Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures-Reference-Cited by-同舟云学术

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Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures

Published:2014-09-12 Issue:20 Volume:33 Page:2408-2421
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Zoll Sebastian¹,Stanchev Stancho¹,Began Jakub¹²,Škerle Jan¹³,Lepšík Martin¹,Peclinovská Lucie¹³,Majer Pavel¹,Strisovsky Kvido¹

Affiliation:

1. Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic Prague Czech Republic

2. Department of Microbiology Faculty of Science Charles University Prague Czech Republic

3. Department of Biochemistry Faculty of Science Charles University Prague Czech Republic

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201489367

Reference55 articles.

1. Tumor Necrosis Factor Signaling Requires iRhom2 to Promote Trafficking and Activation of TACE

2. Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease

3. Allosteric regulation of rhomboid intramembrane proteolysis

4. Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate

5. Architectural and thermodynamic principles underlying intramembrane protease function

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