Completing the family of human Eps15 homology domains: Solution structure of the internal Eps15 homology domain of γ‐synergin

Author:

Kovermann Michael12ORCID,Weininger Ulrich3ORCID,Löw Christian45ORCID

Affiliation:

1. Department of Chemistry University of Konstanz Constance Germany

2. Konstanz Research School Chemical Biology KoRS‐CB University of Konstanz Constance Germany

3. Institute of Physics, Biophysics Martin‐Luther‐University Halle‐Wittenberg Halle (Saale) Germany

4. Centre for Structural Systems Biology (CSSB) Hamburg Germany

5. Molecular Biology Laboratory (EMBL) Hamburg Unit c/o Deutsches Elektronen Synchrotron (DESY) Hamburg Germany

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference42 articles.

1. eps15, a novel tyrosine kinase substrate, exhibits transforming activity;Fazioli F;Mol Cell Biol,1993

2. The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31‐p32;Wong WT;Oncogene,1994

3. A protein‐binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution;Wong WT;Proc Natl Acad Sci U S A,1995

4. The Eps15 homology (EH) domain;Confalonieri S;FEBS Lett,2002

5. Binding specificity and in vivo targets of the EH domain, a novel protein‐protein interaction module;Salcini AE;Genes Dev,1997

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