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Cited by 384

The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.

Structural diversity of ABC transporters

Open access
ter Beek, Josy, Guskov, Albert, Slotboom, Dirk Jan·2014·Journal of General Physiology

Abstract

ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.

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Crossref · 10.1085/jgp.201411164

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Metadata

Authors
ter Beek, J., Guskov, A., & Slotboom, D. J.
Venue
Journal of General Physiology
Published
2014-03-17
Volume
143
Issue
4
Pages
419-435
ISSN
  • 0022-1295 (ISSN-L)
  • 1540-7748
OpenAlex
W2145796553
Cited by
384
References
95
FWCI
14.94
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structural diversity of ABC transporters. https://app.cochat.ai/papers/10.1085/jgp.201411164
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ter Beek, J., Guskov, A., & Slotboom, D. J. (2014). Structural diversity of ABC transporters. Journal of General Physiology. https://doi.org/10.1085/jgp.201411164

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.