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The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins.

Authors: O, Albagli; P, Dhordain; C, Deweindt; G, Lecocq; D, Leprince;

The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins.

Abstract

The BTB/POZ domain defines a newly characterized protein-protein interaction interface. It is highly conserved throughout metazoan evolution and generally found at the NH2 terminus of either actin-binding or, more commonly, nuclear DNA-binding proteins. By mediating protein binding in large aggregates, the BTB/POZ domain serves to organize higher order macromolecular complexes involved in ring canal formation or chromatin folding.

Related Organizations
Keywords

Sequence Homology, Amino Acid, Microfilament Proteins, Molecular Sequence Data, Nuclear Proteins, Zinc Fingers, Chromatin, Protein Structure, Tertiary, DNA-Binding Proteins, Structure-Activity Relationship, Viral Proteins, Animals, Drosophila, Amino Acid Sequence

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Powered by OpenAIRE graph
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
341
Top 10%
Top 1%
Top 1%
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