding at submillisecond time resolution. The method also brings a wealth of structural information about protein folding within reach.

    • Martin Gruebele

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