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Items: 1 to 20 of 65

1.

Large-scale modelling as a route to multiple surface comparisons of the CCP module family.

Soares DC, Gerloff DL, Syme NR, Coulson AF, Parkinson J, Barlow PN.

Protein Eng Des Sel. 2005 Aug;18(8):379-88.

PMID:
15976010
2.

Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded.

Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN.

J Biol Chem. 2004 Nov 12;279(46):48292-306.

3.

Three-dimensional structure of a complement control protein module in solution.

Norman DG, Barlow PN, Baron M, Day AJ, Sim RB, Campbell ID.

J Mol Biol. 1991 Jun 20;219(4):717-25.

PMID:
1829116
4.

Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein.

Henderson CE, Bromek K, Mullin NP, Smith BO, Uhrín D, Barlow PN.

J Mol Biol. 2001 Mar 16;307(1):323-39.

PMID:
11243823
5.
6.

Structure and flexibility of the multiple domain proteins that regulate complement activation.

Kirkitadze MD, Barlow PN.

Immunol Rev. 2001 Apr;180:146-61. Review.

PMID:
11414356
7.

EyeSite: a semi-automated database of protein families in the eye.

Lee DA, Fefeu S, Edo-Ukeh AA, Orengo CA, Slingsby C.

Nucleic Acids Res. 2004 Jan 1;32(Database issue):D148-52.

8.

Central modules of the vaccinia virus complement control protein are not in extensive contact.

Kirkitadze MD, Henderson C, Price NC, Kelly SM, Mullin NP, Parkinson J, Dryden DT, Barlow PN.

Biochem J. 1999 Nov 15;344 Pt 1:167-75.

9.

Prediction of the tertiary structure of the complement control protein module.

Chou KC, Heinrikson RL.

J Protein Chem. 1997 Nov;16(8):765-73.

PMID:
9365925
10.

Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces.

O'Leary JM, Bromek K, Black GM, Uhrinova S, Schmitz C, Wang X, Krych M, Atkinson JP, Uhrin D, Barlow PN.

Protein Sci. 2004 May;13(5):1238-50.

11.
12.

Tools for integrated sequence-structure analysis with UCSF Chimera.

Meng EC, Pettersen EF, Couch GS, Huang CC, Ferrin TE.

BMC Bioinformatics. 2006 Jul 12;7:339.

13.

Structure-function relationship of inhibitory Smads: Structural flexibility contributes to functional divergence.

Hariharan R, Pillai MR.

Proteins. 2008 Jun;71(4):1853-62. doi: 10.1002/prot.21869.

PMID:
18175316
14.

Scoring docking models with evolutionary information.

Tress M, de Juan D, Graña O, Gómez MJ, Gómez-Puertas P, González JM, López G, Valencia A.

Proteins. 2005 Aug 1;60(2):275-80.

PMID:
15981273
15.

Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor.

Smith BO, Mallin RL, Krych-Goldberg M, Wang X, Hauhart RE, Bromek K, Uhrin D, Atkinson JP, Barlow PN.

Cell. 2002 Mar 22;108(6):769-80.

16.

PROMALS3D: a tool for multiple protein sequence and structure alignments.

Pei J, Kim BH, Grishin NV.

Nucleic Acids Res. 2008 Apr;36(7):2295-300. doi: 10.1093/nar/gkn072.

17.

Structural and functional characterization of binding sites in metallocarboxypeptidases based on Optimal Docking Area analysis.

Fernández D, Vendrell J, Avilés FX, Fernández-Recio J.

Proteins. 2007 Jul 1;68(1):131-44.

PMID:
17407161
18.
19.

DMAPS: a database of multiple alignments for protein structures.

Guda C, Pal LR, Shindyalov IN.

Nucleic Acids Res. 2006 Jan 1;34(Database issue):D273-6.

20.

The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module.

Schmidt CQ, Herbert AP, Mertens HD, Guariento M, Soares DC, Uhrin D, Rowe AJ, Svergun DI, Barlow PN.

J Mol Biol. 2010 Jan 8;395(1):105-22. doi: 10.1016/j.jmb.2009.10.010.

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