Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α-Synuclein-Reference-Cited by-同舟云学术

Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α-Synuclein

Published:2022-04-22 Issue:17 Volume:144 Page:7911-7918
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Pan Buyan¹,Shimogawa Marie¹^ORCID,Zhao Jun²,Rhoades Elizabeth¹,Kashina Anna²,Petersson E. James¹^ORCID

Affiliation:

1. Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, United States

2. Department of Biomedical Sciences, University of Pennsylvania School of Veterinary Medicine, 3800 Spruce Street, Philadelphia, Pennsylvania 19104, United States

Funder

Division of Chemistry

National Institute of Neurological Disorders and Stroke

National Center for Research Resources

University of Pennsylvania

Heiwa Nakajima Foundation

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.2c02499

Reference40 articles.

1. Arginyltransferase Is an ATP-Independent Self-Regulating Enzyme that Forms Distinct Functional Complexes In Vivo

2. Global Analysis of Posttranslational Protein Arginylation

3. Identification of N-terminally arginylated proteins and peptides by mass spectrometry

4. Arginyltransferase ATE1 Catalyzes Midchain Arginylation of Proteins at Side Chain Carboxylates In Vivo

5. Role of KCNB1 in the prognosis of gliomas and autophagy modulation

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