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Latest Research

  • Article |

    A chemical method for site-selective deuterium exchange at protein backbone α-carbons, involving conversion of cysteine to dehydroalanine and then to deuterated cysteine, is used to explore the mechanism of a model protein bioconjugation reaction.

    • Sébastien R. G. Galan
    • , James R. Wickens
    • , Jitka Dadova
    • , Wai-Lung Ng
    • , Xinglong Zhang
    • , Robert A. Simion
    • , Robert Quinlan
    • , Elisabete Pires
    • , Robert S. Paton
    • , Stephen Caddick
    • , Vijay Chudasama
    •  & Benjamin G. Davis
  • Article |

    Structural analysis shows that cross-reactivity of the T cell receptor DMF5 is governed by adaptability of the peptide antigen, which can undergo TCR-binding-induced frameshifting forcing the peptide C terminus to extend from the MHC-binding groove.

    • Timothy P. Riley
    • , Lance M. Hellman
    • , Marvin H. Gee
    • , Juan L. Mendoza
    • , Jesus A. Alonso
    • , Kendra C. Foley
    • , Michael I. Nishimura
    • , Craig W. Vander Kooi
    • , K. Christopher Garcia
    •  & Brian M. Baker
  • Article |

    Thalidomide-induced degradation of the transcription factor SALL4 in a cereblon-dependent manner provides an explanation for the teratogenic effects.

    • Mary E. Matyskiela
    • , Suzana Couto
    • , Xinde Zheng
    • , Gang Lu
    • , Julia Hui
    • , Katie Stamp
    • , Clifton Drew
    • , Yan Ren
    • , Maria Wang
    • , Aaron Carpenter
    • , Chung-Wein Lee
    • , Thomas Clayton
    • , Wei Fang
    • , Chin-Chun Lu
    • , Mariko Riley
    • , Polat Abdubek
    • , Kate Blease
    • , James Hartke
    • , Gondi Kumar
    • , Rupert Vessey
    • , Mark Rolfe
    • , Lawrence G. Hamann
    •  & Philip P. Chamberlain
  • Article |

    The asymmetric cortical gradient of PAR-1 is patterned via an integration of its cortical exclusion and stabilization by a circuit consisting of aPKC and the PRBH protein PAR-2.

    • Ravikrishna Ramanujam
    • , Ziyin Han
    • , Zhen Zhang
    • , Pakorn Kanchanawong
    •  & Fumio Motegi
  • Article |

    During the biosynthesis of the lanthipeptide duramycin, DurN catalyzes stereospecific lysinoalanine formation by preorganizing the reactive conformation of the substrate, such that one of the substrate’s own residues serves as the catalytic base.

    • Linna An
    • , Dillon P. Cogan
    • , Claudio D. Navo
    • , Gonzalo Jiménez-Osés
    • , Satish K. Nair
    •  & Wilfred A. van der Donk
  • Article |

    An electrophilic diazene probe (DiaAlk) enables capture and proteomic analysis of cysteine S-sulfinylation modifications, thus illuminating dynamic responses to oxidative stress and enabling the identification of new substrates of sulfiredoxin.

    • Salma Akter
    • , Ling Fu
    • , Youngeun Jung
    • , Mauro Lo Conte
    • , J. Reed Lawson
    • , W. Todd Lowther
    • , Rui Sun
    • , Keke Liu
    • , Jing Yang
    •  & Kate S. Carroll

News & Comment

  • News & Views |

    Duramycin is a small post-translationally modified peptide with antibody-like affinity for phosphatidylethanolamine. As it turns out, the same functionality that is essential for duramycin activity helps to catalyze the formation of its conformationally constrained and compact polycyclic architecture.

    • Albert A. Bowers
  • News & Views |

    T cell cross-reactivity enables the immune system to recognize a large array of peptides. A new study shows that T cells can achieve cross-recognition by using the remarkable plasticity of peptides, through flipping the peptide out of the binding cleft.

    • Stephanie Gras
  • News & Views |

    One mechanism of thalidomide teratogenicity involves binding to the CUL4–CRBN E3 ubiquitin ligase complex, which then mediates the degradation of transcription factors. New studies reveal that species-specific variants of the transcription factor SALL4 are differentially ubiquitinated and degraded via the thalidomide-bound complex.

    • Peter G. Wells

Focus

Focus on Biomolecular Tailoring

In our March 2018 issue, Nature Chemical Biology presents a collection that explores chemical tailoring of biomolecules within cells and highlights how chemical biology expands our mechanistic understanding of these modified biomolecules and provides tools to illuminate their biological functions.

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