ArticleNature methods2013
Interlaboratory reproducibility of large-scale human protein-complex analysis by standardized AP-MS.
Article in Nature methods, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.
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Who cites it
119 citing papers in PubMed.
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- An Integrated High-Throughput Proteocistromic Framework for Mapping the Interactome and Targetome of Human Transcription Factors.Methods in molecular biology (Clifton, N.J.) · 2025Article
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- A uniform data processing pipeline enables harmonized nanoparticle protein corona analysis across proteomics core facilities.Nature communications · 2024Article
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- MATR3 is an endogenous inhibitor of DUX4 in FSHD muscular dystrophy.Cell reports · 2023Article
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- High-resolution structural-omics of human liver enzymes.Cell reports · 2023Article
- The SpACE-CCM: A facile and versatile cell culture medium-based biosensor for detection of SARS-CoV-2 spike-ACE2 interaction.Biosensors & bioelectronics · 2023Article
- Analyzing Protein Interactions by MAC-Tag Approaches.Methods in molecular biology (Clifton, N.J.) · 2023Article
59 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The characterization of all protein complexes of human cells under defined physiological conditions using affinity purification-mass spectrometry (AP-MS) is a highly desirable step in the quest to understand the phenotypic effects of genomic information. However, such a challenging goal has not yet been achieved, as it requires reproducibility of the experimental workflow and high data consistency across different studies and laboratories. We systematically investigated the reproducibility of a standardized AP-MS workflow by performing a rigorous interlaboratory comparative analysis of the interactomes of 32 human kinases. We show that it is possible to achieve high interlaboratory reproducibility of this standardized workflow despite differences in mass spectrometry configurations and subtle sample preparation-related variations and that combination of independent data sets improves the approach sensitivity, resulting in even more-detailed networks. Our analysis demonstrates the feasibility of obtaining a high-quality map of the human protein interactome with a multilaboratory project.
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