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A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution.

Wong WT, Schumacher C, Salcini AE, Romano A, Castagnino P, Pelicci PG, Di Fiore PP.

Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9530-4.


The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R.

Schumacher C, Knudsen BS, Ohuchi T, Di Fiore PP, Glassman RH, Hanafusa H.

J Biol Chem. 1995 Jun 23;270(25):15341-7.


Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites.

Enmon JL, de Beer T, Overduin M.

Biochemistry. 2000 Apr 18;39(15):4309-19.


The Eps15 homology (EH) domain.

Confalonieri S, Di Fiore PP.

FEBS Lett. 2002 Feb 20;513(1):24-9. Review.


Mapping of the molecular determinants involved in the interaction between eps15 and AP-2.

Iannolo G, Salcini AE, Gaidarov I, Goodman OB Jr, Baulida J, Carpenter G, Pelicci PG, Di Fiore PP, Keen JH.

Cancer Res. 1997 Jan 15;57(2):240-5.


Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module.

Salcini AE, Confalonieri S, Doria M, Santolini E, Tassi E, Minenkova O, Cesareni G, Pelicci PG, Di Fiore PP.

Genes Dev. 1997 Sep 1;11(17):2239-49.


The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32.

Wong WT, Kraus MH, Carlomagno F, Zelano A, Druck T, Croce CM, Huebner K, Di Fiore PP.

Oncogene. 1994 Jun;9(6):1591-7.


Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization.

Coda L, Salcini AE, Confalonieri S, Pelicci G, Sorkina T, Sorkin A, Pelicci PG, Di Fiore PP.

J Biol Chem. 1998 Jan 30;273(5):3003-12.


Recognition specificity of individual EH domains of mammals and yeast.

Paoluzi S, Castagnoli L, Lauro I, Salcini AE, Coda L, Fre' S, Confalonieri S, Pelicci PG, Di Fiore PP, Cesareni G.

EMBO J. 1998 Nov 16;17(22):6541-50.


The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins.

Whitehead B, Tessari M, Carotenuto A, van Bergen en Henegouwen PM, Vuister GW.

Biochemistry. 1999 Aug 31;38(35):11271-7.


eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

Fazioli F, Minichiello L, Matoskova B, Wong WT, Di Fiore PP.

Mol Cell Biol. 1993 Sep;13(9):5814-28.


EH domain-dependent interactions between Eps15 and clathrin-coated vesicle protein p95.

McPherson PS, de Heuvel E, Phillie J, Wang W, Sengar A, Egan S.

Biochem Biophys Res Commun. 1998 Mar 27;244(3):701-5.


C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?

Naslavsky N, Caplan S.

J Cell Sci. 2005 Sep 15;118(Pt 18):4093-101.


Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction.

Santonico E, Panni S, Falconi M, Castagnoli L, Cesareni G.

BMC Biochem. 2007 Dec 21;8:29.


eps15 and eps15R are essential components of the endocytic pathway.

Carbone R, Fré S, Iannolo G, Belleudi F, Mancini P, Pelicci PG, Torrisi MR, Di Fiore PP.

Cancer Res. 1997 Dec 15;57(24):5498-504.


Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.

de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M.

Science. 1998 Aug 28;281(5381):1357-60.


Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity.

Rumpf J, Simon B, Jung N, Maritzen T, Haucke V, Sattler M, Groemping Y.

EMBO J. 2008 Feb 6;27(3):558-69. doi: 10.1038/sj.emboj.7601980. Epub 2008 Jan 17.


EHD1 and Eps15 interact with phosphatidylinositols via their Eps15 homology domains.

Naslavsky N, Rahajeng J, Chenavas S, Sorgen PL, Caplan S.

J Biol Chem. 2007 Jun 1;282(22):16612-22. Epub 2007 Apr 5.

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