Phosphatidylethanolamine-binding protein
Short name | PEBP |
Overlapping homologous superfamilies | |
family relationships |
Description
References
1.Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo. Vallee BS, Coadou G, Labbe H, Sy D, Vovelle F, Schoentgen F. J. Pept. Res. 61, 47-57, (2003). View articlePMID: 12492898
2.The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. Hengst U, Albrecht H, Hess D, Monard D. J. Biol. Chem. 276, 535-40, (2001). View articlePMID: 11034991
3.The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator. Banfield MJ, Brady RL. J. Mol. Biol. 297, 1159-70, (2000). View articlePMID: 10764580
4.Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. Corbit KC, Trakul N, Eves EM, Diaz B, Marshall M, Rosner MR. J. Biol. Chem. 278, 13061-8, (2003). View articlePMID: 12551925
5.Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. Yeung KC, Rose DW, Dhillon AS, Yaros D, Gustafsson M, Chatterjee D, McFerran B, Wyche J, Kolch W, Sedivy JM. Mol. Cell. Biol. 21, 7207-17, (2001). View articlePMID: 11585904
6.Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H. J. Mol. Biol. 310, 617-34, (2001). View articlePMID: 11439028
Contributing Member Database Entry
- Pfam:PF01161