15795315
An Efficient Staging Algorithm for Binding-Time Analysis
Binding-Time Analysis (BTA) is one of the compile-time program analyses which is a general framework for program optimization and program generation [1]. The task of BTA is to divide a source program into two parts according to a given binding-time specification [2]. A binding-time specification gives information about availability of data: static data are available at compile-time while dynamic data are available at run time. BTA determines, from a binding-time specification of the input, on which parts computation can take place by propagating information on static data. Partial evaluators specialize the program for the static data by using the information from BTA to generate a more efficient program than the original.
5453797
List Homomorphism with Accumulation
This paper introduces accumulation into list homomorphisms for systematic development of both efficient and correct parallel programs. New parallelizable recursive pattern called H-homomorphism is given, and transformations from sequential patterns in the H-form and Hform into (H-)homomorphism are shown. We illustrate the power of our formalization by developing a novel and general parallel program for a class of interesting and challenging problems, known as maximum marking problems.
21046907
Construction of List Homomorphisms by Tupling and Fusion
List homomorphisms are functions which can be efficiently computed in parallel since they ideally suit the divide- sand-conquer paradigm. However, some interesting functions, e.g., the maximum segment sum problem, are not list homomorphisms. In this paper, we propose a systematic way of embedding them into list homomorphisms so that parallel programs are derived. We show, with an example, how a simple, and “obviously” correct, but possibly inefficient solution to the problem can be successfully turned into a semantically equivalent almost homomorphism by means of two transformations: tupling and fusion.
13526098
Systematic Derivation of Tree Contraction Algorithms
While tree contraction algorithms play an important role in efficient tree computation in parallel, it is difficult to develop such algorithms due to the strict conditions imposed on contracting op...
15997088
A New Parallel Skeleton for General Accumulative Computations
Skeletal parallel programming enables programmers to build a parallel program from ready-made components (parallel primitives) for which efficient implementations are known to exist, making both the parallel program development and the parallelization process easier. Constructing efficient parallel programs is often difficult, however, due to difficulties in selecting a proper combination of parallel primitives and in implementing this combination without having unnecessary creations and exchanges of data among parallel primitives and processors. To overcome these difficulties, we propose a powerful and general parallel skeleton, accumulate, which can be used to naturally code efficient solutions to problems as well as be efficiently implemented in parallel using Message Passing Interface (MPI).
17460651
A calculational fusion system HYLO
Fusion, one of the most useful transformation tactics for deriving efficient programs, is the process whereby separate pieces of programs are fused into a single one, leading to an efficient program without intermediate data structures produced. In this paper, we report our on-going investigation on the design and implementation of an automatic transformation system HYLO which performs fusion transformation in a more systematic and more general way than any other systems. The distinguished point of our system is its calculational feature based on simple application of transformation laws rather than traditional search-based transformations.
10305231
The Protein Information Resource: an integrated public resource of functional annotation of proteins
The Protein Information Resource (PIR) serves as an integrated public resource of functional annotation of protein data to support genomic/proteomic research and scientific discovery. The PIR, in collaboration with the Munich Information Center for Protein Sequences (MIPS) and the Japan International Protein Information Database (JIPID), produces the PIR-International Protein Sequence Database (PSD), the major annotated protein sequence database in the public domain, containing about 250 000 proteins. To improve protein annotation and the coverage of experimentally validated data, a bibliography submission system is developed for scientists to submit, categorize and retrieve literature information. Comprehensive protein information is available from iProClass, which includes family classification at the superfamily, domain and motif levels, structural and functional features of proteins, as well as cross-references to over 40 biological databases. To provide timely and comprehensive protein data with source attribution, we have introduced a non-redundant reference protein database, PIR-NREF. The database consists of about 800 000 proteins collected from PIR-PSD, SWISS-PROT, TrEMBL, GenPept, RefSeq and PDB, with composite protein names and literature data. To promote database interoperability, we provide XML data distribution and open database schema, and adopt common ontologies. The PIR web site (http://pir.georgetown.edu/) features data mining and sequence analysis tools for information retrieval and functional identification of proteins based on both sequence and annotation information. The PIR databases and other files are also available by FTP (ftp://nbrfa.georgetown.edu/pir_databases).
7795322
The Protein Information Resource
The Protein Information Resource (PIR) is an integrated public resource of protein informatics that supports genomic and proteomic research and scientific discovery. PIR maintains the Protein Sequence Database (PSD), an annotated protein database containing over 283 000 sequences covering the entire taxonomic range. Family classification is used for sensitive identification, consistent annotation, and detection of annotation errors. The superfamily curation defines signature domain architecture and categorizes memberships to improve automated classification. To increase the amount of experimental annotation, the PIR has developed a bibliography system for literature searching, mapping, and user submission, and has conducted retrospective attribution of citations for experimental features. PIR also maintains NREF, a non-redundant reference database, and iProClass, an integrated database of protein family, function, and structure information. PIR-NREF provides a timely and comprehensive collection of protein sequences, currently consisting of more than 1 000 000 entries from PIR-PSD, SWISS-PROT, TrEMBL, RefSeq, GenPept, and PDB. The PIR web site (http://pir.georgetown.edu) connects data analysis tools to underlying databases for information retrieval and knowledge discovery, with functionalities for interactive queries, combinations of sequence and text searches, and sorting and visual exploration of search results. The FTP site provides free download for PSD and NREF biweekly releases and auxiliary databases and files.
3641866
The iProClass integrated database for protein functional analysis
Increasingly, scientists have begun to tackle gene functions and other complex regulatory processes by studying organisms at the global scales for various levels of biological organization, ranging from genomes to metabolomes and physiomes. Meanwhile, new bioinformatics methods have been developed for inferring protein function using associative analysis of functional properties to complement the traditional sequence homology-based methods. To fully exploit the value of the high-throughput system biology data and to facilitate protein functional studies requires bioinformatics infrastructures that support both data integration and associative analysis. The iProClass database, designed to serve as a framework for data integration in a distributed networking environment, provides comprehensive descriptions of all proteins, with rich links to over 50 databases of protein family, function, pathway, interaction, modification, structure, genome, ontology, literature, and taxonomy. In particular, the database is organized with PIRSF family classification and maps to other family, function, and structure classification schemes. Coupled with the underlying taxonomic information for complete genomes, the iProClass system (http://pir.georgetown.edu/iproclass/) supports associative studies of protein family, domain, function, and structure. A case study of the phosphoglycerate mutases illustrates a systematic approach for protein family and phylogenetic analysis. Such studies may serve as a basis for further analysis of protein functional evolution, and its relationship to the co-evolution of metabolic pathways, cellular networks, and organisms.
6684027
iProLINK: an integrated protein resource for literature mining
The exponential growth of large-scale molecular sequence data and of the PubMed scientific literature has prompted active research in biological literature mining and information extraction to facilitate genome/proteome annotation and improve the quality of biological databases. Motivated by the promise of text mining methodologies, but at the same time, the lack of adequate curated data for training and benchmarking, the Protein Information Resource (PIR) has developed a resource for protein literature mining--iProLINK (integrated Protein Literature INformation and Knowledge). As PIR focuses its effort on the curation of the UniProt protein sequence database, the goal of iProLINK is to provide curated data sources that can be utilized for text mining research in the areas of bibliography mapping, annotation extraction, protein named entity recognition, and protein ontology development. The data sources for bibliography mapping and annotation extraction include mapped citations (PubMed ID to protein entry and feature line mapping) and annotation-tagged literature corpora. The latter includes several hundred abstracts and full-text articles tagged with experimentally validated post-translational modifications (PTMs) annotated in the PIR protein sequence database. The data sources for entity recognition and ontology development include a protein name dictionary, word token dictionaries, protein name-tagged literature corpora along with tagging guidelines, as well as a protein ontology based on PIRSF protein family names. iProLINK is freely accessible at http://pir.georgetown.edu/iprolink, with hypertext links for all downloadable files.
12615323
PIRSF: family classification system at the Protein Information Resource
The Protein Information Resource (PIR) is an integrated public resource of protein informatics. To facilitate the sensible propagation and standardization of protein annotation and the systematic detection of annotation errors, PIR has extended its superfamily concept and developed the SuperFamily (PIRSF) classification system. Based on the evolutionary relationships of whole proteins, this classification system allows annotation of both specific biological and generic biochemical functions. The system adopts a network structure for protein classification from superfamily to subfamily levels. Protein family members are homologous (sharing common ancestry) and homeomorphic (sharing full-length sequence similarity with common domain architecture). The PIRSF database consists of two data sets, preliminary clusters and curated families. The curated families include family name, protein membership, parent-child relationship, domain architecture, and optional description and bibliography. PIRSF is accessible from the website at http://pir.georgetown.edu/pirsf/ for report retrieval and sequence classification. The report presents family annotation, membership statistics, cross-references to other databases, graphical display of domain architecture, and links to multiple sequence alignments and phylogenetic trees for curated families. PIRSF can be utilized to analyze phylogenetic profiles, to reveal functional convergence and divergence, and to identify interesting relationships between homeomorphic families, domains and structural classes.