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Unknown
(122)
Proteomics
(5)
Organisms
Schizophyllum commune H4-8
(5)
Mycobacterium tuberculosis SP7
(5)
Salmonella enterica subsp. enterica serovar Typhimurium str. T000240
(5)
Oryza sativa Japonica Group
(5)
Crotalus durissus terrificus
(5)
Eriocheir sinensis
(5)
Candidatus Endoriftia persephonae
(5)
Mycobacterium tuberculosis SP10
(5)
Mycobacterium tuberculosis SP13
(5)
Cotesia typhae
(5)
Mycobacterium tuberculosis SP22
(5)
Cepaea nemoralis
(5)
Enterobacter ludwigii
(5)
Trichoderma asperellum CBS 433.97
(5)
Corynebacterium diphtheriae bv. mitis str. ISS 3319
(5)
Nakaseomyces glabratus
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Olea europaea
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Lama
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Planorbella pilsbryi
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Wolbachia sp. wMelPop
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Pyricularia oryzae P131
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Enterococcus mundtii CRL35
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Pongo pygmaeus
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Gryllodes sigillatus
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Oncorhynchus tshawytscha
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Pseudomonas canadensis
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Strongylocentrotus purpuratus
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Craterostigma plantagineum
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Influenza A virus (A/California/04/2009(H1N1))
(5)
Repository
pride
(5)
Tissue
Brain
(1)
Disease
Parkinson's disease
(1)
Technology Type
Mass Spectrometry
(5)
Chemical cross-linking coupled with mass spectrometry proteomics
(2)
SRM/MRM
(1)
Bottom-up proteomics
(1)
Top-down proteomics
(1)
Shotgun proteomics
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Publication Date
2020
(2)
2025
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2022
(14)
2020
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2001
(1)
Lab affiliation
Max Planck Institute for Multidisciplinary Sciences, Bioanalytical Mass Spectrometry Group, Am Fassberg 11, 37077 Göttingen, Germany University Medical Center Goettingen, Institute for Clinical Chemistry, Bioanalytics, Robert-Koch-Strasse 40, 37075 Göttingen, Germany
(1)
1. Institute of Clinical Chemistry, University Medical Center Goettingen, Goettingen, Germany; 2. Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany
(1)
Max Planck Institute for biophysical chemistry
(1)
Max-Planck-Institute for Biophysical Chemistry Bioanalytical Mass Spectrometry Group University Medical Center Goettingen Bioanalytics Institute for Clinical Chemistry
(1)
JGU Mainz
(1)
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Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases.
Not available
S-EPMC1304251
|
biostudies-literature
Cite
NMR hawk-eyed view of AlphaFold2 structures.
Not available
S-EPMC8521308
|
biostudies-literature
Cite
Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation.
Not available
S-EPMC11733250
|
biostudies-literature
Cite
Determination of amyloid core structure using chemical shifts.
Not available
S-EPMC3575924
|
biostudies-literature
Cite
Retention and splicing complex (RES) - the importance of cooperativity.
Not available
S-EPMC4829318
|
biostudies-literature
Cite
Backbone resonance assignment and order tensor estimation using residual dipolar couplings.
Not available
S-EPMC4071608
|
biostudies-literature
Cite
Peptidyl Prolyl Isomerase A Modulates the Liquid-Liquid Phase Separation of Proline-Rich IDPs.
Not available
S-EPMC9460772
|
biostudies-literature
Cite
NMR structural and kinetic characterization of a homeodomain diffusing and hopping on nonspecific DNA.
Not available
S-EPMC1622777
|
biostudies-literature
Cite
Parkinson's disease-linked V15A mutation facilitates α-synuclein aggregation by reducing membrane affinity.
Not available
S-EPMC10357493
|
biostudies-literature
Cite
Lost in translocation: the functions of the 18-kD translocator protein.
Not available
S-EPMC5654500
|
biostudies-literature
Cite
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