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4 Jan 2006: Curvature modules within proteins are conjugated withother protein motifs and domains, and from these collaborativeactivities we can suggest some new ideas for how membrane curva-ture can be generated by multiple ... This proposal that amphipathic

12 Aug 2006: Molecular Cell 23, 457–469, August 18, 2006 ª2006 Elsevier Inc. DOI 10.1016/j.molcel.2006.06.019. Double-Stranded DNA Translocation:Structure and Mechanism of Hexameric FtsK. Thomas H. Massey,2,3 Christopher P. Mercogliano,1,3. James Yates,2

19 Apr 2006: 476Actin. 476ParM. 477MreB. 479FtsA. 482. INTERMEDIATE FILAMENTHOMOLOGUE. 483Crescentin. 483. WALKER A CYTOSKELETALATPASE—A NEW FAMILY OFCYTOSKELETAL PROTEINS? ... New subunits assemble at the pre-ferred end, and after nucleotide hydrolysis

12 Nov 2006: The Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi 1p on multiple conserved repeats; both proteins localize to the SPB half-bridge, where the new SPB is assembled. ... Again, these SPBs show a bimodal distribution of stain, peaking close to the edge

17 Jan 2006: and Cullen, P. J. (2005).Sorting nexins – Unifying trends and new perspectives.

12 Nov 2006: www.sciencedirect.com. Rodriguez-Borlado L, Calvo V et al.: Identification andcharacterization of a new oncogene derived from theregulatory subunit of phosphoinositide 3-kinase.

14 Jun 2006: terest as a new class of drug targets (Ward et al., 2003).

12 Nov 2006: Results from these studies provide new insight into how the PI3K-C2α PX domain specifically recognizes PtdIns(4,5)P2 and how the PX and C2. ... Restriction endonucleases and other enzymes for molecular biology were from New England Biolabs (Beverly, MA).

31 Aug 2006: PLoS BIOLOGY. Figure 1. New Protein Interaction Partners for the a- and b-Appendage Domains of AP2 Adaptors(A) Plot of the network of protein interactions in clathrin-mediated endocytosis. ... Two Interaction Sites for New Motifs on the b-AppendageProtein

18 Apr 2006: Discovery of new ESCRT-I-interacting part-. ners, such as AIP/ALIX, which binds directly to ESCRT-.