Ultrasensitive, multiplexed chemoproteomic profiling with soluble activity-dependent proximity ligation.

ABSTRACT: Chemoproteomic methods can report directly on endogenous, active enzyme populations, which can differ greatly from measures of transcripts or protein abundance alone. Detection and quantification of family-wide probe engagement generally requires LC-MS/MS or gel-based detection methods, which suffer from low resolution, significant input proteome requirements, laborious sample preparation, and expensive equipment. Therefore, methods that can capitalize on the broad target profiling capacity of family-wide chemical probes but that enable specific, rapid, and ultrasensitive quantitation of protein activity in native samples would be useful for basic, translational, and clinical proteomic applications. Here we develop and apply a method that we call soluble activity-dependent proximity ligati

SUBMITTER: Li G 

PROVIDER: S-EPMC6815137 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature