Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design. - Test2 - elhamkhani - TriplyDB

Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design.

Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design.

http://www.wikidata.org/entity/Q33245808

about

The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction Thermodynamic analysis of Jun-Fos coiled coil peptide antagonists A Synthetic Coiled-Coil Interactome Provides Heterospecific Modules for Molecular Engineering Interactions between SIRT1 and AP-1 reveal a mechanistic insight into the growth promoting properties of alumina (Al2O3) nanoparticles in mouse skin epithelial cells Optical control of protein-protein interactions via blue light-induced domain swapping.Predicting helix orientation for coiled-coil dimers An amino acid packing code for α-helical structure and protein design Designing specific protein-protein interactions using computation, experimental library screening, or integrated methods Truncated and helix-constrained peptides with high affinity and specificity for the cFos coiled-coil of AP-1 Electrostatic contacts in the activator protein-1 coiled coil enhance stability predominantly by decreasing the unfolding rate.Heterodimerization with different Jun proteins controls c-Fos intranuclear dynamics and distribution Toward beta-amino acid proteins: a cooperatively folded beta-peptide quaternary structure Truncation, randomization, and selection: generation of a reduced length c-Jun antagonist that retains high interaction stability Free energy of binding of coiled-coil complexes with different electrostatic environments: the influence of force field polarisation and capping Combining intracellular selection with protein-fragment complementation to derive Aβ interacting peptides.Structural specificity in coiled-coil interactions.Protein interaction module-assisted function X (PIMAX) approach to producing challenging proteins including hyperphosphorylated tau and active CDK5/p25 kinase complex Design of protein-interaction specificity gives selective bZIP-binding peptides.Characterization and inhibition of AF10-mediated interaction.Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomers Computational design of selective peptides to discriminate between similar PDZ domains in an oncogenic pathway Library construction, selection and modification strategies to generate therapeutic peptide-based modulators of protein-protein interactions.Intracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation.Deriving Heterospecific Self-Assembling Protein-Protein Interactions Using a Computational Interactome Screen.Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling Coiled-coil networking shapes cell molecular machinery Preferred side-chain constellations at antiparallel coiled-coil interfaces Heterotrimeric coiled coils with core residue urea side chains.Design and development of peptides and peptide mimetics as antagonists for therapeutic intervention.Modular design in natural and biomimetic soft materials.Designing helical peptide inhibitors of protein-protein interactions Photocontrol of coiled-coil proteins in living cells.Optimizing the Photocontrol of bZIP Coiled Coils with Azobenzene Crosslinkers: Role of the Crosslinking Site.Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1 Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems.Increasing the affinity of selective bZIP-binding peptides through surface residue redesign.Heterodimerization with Jun family members regulates c-Fos nucleocytoplasmic traffic.Tropomyosin diffusion over actin subunits facilitates thin filament assembly.Free energy calculations of the interactions of c-Jun-based synthetic peptides with the c-Fos protein.GeBP and GeBP-like proteins are noncanonical leucine-zipper transcription factors that regulate cytokinin response in Arabidopsis.

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P2860

Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design.

http://www.wikidata.org/entity/Q33245808

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2006 nî lūn-bûn

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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2006年の論文

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Semirational design of Jun-Fos ...... zipper prediction and design.

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Proceedings of the National Academy of Sciences of the United States of America

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Semirational design of Jun-Fos ...... zipper prediction and design.

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Katja M Arndt

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Kristian M Müller

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Mark A Schmitz

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P2860

A helix propensity scale based on experimental studies of peptides and proteins

N- and C-capping preferences for all 20 amino acids in alpha-helical peptides

Predicting specificity in bZIP coiled-coil protein interactions

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

Buried polar residues and structural specificity in the GCN4 leucine zipper

Comprehensive identification of human bZIP interactions with coiled-coil arrays

Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

Preferential heterodimer formation by isolated leucine zippers from fos and jun

Stability of alpha-helices

Stability of α-Helices

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