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370 related items for PubMed ID: 28100778
1. Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking. Schumacher MA, Huang KH, Zeng W, Janakiraman A. J Biol Chem; 2017 Mar 03; 292(9):3740-3750. PubMed ID: 28100778 [Abstract] [Full Text] [Related]
3. Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli Cytokinesis. Huang KH, Mychack A, Tchorzewski L, Janakiraman A. PLoS One; 2016 Mar 03; 11(4):e0153337. PubMed ID: 27088231 [Abstract] [Full Text] [Related]
6. Crystallization and preliminary X-ray crystallographic analysis of Z-ring-associated protein (ZapD) from Escherichia coli. Son SH, Lee HH. Acta Crystallogr F Struct Biol Commun; 2015 Feb 03; 71(Pt 2):194-8. PubMed ID: 25664795 [Abstract] [Full Text] [Related]
8. Mapping the Contact Sites of the Escherichia coli Division-Initiating Proteins FtsZ and ZapA by BAMG Cross-Linking and Site-Directed Mutagenesis. Roseboom W, Nazir MG, Meiresonne NY, Mohammadi T, Verheul J, Buncherd H, Bonvin AMJJ, de Koning LJ, de Koster CG, de Jong L, den Blaauwen T. Int J Mol Sci; 2018 Sep 26; 19(10):. PubMed ID: 30261644 [Abstract] [Full Text] [Related]
10. Cross-linking FtsZ polymers into coherent Z rings. Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D. Mol Microbiol; 2010 Nov 26; 78(3):651-68. PubMed ID: 20969647 [Abstract] [Full Text] [Related]
11. The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Mohammadi T, Ploeger GE, Verheul J, Comvalius AD, Martos A, Alfonso C, van Marle J, Rivas G, den Blaauwen T. Biochemistry; 2009 Nov 24; 48(46):11056-66. PubMed ID: 19842714 [Abstract] [Full Text] [Related]
15. FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings. Housman M, Milam SL, Moore DA, Osawa M, Erickson HP. Biochemistry; 2016 Jul 26; 55(29):4085-91. PubMed ID: 27368355 [Abstract] [Full Text] [Related]