Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1.

Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M

We have characterized mammalian endophilin B1, a novel member of the endophilins and a representative of their B subgroup. The endophilins B show the same domain organization as the endophilins A, which contain an N-terminal domain responsible for lipid binding and lysophosphatidic acid acyl transferase activity, a central coiled-coil domain for oligomerization, a less conserved linker region, and a C-terminal ... [more]

J. Biol. Chem. Feb. 07, 2003; 278(6);4160-7 [Pubmed: 12456676]

Throughput

  • Low Throughput

Additional Notes

  • Figure 2

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
DNM1 SH3GL2
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
DNM1 SH3GL2
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.6925BioGRID
2675394

Curated By

  • BioGRID