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Items: 1 to 20 of 92

1.

NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli.

Wu Y, Punta M, Xiao R, Acton TB, Sathyamoorthy B, Dey F, Fischer M, Skerra A, Rost B, Montelione GT, Szyperski T.

PLoS One. 2012;7(6):e37404. doi: 10.1371/journal.pone.0037404. Epub 2012 Jun 5.

2.

The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding.

Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C.

FEBS Lett. 2004 Mar 26;562(1-3):183-8.

3.

Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc.

Schiefner A, Chatwell L, Breustedt DA, Skerra A.

Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1308-15. doi: 10.1107/S0907444910039375. Epub 2010 Nov 16.

PMID:
21123871
5.

The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids.

Campanacci V, Bishop RE, Blangy S, Tegoni M, Cambillau C.

FEBS Lett. 2006 Sep 4;580(20):4877-83. Epub 2006 Aug 10.

6.

The bacterial lipocalins.

Bishop RE.

Biochim Biophys Acta. 2000 Oct 18;1482(1-2):73-83. Review.

PMID:
11058749
7.

YodA from Escherichia coli is a metal-binding, lipocalin-like protein.

David G, Blondeau K, Schiltz M, Penel S, Lewit-Bentley A.

J Biol Chem. 2003 Oct 31;278(44):43728-35. Epub 2003 Aug 8.

8.

Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.

Hirano Y, Hossain MM, Takeda K, Tokuda H, Miki K.

Structure. 2007 Aug;15(8):963-76.

9.

NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.

Hobbs CA, Bobay BG, Thompson RJ, Perego M, Cavanagh J.

J Mol Biol. 2010 Apr 30;398(2):248-63. doi: 10.1016/j.jmb.2010.03.003. Epub 2010 Mar 17.

10.

The menagerie of human lipocalins: a natural protein scaffold for molecular recognition of physiological compounds.

Schiefner A, Skerra A.

Acc Chem Res. 2015 Apr 21;48(4):976-85. doi: 10.1021/ar5003973. Epub 2015 Mar 10. Review.

PMID:
25756749
11.

Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex.

Kim KH, Paetzel M.

J Mol Biol. 2011 Mar 11;406(5):667-78. doi: 10.1016/j.jmb.2010.12.020. Epub 2010 Dec 17.

PMID:
21168416
13.

The lipocalin website.

Paine K, Flower DR.

Biochim Biophys Acta. 2000 Oct 18;1482(1-2):351-2.

PMID:
11058775
14.

Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli.

Ni D, Wang Y, Yang X, Zhou H, Hou X, Cao B, Lu Z, Zhao X, Yang K, Huang Y.

FASEB J. 2014 Jun;28(6):2677-85. doi: 10.1096/fj.13-248450. Epub 2014 Mar 11.

PMID:
24619089
15.

Distantly related lipocalins share two conserved clusters of hydrophobic residues: use in homology modeling.

Adam B, Charloteaux B, Beaufays J, Vanhamme L, Godfroid E, Brasseur R, Lins L.

BMC Struct Biol. 2008 Jan 11;8:1. doi: 10.1186/1472-6807-8-1.

16.
17.

Exon-intron structure and evolution of the Lipocalin gene family.

Sánchez D, Ganfornina MD, Gutiérrez G, Marín A.

Mol Biol Evol. 2003 May;20(5):775-83. Epub 2003 Apr 2.

PMID:
12679526
18.

The Bacillus subtilis chromosome region encoding homologues of the Escherichia coli mssA and rpsA gene products.

Sorokin A, Serror P, Pujic P, Azevedo V, Ehrlich SD.

Microbiology. 1995 Feb;141 ( Pt 2):311-9.

PMID:
7704259
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