The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Structure and Function of the Membrane Anchor Domain of Hepatitis C Virus Nonstructural Protein 5A
Open accessAbstract
Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a membrane-associated, essential component of the viral replication complex. Here, we report the three-dimensional structure of the membrane anchor domain of NS5A as determined by NMR spectroscopy. An alpha-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trprich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic alpha-helix embedded in the cytosolic leaflet of the membrane bilayer. Interestingly, mutations affecting the positioning of fully conserved residues located at the cytosolic surface of the helix impaired HCV RNA replication without interfering with the membrane association of NS5A. In conclusion, the NS5A membrane anchor domain constitutes a unique platform that is likely involved in specific interactions essential for the assembly of the HCV replication complex and that may represent a novel target for antiviral intervention.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Replication of Subgenomic Hepatitis C Virus RNAs in a Hepatoma Cell Line
Lohmann, V., Körner, F., Koch, J.-O., Herian, U., Theilmann, L., & Bartenschlager, R. (1999) · Science · doi:10.1126/science.285.5424.110 · Cited by 2,814
Self-citationRASMOL: biomolecular graphics for all
Sayle, R. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89080-5 · Cited by 2,575
Wishart, D., & Sykes, B. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,143
Viruses and interferon: a fight for supremacy
Katze, M. G., He, Y., & Gale, M. (2002) · Nature Reviews Immunology · doi:10.1038/nri888 · Cited by 1,419
Efficient Initiation of HCV RNA Replication in Cell Culture
Blight, K. J., Kolykhalov, A. A., & Rice, C. M. (2000) · Science · doi:10.1126/science.290.5498.1972 · Cited by 1,412
The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
Picot, D., Loll, P. J., & Garavito, R. M. (1994) · Nature · doi:10.1038/367243a0 · Cited by 1,265
The Preference of Tryptophan for Membrane Interfaces
Yau, W.-M., Wimley, W. C., Gawrisch, K., & White, S. H. (1998) · Biochemistry · doi:10.1021/bi980809c · Cited by 926
Egger, D., Wölk, B., Gosert, R., Bianchi, L., Blum, H. E., Moradpour, D., & Bienz, K. (2002) · Journal of Virology · doi:10.1128/jvi.76.12.5974-5984.2002 · Cited by 867
Self-citation
Cited by
Appel, N., Zayas, M., Miller, S., Krijnse-Locker, J., Schaller, T., Friebe, P., Kallis, S., Engel, U., & Bartenschlager, R. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000035 · Cited by 466
Self-citation
Metadata
- Authors
- Penin, F., Brass, V., Appel, N., Ramboarina, S., Montserret, R., Ficheux, D., Blum, H. E., Bartenschlager, R., & Moradpour, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-09
- Volume
- 279
- Issue
- 39
- Pages
- 40835-40843
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1974750479
- Cited by
- 301
- References
- 35
- FWCI
- 9.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structure and Function of the Membrane Anchor Domain of Hepatitis C Virus Nonstructural Protein 5A. https://app.cochat.ai/papers/10.1074/jbc.m404761200
- The paper
- Penin, F., Brass, V., Appel, N., Ramboarina, S., Montserret, R., Ficheux, D., Blum, H. E., Bartenschlager, R., & Moradpour, D. (2004). Structure and Function of the Membrane Anchor Domain of Hepatitis C Virus Nonstructural Protein 5A. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m404761200
Data sources
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.
