The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
P-Type ATPases
Abstract
P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines. Phylogenetically, P-type ATPases are divided into five subfamilies, P1–P5. These subfamilies differ with respect to transported ligands and the way they are regulated.
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Cites
Ramirez, A., Heimbach, A., Gründemann, J., Stiller, B., Hampshire, D., Cid, L. P., Goebel, I., Mubaidin, A. F., Wriekat, A.-L., Roeper, J., et al. (2006) · Nature Genetics · doi:10.1038/ng1884 · Cited by 1,208
DNA end-joining: from yeast to man
Critchlow, S. E., & Jackson, S. P. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01284-5 · Cited by 584
The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase
Rensing, C., Mitra, B., & Rosen, B. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14326 · Cited by 419
Nucifora, G., Chu, L., Misra, T. K., & Silver, S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3544 · Cited by 359
Cited by
Copper bioavailability, uptake, toxicity and tolerance in plants: A comprehensive review
Kumar, V., Pandita, S., Singh Sidhu, G. P., Sharma, A., Khanna, K., Kaur, P., Bali, A. S., & Setia, R. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2020.127810 · Cited by 594
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Calcium-dependent Phospholipid Scramblase Activity of TMEM16 Protein Family Members
Suzuki, J., Fujii, T., Imao, T., Ishihara, K., Kuba, H., & Nagata, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457937 · Cited by 371
Copper in Microbial Pathogenesis: Meddling with the Metal
Samanovic, M. I., Ding, C., Thiele, D. J., & Darwin, K. H. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.009 · Cited by 278
The Role of Copper Homeostasis at the Host-Pathogen Axis: From Bacteria to Fungi
Li, C., Li, Y., & Ding, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010175 · Cited by 107
Metadata
- Authors
- Palmgren, M. G., & Nissen, P.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2011-06-09
- Volume
- 40
- Issue
- 1
- Pages
- 243-266
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2107872932
- Cited by
- 687
- References
- 4
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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