Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR-Reference-Cited by-同舟云学术

Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR

Published:2019-10-11 Issue:43 Volume:141 Page:17314-17321
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Shi Chaowei¹²,Öster Carl¹,Bohg Claudia¹,Li Longmei²,Lange Sascha¹,Chevelkov Veniamin¹,Lange Adam¹³^ORCID

Affiliation:

1. Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin 13125, Germany

2. Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Huangshan Road 443, Hefei 230027, People’s Republic of China

3. Institut für Biologie, Humboldt-Universität zu Berlin, Invalidenstraße 42, Berlin 10115, Germany

Funder

Deutsche Forschungsgemeinschaft

Human Frontier Science Program

Chinese Academy of Sciences

Leibniz-Forschungsinstitut f?r Molekulare Pharmakologie

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.9b08952

Reference43 articles.

1. Rhomboid proteases in human disease: Mechanisms and future prospects

2. Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine Proteases

3. Crystal structure of a rhomboid family intramembrane protease

4. Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry

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