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N-glycosylation site identification in Arabidopsis thaliana apoplastic fluid proteome

ABSTRACT: N-glycosylation site identification in Arabidopsis thaliana apoplastic fluid proteome by legumain using two alternative workflows to cross validate with dimethylation.

INSTRUMENT(S): maXis

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Fatih Demir

LAB HEAD: Pitter Florien Huesgen

PROVIDER: PXD014680 | Pride | 2020-01-20

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Glyco_Site_Mapping_MQ_txt.zip	Other
	Glyco_Site_Mapping_Raw_Data.zip	Other
	Glyco_Site_Mapping_Spectra.zip	Other

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Publications

ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease.

Soh Wai Tuck WT Demir Fatih F Dall Elfriede E Perrar Andreas A Dahms Sven O SO Kuppusamy Maithreyan M Brandstetter Hans H Huesgen Pitter F PF

Analytical chemistry 20200131 4

Bottom-up mass spectrometry-based proteomics utilizes proteolytic enzymes with well characterized specificities to generate peptides amenable for identification by high-throughput tandem mass spectrometry. Trypsin, which cuts specifically after the basic residues lysine and arginine, is the predominant enzyme used for proteome digestion, although proteases with alternative specificities are required to detect sequences that are not accessible after tryptic digest. Here, we show that the human cy ...[more]

PMID: 31951383

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