| scholarly article | Q13442814 |
| P356 | DOI | 10.3389/FGENE.2014.00010 |
| P8608 | Fatcat ID | release_qyhu6h75o5dipdvq5s7xeveddm |
| P932 | PMC publication ID | 3909831 |
| P698 | PubMed publication ID | 24550932 |
| P5875 | ResearchGate publication ID | 260254412 |
| P2093 | author name string | Diego M Bustos | |
| Marina Uhart | |||
| P2860 | cites work | Protein-protein interactions essentials: key concepts to building and analyzing interactome networks | Q21145336 |
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| Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine | Q24322674 | ||
| Non-adaptive origins of interactome complexity | Q24607502 | ||
| Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions | Q24813518 | ||
| Molecular tweezers modulate 14-3-3 protein-protein interactions | Q27684041 | ||
| Collective dynamics of 'small-world' networks | Q27861064 | ||
| The enzymatic phosphorylation of proteins | Q28211257 | ||
| An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell | Q28248982 | ||
| The importance of intrinsic disorder for protein phosphorylation | Q28776125 | ||
| Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation | Q30009920 | ||
| Local structural disorder imparts plasticity on linear motifs. | Q30158016 | ||
| Flexible nets. The roles of intrinsic disorder in protein interaction networks. | Q30351593 | ||
| The unfoldomics decade: an update on intrinsically disordered proteins. | Q30372413 | ||
| Toward a quantitative theory of intrinsically disordered proteins and their function | Q30382415 | ||
| Understanding protein non-folding. | Q30385084 | ||
| Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners | Q33325589 | ||
| Dimerization is essential for 14-3-3zeta stability and function in vivo | Q33581858 | ||
| 14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesis | Q33584128 | ||
| Subfunctionalization reduces the fitness cost of gene duplication in humans by buffering dosage imbalances | Q34100871 | ||
| How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis | Q34120299 | ||
| Unstructural biology coming of age. | Q34180028 | ||
| Attributes of short linear motifs. | Q34215453 | ||
| Rapid subfunctionalization accompanied by prolonged and substantial neofunctionalization in duplicate gene evolution | Q34570892 | ||
| Understanding eukaryotic linear motifs and their role in cell signaling and regulation. | Q34782197 | ||
| Tight regulation of unstructured proteins: from transcript synthesis to protein degradation | Q34890013 | ||
| Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants | Q35040486 | ||
| Structural basis for protein-protein interactions in the 14-3-3 protein family | Q35768552 | ||
| 14-3-3 Proteins--a focus on cancer and human disease | Q35879488 | ||
| 14-3-3 phosphoprotein interaction networks - does isoform diversity present functional interaction specification? | Q36175373 | ||
| 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 isoforms | Q36470001 | ||
| 14-3-3 proteins: a historic overview | Q36470005 | ||
| Does isoform diversity explain functional differences in the 14-3-3 protein family? | Q36514259 | ||
| Proteome-wide discovery of evolutionary conserved sequences in disordered regions | Q36926540 | ||
| The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development | Q37332559 | ||
| Linking folding and binding | Q37373866 | ||
| Anchor residues in protein-protein interactions | Q37388622 | ||
| The role of protein disorder in the 14-3-3 interaction network | Q37938718 | ||
| Oligomeric structure of 14-3-3 protein: what do we know about monomers? | Q38060462 | ||
| Alternative splicing of intrinsically disordered regions and rewiring of protein interactions | Q38109334 | ||
| Bioinformatic and experimental survey of 14-3-3-binding sites. | Q39918674 | ||
| A combined proteome and ultrastructural localization analysis of 14-3-3 proteins in transformed human amnion (AMA) cells: definition of a framework to study isoform-specific differences. | Q39996618 | ||
| Evolution of signal multiplexing by 14-3-3-binding 2R-ohnologue protein families in the vertebrates. | Q41778553 | ||
| Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6. | Q41824229 | ||
| Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks | Q41884066 | ||
| The role of structural disorder in the rewiring of protein interactions through evolution. | Q41969384 | ||
| 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking | Q42125847 | ||
| The role of disorder in interaction networks: a structural analysis | Q42924615 | ||
| Sphingosine and FTY720 directly bind pro-survival 14-3-3 proteins to regulate their function. | Q43093438 | ||
| Integrated network analysis platform for protein-protein interactions | Q43961965 | ||
| Protein disorder and the evolution of molecular recognition: theory, predictions and observations | Q47715145 | ||
| Molecular evolution of the 14-3-3 protein family | Q48059858 | ||
| Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins. | Q52664522 | ||
| Focus issue: systems analysis of protein phosphorylation. | Q54652603 | ||
| Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiens | Q57944743 | ||
| Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner | Q83153565 | ||
| Identification of novel 14-3-3ζ interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK) | Q85109351 | ||
| P921 | main subject | network connectivity | Q123759594 |
| P304 | page(s) | 10 | |
| P577 | publication date | 2014-02-03 | |
| P1433 | published in | Frontiers in Genetics | Q2499875 |
| P1476 | title | Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins | |
| P478 | volume | 5 |
| Q28547577 | 14-3-3 Proteins Buffer Intracellular Calcium Sensing Receptors to Constrain Signaling |
| Q91985663 | Activation of the Ca2+ sensing receptor and the PKC/WNK4 downstream signaling cascade induces incorporation of ZO-2 to tight junctions and its separation from 14-3-3 |
| Q32884577 | An inflammatory bowel disease-risk variant in INAVA decreases pattern recognition receptor-induced outcomes |
| Q58791363 | Cellular stress and redox activity proteins are involved in gastric carcinogenesis associated with Helicobacter pylori infection expressing high levels of thioredoxin-1 |
| Q36658914 | Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. |
| Q90812107 | Concatenation of 14-3-3 with partner phosphoproteins as a tool to study their interaction |
| Q42777346 | Controllability of protein-protein interaction phosphorylation-based networks: Participation of the hub 14-3-3 protein family |
| Q51336908 | Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation. |
| Q42479303 | Distilling a Visual Network of Retinitis Pigmentosa Gene-Protein Interactions to Uncover New Disease Candidates |
| Q35606898 | Evolutionarily conserved network properties of intrinsically disordered proteins |
| Q35564759 | Exo1 phosphorylation status controls the hydroxyurea sensitivity of cells lacking the Pol32 subunit of DNA polymerases delta and zeta |
| Q57454686 | Generation and characterization of monoclonal antibodies that recognize human and murine supervillin protein isoforms |
| Q28604036 | K-shell Analysis Reveals Distinct Functional Parts in an Electron Transfer Network and Its Implications for Extracellular Electron Transfer |
| Q26826940 | Protein flexibility in the light of structural alphabets |
| Q39303596 | Regulation of katanin activity in the ciliate Tetrahymena thermophila. |
| Q35194362 | Small molecules, peptides and natural products: getting a grip on 14-3-3 protein-protein modulation |
| Q21131783 | Structural Analysis of the 14-3-3ζ/Chibby Interaction Involved in Wnt/β-Catenin Signaling |
| Q27935625 | The GCKIII kinase Sps1 and the 14-3-3 isoforms, Bmh1 and Bmh2, cooperate to ensure proper sporulation in Saccharomyces cerevisiae |
| Q43240833 | The pro-inflammatory cytokine 14-3-3ε is a ligand of CD13 in cartilage |
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