If you would like to write for this, or any other Emerald publication, then please use our Emerald for Authors service information about how to choose which publication to write for and submission guidelines are available for all. Please visit www.emeraldinsight.com/authors for more information. About Emerald www.emeraldinsight.comEmerald is a global publisher linking research and practice to the benefit of society. The company manages a portfolio of more than 290 journals and over 2,350 books and book series volumes, as well as providing an extensive range of online products and additional customer resources and services.Emerald is both COUNTER 4 and TRANSFER compliant. The organization is a partner of the Committee on Publication Ethics (COPE) and also works with Portico and the LOCKSS initiative for digital archive preservation. Structured Abstract:Purpose: As traditional supply chains are increasingly becoming intelligent with more objects embedded with sensors and better communication, intelligent decision-making and automation capabilities, the new smart supply chain presents unprecedented opportunities for achieving cost reduction and enhancing efficiency improvement. The purpose of the paper is to study and explore the currents status and remaining issues of smart supply chain management (SSCM) .Design/methodology/approach: A literature review is conducted to synthesize the earlier work in this area, and to conceptualize and discuss the smart supply chain characteristics. Further, we formulate and investigate the five key research topics including information management, IT, process automation, advanced analytics, and supply chain integration.Findings: Studies in those aforementioned subject fields are reviewed, categorized, and analysed based on the review questions defined in the study. It is notable that while the topics of converging atoms with digits are increasingly attracting attention from researchers and practitioners alike, there are many more interesting research questions needing to be addressed.Originality/value: The paper provides original and relevant guidance for SCM researchers and practitioners on developing smart supply chains.

During cytokinesis, most bacteria assemble a ring-like structure that is composed of the tubulin homolog FtsZ. The mechanisms regulating assembly and organization of FtsZ molecules into rings are not fully understood. Here, we express bacterial FtsZ in the fission yeast Schizosaccharomyces pombe and find that FtsZ filaments assemble into cytoplasmic rings. Investigation of the Escherichia coli FtsZ revealed that ring assembly occurred by a process of closure and/or spooling of linear bundles. We conclude that FtsZ rings can assemble in the absence of all other bacterial cytokinetic proteins and that the process might involve hydrolysis of FtsZ-bound GTP and lateral associations between FtsZ filaments.Supplemental material is available at http://www.genesdev.org. February 7, 2008; revised version accepted May 5, 2008. Cytokinesis in a majority of bacteria requires the function of the prokaryotic ancestor of tubulin, FtsZ (Lutkenhaus et al. 1980;Lowe and Amos 1998;Errington et al. 2003;Erickson 2007). FtsZ is the first protein to localize to the mid-cell site, where it plays a critical role in the recruitment of a dozen other proteins that are required for assembly of the division septum (Bi and Lutkenhaus 1991;Weiss 2004;Goehring and Beckwith 2005). FtsZ has been shown to be a GTPase capable of forming a variety of polymeric structures in vitro (de Boer et al. 1992;RayChaudhuri and Park 1992;Bramhill and Thompson 1994;Mukherjee and Lutkenhaus 1994;Erickson et al. 1996;Romberg and Levin 2003). In vivo it localizes to the division site to form a ring-like structure (termed the FtsZ-ring or the Z-ring) and remains at the leading edge of the septum throughout cytokinesis (Bi and Lutkenhaus 1991;Wang and Lutkenhaus 1993;Ma et al. 1996). We previously established the fission yeast as a cellular model for studying prokaryotic cytoskeletal proteins (Srinivasan et al. 2007). In this study, we express wildtype and mutant versions of E. coli FtsZ (EcFtsZ) in fission yeast. Surprisingly, we find that EcFtsZ assembles into ring-like structures in fission yeast in a mechanism involving closure and/or spooling of linear cables. Received Results and DiscussionPrevious studies have shown that EcFtsZ expressed in fission yeast assembles into spot-like structures and cables (Fig. 1A, panels i,ii; Srinivasan et al. 2007), which are largely abolished upon coexpression of SulA (Srinivasan et al. 2007), a known inhibitor of FtsZ polymerization in bacterial cells. These spot-like structures were very similar in appearance to the spots observed when FtsZ was expressed in mammalian cells lines by Cabral and coworkers (Yu et al. 1999). In addition, as in fission yeast cells, FtsZ expressed in mammalian cells was also observed to form a filamentous network interconnecting the dots (Yu et al. 1999). Fluorescence recovery after photobleaching experiments (FRAP) revealed that FtsZ turns over with a recovery half-time t 1/2 of ∼11 sec (n = 22), which is very close to the FtsZ turnover rates determined in bacterial cells (Anderson et al. 200...

No abstract

No abstract

No abstract

No abstract

No abstract

No abstract