Dataset Information


Multiplexed proteome dynamics profiling of HSP90 inhibitor 17-AAG

ABSTRACT: Investigation of proteostatic effects of HSP90 inhibition by 17-AAG and differentiation of maturation state dependent HSP90 requirements of proteins.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo sapiens  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Maria Faelth Savitski  

LAB HEAD: Marcus Bantscheff

PROVIDER: PXD008633 | Pride | 2018-04-05


Dataset's files

Action DRS
0231_F1_R1_P73995B01_TMT8.raw.gz Raw
0231_F1_R1_P73995B02_TMT8.raw.gz Raw
0231_F1_R1_P73995B03_TMT8.raw.gz Raw
0231_F1_R1_P73995B04_TMT8.raw.gz Raw
0231_F1_R1_P73995B05_TMT8.raw.gz Raw
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Protein degradation plays important roles in biological processes and is tightly regulated. Further, targeted proteolysis is an emerging research tool and therapeutic strategy. However, proteome-wide technologies to investigate the causes and consequences of protein degradation in biological systems are lacking. We developed "multiplexed proteome dynamics profiling" (mPDP), a mass-spectrometry-based approach combining dynamic-SILAC labeling with isobaric mass tagging for multiplexed analysis of  ...[more]

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