Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions-Reference-Cited by-同舟云学术

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Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions

Published:2016-02 Issue:2 Volume:1858 Page:374-385
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Milenkovic Stefan,Bondar Ana-Nicoleta

Funder

Marie Curie International Reintegration Award IRG

Excellence Initiative of the German State and Federal Governments

HLRN North-German Supercomputing Alliance

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference87 articles.

1. The binding cascade of SecB to SecA to SecY/E mediates preprotein targetting to the E. coli plasma membrane;Hartl;Cell,1990

2. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins;Lill;Cell,1990

3. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation;Brundage;Cell,1990

4. SecYEG and SecA are the stoichiometric components of preprotein translocase;Douville;J. Biol. Chem.,1995

5. SecA-mediated targeting and translocation of secretory proteins;Chatzi;Biochim. Biophys. Acta,2014

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3. Diversity and sequence motifs of the bacterial SecA protein motor;Biochimica et Biophysica Acta (BBA) - Biomembranes;2020-10

4. Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles;Microorganisms;2019-12-29

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