The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition-Reference-Cited by-同舟云学术

The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition

Published:2006-10-01 Issue:43 Volume:45 Page:12917-12928
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Casal Eva¹,Federici Luca¹,Zhang Wei¹,Fernandez-Recio Juan¹,Priego Eva-Maria¹,Miguel Ricardo Nuñez¹,DuHadaway James B.¹,Prendergast George C.¹,Luisi Ben F.¹,Laue Ernest D.¹

Affiliation:

1. Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K., Ce.S.I. Centro Studi sull'Invecchiamento and Dipartimento di Scienze Biomediche, Università di Chieti “G. D'Annunzio”, Via dei Vestini 31, 66013 Chieti, Italy, Institute of Biomedical Research, Barcelona Science Park, Josep Samitier 1-5, 08028 Barcelona, Spain, and Lankenau Institute for Medical Research, 100 Lancaster Avenue, Wynnewood, Pennsylvania 19096

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi060717k

Reference45 articles.

1. BIN1 is a novel MYC–interacting protein with features of a tumour suppressor

2. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53

3. Crystal Structure of the Endophilin-A1 BAR Domain

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