An essential role for Pin1 in <i>Xenopus laevis</i> embryonic development revealed by specific inhibitors
Dirk Wildemann(Max Planck Research Unit for Enzymology of Protein Folding), Gunter Fischer(Leibniz Institute for High Performance Microelectronics), Frank Erdmann(Max Planck Research Unit for Enzymology of Protein Folding), Kun Ping Lu(University of North Carolina at Chapel Hill), Birte Hernandez Alvarez(Max Planck Research Unit for Enzymology of Protein Folding), Gerlind Stoller(Max Planck Research Unit for Enzymology of Protein Folding), David M. Ferrari(Universitätsmedizin Göttingen), Xiao Zhen Zhou(Western University)
Cited by 7
Related Papers
The protein disulphide-isomerase family: unravelling a string of folds
|Biochemical Journal|1999|500
Arsenic targets Pin1 and cooperates with retinoic acid to inhibit cancer-driving pathways and tumor-initiating cells
|Nature Communications|2018|161
The protein disulphide-isomerase family: unravelling a string of folds
|Biochemical Journal|1999|140
ERp28, a human endoplasmic‐reticulum‐lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin‐box motif
|European Journal of Biochemistry|1998|85
Reduction of protein disulfide bonds in an oxidizing environment
|FEBS Letters|1997|80