Isoenzymes articles within Nature Communications

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  • Article
    | Open Access

    Maintaining systemic acid-base balance is a central task of the kidneys, but it is still undetermined how acid-base alterations are perceived by the kidney. Here, the authors show that the solute transporter AE4 in β-intercalated cells is an essential part of the renal acid-base sensing mechanism

    • H. Vitzthum
    • , M. Koch
    •  & H. Ehmke
  • Article
    | Open Access

    The colonic mucus layer is an organized system providing a physical barrier against pathogens and simultaneously harbouring the commensal flora. Here the authors report that transglutaminase 3 activity contributes to homeostasis of the colonic mucus layer and the lack of this enzymatic activity leads to increased susceptibility against DSS-induced colitis in mice.

    • Jack D. A. Sharpen
    • , Brendan Dolan
    •  & Christian V. Recktenwald
  • Article
    | Open Access

    Apart from the enzymatic role of ketohexokinase isoform A (KHK-A) in fructose metabolism the alternative physiological functions of the enzyme are unclear. Here, the authors show that KHK-A mediates fructose-induced metastasis in breast cancer through a nuclear role in repressing the transcriptional activity of the cell-adhesion molecule CDH1.

    • Jiyoung Kim
    • , Jengmin Kang
    •  & Jong-Wan Park
  • Article
    | Open Access

    A major drawback in the clinical use of the oral anticoagulants that directly inhibit factor Xa in order to prevent blood clot formation is the potential for life threatening bleeding events. Here the authors describe factor Xa variants that are refractory to inhibition by these anticoagulants and could serve as rescue agents in treated patients.

    • Daniël Verhoef
    • , Koen M. Visscher
    •  & Mettine H. A. Bos
  • Article
    | Open Access

    River blindness, a disease affecting millions throughout the tropics, is caused by parasitic worms. Here, Yuet al. report the discovery and structural characterization of potent macrocyclic peptide inhibitors of iPGM, a nematode-specific phosphoglycerate mutase, as potential leads for novel antimicrobial agents.

    • Hao Yu
    • , Patricia Dranchak
    •  & James Inglese