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Dancing Molecules: Rewiring Cooperative Communications within 14-3-3 ζ Docking Proteins
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/jcc.20035openalex-snapshot
Development and testing of a general amber force field
inferredcites →https://doi.org/10.1002/jcc.20084openalex-snapshot
UCSF Chimera—A visualization system for exploratory research and analysis
inferredcites →https://doi.org/10.1002/jcc.20290openalex-snapshot
The Amber biomolecular simulation programs
inferredcites →https://doi.org/10.1002/prot.340230412openalex-snapshot
Knowledge‐based protein secondary structure assignment
inferredcites →https://doi.org/10.1002/wcms.1121openalex-snapshot
An overview of the Amber biomolecular simulation package
inferredcites →https://doi.org/10.1007/s00249-011-0754-8openalex-snapshot
Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles
inferredcites →https://doi.org/10.1016/j.biosystems.2014.06.007openalex-snapshot
Engineering cellulosic bioreactors by template assisted DNA shuffling and in vitro recombination (TADSir)
inferredcites →https://doi.org/10.1016/j.cell.2011.10.049openalex-snapshot
Hot Spots for Allosteric Regulation on Protein Surfaces
inferredcites →https://doi.org/10.1016/j.cell.2013.03.034openalex-snapshot
Allostery in Disease and in Drug Discovery
inferredcites →https://doi.org/10.1016/j.coph.2010.09.002openalex-snapshot
Allostery and population shift in drug discovery
inferredcites →https://doi.org/10.1016/j.jmgm.2005.12.005openalex-snapshot
Automatic atom type and bond type perception in molecular mechanical calculations
inferredcites →https://doi.org/10.1016/j.phrs.2017.09.007openalex-snapshot
14-3-3 adaptor protein-protein interactions as therapeutic targets for CNS diseases
inferredcites →https://doi.org/10.1016/j.sbi.2018.09.004openalex-snapshot
Modulation of allosteric coupling by mutations: from protein dynamics and packing to altered native ensembles and function
inferredcites →https://doi.org/10.1016/j.semcdb.2011.08.009openalex-snapshot
14-3-3 Proteins: Diverse functions in cell proliferation and cancer progression
inferredcites →https://doi.org/10.1016/j.str.2009.06.008openalex-snapshot
The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways
inferredcites →https://doi.org/10.1016/j.str.2011.04.006openalex-snapshot
Protein-Protein Complex Structure Predictions by Multimeric Threading and Template Recombination
inferredcites →https://doi.org/10.1016/j.str.2011.06.002openalex-snapshot
Dynamic Allostery: Linkers Are Not Merely Flexible
inferredcites →https://doi.org/10.1016/j.str.2017.01.008openalex-snapshot
Predicting Protein Dynamics and Allostery Using Multi-Protein Atomic Distance Constraints
inferredcites →https://doi.org/10.1016/s0065-3233(00)54003-0openalex-snapshot
Amino acid substitution matrices
inferredcites →https://doi.org/10.1016/s0092-8674(01)00316-6openalex-snapshot
Crystal Structure of the 14-3-3ζ:Serotonin N-Acetyltransferase Complex
inferredcites →https://doi.org/10.1021/acsomega.8b03100openalex-snapshot
Intelligent Design of 14-3-3 Docking Proteins Utilizing Synthetic Evolution Artificial Intelligence (SYN-AI)
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Predicting Stability of DNA Duplexes in Solutions Containing Magnesium and Monovalent Cations
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Potential Energy and Free Energy Landscapes
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The role of dynamic conformational ensembles in biomolecular recognition
inferredcites →https://doi.org/10.1038/nsb0197-10openalex-snapshot
From Levinthal to pathways to funnels
inferredcites →https://doi.org/10.1039/b819720bopenalex-snapshot
Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms
inferredcites →https://doi.org/10.1073/pnas.0307898101openalex-snapshot
Simulations of the role of water in the protein-folding mechanism
inferredcites →https://doi.org/10.1073/pnas.051399098openalex-snapshot
Point mutations and sequence variability in proteins: Redistributions of preexisting populations
inferredcites →https://doi.org/10.1073/pnas.0605779103openalex-snapshot
Structural basis for protein–protein interactions in the 14-3-3 protein family
inferredcites →https://doi.org/10.1073/pnas.89.22.10915openalex-snapshot
Amino acid substitution matrices from protein blocks.
inferredcites →https://doi.org/10.1074/jbc.273.26.16305openalex-snapshot
14-3-3ζ Binds a Phosphorylated Raf Peptide and an Unphosphorylated Peptide via Its Conserved Amphipathic Groove
inferredcites →https://doi.org/10.1093/bioinformatics/16.4.404openalex-snapshot
The PSIPRED protein structure prediction server
inferredcites →https://doi.org/10.1093/bioinformatics/btu847openalex-snapshot
The anisotropic network model web server at 2015 (ANM 2.0)
inferredcites →https://doi.org/10.1093/nar/gkh368openalex-snapshot
ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
inferredcites →https://doi.org/10.1093/protein/9.1.27openalex-snapshot
Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins
inferredcites →https://doi.org/10.1101/585042openalex-snapshot
Fundamental Theory of the Evolution Force (FTEF): Gene Engineering utilizing Synthetic Evolution Artificial Intelligence (SYN-AI)
inferredcites →https://doi.org/10.1107/s0907444904001982openalex-snapshot
On the potential of normal-mode analysis for solving difficult molecular-replacement problems
inferredcites →https://doi.org/10.1110/ps.9.1.10openalex-snapshot
Folding and binding cascades: Dynamic landscapes and population shifts
inferredcites →https://doi.org/10.1126/science.1749933openalex-snapshot
The Energy Landscapes and Motions of Proteins
inferredcites →https://doi.org/10.1126/science.278.5338.609openalex-snapshot
Gene Families: The Taxonomy of Protein Paralogs and Chimeras
inferredcites →https://doi.org/10.1146/annurev.bi.64.070195.001443openalex-snapshot
THE MULTIPLICITY OF DOMAINS IN PROTEINS
inferredcites →https://doi.org/10.1167/iovs.15-17438openalex-snapshot
Down-regulation of 14-3-3 Zeta Inhibits TGF-β1–Induced Actomyosin Contraction in Human Trabecular Meshwork Cells Through RhoA Signaling Pathway
inferredcites →https://doi.org/10.1515/hmbci-2017-0032openalex-snapshot
The functional significance of 14-3-3 proteins in cancer: focus on lung cancer
inferredcites →https://doi.org/10.1517/14728222.2010.531011openalex-snapshot
14-3-3ζ as a prognostic marker and therapeutic target for cancer
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