The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment
Open accessAbstract
Human islet amyloid polypeptide is a hormone coexpressed with insulin by pancreatic beta-cells. For reasons not clearly understood, hIAPP aggregates in type II diabetics to form oligomers that interfere with beta-cell function, eventually leading to the loss of insulin production. The cellular membrane catalyzes the formation of amyloid deposits and is a target of amyloid toxicity through disruption of the membrane’s structural integrity. Therefore, there is considerable current interest in solving the 3D structure of this peptide in a membrane environment. NMR experiments could not be directly utilized in lipid bilayers due to the rapid aggregation of the peptide. To overcome this difficulty, we have solved the structure of the naturally occurring peptide in detergent micelles at a neutral pH. The structure has an overall kinked helix motif, with residues 7–17 and 21–28 in a helical conformation, and with a 310 helix from Gly 33 – Asn 35. In addition, the angle between the N- and C-terminal helices is constrained to 85º. The greater helical content of human IAPP in the amidated versus free acid form is likely to play a role in its aggregation and membrane disruptive activity.
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Cites
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163
NMR of Proteins and Nucleic Acids
(2006) · Nuclear Magnetic Resonance · doi:10.1039/9781847555236-00336 · Cited by 5,863
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957 · cited 1×
“NOE connectivities were used for the calculation of dihedral angle restraints [30].”
MethodTorsion angle dynamics for NMR structure calculation with the new program Dyana
Güntert, P., Mumenthaler, C., & Wüthrich, K. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1284 · Cited by 2,782
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1992) · Biochemistry · doi:10.1021/bi00121a010 · Cited by 2,051
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996
Herrmann, T., Güntert, P., & Wüthrich, K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00241-3 · Cited by 1,460
Structure and Dynamics of Micelle-bound Human α-Synuclein
Ulmer, T. S., Bax, A., Cole, N. B., & Nussbaum, R. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411805200 · Cited by 966
Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D., & Baldus, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506109102 · Cited by 647
Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis
Haataja, L., Gurlo, T., Huang, C. J., & Butler, P. C. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0037 · Cited by 612
Cited by
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Self-citationIslet amyloid polypeptide: structure, function, and pathophysiology
Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2798269 · Cited by 273
Metadata
- Authors
- Nanga, R. P. R., Brender, J. R., Vivekanandan, S., & Ramamoorthy, A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 1808
- Issue
- 10
- Pages
- 2337-2342
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2098651156
- Cited by
- 278
- References
- 63
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Nanga, R. P. R., Brender, J. R., Vivekanandan, S., & Ramamoorthy, A. (2011). Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment. Biochimica et Biophysica Acta (BBA) - Biomembranes. https://doi.org/10.1016/j.bbamem.2011.06.012
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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.
