Perspectives in Medicinal Chemistry
Synopsis: An open access, peer reviewed electronic journal that covers drug design in the form of commentaries and reviews which do not require disclosure of proprietary information.
Indexing: Pubmed, Pubmed Central, Embase, Google Scholar, CAS, DOAJ, OAIster
Processing time: Decision in 2 weeks for 90% of papers.
Latest news:
Small Family with Key Contacts: Par14 and Par17 Parvulin Proteins, Relatives of Pin1, Now Emerge in Biomedical Research
Jonathan W Mueller1 and Peter Bayer1
1Institute for Structural and Medicinal Biochemistry, Centre for Medical Biotechnology—ZMB, University of Duisburg-Essen, 45117 Essen, Germany.
Abstract
The parvulin-type peptidyl-prolyl cis/trans isomerase Pin1 is subject of intense biochemical and clinical research as it seems to be involved in the pathogenesis of certain cancers and protein folding illnesses like Alzheimer’s and Parkinson’s disease. In addition to Pin1, the human genome only contains a single other parvulin locus encoding two protein species—Par14 and Par17. Much less is known about these enzymes although their sequences are highly conserved in all metazoans. Parvulin has been proposed to function as Pin1 complementing enzyme in cell cycle regulation and in chromatin remodelling. Pharmaceutical modulation of Par14 might therefore have benefi ts for certain types of cancer. Moreover, the Par17 protein that has been shown to be confi ned to anthropoid primate species only might provide a deeper understanding for human-specifi c brain development. This review aims at stimulating further research on Par14 and Par17 that are overlooked drug targets in the shadow of an overwhelming plethora of Pin1 literature by summarising all current knowledge on these parvulin proteins.
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Perspectives in Medicinal Chemistry
Yitzhak Tor, Editor in Chief
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