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Cited by 2,377

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

Song, Langzhou, Hobaugh, Michael R., Shustak, Christopher, Cheley, Stephen, Bayley, Hagan, Gouaux, J. Eric·1996·Science

Abstract

The structure of the Staphylococcus aureus α-hemolysin pore has been determined to 1.9 Å resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 Å in length, that runs along the sevenfold axis and ranges from 14 Å to 46 Å in diameter. The lytic, transmembrane domain comprises the lower half of a 14-strand antiparallel β barrel, to which each protomer contributes two β strands, each 65 Å long. The interior of the β barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 Å wide. The structure proves the heptameric subunit stoichiometry of the α-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of β barrel pore-forming toxins.

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Metadata

Authors
Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E.
Venue
Science
Published
1996-12-13
Volume
274
Issue
5294
Pages
1859-1865
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2030683115
Cited by
2,377
References
41
FWCI
50.38
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore. https://app.cochat.ai/papers/10.1126/science.274.5294.1859
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Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996). Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore. Science. https://doi.org/10.1126/science.274.5294.1859

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