Multi-Scale Link Prediction

The automated analysis of social networks has become an important problem due to the proliferation of social networks, such as LiveJournal, Flickr and Facebook. The scale of these social networks is massive and continues to grow rapidly. An important problem in social network analysis is proximity estimation that infers the closeness of different users. Link prediction, in turn, is an important application of proximity estimation. However, many methods for computing proximity measures have high computational complexity and are thus prohibitive for large-scale link prediction problems. One way to address this problem is to estimate proximity measures via low-rank approximation. However, a single low-rank approximation may not be sufficient to represent the behavior of the entire network. In this paper, we propose Multi-Scale Link Prediction (MSLP), a framework for link prediction, which can handle massive networks. The basis idea of MSLP is to construct low rank approximations of the network at multiple scales in an efficient manner. Based on this approach, MSLP combines predictions at multiple scales to make robust and accurate predictions. Experimental results on real-life datasets with more than a million nodes show the superior performance and scalability of our method.Comment: 20 pages, 10 figure

High Speed CAN Transmission Scheme Supporting Data Rate of over 100 Mb/s

As the number of electronic components in the car increases, the requirement for the higher data transmission scheme among them is on the sharp rise. The control area network (CAN) has been widely adopted to support the in-car communications needs but the data rate is far below what other schemes such as Ethernet and optical fibers can offer. A new scheme for enhancing the speed of CANs has been proposed, where a carrier modulated signal is introduced on top of the existing CAN signal, whereby the data rate can be enhanced over 100 Mb/s. The proposed scheme is compatible with the existing CAN network and accordingly enables seamless upgrade of the existing network to support high-speed demand using CAN protocol. © 2016 IEEE.

HopF2 and RIN4 co-purifty during immunoaffinity purification from high-molecular weight FPLC fractions.

<p>High Mr fractions containing HA immunoreactive (V_e 36–46 ml) bands were pooled (input, pool) and concentrated for one hour in a 10,000 Da Mr cutoff concentrator (input, [pool]). Concentrated pooled fractions were incubated with anti-HA magnetic resin (µMACS), immobilized, flow through (FT) collected and resin washed with low salt (LSW), no salt (NSW) buffer then eluted over four fractions with 0.1 M NH₄OH. Samples were resolved by SDS-PAGE and immunoblotted (IB) with α (RIN4) immunosera and α (HA) IgG. All bands are from the same blot exposure. Blots were cropped to remove molecular weight standards between lanes containing NSW and eluate fractions. Blots of purifications from -DEX tissue were overexposed relative to blots from +DEX purifications. Results are representative of 3 independent replicates.</p

The <i>Pseudomonas syringae</i> Type III Effector HopF2 Suppresses Arabidopsis Stomatal Immunity

<div><p><i>Pseudomonas syringae</i> subverts plant immune signalling through injection of type III secreted effectors (T3SE) into host cells. The T3SE HopF2 can disable Arabidopsis immunity through Its ADP-ribosyltransferase activity. Proteomic analysis of HopF2 interacting proteins identified a protein complex containing ATPases required for regulating stomatal aperture, suggesting HopF2 may manipulate stomatal immunity. Here we report HopF2 can inhibit stomatal immunity independent of its ADP-ribosyltransferase activity. Transgenic expression of HopF2 in Arabidopsis inhibits stomatal closing in response to <i>P. syringae</i> and increases the virulence of surface inoculated <i>P. syringae.</i> Further, transgenic expression of HopF2 inhibits flg22 induced reactive oxygen species production. Intriguingly, ADP-ribosyltransferase activity is dispensable for inhibiting stomatal immunity and flg22 induced reactive oxygen species. Together, this implies HopF2 may be a bifunctional T3SE with ADP-ribosyltransferase activity required for inhibiting apoplastic immunity and an independent function required to inhibit stomatal immunity.</p></div

Identification of HopF2/RIN4 complexes by gel filtration chromatography and immunoblotting.

<p>Clarified extracts from HopF2:HA overexpressing plants were subjected to gel filtration chromatography on a Sephacryl S-300 HR 16/60 column. Every second fraction from the void volume was resolved by SDS-PAGE and immunoblotted with anti RIN4 immunosera and anti-HA IgG. Bands were visualized with HRP-conjugated secondary anti-bodies and Amersham ECL Advance detection kit. (a) Elution profile of dexamethasone treated Arabidopsis HopF2:HA clarified extract fractionated by gel filtration chromatography. Solid Arrow indicates elution of HA and RIN4 immunoreactive bands. Dashed arrow indicates elution of HA immunoreactive bands alone. Elution volumes of six molecular weight standards are shown as triangles. (b) Immunoblots (IB) showing co-elution of RIN4 and HA immunoreactive bands at high molecular weight. Results are representative of 3 independent replicates. Arrows indicate expected band size for RIN4 (25 kDa) and HopF2 (25 kDa), respectively.</p

Proteins of the HopF2 complex identified by mass spectrometry.

a<p>Counts are the number of unique peptides identified in each + DEX HopF2 experiment. Protein ID required P<0.01 (Peptide Prophet), minimum two unique peptides in each experiment and zero peptides in any negative control. None of these proteins were identified in any – DEX experiment. Bold text indicates proteins associated with RIN4 or RPS2 protein complexes <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0114921#pone.0114921-Liu2" target="_blank">[29]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0114921#pone.0114921-Qi1" target="_blank">[39]</a>.</p><p>*Proteins identified as differentially phosphorylated in response to flg22 <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0114921#pone.0114921-Benschop1" target="_blank">[42]</a>.</p><p>**Proteins identified as differentially phosphorylated in response to ABA <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0114921#pone.0114921-Kline1" target="_blank">[43]</a>.</p>†<p>Proteins enriched in plasma membrane subdomains after flg22 treatment <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0114921#pone.0114921-Keinath1" target="_blank">[41]</a>.</p><p>Proteins of the HopF2 complex identified by mass spectrometry.</p