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HUNTER N-termini profiling of Arabidopsis thaliana wt and vpe0 mutants

ABSTRACT: Comparison of protein termini in Arabidopsis thaliana vpe0 quadruple mutant and wildtype seedlings shortly after germination to identify differential processed proteins.

INSTRUMENT(S): maXis

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

TISSUE(S): Seedling

SUBMITTER: Fatih Demir

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD012804 | Pride | 2019-09-03

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	vpe0-II_181030Col-8_VPE0HUNTERSTR1_RC1_01_5767.d.zip	Other
	vpe0-II_181030Col-8_VPE0HUNTERSTR2_RC2_01_5768.d.zip	Other
	vpe0-II_181030Col-8_VPE0HUNTERSTR3_RC3_01_5769.d.zip	Other
	vpe0-II_181030Col-8_VPE0HUNTERSTR4_RC4_01_5770.d.zip	Other
	vpe0-II_181030Col-8_VPE0HUNTERSTR5_RC5_01_5771.d.zip	Other

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Publications

Sensitive Determination of Proteolytic Proteoforms in Limited Microscale Proteome Samples.

Weng Samuel S H SSH Demir Fatih F Ergin Enes K EK Dirnberger Sabrina S Uzozie Anuli A Tuscher Domenic D Nierves Lorenz L Tsui Janice J Huesgen Pitter F PF Lange Philipp F PF

Molecular & cellular proteomics : MCP 20190830 11

Protein N termini unambiguously identify truncated, alternatively translated or modified proteoforms with distinct functions and reveal perturbations in disease. Selective enrichment of N-terminal peptides is necessary to achieve proteome-wide coverage for unbiased identification of site-specific regulatory proteolytic processing and protease substrates. However, many proteolytic processes are strictly confined in time and space and therefore can only be analyzed in minute samples that provide i ...[more]

PMID: 31471496

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