CtBPs (C-terminal Binding Protein) were initially discovered as proteins binding to the C-terminal domain of adenovirus EA-1 [ 23].
CIB1 was first discovered as a binding partner of platelet integrin αIIbβ3 and has been shown to regulate outside-in signaling during platelet activation [17], [18], [28], [29].
TSPO was originally discovered as a binding site for the benzodiazepines in peripheral tissue, hence its original name, peripheral benzodiazepine receptor (PBR) (59, 60).
The DNA-dependent adenosine triphosphatase (ATPase) Plk1-interacting checkpoint helicase (PICH) was discovered as a binding partner and substrate of the mitotic kinase Plk1 (Baumann et al. 2007).
Plk1-interacting checkpoint helicase (PICH) was discovered as a binding protein of the mitotic kinase Plk1 (Baumann et al, 2007; Leng et al, 2008).
The RGD sequence was originally discovered as a binding site of a number of extracellular matrix, blood, and cell surface proteins for integrins, a large class of αβ heterodimeric membrane receptors involved in cell adhesion [ 94, 95].
Yin Yang 1 (YY1), a member of the GLI-Krüppel class proteins, was first discovered as a DNA binding protein (Shi et al. 1991; Seto et al. 1991; Park and Atchison 1991; Hariharan et al. 1991).
HMGB1 was originally discovered as a DNA binding protein that facilitates DNA replication and repair.
Translocator Protein 18 kDa (TSPO) was originally discovered as a secondary binding site for the widely prescribed antianxiety drugs, benzodiazepines, in the mitochondria of rat kidney.
The T15-id was originally discovered as a phosphocholine binding antibody of the IgA subtype from hybridomas obtained after pristane injection.
