Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone.
- DOI
- 10.1093/jb/mvag041
- Published
- 2026 Sep 3
- Container
- Journal of biochemistry
- Publisher
- Not recorded
- Open access
- unknown
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Cite this work
BibTeX
@article{allodium:10.1093/jb/mvag041,
title = {Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone.},
author = {Torii M and Kanno R and Mizoguchi A and Humbel BM and Tani K and Masui R},
year = {2026},
journal = {Journal of biochemistry},
doi = {10.1093/jb/mvag041},
url = {https://doi.org/10.1093/jb/mvag041}
}RIS
TY - JOUR TI - Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone. AU - Torii M AU - Kanno R AU - Mizoguchi A AU - Humbel BM AU - Tani K AU - Masui R PY - 2026 JO - Journal of biochemistry DO - 10.1093/jb/mvag041 UR - https://doi.org/10.1093/jb/mvag041 ER -
APA
M, T., R, K., A, M., BM, H., K, T., & R, M. (2026). Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone.. Journal of biochemistry. https://doi.org/10.1093/jb/mvag041
Source records
- pubmed · retrieved 2026-09-25T14:38:23.848Z