Aryl Indanyl Ketones: Efficient Inhibitors of the Human Peptidyl Prolyl  cis / trans  Isomerase Pin1 | Zendy

Daum Sebastian | Zendy; Erdmann Frank | Zendy; Fischer Gunter | Zendy; Féaux de Lacroix Boris | Zendy; HessamianAlinejad Anahita | Zendy; Houben Sabine | Zendy; Frank Walter | Zendy; Braun Manfred | Zendy

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Aryl Indanyl Ketones: Efficient Inhibitors of the Human Peptidyl Prolyl cis / trans Isomerase Pin1

Author(s) -

Daum Sebastian,

Erdmann Frank,

Fischer Gunter,

Féaux de Lacroix Boris,

HessamianAlinejad Anahita,

Houben Sabine,

Frank Walter,

Braun Manfred

Publication year - 2006

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200601569

Subject(s) - isomerase , pin1 , chemistry , stereochemistry , aryl , residue (chemistry) , proline , prolyl isomerase , peptide , enzyme , biochemistry , organic chemistry , amino acid , alkyl

A good imitation : Aryl‐1‐indanyl ketones are found to be highly efficient, reversible, cell‐penetrating inhibitors of the human peptidyl prolyl cis/trans isomerase Pin1. Owing to their structure 1 , they are assumed to mimic the transition state 2 of the enzymatically catalyzed rotation about the imidic peptide bond preceding a proline residue.

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