The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution
Open accessAbstract
The structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8 Å. The analysis started from a closely related crystal structure that had been solved at a medium resolution of 3 Å using multiple isomorphous replacement and solvent flattening. The new structure contains the complete sequence of 301 amino acid residues. Refinement of the model is under way: the present R‐factor is 22% with good geometry. Except for the lengths of several loops, the resulting chain fold corresponds to the medium resolution model. The membrane channel is lined by a large number of ionogenic side chains with characteristic segregation of differently charged groups.
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Cites
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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
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Molecular basis of bacterial outer membrane permeability
Nikaido, H., & Vaara, M. (1985) · Microbiological Reviews · doi:10.1128/mmbr.49.1.1-32.1985 · Cited by 2,447
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,956
Improved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,873
Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
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Structure and function of bacterial photosynthetic reaction centres
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Permeation of hydrophilic molecules through the outer membrane of gram‐negativ bacteria
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Three-dimensional structure of glutathione reductase at 2 Å resolution
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Self-citationThe three‐dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
Weiss, M. S., Wacker, T., Weckesser, J., Weite, W., & Schulz, G. E. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80942-c · Cited by 201
Self-citation
Cited by
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective
Bloom, M., Evans, E., & Mouritsen, O. G. (1991) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500003735 · Cited by 872
Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L., Winter, N., Xu, Z., Bernlohr, D. A., Cowan, S., & Jones, A. T. (1994) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60639-7 · Cited by 485
Bennett, J. A., & Dingledine, R. (1995) · Neuron · doi:10.1016/0896-6273(95)90293-7 · Cited by 287
Saier, M. H. (1994) · Microbiological Reviews · doi:10.1128/mmbr.58.1.71-93.1994 · Cited by 275
Metadata
- Authors
- Weiss, M. S., Kreusch, A., Schiltz, E., Nestel, U., Welte, W., Weckesser, J., & Schulz, G. E.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1991-03-25
- Volume
- 280
- Issue
- 2
- Pages
- 379-382
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2066947455
- Cited by
- 300
- References
- 16
- FWCI
- 39.08
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Weiss, M. S., Kreusch, A., Schiltz, E., Nestel, U., Welte, W., Weckesser, J., & Schulz, G. E. (1991). The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Letters. https://doi.org/10.1016/0014-5793(91)80336-2
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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.
