Interkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins

scientific article (publication date: 2013)

Interkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins is …
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scholarly articleQ13442814

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P819ADS bibcode2013PLoSO...878090L
P356DOI10.1371/JOURNAL.PONE.0078090
P8608Fatcat IDrelease_3jxdkgpjevcx5diaaawkyb6o5m
P932PMC publication ID3795638
P698PubMed publication ID24147113
P5875ResearchGate publication ID258066404

P50authorEdoardo PozioQ89390175
Marco LalleQ43218678
Serena CameriniQ42826434
P2093author name stringEfthimios M C Skoulakis
Flora Leptourgidou
P2860cites workInvolvement of 14-3-3 protein post-translational modifications in Giardia duodenalis encystation.Q43280507
A third functional isoform enriched in mushroom body neurons is encoded by the Drosophila 14-3-3zeta geneQ43295983
Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo.Q43770539
Transcription of metabolic enzyme genes during the excystation of Giardia lambliaQ44686302
Interaction network of the 14-3-3 protein in the ancient protozoan parasite Giardia duodenalisQ47214623
Targeting of proteins to the nuclei of Giardia lambliaQ47880706
14-3-3 proteins in neuronal development and functionQ47974700
Molecular evolution of the 14-3-3 protein familyQ48059858
Olfactory learning deficits in mutants for leonardo, a Drosophila gene encoding a 14-3-3 proteinQ48875098
Axonemal tubulin polyglycylation probed with two monoclonal antibodies: widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motilityQ71287473
Genomic Minimalism in the Early Diverging Intestinal Parasite Giardia lambliaQ22065868
Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserineQ24322674
Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylationQ24338059
14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphataseQ24681544
The 14-3-3sQ24792401
14-3-3ε Is required for germ cell migration in DrosophilaQ27303211
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide GelsQ27860531
Targeted gene expression as a means of altering cell fates and generating dominant phenotypesQ27861039
The structural basis for 14-3-3:phosphopeptide binding specificityQ29547190
Mosaic analysis with a repressible cell marker for studies of gene function in neuronal morphogenesisQ29615747
The Giardia duodenalis 14-3-3 protein is post-translationally modified by phosphorylation and polyglycylation of the C-terminal tailQ33230030
Dimerization is essential for 14-3-3zeta stability and function in vivoQ33581858
How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesisQ34120299
14-3-3 proteins: key regulators of cell division, signalling and apoptosis.Q34400246
Current trends in research into the waterborne parasite GiardiaQ34730288
The neuron-specific RNA-binding protein ELAV regulates neuroglian alternative splicing in neurons and binds directly to its pre-mRNA.Q35081666
14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteinsQ35624026
In vivo functional specificity and homeostasis of Drosophila 14-3-3 proteinsQ36052151
Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoformsQ36470001
The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer developmentQ37332559
Behind the smile: cell biology and disease mechanisms of Giardia speciesQ37733242
Post-translational modification of 14-3-3 isoforms and regulation of cellular functionQ37921878
Structural basis of 14-3-3 protein functions.Q37932715
Giardia--from genome to proteomeQ38004154
Evolution of signal multiplexing by 14-3-3-binding 2R-ohnologue protein families in the vertebrates.Q41778553
Giardia duodenalis 14-3-3 protein is polyglycylated by a tubulin tyrosine ligase-like member and deglycylated by two metallocarboxypeptidasesQ41917153
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue10
P407language of work or nameEnglishQ1860
P304page(s)e78090
P577publication date2013-01-01
P1433published inPLOS OneQ564954
P1476titleInterkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins
P478volume8