A quantitative protein interaction network for the ErbB receptors using protein microarrays

By Richard B. Jones, A. Gordus, Jordan A. Krall, G. MacBeath. Nature, 2006

760 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/a699457d9a05a27822f2055d8e5d4aaaffc1fed5

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In Molecular Biology

In Oncology

In Radiology, Nuclear Medicine and Imaging

Citations in the corpus

Motif switches: decision-making in cell regulation. (2012, background): “Furthermore, motif specificity is highly sensitive, determined by both the intrinsic affinity of the motif, which can be modulated by PTM, and the local abundance of the different interactors, which is determined by cell state-dependent expression levels, scaffolding and subcellular localisation [13”
Structural systems biology: modelling protein interactions (2006, background): “, or to develop specific high-throughput quantitative assays to measure such constants directl”
Robust associations of four new chromosome regions from genome-wide analyses of type 1 diabetes (2007, background): “We also noted that SH2B3 binds ERBB3 (v-erb-b2 erythroblastic leukemia viral oncogene homolog 3 (avian)”
Input–output behavior of ErbB signaling pathways as revealed by a mass action model trained against dynamic data (2009, background): “Careful treatment of these phospho-states is likely to be important, as ErbB1 binds B 8 distinct SH2 proteins and in some cases, multiple SH2 domains compete for binding to a single tyrosine residue (Jones et al , 2006).”
Intrinsically disordered proteins: regulation and disease. (2011, background): “Therefore, they are likely to bind to each others’ physiological targets if their concentration is increased [7 ,15].”
Reading protein modifications with interaction domains (2006, background): “This experiment indicated that the overexpression of the ERBB2 RTK ? as has been observed in some human cancers ? could lead to the recruitment of SH2-domain-containing proteins that would not normally bind to the activated receptor at physiological expression levels, and this recruitment potentiall”