2016
DOI: 10.1038/ncomms12299
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Genetically encoded protein photocrosslinker with a transferable mass spectrometry-identifiable label

Abstract: Coupling photocrosslinking reagents with mass spectrometry has become a powerful tool for studying protein–protein interactions in living systems, but it still suffers from high rates of false-positive identifications as well as the lack of information on interaction interface due to the challenges in deciphering crosslinking peptides. Here we develop a genetically encoded photo-affinity unnatural amino acid that introduces a mass spectrometry-identifiable label (MS-label) to the captured prey proteins after p… Show more

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Cited by 78 publications
(69 citation statements)
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“…This result agrees reasonably with that determined by ITC (K D = 9.4 μM) (20). In addition, this affinity agrees well with that determined using the oriented immobilization strategy [K D = 8.2 ± 0.7 μM, C-terminal biotin labeled H3 (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) K4me3 peptide] (SI Appendix, Fig. S3).…”
Section: Resultssupporting
confidence: 80%
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“…This result agrees reasonably with that determined by ITC (K D = 9.4 μM) (20). In addition, this affinity agrees well with that determined using the oriented immobilization strategy [K D = 8.2 ± 0.7 μM, C-terminal biotin labeled H3 (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) K4me3 peptide] (SI Appendix, Fig. S3).…”
Section: Resultssupporting
confidence: 80%
“…First, we checked the positive controls in this peptide array. The H3K4me3 readers binds to H3 (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) K4me3 instead of H3 (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) K4un peptides as expected (Fig. 4B).…”
Section: Resultssupporting
confidence: 51%
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