An Elegant Four-Helical Fold in NOX and STEAP Enzymes Facilitates Electron Transport across Biomembranes—Similar Vehicle, Different Destination-Reference-Cited by-同舟云学术

An Elegant Four-Helical Fold in NOX and STEAP Enzymes Facilitates Electron Transport across Biomembranes—Similar Vehicle, Different Destination

Published:2020-08-20 Issue:9 Volume:53 Page:1969-1980
ISSN:0001-4842
Container-title:Accounts of Chemical Research
language:en
Short-container-title:Acc. Chem. Res.

Author:

Oosterheert Wout¹^ORCID,Reis Joana²,Gros Piet¹,Mattevi Andrea²^ORCID

Affiliation:

1. Crystal and Structural Chemistry, Bijvoet Centre for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

2. Department of Biology and Biotechnology ‘L. Spallanzani’, University of Pavia, 27100 Pavia, Italy

Funder

Ministero dell’Istruzione, dell’Università e della Ricerca

Associazione Italiana per la Ricerca sul Cancro

H2020 Marie Sklodowska-Curie Actions

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

American Chemical Society (ACS)

Subject

General Medicine,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.accounts.0c00400

Reference63 articles.

1. Crystal structures and atomic model of NADPH oxidase

2. Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction

3. A closer look into NADPH oxidase inhibitors: Validation and insight into their mechanism of action

4. Cryo-electron microscopy structure and potential enzymatic function of human six-transmembrane epithelial antigen of the prostate 1 (STEAP1)

5. Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution

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