Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries-Reference-Cited by-同舟云学术

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Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries

Published:2019-05 Issue:5 Volume:5 Page:e01587
ISSN:2405-8440
Container-title:Heliyon
language:en
Short-container-title:Heliyon

Author:

Ghosh Deepanjan,Boral Debjyoti,Vankudoth Koteswara Rao,Ramasamy Sureshkumar

Funder

Council of Scientific and Industrial Research

University Grant Commision (UGC), India.

Publisher

Elsevier BV

Subject

Multidisciplinary

Reference48 articles.

1. The twin-arginine translocation (Tat) protein export pathway;Palmer;Nat. Rev. Microbiol.,2012

2. The Tat protein export pathway;Berks;Mol. Microbiol.,2000

3. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway;Berks;Curr. Opin. Microbiol.,2005

4. Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo-designed heme protein;Sutherland;J. Biol. Chem.,2018

5. Mechanisms of Sec61/SecY-mediated protein translocation across membranes;Park;Annu. Rev. Biophys.,2012

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The polar amino acid in the TatA transmembrane helix is not strictly necessary for protein function;Journal of Biological Chemistry;2023-04

2. Survival Strategies and Stress Adaptations in Halophilic Archaebacteria;ACS Symposium Series;2023-01-12

3. Functional analysis of the polar amino acid in TatA transmembrane helix;2021-11-30

4. In Silico Analysis of the Enzymes Involved in Haloarchaeal Denitrification;Biomolecules;2021-07-16

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