Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin-Reference-Cited by-同舟云学术

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Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin

Published:2010-09 Issue:3 Volume:171 Page:353-360
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Hein Kim Langmach,Kragh-Hansen Ulrich,Morth J. Preben,Jeppesen Martin D.,Otzen Daniel,Møller Jesper V.,Nissen Poul

Funder

Foundation for the Advancement of Medical Science

Novo-Nordisk Foundation

Publisher

Elsevier BV

Subject

Structural Biology

Reference37 articles.

1. PHENIX: building new software for automated crystallographic structure determination;Adams;Acta Crystallogr. D Biol. Crystallogr.,2002

2. Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels;Ahern;Circ. Res.,2008

3. The binding of selected therapeutic drugs to human serum α-1 acid glycoprotein and to human serum albumin in vitro;Bailey;Ther. Drug Monit.,2004

4. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin;Bhattacharya;J. Mol. Biol.,2000

5. Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures;Bhattacharya;J. Biol. Chem.,2000

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