| scholarly article | Q13442814 |
| P50 | author | Chris Oostenbrink | Q30505204 |
| Zuzana Trosanova | Q61829501 | ||
| P2093 | author name string | Zuzana Jandova | |
| Jozef Hritz | |||
| Veronika Weisova | |||
| P2860 | cites work | The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3 | Q24532906 |
| Contribution of surface salt bridges to protein stability | Q27621505 | ||
| Characterization of 14-3-3-ζ Interactions with Integrin Tails | Q27678611 | ||
| Crystal structure of the zeta isoform of the 14-3-3 protein | Q27729754 | ||
| Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
| Signaling through scaffold, anchoring, and adaptor proteins | Q28131792 | ||
| Interaction domains: from simple binding events to complex cellular behavior | Q28209614 | ||
| Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect | Q28292427 | ||
| Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins | Q28293607 | ||
| Protein stability curves | Q28303038 | ||
| The structural basis for 14-3-3:phosphopeptide binding specificity | Q29547190 | ||
| Dominant forces in protein folding | Q29616390 | ||
| Insight into conformational change for 14-3-3σ protein by molecular dynamics simulation. | Q30359261 | ||
| Testing of the GROMOS Force-Field Parameter Set 54A8: Structural Properties of Electrolyte Solutions, Lipid Bilayers, and Proteins | Q30590273 | ||
| Dimerization is essential for 14-3-3zeta stability and function in vivo | Q33581858 | ||
| Strong hydrophobic nature of cysteine residues in proteins | Q33876778 | ||
| How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis | Q34120299 | ||
| 14-3-3 proteins; bringing new definitions to scaffolding | Q34405540 | ||
| 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins | Q35624026 | ||
| Structural basis for protein-protein interactions in the 14-3-3 protein family | Q35768552 | ||
| Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. | Q35787179 | ||
| 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 | ||
| Lessons in stability from thermophilic proteins | Q36525476 | ||
| Some thermodynamic implications for the thermostability of proteins | Q36640421 | ||
| Basic ingredients of free energy calculations: a review | Q37662435 | ||
| Oligomeric structure of 14-3-3 protein: what do we know about monomers? | Q38060462 | ||
| Bioinformatic and experimental survey of 14-3-3-binding sites. | Q39918674 | ||
| Dependence of protein stability on the structure of the denatured state: free energy calculations of I56V mutation in human lysozyme | Q40131035 | ||
| 14-3-3 proteins. Hot numbers in signal transduction | Q40521393 | ||
| The effects of phosphorylation on the structure and function of proteins | Q40832954 | ||
| On target with a new mechanism for the regulation of protein phosphorylation | Q40855882 | ||
| Exploring the binding pathways of the 14-3-3ζ protein: Structural and free-energy profiles revealed by Hamiltonian replica exchange molecular dynamics with distancefield distance restraints | Q41071276 | ||
| Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3zeta: A complex story elucidated by NMR. | Q42091637 | ||
| 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking | Q42125847 | ||
| Net charge changes in the calculation of relative ligand-binding free energies via classical atomistic molecular dynamics simulation | Q43013072 | ||
| The key to predicting the stability of protein mutants lies in an accurate description and proper configurational sampling of the folded and denatured states. | Q46040127 | ||
| Contribution of surface salt bridges to protein stability: guidelines for protein engineering | Q48007914 | ||
| Molecular evolution of the 14-3-3 protein family | Q48059858 | ||
| Can the stability of protein mutants be predicted by free energy calculations? | Q70747550 | ||
| Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity? | Q73194933 | ||
| P433 | issue | 3 | |
| P1104 | number of pages | 9 | |
| P304 | page(s) | 442-450 | |
| P577 | publication date | 2017-12-05 | |
| P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
| P1476 | title | Free energy calculations on the stability of the 14-3-3ζ protein | |
| P478 | volume | 1866 |
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