ArticleProceedings of the National Academy of Sciences of the United States of America2022
Novel biochemical, structural, and systems insights into inflammatory signaling revealed by contextual interaction proteomics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- dia-PASEF Enables Rapid Profiling of the Human Secretome for Deeper Insights Into Cellular Dynamics and Inflammatory Mechanisms.Molecular & cellular proteomics : MCP · 2026Article
- Concatemer-assisted stoichiometry analysis: targeted mass spectrometry for protein quantification.Life science alliance · 2025Article
- Progress in mass spectrometry approaches to profiling protein-protein interactions in the studies of the innate immune system.Journal of proteins and proteomics · 2024Article
- A RIPK1-specific PROTAC degrader achieves potent antitumor activity by enhancing immunogenic cell death.Immunity · 2024Article
- DIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes.Nature methods · 2024Article
- The 2023 Report on the Proteome from the HUPO Human Proteome Project.Journal of proteome research · 2024Review
- Roles of RIPK1 as a stress sentinel coordinating cell survival and immunogenic cell death.Nature reviews. Molecular cell biology · 2023Review
- Rapid Profiling of Protein Complex Reorganization in Perturbed Systems.Journal of proteome research · 2023Article
- Phosphorylation-linked complex profiling identifies assemblies required for Hippo signal integration.Molecular systems biology · 2023Article
- Understanding How Cells Probe the World: A Preliminary Step towards Modeling Cell Behavior?International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
Protein-protein interactions (PPIs) represent the main mode of the proteome organization in the cell. In the last decade, several large-scale representations of PPI networks have captured generic aspects of the functional organization of network components but mostly lack the context of cellular states. However, the generation of context-dependent PPI networks is essential for structural and systems-level modeling of biological processes-a goal that remains an unsolved challenge. Here we describe an experimental/computational strategy to achieve a modeling of PPIs that considers contextual information. This strategy defines the composition, stoichiometry, temporal organization, and cellular requirements for the formation of target assemblies. We used this approach to generate an integrated model of the formation principles and architecture of a large signalosome, the TNF-receptor signaling complex (TNF-RSC). Overall, we show that the integration of systems- and structure-level information provides a generic, largely unexplored link between the modular proteome and cellular function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.