G
Gunter Fischer
Researcher at Max Planck Society
Publications - 253
Citations - 15039
Gunter Fischer is an academic researcher from Max Planck Society. The author has contributed to research in topics: Isomerase & Peptide bond. The author has an hindex of 62, co-authored 252 publications receiving 14353 citations. Previous affiliations of Gunter Fischer include Institut Gustave Roussy & Martin Luther University of Halle-Wittenberg.
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Journal ArticleDOI
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.
TL;DR: The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A (CsA), which is thought to be linked to the immunosuppressive action of CsA.
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Sequence-specific and phosphorylation dependent proline isomerization: A potential mitotic regulatory mechanism
Michael B. Yaffe,Mike Schutkowski,Minhui Shen,Xiao Zhen Zhou,P. Todd Stukenberg,Jens Rahfeld,Jian Xu,Jian Kuang,Marc W. Kirschner,Gunter Fischer,Lewis C. Cantley,Kun Ping Lu +11 more
TL;DR: Pin1 is shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine- Proline bonds present in mitotic phosphoproteins, providing the basis for the specific interaction between Pin1 and MPM-2 antigens.
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Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins.
Xiao Zhen Zhou,Oliver Kops,Andreas Werner,Pei Jung Lu,Minhui Shen,Gerlind Stoller,Gerhard Küllertz,Michael J. R. Stark,Gunter Fischer,Kun Ping Lu +9 more
TL;DR: It is shown that the major Pro-directed phosphatase PP2A is conformation-specific and effectively dephosphorylates only the trans pSer/Thr-Pro isomer, and prolyl isomerase activity of Pin1 is essential for cell division in vivo.
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Catalysis of protein folding by prolyl isomerase.
TL;DR: The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was discovered and purified from pig kidney and it is shown that it also catalyses slow steps in the refolding of a number of proteins of which fast- and slow-folding species have been observed and where it was suggested that proline isomerization was involved in slow refolding.