Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry (Q33935711)

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English	Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 July 2017

Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry (English)

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Europe PubMed Central

PubMed publication ID

30 July 2017

Parkinson's disease

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based on heuristic

inferred from title

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based on heuristic

inferred from title

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based on heuristic

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Charles H Adler

6

object named as

Charles H Adler

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Europe PubMed Central

PubMed publication ID

30 July 2017

5

object named as

Thomas G Beach

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Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

John F Kellie

1

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Europe PubMed Central

PubMed publication ID

30 July 2017

Richard E Higgs

2

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Europe PubMed Central

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30 July 2017

John W Ryder

3

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Europe PubMed Central

PubMed publication ID

30 July 2017

Anthony Major

4

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Europe PubMed Central

PubMed publication ID

30 July 2017

Kalpana Merchant

7

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30 July 2017

Michael D Knierman

8

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30 July 2017

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publication date

23 July 2014

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30 July 2017

Scientific Reports

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30 July 2017

4

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30 July 2017

5797

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Europe PubMed Central

PubMed publication ID

30 July 2017

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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International

23 July 2014

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April 2022 Public Data File from Crossref

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Quantitative Proteomics via High Resolution MS Quantification: Capabilities and Limitations

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Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains

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5 July 2018

Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies

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Identification of novel α-synuclein isoforms in human brain tissue by using an online nanoLC-ESI-FTICR-MS method

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Mass spectrometric immunoassay of intact insulin and related variants for population proteomics studies.

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Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

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Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system

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The Sun Health Research Institute Brain Donation Program: description and experience, 1987-2007

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A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease

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Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

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The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct

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Accurate quantitation of protein expression and site-specific phosphorylation

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Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

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α-Synuclein in Lewy bodies

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Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease.

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Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress.

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Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease

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Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein.

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Alpha-synuclein cortical Lewy bodies correlate with dementia in Parkinson's disease

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Strategy and its implications of protein bioanalysis utilizing high-resolution mass spectrometric detection of intact protein

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Characterization of oligomerization-aggregation products of neurodegenerative target proteins by ion mobility mass spectrometry

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based on heuristic

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10.1038/SREP05797

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Europe PubMed Central

PubMed publication ID

30 July 2017

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PMC publication ID

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Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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