Quantitative Measurement of Intact Alpha-Synuclein Proteoforms from Post-Mortem Control and Parkinson's Disease Brain Tissue by Intact Protein Mass Spectrometry
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A robust top down proteomics method is presented for profiling alpha-synuclein species from autopsied human frontal cortex brain tissue from Parkinson's cases and controls. The method was used to test the hypothesis that pathology associated brain tissue will have a different profile of post-translationally modified alpha-synuclein than the control samples. Validation of the sample processing steps, mass spectrometry based measurements, and data processing steps were performed. The intact protein quantitation method features extraction and integration of m/z data from each charge state of a detected alpha-synuclein species and fitting of the data to a simple linear model which accounts for concentration and charge state variability. The quantitation method was validated with serial dilutions of intact protein standards. Using the method on the human brain samples, several previously unreported modifications in alpha-synuclein were identified. Low levels of phosphorylated alpha synuclein were detected in brain tissue fractions enriched for Lewy body pathology and were marginally significant between PD cases and controls (p = 0.03).
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In neurological disease and aging, modified proteins are the histopathological hallmarks of a number of diseases, such as SOD1 in amyotrophic lateral sclerosis (ALS), and a class of diseases long referred to as the proteinopathies, including tauopathies in Alzheimer's disease and inclusions of amyloid beta, alpha-synuclein in Parkinson's and multiple secondary ubiquitinopathies.
“In neurological disease and aging, modified proteins are the histopathological hallmarks of a number of diseases, such as SOD1 in amyotrophic lateral sclerosis (ALS) 56,57 , and a class of diseases long referred to as the proteinopathies 57 , including tauopathies in Alzheimer's disease 58 and inclusions of amyloidβ 59 , α -synuclein in Parkinson's 60,61 and multiple secondary ubiquitinopathies”
From How many human proteoforms are there? (2018) · cites this paper as [60]
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Biomarkers in Neurodegenerative Diseases: Proteomics Spotlight on ALS and Parkinson’s Disease
Raghunathan, R., Turajane, K., & Wong, L. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169299 · Cited by 60 · see citing works
C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson's disease
McGlinchey, R., Lacy, S., Huffer, K., Tayebi, N., Sidransky, E., & Lee, J. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008930 · Cited by 51 · see citing works
Structure of alpha-synuclein fibrils derived from human Lewy body dementia tissue
Dhavale, D. D., Barclay, A. M., Borcik, C. G., Basore, K., Berthold, D. A., Gordon, I. R., Liu, J., Milchberg, M. H., O’Shea, J. Y., Rau, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46832-5 · Cited by 72 · see citing works
Altay, M. F., Kumar, S. T., Burtscher, J., Jagannath, S., Strand, C., Miki, Y., Parkkinen, L., Holton, J. L., & Lashuel, H. A. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00604-y · Cited by 48 · see citing works
“…2a (PDB-6SSX, EMD-10307); and polymorph 2b (PDB-6SST, EMD-10305). c aSyn PTMs identi fi ed in synucleinopathy brain tissues, which include acetylation 29,30,81,82 , ubiquitination 29,30,32,52,72 – 78 , phosphorylation 7,29,30, 50 – 71 , nitration 79, 80 , and truncation 1 , antibodies (Fig.”
Deciphering combinatorial post-translational modifications by top-down mass spectrometry
Brodbelt, J. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102180 · Cited by 50 · see citing works
Role of α-Synuclein regions in nucleation and elongation of amyloid fibres assembly.
Gallardo, J., Escalona-Noguero, C., & Sot, B. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00527 · Cited by 49
In situ proximity labeling identifies Lewy pathology molecular interactions in the human brain
Killinger, B., Marshall, L. L., Chatterjee, D., Chu, Y., Bras, J., Guerreiro, R., & Kordower, J. (2022) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2114405119 · Cited by 48 · see citing works
“Alpha-synuclein phosphorylated at serine 129 (PSER129) is a marker of LP. PSER129 is enriched in LP with only trace quantities ( 5% of total alpha-synuclein pool) of endogenous alpha-synuclein being phosphorylated (2).”
Quantifying Co-Oligomer Formation by α-Synuclein
Iljina, M., Dear, A. J., Garcia, G. A., De, S., Tosatto, L., Flagmeier, P., Whiten, D. R., Michaels, T. C. T., Frenkel, D., Dobson, C. M., et al. (2018) · ACS Nano · doi:10.1021/acsnano.8b03575 · Cited by 48 · see citing works
Neurons and Glia Interplay in α-Synucleinopathies
Mavroeidi, P., & Xilouri, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094994 · Cited by 52 · see citing works
Mahul‐Mellier, A., Altay, M. F., Burtscher, J., Maharjan, N., Ait‐Bouziad, N., Chiki, A., Vingill, S., Wade‐Martins, R., Holton, J. L., Strand, C., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/500058 · Cited by 45 · see citing works
Bell, R., & Vendruscolo, M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.661117 · Cited by 52 · see citing works
Pieri, L., Chafey, P., Gall, M. L., Clary, G., Melki, R., & Redeker, V. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.10.007 · Cited by 64 · see citing works
“Indeed, most of the truncation sites identified in this work were previously identified onα-Syn extracted from LBs or from healthy or PD post-mortemwhole brain tissues [32,75].”
InfluentialExtracellular alpha-synuclein: Sensors, receptors, and responses
Domingues, R., Sant’Anna, R., da Fonseca, A. C. C., Robbs, B. K., Foguel, D., & Outeiro, T. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105696 · Cited by 37 · see citing works
Limegrover, C. S., Yurko, R., Izzo, N. J., Mozzoni, K., Rehak, C., Look, G. C., Rishton, G. M., Safferstein, H., & Catalano, S. M. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24782 · Cited by 42 · see citing works
“…that extreme non-physiological conditions, such as high detergent and temperature, are required to isolate appreciable concentrations of α-synuclein from postmortem PD-patient brain tissue (Deramecourt et al., 2006; Garcia-Esparcia et al., 2015; Kellie et al., 2014; Paleologou et al., 2009).”
Alpha-synuclein fragments trigger distinct aggregation pathways
Chakroun, T., Evsyukov, V., Nykänen, N.-P., Höllerhage, M., Schmidt, A., Kamp, F., Ruf, V., Wurst, W., Rösler, T. W., & Höglinger, G. U. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2285-7 · Cited by 41 · see citing works
Deep and quantitative top-down proteomics in clinical and translational research
Kelleher, N. L., Thomas, P. M., Ntai, I., Compton, P. D., & LeDuc, R. D. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.976559 · Cited by 43 · see citing works
“An increasing number of labs working at the interface of technology and human health are showing the emergent use of top-down proteomics in translational research [14–17].”
Genotype-driven therapeutic developments in Parkinson’s disease
Prasuhn, J., & Brüggemann, N. (2021) · Molecular Medicine · doi:10.1186/s10020-021-00281-8 · Cited by 38 · see citing works
Protein Quality Control Pathways at the Crossroad of Synucleinopathies
de Mattos, E. P., Wentink, A. S., Nussbaum-Krammer, C. I., Hansen, C., Bergink, S., Melki, R., & Kampinga, H. H. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-191790 · Cited by 45 · see citing works
Mass Spectrometry for Neurobiomarker Discovery: The Relevance of Post-Translational Modifications
Azevedo, R., Jacquemin, C., Villain, N., Fenaille, F., Lamari, F., & Bécher, F. (2022) · Cells · doi:10.3390/cells11081279 · Cited by 42 · see citing works
The Appendix in Parkinson’s Disease: From Vestigial Remnant to Vital Organ?
Killinger, B. A., & Labrie, V. (2019) · Journal of Parkinson s Disease · doi:10.3233/jpd-191703 · Cited by 33 · see citing works
Nanotechnology‐Based Strategies for Early Diagnosis of Central Nervous System Disorders
Hanif, S., Muhammad, P., Niu, Z., Ismail, M., Morsch, M., Zhang, X., Li, M., & Shi, B. (2021) · Advanced NanoBiomed Research · doi:10.1002/anbr.202100008 · Cited by 44 · see citing works
Battis, K., Xiang, W., & Winkler, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713270 · Cited by 36 · see citing works
“α-syn is irreversibly truncated at the N- or C-terminus and present in over 15% of α-syn in Lewy bodies [197].”
Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms
Röntgen, A., Toprakcioglu, Z., Tomkins, J. E., & Vendruscolo, M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313465121 · Cited by 28 · see citing works
“This is also the case for α Syn (8–13), prompting the question of whether different α Syn proteoforms could contribute to the association with disease of this protein.”
Truncation or proteolysis of α-synuclein in Parkinsonism
Suthar, S. K., & Lee, S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101978 · Cited by 32 · see citing works
Poggiolini, I., Erskine, D., Vaikath, N., Ponraj, J., Mansour, S., Morris, C., & El-Agnaf, O. (2021) · Biomolecules · doi:10.3390/biom11060820 · Cited by 28 · see citing works
“While αSyn forms have been quantified in brains of PD patients [27], to the best our knowledge, few studies have compared the presence of C-terminal truncated αSyn forms in different αSynucleinopathies and in different brain regions.”
SUMOylation in α-Synuclein Homeostasis and Pathology
Savyon, M., & Engelender, S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00167 · Cited by 39 · see citing works
Genetic causes of PD: A pathway to disease modification
Toffoli, M., Vieira, S. R. L., & Schapira, A. H. V. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108022 · Cited by 28 · see citing works
Current Evidence for a Bidirectional Loop Between the Lysosome and Alpha-Synuclein Proteoforms
Wildburger, N. C., Hartke, A.-S., Schidlitzki, A., & Richter, F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598446 · Cited by 26 · see citing works
“, 2003; Chavarría and Souza, 2013), oxidation (Chavarría and Souza, 2013), deamidation (Kellie et al., 2014), and ubiquitination (Anderson et al.”
InfluentialIn Search of Effective Treatments Targeting α-Synuclein Toxicity in Synucleinopathies: Pros and Cons
Fouka, M., Mavroeidi, P., Tsaka, G., & Xilouri, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.559791 · Cited by 26 · see citing works
Miller, S., Campbell, C. E., Jimenez-Corea, H. A., Wu, G., & Logan, R. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.824191 · Cited by 32 · see citing works
“Likewise, α-synuclein in Lewy bodies is phosphorylated and nitrated, indicating oxidative stress is intrinsic to their formation (Giasson et al., 2000; Foulds et al., 2011; McCormack et al., 2012; Wang et al., 2012; Kellie et al., 2014).”
The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates
Creekmore, B. C., Chang, Y., & Lee, E. B. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab039 · Cited by 26 · see citing works
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Savaryn, J. P., Toby, T. K., Catherman, A. D., Fellers, R. T., LeDuc, R. D., Thomas, P. M., Friedewald, J., Salomon, D., Abecassis, M., & Kelleher, N. L. (2016) · Proteomics · doi:10.1002/pmic.201600008 · Cited by 23 · see citing works
Carboxy‐terminal truncations of mouse α‐synuclein alter aggregation and prion‐like seeding
Sorrentino, Z. A., Xia, Y., Gorion, K.-M. M., Hass, E. W., & Giasson, B. I. (2020) · FEBS Letters · doi:10.1002/1873-3468.13728 · Cited by 23 · see citing works
Vasicek, L., Zhu, X., Spellman, D. S., & Bateman, K. (2019) · Bioanalysis · doi:10.4155/bio-2018-0240 · Cited by 21 · see citing works
Aggregation of α-synuclein splice isoforms through a phase separation pathway
Röntgen, A., Toprakcioglu, Z., Dada, S. T., Morris, O. M., Knowles, T. P. J., & Vendruscolo, M. (2025) · Science Advances · doi:10.1126/sciadv.adq5396 · Cited by 24 · see citing works
Lázaro, D. F., & Lee, V. M. ‐. (2024) · Neuron · doi:10.1016/j.neuron.2024.05.017 · Cited by 19 · see citing works
Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation
Mahul‐Mellier, A., Altay, M. F., Maharjan, N., Ait‐Bouziad, N., Chiki, A., Jagannath, S., Limorenko, G., Novello, S., Ricci, J., Jasiqi, Y., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01084-y · Cited by 17 · see citing works
Nagarajan, S., & Lapidus, L. J. (2017) · ChemBioChem · doi:10.1002/cbic.201700387 · Cited by 23 · see citing works
Phukan, B. C., Roy, R., Gahatraj, I., Bhattacharya, P., & Borah, A. (2023) · Phytotherapy Research · doi:10.1002/ptr.8012 · Cited by 22 · see citing works
“…dopaminergic neuron degeneration, another major contributor to the same is the abnormal presence of eosinophilic intracytoplasmic proteinaceous inclusions called Lewy bodies (LBs) in the neurons are regarded as the hallmark pathology of the disease (Bhattacharjee et al., 2019; Kellie et al., 2014).”
Quintin, S. S., Lloyd, G. M., Paterno, G., Xia, Y., Sorrentino, Z. A., Bell, B. M., Gorion, K.-M. M., Lee, E. B., Prokop, S., & Giasson, B. I. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104912 · Cited by 19 · see citing works
Pons, M., Loftus, N., Vialaret, J., Moreau, S., Lehmann, S., & Hirtz, C. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.818606 · Cited by 16 · see citing works
Lin, W.-C., Lu, C.-H., Chiu, P.-Y., & Yang, S.-Y. (2020) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000510325 · Cited by 16
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Makey, D. M., Gadkari, V. V., Kennedy, R. T., & Ruotolo, B. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c00477 · Cited by 16 · see citing works
Dewison, K. M., Rowlinson, B., Machin, J. M., Crossley, J. A., Thacker, D., Wilkinson, M., Ulamec, S. M., Khan, G. N., Ranson, N. A., van Oosten‐Hawle, P., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315006121 · Cited by 15 · see citing works
“Such sensitivity also rationalizes why truncations in the N - terminal region of α Syn are found in Lewy bodies in Parkinson’s patients (49), why post-translational modifications in the N - terminal region [such as N - terminal acetylation (19, 20)] and mutations associated with familial disease…”
Top-down and bottom-up proteomics of circulating S100A8/S100A9 in plasma of septic shock patients.
Dubois, C., Payen, D., Simon, S., Junot, C., Fenaille, F., Morel, N., & Becher, F. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00690 · Cited by 14 · see citing works
Lantz, C., Lopez, J., Goring, A. K., Zenaidee, M. A., Biggs, K. E., Whitelegge, J. P., Loo, R. R. O., Klärner, F., Schrader, T. H., Bitan, G., et al. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00281 · Cited by 17 · see citing works
Venere, M. D., Viglio, S., Sassera, D., Fumagalli, M., Bardoni, A., Salvini, R., Cagnone, M., & Iadarola, P. (2017) · Electrophoresis · doi:10.1002/elps.201600504 · Cited by 12 · see citing works
Vidyadhara, D. J., Bäckström, D. C., Chakraborty, R., Ruan, J., Park, J.-M., Mistry, P. K., & Chandra, S. S. (2025) · Nature Communications · doi:10.1038/s41467-025-63444-9 · Cited by 13 · see citing works
Kallunki, P., Sotty, F., Willén, K. I., Lubas, M., David, L., Ambjørn, M., Bergström, A., Vesterager, L. B., Malik, I., Nyegaard, S., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-024-00849-1 · Cited by 14 · see citing works
Prasinezumab slows motor progression in Parkinsons disease: beyond the clinical data
Xiao, B., & Tan, E. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00886-4 · Cited by 15 · see citing works
Petricca, L., Chiki, N., Hanna-El-Daher, L., Aeschbach, L., Burai, R., Stoops, E., Fares, M.-B., & Lashuel, H. (2022) · bioRxiv · doi:10.1101/2022.03.11.483980 · Cited by 12
“5 conformations, including different phosphorylated, truncated, nitrated, and ubiquitinated forms of αSYN [38,39][40] [41].”
InfluentialTransgenic Mice Expressing Human α-Synuclein 1-103 Fragment as a Novel Model of Parkinson’s Disease
Tian, Y., He, M., Pan, L., Yuan, X., Xiong, M., Meng, L., Yao, Z., Yu, Z., Ye, K., & Zhang, Z. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.760781 · Cited by 12 · see citing works
“…of this mouse model was not agedependent and seemed to happen during embryogenesis (Wakamatsu et al., 2008a,b). α-Synuclein 1-119 fragments have been found to be present in the PD brains (Li et al., 2005; Anderson et al., 2006; Lewis et al., 2010; Prasad et al., 2012; Kellie et al., 2015).”
Moors, T. E., Maat, C. A., Niedieker, D., Mona, D., Petersen, D., Huisman, E., Kole, J., El-Mashtoly, S. F., Spycher, L., Zago, W., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/470476 · Cited by 28 · see citing works
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The Diagnostic Potential of Amyloidogenic Proteins
Jin, Y., Vadukul, D. M., Gialama, D., Ge, Y., Thrush, R. J., White, J. T., & Aprile, F. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084128 · Cited by 9 · see citing works
“These include N-terminal acetylation, several truncations at the N-terminus (e.g., α-syn7-140, 14-140, 40-140, and 72–140 found in vitro, 5–140 and 68–140 found in vivo and several in both) and C-terminus (e.g., α-syn1-115, 1-119, 1-122, 1-124, 1-125, 1-129, 1-133, and 1-135), phosphorylation of Ser87 and Ser129, oxid…”
High-Resolution Group Quantization Phase Processing Method in Radio Frequency Measurement Range
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“= f f N N / (3) 2 1 2 1 where T1 and T2 are their periods, N1 is counter value of the reference signal f1 from counter I, N2 is counter value of the measured signal f2 from counter II.”
The Genetics of Parkinson Disease
Mastrangelo, L. (2017) · Advances in genetics · doi:10.1016/bs.adgen.2017.08.001 · Cited by 9 · see citing works
Surface wetting is a key determinant of α-synuclein condensate maturation
Thrush, R. J., Vadukul, D. M., Allerton, S. C., Storch, M., & Aprile, F. A. (2025) · bioRxiv · doi:10.1038/s42004-025-01764-z · Cited by 7 · see citing works
“We selected three different truncations (Table S2): 5-140, isolated from PD brains and following in vitro incubation, 13,22 11-140, found in Lund human mesencephalic cells, 15 and 19-140, found in human appendices.”
InfluentialDuechs, M. J., Blazevic, D., Rechtsteiner, P., Kenny, C. H., Lamla, T., Low, S. H. H., Savistchenko, J., Neumann, M., Melki, R., Schönberger, T., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00542-9 · Cited by 9 · see citing works
“…~15 – 30% of total deposited α -synuclein with the majority of α - synuclein detected via MS-based analysis corresponding to the full-length protein, with abundancies of 0.23 to 0.26 of 1 – 122, 1 – 135, and 1 – 119 truncated forms compared with full-length 1 – 140 α -synuclein (set to 1.00 60 ).”
InfluentialHu, D., Sun, X., & Qi, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00918-w · Cited by 9 · see citing works
Wang, P., Okada-Rising, S. L., Scultetus, A. H., & Bailey, Z. S. (2024) · Biomedicines · doi:10.3390/biomedicines12122698 · Cited by 3 · see citing works
- Authors
- Kellie, J. F., Higgs, R. E., Ryder, J. W., Major, A., Beach, T. G., Adler, C. H., Merchant, K., & Knierman, M. D.
- Affiliations
- GlaxoSmithKline (United States) (US)
- Eli Lilly (United States) (US)
- Banner Sun Health Research Institute (US)
- Mayo Clinic in Arizona (US)
- Corresponding author
- Knierman, Michael D.
- ORCID
- Venue
- Scientific Reports
- Published
- 2014-07-23
- Volume
- 4
- Issue
- 1
- Pages
- 5797-5797
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC4107347
- OpenAlex
- W1998388651
- Cited by
- 182
- References
- 44
- Citations by year
- 2026: 13 · 2025: 17 · 2024: 13 · 2023: 16 · 2022: 18 · 2021: 22 · 2020: 20 · 2019: 14 · 2018: 18 · 2017: 12 · 2016: 7 · 2015: 10 · 2014: 1
- FWCI
- 4.29
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Scientific Reports (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- IUScholarWorks (Indiana University) (submittedVersion, cc-by)
- Funders
- Michael J. Fox Foundation for Parkinson's Research (U24 NS072026, 05-901, 211002, P30 AG19610)
- Arizona Department of Health Services (P30 AG19610, U24 NS072026, 05-901, 211002, Contract 211002)
- Arizona Biomedical Research Commission (P30 AG19610, 05–901, Contracts 4001, 0011, 05‐901 and 1001, U24 NS072026, 4001, 0011, 05-901, and 1001, 211002)
- National Institute on Aging (211002, P30-AG-19610, AG-19610, P30AG019610, 05-901)
- National Institute of Neurological Disorders and Stroke (NS072026, 211002, U24NS072026, 05-901, U24 NS072026 National Brain, P30 AG19610)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- alpha-synuclein, Parkinson's disease, post-translational modification, top-down proteomics, phosphorylation, Lewy bodies, frontal cortex, human brain tissue
- MeSH terms
- Aged, 80 and over, Brain, Cadaver, Chromatography, Liquid, Data Interpretation, Statistical, Female, Humans, Parkinson Disease, Blotting, Western, Biomarkers, Case-Control Studies, Spectrometry, Mass, Electrospray Ionization, alpha-Synuclein, Tandem Mass Spectrometry
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