Network Embedding Algorithm Taking in Variational Graph AutoEncoder

Complex networks with node attribute information are employed to represent complex relationships between objects. Research of attributed network embedding fuses the topology and the node attribute information of the attributed network in the common latent representation space, to encode the high-dimensional sparse network information to the low-dimensional dense vector representation, effectively improving the performance of the network analysis tasks. The current research on attributed network embedding is presently facing problems of high-dimensional sparsity of attribute eigenmatrix and underutilization of attribute information. In this paper, we propose a network embedding algorithm taking in a variational graph autoencoder (NEAT-VGA). This algorithm first pre-processes the attribute features, i.e., the attribute feature learning of the network nodes. Then, the feature learning matrix and the adjacency matrix of the network are fed into the variational graph autoencoder algorithm to obtain the Gaussian distribution of the potential vectors, which more easily generate high-quality node embedding representation vectors. Then, the embedding of the nodes obtained by sampling this Gaussian distribution is reconstructed with structural and attribute losses. The loss function is minimized by iterative training until the low-dimension vector representation, containing network structure information and attribute information of nodes, can be better obtained, and the performance of the algorithm is evaluated by link prediction experimental results

A HUPO test sample study reveals common problems in mass spectrometry-based proteomics

We performed a test sample study to try to identify errors leading to irreproducibility, including incompleteness of peptide sampling, in liquid chromatography-mass spectrometry-based proteomics. We distributed an equimolar test sample, comprising 20 highly purified recombinant human proteins, to 27 laboratories. Each protein contained one or more unique tryptic peptides of 1,250 Da to test for ion selection and sampling in the mass spectrometer. Of the 27 labs, members of only 7 labs initially reported all 20 proteins correctly, and members of only 1 lab reported all tryptic peptides of 1,250 Da. Centralized analysis of the raw data, however, revealed that all 20 proteins and most of the 1,250 Da peptides had been detected in all 27 labs. Our centralized analysis determined missed identifications (false negatives), environmental contamination, database matching and curation of protein identifications as sources of problems. Improved search engines and databases are needed for mass spectrometry-based proteomics

Association of chromosome 19 to lung cancer genotypes and phenotypes

et al.The Chromosome 19 Consortium, a part of the Chromosome-Centric Human Proteome Project (C-HPP, http://​www.​C-HPP.​org), is tasked with the understanding chromosome 19 functions at the gene and protein levels, as well as their roles in lung oncogenesis. Comparative genomic hybridization (CGH) studies revealed chromosome aberration in lung cancer subtypes, including ADC, SCC, LCC, and SCLC. The most common abnormality is 19p loss and 19q gain. Sixty-four aberrant genes identified in previous genomic studies and their encoded protein functions were further validated in the neXtProt database (http://​www.​nextprot.​org/​). Among those, the loss of tumor suppressor genes STK11, MUM1, KISS1R (19p13.3), and BRG1 (19p13.13) is associated with lung oncogenesis or remote metastasis. Gene aberrations include translocation t(15, 19) (q13, p13.1) fusion oncogene BRD4-NUT, DNA repair genes (ERCC1, ERCC2, XRCC1), TGFβ1 pathway activation genes (TGFB1, LTBP4), Dyrk1B, and potential oncogenesis protector genes such as NFkB pathway inhibition genes (NFKBIB, PPP1R13L) and EGLN2. In conclusion, neXtProt is an effective resource for the validation of gene aberrations identified in genomic studies. It promises to enhance our understanding of lung cancer oncogenesis.The work was supported by Zhongshan Distinguished Professor Grant (XDW), The National Nature Science Foundation of China (91230204, 81270099, 81320108001, 81270131, 81300010), The Shanghai Committee of Science and Technology (12JC1402200, 12431900207, 11410708600, 14431905100), Operation funding of Shanghai Institute of Clinical Bioinformatics, and Ministry of Education, Academic Special Science and Research Foundation for PhD Education (20130071110043). MF is supported by grant FIS14/01538 (ISCIII- Fondos FEDER EU) and Proteomics Units at CIC belongs to ProteoRed-PRB2 (PT13-001, ISCIII, Fondos FEDER-EU).Peer Reviewe