Tunable Heteroassembly of a Plant Pseudoenzyme–Enzyme Complex-Reference-Cited by-同舟云学术

Tunable Heteroassembly of a Plant Pseudoenzyme–Enzyme Complex

Published:2021-09-14 Issue:11 Volume:16 Page:2315-2325
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Novikova Irina V.¹,Zhou Mowei¹^ORCID,Du Chen²³,Parra Marcelina⁴,Kim Doo Nam⁵,VanAernum Zachary L.²³,Shaw Jared B.¹,Hellmann Hanjo⁴,Wysocki Vicki H.²³^ORCID,Evans James E.¹⁴^ORCID

Affiliation:

1. Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99354, United States

2. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States

3. Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio 43210, United States

4. School of Biological Sciences, Washington State University, Pullman, Washington 99164, United States

5. Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99354, United States

Funder

Biological and Environmental Research

National Institutes of Health

EMSL Strategic Science Area Projects

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.1c00475

Reference50 articles.

1. Live and let die: insights into pseudoenzyme mechanisms from structure

2. Mechanism of procaspase-8 activation by c-FLIPL

3. The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism

4. Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties

5. Emerging concepts in pseudoenzyme classification, evolution, and signaling

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