14-3-3 proteins: structure, function, and regulation.

By H. Fu, Romesh R. Subramanian, S. Masters. Annual Review of Pharmacology and Toxicology, 2000

1,622 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b90a0df2b43d5fa0aaadb423f27d3a7369ea712f

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Citations in the corpus

TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. (2001, background): “7A, lane 4) suggested that 14-3-3 protein, which is involved in transporting proteins from the nucleus to the cytoplasm (Fu et al. 2000),”
hERG K(+) channels: structure, function, and clinical significance. (2012, background): “The family of 14–3-3 proteins are highly conserved regulatory molecules expressed in all eukaryotic cells (188).”
Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling (2002, background): “However, proteins such as 14-3-3 are scaffolds for known signaling cascades such as the ras-raf-MAPK cascade (Fu et al., 2000), without which activation of downstream binding partners does not occur.”
Salt-tolerant genes from halophytes are potential key players of salt tolerance in glycophytes (2016, background): “…capacity to bind with functionally diverse signaling proteins, including phosphatases, kinases and transmembrane receptors and play important roles in a wide range of vital regulatory processes, such as cell cycle control, mitogenic signal transduction and apoptotic cell death (Fu et al., 2000).”
TAZ: a novel transcriptional co‐activator regulated by interactions with 14‐3‐3 and PDZ domain proteins (2000, background): “Most proteins bind to 14-3-3 after they have been phosphorylated on serine or threonine residues, although a few proteins have been shown to bind to 14-3-3 via non-phospho motifs (Muslin et al., 1996; Yaffe et al., 1997; Fu et al., 2000).”
Identification of a novel interaction between integrin β1 and 14-3-3β (2001, background): “14-3-3 proteins are a highly conserved family of dimeric proteins ubiquitously expressed in all eukaryotic cells (for review, see Fu et al., 2000; Aitken et al., 1995).”
Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials (2020, background): “The 14-3-3 proteins bind to various ligand proteins including kinases, phosphatases, and transmembrane receptors.(215) The 14-3-3 proteins regulate more than 500 endogenous molecules’ activity through binding to them.”
Proteomic Analysis of Dendritic Cell-Derived Exosomes: A Secreted Subcellular Compartment Distinct from Apoptotic Vesicles1 (2001, background): “The many isoforms of 14-3-3, four of which are present in exosomes, are ligands for various intracellular proteins, especially serine-phosphorylated transmembrane receptors or actors of signaling cascades (44).”