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Cover Picture: Evaluating p97 Inhibitor Analogues for Potency against p97–p37 and p97–Npl4–Ufd1 Complexes (ChemMedChem 9/2016)
Author(s) -
Gui Lin,
Zhang Xiaoyi,
Li Kelin,
Frankowski Kevin J.,
Li Shan,
Wong Daniel E.,
Moen Derek R.,
Porubsky Patrick R.,
Lin Henry J.,
Schoenen Frank J.,
Chou TsuiFen
Publication year - 2016
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201600214
Subject(s) - endoplasmic reticulum , chemistry , autophagy , aaa proteins , proteasome , cofactor , small molecule , biochemistry , atpase , computational biology , microbiology and biotechnology , biophysics , biology , enzyme , apoptosis
The front cover picture shows p97 as it forms complexes with three different p97 cofactors. Each complex is unique and can be targeted by small molecule inhibitors. P97 performs multiple cellular functions, such as ubiquitin‐proteasome‐dependent degradation, endoplasmic‐reticulum‐associated degradation, membrane fusion, and autophagy–with help from cofactor proteins. Inhibitors of p97 ATPase activity are potential anticancer agents, which are being developed for clinical use. Developing inhibitors for specific p97 complexes is an exciting challenge and will be critical for studying p97’s biological functions, as well as targeting p97 complexes in cancer, to reduce unwanted cytotoxicity. More information can be found in the Full Paper by Tsui‐Fen Chou et al. on page 953 in Issue 9, 2016 (DOI: 10.1002/cmdc.201600036).