The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities-Reference-Cited by-同舟云学术

The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities

Published:2014-10 Issue:1 Volume:453 Page:138-142
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Floyd Jeanetta Holley,You Zhipeng,Hsieh Ying-Hsin,Ma Yamin,Yang Hsuichin,Tai Phang C.

Funder

NIH

Georgia Research Alliance

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference38 articles.

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2. Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli;Oliver;J. Bacteriol.,1982

3. Regulation of a membrane component required for protein secretion in Escherichia coli;Oliver;Cell,1982

4. ATP is essential for protein translocation into Escherichia coli membrane vesicles;Chen;PNAS,1985

5. Escherichia coli translocase: the unravelling of a molecular machine;Manting;Mol. Microbiol.,2000

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