• Journal of the Korean Mathematical Society
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• v.44 no.4
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• pp.863-872
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• 2007

Let D be an integral domain with quotient field K, A a nonempty set of height-one maximal t-ideals of D, F$({\Lambda})={I{\subseteq}D|I$ is an ideal of D such that $I{\subseteq}P$ for all $P{\in}A}$, and $D_F({\Lambda})={x{\in}K|xA{\subseteq}D$ for some $A{\in}F({\Lambda})}$. In this paper, we prove that if each $P{\in}A$ is the radical of a finite type v-ideal (resp., a principal ideal), then $D_{F({\Lambda})}$ is a weakly Krull domain (resp., generalized weakly factorial domain) if and only if the intersection $D_{F({\Lambda})}={\cap}_{P{\in}A}D_P$ has finite character, if and only if $F({\Lambda})$ is a t-splitting set of ideals, if and only if $F({\Lambda})$ is v-finite.

• Journal of KIISE:Software and Applications
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• v.34 no.10
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• pp.889-899
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• 2007

In proteomics, recent advancements In mass spectrometry technology and in protein extraction and separation technology made high-throughput analysis possible. This leads to thousands to hundreds of thousands of MS/MS spectra per single LC-MS/MS experiment. Such a large amount of data creates significant computational challenges and therefore effective data analysis methods that make efficient use of computational resources and, at the same time, provide more peptide identifications are in great need. Here, SIFTER system is designed to avoid inefficient processing of shotgun proteomic data. SIFTER provides software tools that can improve throughput of mass spectrometry-based peptide identification by filtering out poor-quality tandem mass spectra and estimating a Peptide charge state prior to applying analysis algorithms. SIFTER tools characterize and assess spectral features and thus significantly reduce the computation time and false positive rates by localizing spectra that lead to wrong identification prior to full-blown analysis. SIFTER enables fast and in-depth interpretation of tandem mass spectra.