Polytechnic University of Valencia

About: Polytechnic University of Valencia is a education organization based out in Valencia, Spain. It is known for research contribution in the topics: Catalysis & Population. The organization has 16282 authors who have published 40162 publications receiving 850234 citations.

On the way towards fourth-generation mobile: 3GPP LTE and LTE-advanced

Abstract: Long-TermEvolution (LTE) is the new standard recently specified by the 3GPP on the way towards fourth-generation mobile. This paper presents the main technical features of this standard as well as its performance in terms of peak bit rate and average cell throughput, among others. LTE entails a big technological improvement as compared with the previous 3G standard. However, this paper also demonstrates that LTE performance does not fulfil the technical requirements established by ITU-R to classify one radio access technology as a member of the IMT-Advanced family of standards. Thus, this paper describes the procedure followed by the 3GPP to address these challenging requirements. Through the design and optimization of new radio access techniques and a further evolution of the system, the 3GPP is laying down the foundations of the future LTE-Advanced standard, the 3GPP candidate for 4G. This paper offers a brief insight into these technological trends.

Holons and agents

Abstract: The future of the manufacturing sector in the world will be determined by how it meets the challenges of the 21st century Two paradigms promise to meet these challenges, multi-agent systems (MAS) and holonic system (HS) Currently, there is some misunderstanding about the relationships between these two approaches The aim of this work is to make a study of all the characteristics of the HS and the MAS approach, in order to illustrate a comprehensive comparison of holons and agents, and, at the same time, to present a survey about the main research works in both areas

A polyamine metabolon involving aminopropyl transferase complexes in Arabidopsis

Abstract: The conversion of putrescine to spermidine in the biosynthetic pathway of plant polyamines is catalyzed by two closely related spermidine synthases, SPDS1 and SPDS2, in Arabidopsis. In the yeast two-hybrid system, SPDS2 was found to interact with SPDS1 and a novel protein, SPMS (spermine synthase), which is homologous with SPDS2 and SPDS1. SPMS interacts with both SPDS1 and SPDS2 in yeast and in vitro. Unlike SPDS1 and SPDS2, SPMS failed to suppress the speΔ3 deficiency of spermidine synthase in yeast. However, SPMS was able to complement the speΔ4 spermine deficiency in yeast, indicating that SPMS is a novel spermine synthase. The SPDS and SPMS proteins showed no homodimerization but formed heterodimers in vitro. Pairwise coexpression of hemagglutinin- and c-Myc epitope–labeled proteins in Arabidopsis cells confirmed the existence of coimmunoprecipitating SPDS1-SPDS2 and SDPS2-SPMS heterodimers in vivo. The epitope-labeled SPDS and SPMS proteins copurified with protein complexes ranging in size from 650 to 750 kD. Our data demonstrate the existence of a metabolon involving at least the last two steps of polyamine biosynthesis in Arabidopsis.