ArticleScientific reports2017
Facilitating identification of minimal protein binding domains by cross-linking mass spectrometry.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.Nature communications · 2025Article
- Photo-crosslinkers boost structural information from crosslinking mass spectrometry.Current opinion in structural biology · 2025Review
- Article
- The nuclear GYF protein CD2BP2/U5-52K is required for T cell homeostasis.Frontiers in immunology · 2024Article
- Structural insights into the multifunctionality of rabies virus P3 protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cross-linking mass spectrometry for mapping protein complex topologies in situ.Essays in biochemistry · 2023Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021Review
- Mapping the native interaction surfaces of PREP1 with PBX1 by cross-linking mass-spectrometry and mutagenesis.Scientific reports · 2020Article
- Stitching the synapse: Cross-linking mass spectrometry into resolving synaptic protein interactions.Science advances · 2020Article
- Considerations of AOX Functionality Revealed by Critical Motifs and Unique Domains.International journal of molecular sciences · 2018Article
- Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease.Current opinion in chemical biology · 2018Review
- Cross-Linking Mass Spectrometry: An Emerging Technology for Interactomics and Structural Biology.Analytical chemistry · 2018Review
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterization of protein interaction domains is crucial for understanding protein functions. Here we combine cross-linking mass spectrometry (XL-MS) with deletion analysis to accurately locate minimal protein interaction domains. As a proof of concept, we investigated in detail the binding interfaces of two protein assemblies: the complex formed by MICAL3, ELKS and Rab8A, which is involved in exocytosis, and the complex of SLAIN2, CLASP2 and ch-TOG, which controls microtubule dynamics. We found that XL-MS provides valuable information to efficiently guide the design of protein fragments that are essential for protein interaction. However, we also observed a number of cross-links between polypeptide regions that were dispensable for complex formation, especially among intrinsically disordered sequences. Collectively, our results indicate that XL-MS, which renders distance restrains of linked residue pairs, accelerates the characterization of protein binding regions in combination with other biochemical approaches.
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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 Socratic graph.