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De Gruyter, Biological Chemistry, 2(399), p. 101-125, 2018

DOI: 10.1515/hsz-2017-0137

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Structure and function of the human parvulins Pin1 and Par14/17

Journal article published in 2018 by Anja Matena, Edisa Rehic, Dana Hönig, Bianca Kamba, Peter Bayer ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

AbstractParvulins belong to the family of peptidyl-prolylcis/transisomerases (PPIases) assisting in protein folding and in regulating the function of a broad variety of proteins in all branches of life. The human representatives Pin1 and Par14/17 are directly involved in processes influencing cellular maintenance and cell fate decisions such as cell-cycle progression, metabolic pathways and ribosome biogenesis. This review on human parvulins summarizes the current knowledge of these enzymes and intends to oppose the well-studied Pin1 to its less well-examined homolog human Par14/17 with respect to structure, catalytic and cellular function.