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Issue Information In this issue, Leah G. Helton, Eileen J. Kennedy & team discuss how constrained peptides can be developed to allosterically inhibit the pathogenic activity of Leucine Rich Repeat Kinase 2 (LRRK2). LRRK2 is a large, multi-domain protein kinase commonly mutated in Parkinson's Disease (PD). Pathogenic mutations within LRRK2 often induce increased kinase activity, an effect that can be abolished with small molecule inhibitors. Currently however, many of these inhibitors are limited by their toxicity. Given the complex nature of LRRK2, recent efforts have focused on resolving LRRK2 structures, as well as studying protein–protein interactions involving LRRK2 and how they contribute to PD. (doi: 10.1002/ pep2.24251) EDITOR-IN-CHIEF P. Balaram Shiroh Futaki Beate Koksch Carles Mas Moruno Indian Institute of Kyoto University Freie Universität Berlin Universitat Politècnica de Hilary J. Crichton Science Kyoto, Japan Berlin, Germany Catalunya Bangalore, India Barcelona, Spain ASSOCIATE EDITOR Samuel H. Gellman Yoshiaki Kiso Conor H. Doss Miguel Castanho University of Wisconsin- Nagahama Institute of James S. Nowick University of Lisbon Madison Bio-Science and Technology University of California, EXECUTIVE EDITORS Lisbon, Portugal Madison, WI, U.S.A. Nagahama, Japan Irvine Joel P. Schneider Irvine, CA, U.S.A. Frederick, MD, U.S.A. Jean Chmielewski Gilles Guichard Kit S. Lam Purdue University University http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Peptide Science Wiley

Issue Information

Peptide Science , Volume 114 (1) – Jan 1, 2022
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Publisher
Wiley
Copyright
© 2022 Wiley Periodicals LLC.
eISSN
2475-8817
DOI
10.1002/pep2.24257
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Abstract

In this issue, Leah G. Helton, Eileen J. Kennedy & team discuss how constrained peptides can be developed to allosterically inhibit the pathogenic activity of Leucine Rich Repeat Kinase 2 (LRRK2). LRRK2 is a large, multi-domain protein kinase commonly mutated in Parkinson's Disease (PD). Pathogenic mutations within LRRK2 often induce increased kinase activity, an effect that can be abolished with small molecule inhibitors. Currently however, many of these inhibitors are limited by their toxicity. Given the complex nature of LRRK2, recent efforts have focused on resolving LRRK2 structures, as well as studying protein–protein interactions involving LRRK2 and how they contribute to PD. (doi: 10.1002/ pep2.24251) EDITOR-IN-CHIEF P. Balaram Shiroh Futaki Beate Koksch Carles Mas Moruno Indian Institute of Kyoto University Freie Universität Berlin Universitat Politècnica de Hilary J. Crichton Science Kyoto, Japan Berlin, Germany Catalunya Bangalore, India Barcelona, Spain ASSOCIATE EDITOR Samuel H. Gellman Yoshiaki Kiso Conor H. Doss Miguel Castanho University of Wisconsin- Nagahama Institute of James S. Nowick University of Lisbon Madison Bio-Science and Technology University of California, EXECUTIVE EDITORS Lisbon, Portugal Madison, WI, U.S.A. Nagahama, Japan Irvine Joel P. Schneider Irvine, CA, U.S.A. Frederick, MD, U.S.A. Jean Chmielewski Gilles Guichard Kit S. Lam Purdue University University

Journal

Peptide Science – Wiley

Published: Jan 1, 2022

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