Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Analysis of phosphorylation-dependent protein-protein interactions of histone h3.

Klingberg R, Jost JO, Schuemann M, Gelato KA, Fischle W, Krause E, Schwarzer D

Multiple posttranslational modifications (PTMs) of histone proteins including site-specific phosphorylation of serine and threonine residues govern the accessibility of chromatin. According to the histone code theory, PTMs recruit regulatory proteins or block their access to chromatin. Here, we report a general strategy for simultaneous analysis of both of these effects based on a SILAC MS scheme. We applied this approach ... [more]

ACS Chem. Biol. Jan. 16, 2015; 10(1);138-45 [Pubmed: 25330109]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HIST1H3A YWHAG
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Low-BioGRID
-
YWHAG HIST1H3A
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID