A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer
- Authors:
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- NCINIHOTHER
- OSTI Identifier:
- 1504990
- Resource Type:
- Journal Article
- Journal Name:
- Nature Structural & Molecular Biology
- Additional Journal Information:
- Journal Volume: 24; Journal Issue: 8; Journal ID: ISSN 1545-9993
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
Citation Formats
Robertson, Rosanna M., Yao, Jiangwei, Gajewski, Stefan, Kumar, Gyanendra, Martin, Erik W., Rock, Charles O., and White, Stephen W. A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer. United States: N. p., 2017.
Web. doi:10.1038/nsmb.3436.
Robertson, Rosanna M., Yao, Jiangwei, Gajewski, Stefan, Kumar, Gyanendra, Martin, Erik W., Rock, Charles O., & White, Stephen W. A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer. United States. doi:10.1038/nsmb.3436.
Robertson, Rosanna M., Yao, Jiangwei, Gajewski, Stefan, Kumar, Gyanendra, Martin, Erik W., Rock, Charles O., and White, Stephen W. Mon .
"A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer". United States. doi:10.1038/nsmb.3436.
@article{osti_1504990,
title = {A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer},
author = {Robertson, Rosanna M. and Yao, Jiangwei and Gajewski, Stefan and Kumar, Gyanendra and Martin, Erik W. and Rock, Charles O. and White, Stephen W.},
abstractNote = {},
doi = {10.1038/nsmb.3436},
journal = {Nature Structural & Molecular Biology},
issn = {1545-9993},
number = 8,
volume = 24,
place = {United States},
year = {2017},
month = {7}
}
DOI: 10.1038/nsmb.3436
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