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Structural features of Argonaute-GW182 protein interactions
Janina Pfaff
, Janosch Hennig
, Franz Herzog
, Ruedi Aebersold
,
Michael Sattler
, Dierk Niessing
, Gunter Meister
University of Regensburg
Helmholtz Zentrum München German Research Center for Environmental Health
Center for Integrated Protein Science
ETH Zurich
University of Munich
Research output
:
Contribution to journal
›
Article
›
peer-review
94
Scopus citations
Overview
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Keyphrases
Structural Features
100%
Protein-protein Interaction
100%
Argonaute
100%
GW182
100%
GW Proteins
83%
Argonaute Proteins
66%
Gene Silencing
50%
Tryptophan
33%
Ligand-binding Domain
33%
Weak Interactions
16%
NMR Experiments
16%
Direct Interaction
16%
Minimal Length
16%
Mass Spectrometry
16%
Structural Modeling
16%
Ago2
16%
MicroRNA
16%
Protein Family
16%
Biochemical Experiment
16%
Sequential Binding
16%
Target mRNA
16%
Globular Domain
16%
Downstream Steps
16%
Intrinsically Disordered Region
16%
Step Processes
16%
Biochemistry, Genetics and Molecular Biology
Protein Interaction
100%
Argonaute
100%
Gene Inactivation
30%
Binding Domain
20%
Tryptophan
20%
Cross-Link
10%
N-Terminus
10%
MicroRNA
10%
Mass Spectrometry
10%
Protein Family
10%
Mediator
10%
C-Terminus
10%
Immunology and Microbiology
Protein Interaction
100%
Argonaute Protein
100%
Gene Inactivation
30%
Tryptophan
20%
Cross Linking
10%
Mediator
10%
Amino Terminal Sequence
10%
Carboxy Terminal Sequence
10%
Protein Family
10%