14-3-3 protein

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14‐3‐3 protein

14-3-3 proteins

Modulation of 14-3-3 Protein Interactions with Target Polypeptides by Physical and Metabolic Effectors

Polycations Globally Enhance Binding of 14-3-3ω to Target Proteins in Spinach Leaves

Clearance of 14-3-3 Protein from Cerebrospinal Fluid Heralds the Resolution of Bacterial Meningitis

Rapidly progressive Alzheimer's disease and elevated 14-3-3 proteins in cerebrospinal fluid

Protein Phosphorylation and Binding of a 14-3-3 Protein in Vicia Guard Cells in Response to ABA

Interaction of a 14-3-3 protein with the plant microtubule-associated protein EDE1

The 14-3-3 Protein GF14c Acts as a Negative Regulator of Flowering in Rice by Interacting with the Florigen Hd3a


Identification of a Rat 30-kDa Protein Recognized by the Antibodies to a Recombinant Rat Cutaneous Fatty Acid-Binding Protein as a 14-3-3 Protein

Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae

Characterization of an excreted/secreted antigen form of 14-3-3 protein in Toxoplasma gondii tachyzoites

The value of serial cerebrospinal fluid 14-3-3 protein levels in adult community-acquired bacterial meningitis

Biological Significance of Divalent Metal Ion Binding to 14-3-3 Proteins In Relationship to Nitrate Reductase Inactivation1

Transcriptional activation by the PHD finger is inhibited through an adjacent leucine zipper that binds 14-3-3 proteins

Involvement of 14-3-3 protein GRF9 in root growth and response under polyethylene glycol-induced water stress

Subcellular localization of 14-3-3 proteins in Toxoplasma gondii tachyzoites and evidence for a lipid raft-associated form

Role of the β isoform of 14-3-3 proteins in cellular proliferation and oncogenic transformation


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A family of conserved regulatory adaptor molecules (˜250 aa) that bind to phosphoserine-containing proteins, including a wide range of functionally diverse signalling proteins, including kinases, phosphatases, and transmembrane receptors. There are seven highly conserved human 14-3-3 proteins (β, γ, ε, η, σ, θ, ζ) and they are involved in cellular proliferation, checkpoint control, and apoptosis. For example, 14-3-3-σ (stratifin, 248 aa) is particularly abundant in stratified keratinizing epithelium and is strongly induced by γ-irradiation and other DNA-damaging agents.

Subjects: Chemistry — Medicine and Health.

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