Fuzzy complexes: Specific binding without complete folding
about
Modeling disordered protein interactions from biophysical principlesThe Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.The nuclear pore complex core scaffold and permeability barrier: variations of a common theme.Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.The herpes viral transcription factor ICP4 forms a novel DNA recognition complex.Glycogen phosphorylase inhibition improves beta cell function.Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly.FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies.Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from Anopheles gambiae.A new role for FBP21 as regulator of Brr2 helicase activity.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.Intrinsically disordered proteins and prostate cancer: pouring new wine in an old bottleThe peroxisomal matrix protein translocon is a large cavity-forming protein assembly into which PEX5 protein enters to release its cargo.The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions.The Thermodynamic Basis of the Fuzzy Interaction of an Intrinsically Disordered Protein.Fuzziness enables context dependence of protein interactions.Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex.Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering.NoLogo: a new statistical model highlights the diversity and suggests new classes of Crm1-dependent nuclear export signals.Molecular Mechanisms of Tight Binding through Fuzzy Interactions.Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2.Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains.Transient antibody-antigen interactions mediate the strain-specific recognition of a conserved malaria epitopeA hidden competitive advantage of disorder
P2860
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P2860
Fuzzy complexes: Specific binding without complete folding
description
2015 nî lūn-bûn
@nan
2015 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Fuzzy complexes: Specific binding without complete folding
@ast
Fuzzy complexes: Specific binding without complete folding
@en
Fuzzy complexes: Specific binding without complete folding
@nl
type
label
Fuzzy complexes: Specific binding without complete folding
@ast
Fuzzy complexes: Specific binding without complete folding
@en
Fuzzy complexes: Specific binding without complete folding
@nl
prefLabel
Fuzzy complexes: Specific binding without complete folding
@ast
Fuzzy complexes: Specific binding without complete folding
@en
Fuzzy complexes: Specific binding without complete folding
@nl
P2093
P2860
P3181
P1433
P1476
Fuzzy complexes: Specific binding without complete folding
@en
P2093
Marton Miskei
Monika Fuxreiter
Rashmi Sharma
Zsolt Raduly
P2860
P304
P3181
P356
10.1016/J.FEBSLET.2015.07.022
P407
P433
P577
2015-09-14T00:00:00Z