Premium
Issue Cover (May 2019)
Publication year - 2019
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.14504
Subject(s) - gene isoform , stable isotope labeling by amino acids in cell culture , proteomics , computational biology , computer science , biology , biochemistry , gene
Front cover: Amyloid precursor protein (APP) is processed to form the amyloid‐β (Aβ) which is a key component in the initiation of Alzheimer‘s disease. Aβ is preferentially produced from the 695 isoform of APP indicating that the different isoforms are differentially processed and may have different interactomes that regulate their processing. Stable isotope labelling of amino acids in cell culture (SILAC) and quantitative proteomics identified different interactomes for the 695 and 751 isoforms of APP. These data identify new proteins that may be important in regulating Aβ production. Image content: Immunofluorescent microscopy image of APP695‐FLAG (green) and its subcellular localisation in relation to the trans‐Golgi network marker TGN‐46 (red). APP695‐FLAG has punctate staining within the cell and its localisation overlapped with that of TGN‐46 (yellow) indicating that APP is located in the trans‐Golgi network.Read the full article ‘ Quantitative interaction proteomics reveals differences in the interactomes of amyloid precursor protein isoforms ’ by R. J. Andrew, K. Fisher, K. J. Heesom, K. A. B. Kellett, N. M. Hooper ( J. Neurochem . 2019, vol. 149 (3), pp. 399–412) on doi: 10.1111/jnc.14666