Literature: 14-3-3 domain (IPR023410)
References used in this entry
The following publications were referred to in the abstract:
How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis.
FEBS Lett. 513 53-7 2002
PMID: 11911880 Related citations
Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases.
Isobe T, Ichimura T, Sunaya T, Okuyama T, Takahashi N, Kuwano R, Takahashi Y.
J. Mol. Biol. 217 125-32 1991
PMID: 1671102 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Ferl RJ, Manak MS, Reyes MF.
Genome Biol. 3 REVIEWS3010 2002
PMID: 12184815 Related citations
Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.
Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ.
Nature 376 188-91 1995
PMID: 7603573 Related citations
Crystal structure of the zeta isoform of the 14-3-3 protein.
Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R.
Nature 376 191-4 1995
PMID: 7603574 Related citations
Function of 14-3-3 proteins.
Jin DY, Lyu MS, Kozak CA, Jeang KT.
Nature 382 308 1996
PMID: 8684458 Related citations
Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.
Muslin AJ, Tanner JW, Allen PM, Shaw AS.
Cell 84 889-97 1996
PMID: 8601312 Related citations
The 14-3-3 protein binds its target proteins with a common site located towards the C-terminus.
Ichimura T, Ito M, Itagaki C, Takahashi M, Horigome T, Omata S, Ohno S, Isobe T.
FEBS Lett. 413 273-6 1997
PMID: 9280296 Related citations
Molecular evolution of the 14-3-3 protein family.
Wang W, Shakes DC.
J. Mol. Evol. 43 384-98 1996
PMID: 8798343 Related citations