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Reconsideration of Network Types
Xiao Xiao,Natsumi Takahashi,Daichi Enomoto,Hisashi Yamamoto 대한산업공학회 2015 대한산업공학회 추계학술대회논문집 Vol.2015 No.11
The computation of network system reliability is a classical problem. It becomes more and more difficult to calculate the maximal all-terminal reliability of a network system as the number of nodes and edges increase. One approach is to firstly classify the network systems into several types, and secondly identify the type which has the greatest all-terminal reliability, then finally calculate the maximal all-terminal reliability of the identified type of network system. This allows the exact maximal all-terminal reliability of a complex network system to be derived rather easily, because it can be achieved by considering the failure patterns of only the identified type. This paper employs three propositions to logically classify the network types for e = n + 4. Several types are found to be ignored in the existing works. We list up them for further discussions. This work is unconcluded.
Andrew T. Baker,Natsumi Takahashi,Sathees B. Chandra 한국유전체학회 2010 Genomics & informatics Vol.8 No.2
Monofunctional biosynthetic peptidoglycan transglycosylase (MBPT) catalyzes the formation of the glycan chain in bacterial cell walls from peptidoglycan subunits: N-acetylglucosamine (NAG) and acetylmuramic acid (NAM). Bifunctional glycosyltransferases such as the penicillin binding protein (PBP) have peptidoglycan glycosyltransferase (PGT) on their C terminal end which links together the peptidoglycan subunits while transpeptidase (TP) on the N terminal end cross-links the peptide moieties on the NAM monosaccharide of the peptide subunits to create the bacterial cell wall. The singular function of MBPT resembles the C terminal end of PBP as it too contains and utilizes a similar PGT domain. In this article we analyzed the infectious and non infectious protein sequences of MBPT from 31 different strains of bacteria using a variety of bioinformatic tools. Motif analysis, dot-plot comparison, and phylogenetic analysis identified a number of significant differences between infectious and non-infectious protein sequences. In this paper we have made an attempt to explain, analyze and discuss these differences from an evolutionary perspective. The results of our sequence analysis may open the door for utilizing MBPT as a new target to fight a variety of infectious bacteria.
Baker, Andrew T.,Takahashi, Natsumi,Chandra, Sathees B. Korea Genome Organization 2010 Genomics & informatics Vol.8 No.2
Monofunctional biosynthetic peptidoglycan transglycosylase (MBPT) catalyzes the formation of the glycan chain in bacterial cell walls from peptidoglycan subunits: N-acetylglucosamine (NAG) and acetylmuramic acid (NAM). Bifunctional glycosyltransferases such as the penicillin binding protein (PBP) have peptidoglycan glycosyltransferase (PGT) on their C terminal end which links together the peptidoglycan subunits while transpeptidase (TP) on the N terminal end cross-links the peptide moieties on the NAM monosaccharide of the peptide subunits to create the bacterial cell wall. The singular function of MBPT resembles the C terminal end of PBP as it too contains and utilizes a similar PGT domain. In this article we analyzed the infectious and non infectious protein sequences of MBPT from 31 different strains of bacteria using a variety of bioinformatic tools. Motif analysis, dot-plot comparison, and phylogenetic analysis identified a number of significant differences between infectious and non-infectious protein sequences. In this paper we have made an attempt to explain, analyze and discuss these differences from an evolutionary perspective. The results of our sequence analysis may open the door for utilizing MBPT as a new target to fight a variety of infectious bacteria.