Proteomics

Dataset Information

0

TAILS analysis of viral protease 3C substrates


ABSTRACT: Human Hela and murine HL1 cells were cultured and infected in vitro with C3 protease and inactive mutant protease. Cellular proteomes were collected, labeled by isotopic dimethylation and N-terminal peptides were enriched using TALS proteomics.

INSTRUMENT(S): impact II, Q Exactive

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Theo Klein  

LAB HEAD: Christopher M. Overall

PROVIDER: PXD008718 | Pride | 2018-03-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
OK20130920_J2C1_1.raw Raw
OK20130920_J3C2_2.raw Raw
OK20130920_J3C2_3.raw Raw
Orbi_Ndm_PEAKS.zip Other
Orbi_Ndm_SEARCH.zip Other
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Publications

N-Terminomics TAILS Identifies Host Cell Substrates of Poliovirus and Coxsackievirus B3 3C Proteinases That Modulate Virus Infection.

Jagdeo Julienne M JM   Dufour Antoine A   Klein Theo T   Solis Nestor N   Kleifeld Oded O   Kizhakkedathu Jayachandran J   Luo Honglin H   Overall Christopher M CM   Jan Eric E  

Journal of virology 20180328 8


Enteroviruses encode proteinases that are essential for processing of the translated viral polyprotein. In addition, viral proteinases also target host proteins to manipulate cellular processes and evade innate antiviral responses to promote replication and infection. Although some host protein substrates of enterovirus proteinases have been identified, the full repertoire of targets remains unknown. We used a novel quantitative <i>in vitro</i> proteomics-based approach, termed <u>t</u>erminal <  ...[more]

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