The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles
Open accessAbstract
We apply pulsed dipolar ESR spectroscopy (Ku-band DEER) to elucidate the global conformation of the Parkinson's disease-associated protein, alpha-synuclein (alphaS) bound to small unilamellar phospholipid vesicles, rodlike SDS micelles, or lipid bicelles. By measuring distances as long as approximately 7 nm between introduced pairs of nitroxide spin labels, we show that distances are close to the expectations for a single continuous helix in all cases studied. In particular, we find distances of 7.5 nm between sites 24 and 72; 5.5 nm between sites 24 and 61; and 2 nm between sites 35 and 50. We conclude that alphaS does not retain a "hairpin" structure with two antiparallel helices, as is known to occur with spheroidal micelles, in agreement with our earlier finding that the protein's geometry is determined by the surface topology rather than being constrained by the interhelix linker. While the possibility of local helix discontinuities in the structure of membrane-bound alphaS remains, our data are more consistent with one intact helix. Importantly, we demonstrate that bicelles produce very similar results to liposomes, while offering a major improvement in experimentally accessible distance range and resolution, and thus are an excellent lipid membrane mimetic for the purpose of pulse dipolar ESR spectroscopy.
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Citations
Cites
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,641
Eliezer, D., Kutluay, E., Bussell, R., & Browne, G. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4538 · Cited by 1,090
Self-citationStructure 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
Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance
Jeschke, G., & Polyhach, Y. (2007) · Physical Chemistry Chemical Physics · doi:10.1039/b614920k · Cited by 611
Long-range distance determinations in biomacromolecules by EPR spectroscopy
Schiemann, O., & Prisner, T. F. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s003358350700460x · Cited by 557
A Broken α-Helix in Folded α-Synuclein
Chandra, S., Chen, X., Rizo, J., Jahn, R., & Südhof, T. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213128200 · Cited by 540
Bussell, R., & Eliezer, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00520-5 · Cited by 418
Self-citationStructure of membrane-bound α-synuclein studied by site-directed spin labeling
Jao, C. C., Der-Sarkissian, A., Chen, J., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400553101 · Cited by 359
Borbat, P. P., Mchaourab, H. S., & Freed, J. H. (2002) · Journal of the American Chemical Society · doi:10.1021/ja020040y · Cited by 281
Self-citationNeural Activity Controls the Synaptic Accumulation of α-Synuclein
Fortin, D. L., Nemani, V. M., Voglmaier, S. M., Anthony, M. D., Ryan, T. A., & Edwards, R. H. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2922-05.2005 · Cited by 271
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Amyloidogenic Protein–Membrane Interactions: Mechanistic Insight from Model Systems
Butterfield, S. M., & Lashuel, H. A. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906670 · Cited by 592
Cell Biology and Pathophysiology of α-Synuclein
Burré, J., Sharma, M., & Südhof, T. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 579
The Synaptic Function of α-Synuclein
Burré, J. (2015) · Journal of Parkinson's Disease · doi:10.3233/jpd-150642 · Cited by 573
Fauvet, B., Mbefo, M. K., Fares, M.-B., Desobry, C., Michael, S., Ardah, M. T., Tsika, E., Coune, P., Prudent, M., Lion, N., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.318949 · Cited by 566
Self-citationPhysicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
The Transcellular Spread of Cytosolic Amyloids, Prions, and Prionoids
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Rotamer libraries of spin labelled cysteines for protein studies
Polyhach, Y., Bordignon, E., & Jeschke, G. (2011) · Phys. Chem. Chem. Phys. · doi:10.1039/c0cp01865a · Cited by 425
The Magic of Bicelles Lights Up Membrane Protein Structure
Dürr, U. H. N., Gildenberg, M., & Ramamoorthy, A. (2012) · Chemical Reviews · doi:10.1021/cr300061w · Cited by 362
Uversky, V. N. (2009) · The Protein Journal · doi:10.1007/s10930-009-9201-4 · Cited by 360
C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
Lautenschläger, J., Stephens, A. D., Fusco, G., Ströhl, F., Curry, N., Zacharopoulou, M., Michel, C. H., Laine, R., Nespovitaya, N., Fantham, M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03111-4 · Cited by 334
The physiological role of α‐synuclein and its relationship to Parkinson’s Disease
Sulzer, D., & Edwards, R. H. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14810 · Cited by 312
Interactions by disorder – A matter of context
Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155
“A similar behavior was also observed for the IDP α -synuclein (aSN) (Georgieva et al., 2008; Fusco et al., 2014; Cholak et al., 2020).”
Background
Metadata
- Authors
- Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., & Eliezer, D.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-09-06
- Volume
- 130
- Issue
- 39
- Pages
- 12856-12857
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2026665110
- Cited by
- 275
- References
- 23
- FWCI
- 12.46
- Type
- journal article
- Language
- en
- Open access
- green
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