Nucleic Acids Research, 2002, Vol. 30, No. 1 235-238
© 2002 Oxford University Press
The PROSITE database, its status in 2002
Swiss Institute of Bioinformatics (SIB), Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges /Lausanne, Switzerland, 1Swiss Institute of Bioinformatics (SIB), CMU, University of Geneva, 1 rue Michel Servet, CH-1211 Geneva 4, Switzerland and 2MEMOREC, Stoffel GmbH, Stoeckheimer Weg 1, D-50829 Koeln, Germany
Received September 24, 2001; Accepted October 2, 2001.
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ABSTRACT |
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 TOP ABSTRACT BACKGROUNDLEADING CONCEPTSFORMAT AND DOCUMENT FILESCONTENT OF THE CURRENT...SPECIAL PROFILES AND FUTURE...OBTAINING A LOCAL COPY...MAKING USE OF PROSITEREFERENCES |
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PROSITE [Bairoch and Bucher (1994) Nucleic Acids Res., 22, 3583–3589; Hofmann et al. (1999) Nucleic Acids Res., 27, 215–219] is a method of identifying the functions of uncharacterized proteins translated from genomic or cDNA sequences. The PROSITE database (http://www.expasy.org/prosite/) consists of biologically significant patterns and profiles designed in such a way that with appropriate computational tools it can rapidly and reliably help to determine to which known family of proteins (if any) a new sequence belongs, or which known domain(s) it contains.
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BACKGROUND |
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In some cases the sequence of an unknown protein is too distantly related to any protein of known structure to detect its resemblance by pairwise sequence alignment. However, relationships can be revealed by the occurrence in its sequence of a particular cluster of residue types, which is variously known as a pattern, motif, signature or fingerprint. These motifs arise because specific region(s) of a protein which may be important, for example, for their binding properties or for their enzymatic activity are conserved in both structure and sequence. Based on these observations, we decided in 1988, to actively pursue the development of a database of regular expression-like patterns, which would be used to search against sequences of unknown function.
But, while sequence patterns are very useful, there are a number of protein families as well as functional or structural domains that cannot be detected using patterns due to their extreme sequence divergence. Typical examples of important functional domains, which are weakly conserved, are the globins, and the SH2 and SH3 domains. In such domains there are only a few sequence positions which are well conserved.
The use of techniques based on profiles or weight matrices (the two terms are used synonymously here) allows the detection of such proteins or domains (1,2). A profile is a table of position-specific amino acid weights and gap costs. These numbers (also referred to as scores) are used to calculate a similarity score for any alignment between a profile and a sequence, or parts of a profile and a sequence. An alignment with a similarity score higher than or equal to a given cut-off value constitutes a motif occurrence. A distinguishing feature between a pattern and a profile is that the former is usually confined to a small region with high sequence similarity whereas the latter attempts to characterize a protein family or domain over its entire length.
We thus started in 1994 to complement the approach based on patterns by gradually adding profile entries to PROSITE (3,4). The profile structure (5,6) used in PROSITE is an extension of the profiles introduced by Gribskov et al. (7) and very similar to the HMM-profiles used in the Pfam database (8). Most profiles in PROSITE were generated from multiple sequence alignments using Gribskov’s method (9) with modifications described previously (10,11).
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LEADING CONCEPTS |
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The design of PROSITE follows five leading concepts:
1. Completeness. For such a compilation to be helpful in the determination of protein function, it is important that it contains as many biologically meaningful patterns and profiles as possible.
2. High specificity. In the majority of cases we have chosen patterns or profiles that are specific enough that they do not detect too many unrelated sequences, yet they will detect most, if not all, sequences that clearly belong to the set in consideration.
3. Documentation. Each of the entries in PROSITE is fully documented; the documentation includes a concise description of the protein family or domain that it is designed to detect, as well as a summary of the reasons leading to the development of the pattern or profile.
4. Periodic reviewing. It is important that each entry be periodically reviewed to insure that it is still valid.
5. A very close relationship with the SWISS-PROT protein sequence data bank (12). Updating of PROSITE and of the annotations of the relevant SWISS-PROT entries are very often carried out in parallel. Software tools based on PROSITE are used to automatically update the feature table lines of SWISS-PROT entries relevant to the presence and extent of specific domains.
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FORMAT AND DOCUMENT FILES |
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The core of the PROSITE database is composed of two ASCII (text) files. The first file (PROSITE.DAT) is a computer-readable file that contains all the information necessary for programs that make use of PROSITE to scan sequence(s) for the occurrence of the patterns and/or profiles. This file also includes, for each of the entries described, statistics on the number of hits obtained while scanning for that pattern or profile in SWISS-PROT. Cross-references to the corresponding SWISS-PROT and PDB entries are also present in the file. The second file (PROSITE.DOC), which we call the textbook, contains textual information that documents each pattern.
A sample textbook entry is accessible at http://www.expasy.org/cgi-bin/nicesite.pl?PS00041; this particular entry is linked to two entries in the PROSITE.DAT file: a pattern, http://www.expasy.org/cgi-bin/prosite-search-ac?pdoc00040; and a profile, http://www.expasy.org/cgi-bin/nicesite.pl?PS01124.
Several document files are also distributed with the database: PROSUSER.TXT, the database user’s manual; PROFILE.TXT, a detailed description of the syntax for the profiles; PROSITE.LIS, a list of PROSITE documentation entries; PROSITE.GET, a document on how to obtain a local copy of PROSITE; PROSITE.PRG, a description of programs and electronic mail servers that make use of PROSITE; PAUTINDX.TXT, an index of authors cited in the PROSITE.DOC file.
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CONTENT OF THE CURRENT RELEASE |
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Release 16.46 of PROSITE (August 30, 2001) contains 1096 documentation entries describing 1483 different patterns, rules and profiles/matrices. In addition to these entries, a collection of 215 preliminary profiles is available in the pre-release distribution from the FTP server of the ISREC group (see below). The list of the documentation entries that have been added since the last release of PROSITE (15.0) is provided in Table 1; furthermore, many entries were updated.
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SPECIAL PROFILES AND FUTURE DEVELOPMENT |
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Profiles can be used to represent a great variety of sequence features besides protein families and domains. We briefly mention a few special cases and how they can be recognized by software for different treatment.
CC /SKIP-FLAG=TRUE: as for patterns this means that the profile is a frequent hit producer. Such profiles may be skipped in order to keep the output short. Current profile belonging to this type: NLS_BP, bipartite nuclear localization signal.
MA TOPOLOGY=CIRCULAR and CC /MATRIX_TYPE= repeat_region: these two lines identify a circular profile which will produce one match for a repeat region consisting of several tandem repeated units. Current profiles belonging to this type: ANK_REP_REGION, ankyrin repeat region; COLLAGEN_REP, collagen repeat (G-x-x); TPR_REGION, TPR repeat region; WD40_REGION, WD40 repeat region; PUM_REPEATS, pumilio RNA-binding domain.
CC /MATRIX_TYPE=composition: this identifies a profile for compositionally biased regions; for example, PRO_RICH, proline-rich region. There is currently one such profile for each amino acid. We plan to add more such profiles in the future, especially profiles to identify subcellular localization signals and simple repeat domains.
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OBTAINING A LOCAL COPY OF PROSITE |
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PROSITE is freely available to academic users. As of Release 16, the documentation entries are copyrighted. To obtain a license, commercial users should contact: The Swiss Institute of Bioinformatics by email: license{at}isb-sib.ch. Or its commercial representative: Geneva Bioinformatics (GeneBio) S.A., Case Postale 210, CH-1211 Geneva 12, Switzerland. Tel: +41 22 702 99 00; Fax: +41 22 702 99 99; Email: info{at}genebio.com.
PROSITE is distributed on CD-ROM and email server (4,13,14), or can be directly downloaded via anonymous FTP from the following FTP sites: ExPASy, ftp://ftp.expasy.org/databases/prosite/; EBI, ftp://ftp.ebi.ac.uk/pub/databases/prosite/.
A complete profile collection including pre-release profiles and corresponding preliminary documentation can be downloaded from: ISREC, ftp://ftp.isrec.isb-sib.ch/sib-isrec/profiles/. This site also offers so-called frame search versions of the profiles which can be used for searching DNA sequences for matches in open reading frames using an error-tolerant method (described in the manual pages of the pftools package discussed below).
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MAKING USE OF PROSITE |
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Computer programs
Many academic groups and commercial companies have developed computer programs that make use of the pattern entries in PROSITE. The PROSITE.PRG file contains a full list of these programs, their operating system specificity, characteristics as well as information on how to obtain them.
Two software packages are distributed to make use of profile entries:
1. pftools (version 2.2 in FORTRAN77) written by Philipp Bucher. These tools are available by anonymous FTP from the server: ftp://ftp.isrec.isb-sib.ch/sib-isrec/pftools. Several versions are available, as well as executables compiled for many Unix platforms (including a recent MacOSX version) and for Windows 95, 98 or 2000.
2. PrfLib (version 1.0 in ANSI C) written by Nicolas Moeri. These tools are available from the server: ftp://ftp.isrec.isb-sib.ch/sib-isrec/PrfLib/.
A specialized hardware called GeneMatcher from Paracel Inc. allows very fast searches over entire databases using profiles or HMMs. The software distributed with this hardware supports PROSITE profiles although with some limitations: http://www.paracel.com.
One software package is distributed that makes use of pattern entries: DeepView [Swiss-PDB viewer (15)] allows you to search for and to highlight the different patterns in the structure http://www.expasy.org/spdbv/.
Interactive access to PROSITE using the World Wide Web
The most efficient and user-friendly way to browse interactively in PROSITE as well as to analyze a sequence for the occurrence of a pattern or a profile is to use the World Wide Web molecular biology server ExPASy (16).
You can directly access the ‘top’ page of the section of ExPASy that allows you to browse through the PROSITE documentation and data entries by going to http://www.expasy.org/prosite/.
To use the PROSITE patterns and profiles, you can make use of the following software tools:
ScanProsite. ScanProsite allows to either scan a protein sequence—from SWISS-PROT or provided by the user—for the occurrence of patterns stored in PROSITE or to scan the SWISS-PROT and/or TrEMBL database, including weekly releases, for the occurrence of a pattern that can originate from PROSITE or be provided by the user. The URL for ScanProsite is http://www.expasy.org/tools/scnpsite.html.
ProfileScan. ProfileScan allows to scan a protein sequence—from SWISS-PROT or provided by the user—for the occurrence of profiles stored in PROSITE and in the pre-release collection. Our new PFSCAN server page generates a graphical representation of a match (Fig. 1). We developed this tool to provide users with a much more informative display than a simple pairwise alignment between the query sequence and the consensus of the profile. It can be immediately visible that the scoring system is position-specific and that some regions of a sequence are scored differently and thus are responsible for a good or a bad overall score. The new URL for ProfileScan is http://hits.isb-sib.ch/cgi-bin/PFSCAN.
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FrameProfileScan. FrameProfileScan allows one to scan a DNA sequence (translated on the fly into protein)—from EMBL or provided by the user—for the occurrence of profiles stored in PROSITE. The URL for FrameProfileScan is http://www.isrec.isb-sib.ch/software/PFRAMESCAN_form.html.
InterProScan. InterProScan allows one to scan a protein sequence provided by the user for the occurrence of profiles stored in InterPro resource of protein families, domains and sites (17). The URL for InterProScan is http://www.ebi.ac.uk/interpro/scan.html.
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FOOTNOTES |
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* To whom correspondence should be addressed. Tel: +41 21 692 5892; Fax: +41 21 692 5945; Email: philipp.bucher{at}isrec.unil.ch
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REFERENCES |
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A. V. Lobanov, S. Gromer, G. Salinas, and V. N. Gladyshev Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a Kinetoplastida-specific selenoprotein Nucleic Acids Res., September 1, 2006; 34(14): 4012 - 4024. [Abstract] [Full Text] [PDF]
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K. Bryson, V. Loux, R. Bossy, P. Nicolas, S. Chaillou, M. van de Guchte, S. Penaud, E. Maguin, M. Hoebeke, P. Bessieres, et al. AGMIAL: implementing an annotation strategy for prokaryote genomes as a distributed system Nucleic Acids Res., July 19, 2006; 34(12): 3533 - 3545. [Abstract] [Full Text] [PDF]
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J.-C. Nebel Generation of 3D templates of active sites of proteins with rigid prosthetic groups Bioinformatics, May 15, 2006; 22(10): 1183 - 1189. [Abstract] [Full Text] [PDF]
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D. Schubert, M. Raudaskoski, N. Knabe, and E. Kothe Ras GTPase-Activating Protein Gap1 of the Homobasidiomycete Schizophyllum commune Regulates Hyphal Growth Orientation and Sexual Development. Eukaryot. Cell, April 1, 2006; 5(4): 683 - 695. [Abstract] [Full Text] [PDF]
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K. P. Forbes, B. Addepalli, and A. G. Hunt An Arabidopsis Fip1 Homolog Interacts with RNA and Provides Conceptual Links with a Number of Other Polyadenylation Factor Subunits J. Biol. Chem., January 6, 2006; 281(1): 176 - 186. [Abstract] [Full Text] [PDF]
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G. Pugalenthi, A. Bhaduri, and R. Sowdhamini iMOTdb--a comprehensive collection of spatially interacting motifs in proteins Nucleic Acids Res., January 1, 2006; 34(suppl_1): D285 - D286. [Abstract] [Full Text] [PDF]
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J. Wennerhold, A. Krug, and M. Bott The AraC-type Regulator RipA Represses Aconitase and Other Iron Proteins from Corynebacterium under Iron Limitation and Is Itself Repressed by DtxR J. Biol. Chem., December 9, 2005; 280(49): 40500 - 40508. [Abstract] [Full Text] [PDF]
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R. J. Siezen, B. Renckens, I. van Swam, S. Peters, R. van Kranenburg, M. Kleerebezem, and W. M. de Vos Complete Sequences of Four Plasmids of Lactococcus lactis subsp. cremoris SK11 Reveal Extensive Adaptation to the Dairy Environment Appl. Envir. Microbiol., December 1, 2005; 71(12): 8371 - 8382. [Abstract] [Full Text] [PDF]
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E. M. Davison, M. M. Harrison, A. J. M. Walhout, M. Vidal, and H. R. Horvitz lin-8, Which Antagonizes Caenorhabditis elegans Ras-Mediated Vulval Induction, Encodes a Novel Nuclear Protein That Interacts With the LIN-35 Rb Protein Genetics, November 1, 2005; 171(3): 1017 - 1031. [Abstract] [Full Text] [PDF]
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Y. Liu, J.-E. Ahn, S. Datta, R. A. Salzman, J. Moon, B. Huyghues-Despointes, B. Pittendrigh, L. L. Murdock, H. Koiwa, and K. Zhu-Salzman Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase Plant Physiology, November 1, 2005; 139(3): 1545 - 1556. [Abstract] [Full Text] [PDF]
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J. Y. Kim and D. Saffen Activation of M1 Muscarinic Acetylcholine Receptors Stimulates the Formation of a Multiprotein Complex Centered on TRPC6 Channels J. Biol. Chem., September 9, 2005; 280(36): 32035 - 32047. [Abstract] [Full Text] [PDF]
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B. Zhang, Q. Cao, A. Guo, H. Chu, Y. G. Chan, J. P. Buschdorf, B. C. Low, E. A. Ling, and F. Liang Juxtanodin: An oligodendroglial protein that promotes cellular arborization and 2',3'-cyclic nucleotide-3'-phosphodiesterase trafficking PNAS, August 9, 2005; 102(32): 11527 - 11532. [Abstract] [Full Text] [PDF]
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C. Langlet, I. Langer, P. Vertongen, N. Gaspard, J.-M. Vanderwinden, and P. Robberecht Contribution of the Carboxyl Terminus of the VPAC1 Receptor to Agonist-induced Receptor Phosphorylation, Internalization, and Recycling J. Biol. Chem., July 29, 2005; 280(30): 28034 - 28043. [Abstract] [Full Text] [PDF]
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A. Gibson, A. P. Lewis, K. Affleck, A. J. Aitken, E. Meldrum, and N. Thompson hCLCA1 and mCLCA3 Are Secreted Non-integral Membrane Proteins and Therefore Are Not Ion Channels J. Biol. Chem., July 22, 2005; 280(29): 27205 - 27212. [Abstract] [Full Text] [PDF]
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V. Soukoulis, S. Reddy, R. D. Pooley, Y. Feng, C. A. Walsh, and D. M. Bader Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway PNAS, June 14, 2005; 102(24): 8549 - 8554. [Abstract] [Full Text] [PDF]
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D. Plewczynski, A. Tkacz, L. S. Wyrwicz, and L. Rychlewski AutoMotif server: prediction of single residue post-translational modifications in proteins Bioinformatics, May 15, 2005; 21(10): 2525 - 2527. [Abstract] [Full Text] [PDF]
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T. Burgdorf, E. van der Linden, M. Bernhard, Q. Y. Yin, J. W. Back, A. F. Hartog, A. O. Muijsers, C. G. de Koster, S. P. J. Albracht, and B. Friedrich The Soluble NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 Consists of Six Subunits and Can Be Specifically Activated by NADPH J. Bacteriol., May 1, 2005; 187(9): 3122 - 3132. [Abstract] [Full Text] [PDF]
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D. Hoper, U. Volker, and M. Hecker Comprehensive Characterization of the Contribution of Individual SigB-Dependent General Stress Genes to Stress Resistance of Bacillus subtilis J. Bacteriol., April 15, 2005; 187(8): 2810 - 2826. [Abstract] [Full Text] [PDF]
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S. Orchard, H. Hermjakob, and R. Apweiler Annotating the Human Proteome Mol. Cell. Proteomics, April 1, 2005; 4(4): 435 - 440. [Abstract] [Full Text] [PDF]
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C.-Y. Lin, C.-L. Chen, C.-S. Cho, L.-M. Wang, C.-M. Chang, P.-Y. Chen, C.-Z. Lo, and C. A. Hsiung hp-DPI: Helicobacter pylori Database of Protein Interactomes--embracing experimental and inferred interactions Bioinformatics, April 1, 2005; 21(7): 1288 - 1290. [Abstract] [Full Text] [PDF]
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I. G. Haas, M. Frank, N. Veron, and R. Kemler Presenilin-dependent Processing and Nuclear Function of {gamma}-Protocadherins J. Biol. Chem., March 11, 2005; 280(10): 9313 - 9319. [Abstract] [Full Text] [PDF]
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J. Xue, I. Hunter, T. Steinmetz, A. Peters, B. Ray, and K. W. Miller Novel Activator of Mannose-Specific Phosphotransferase System Permease Expression in Listeria innocua, Identified by Screening for Pediocin AcH Resistance Appl. Envir. Microbiol., March 1, 2005; 71(3): 1283 - 1290. [Abstract] [Full Text] [PDF]
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C. Gomes, S.-D. Oh, J.-W. Kim, S.-Y. Chun, K. Lee, H.-B. Kwon, and J. Soh Expression of the Putative Sterol Binding Protein Stard6 Gene Is Male Germ Cell Specific Biol Reprod, March 1, 2005; 72(3): 651 - 658. [Abstract] [Full Text] [PDF]
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M. H. H. Schmidt, I. Dikic, and O. Bogler Src Phosphorylation of Alix/AIP1 Modulates Its Interaction with Binding Partners and Antagonizes Its Activities J. Biol. Chem., February 4, 2005; 280(5): 3414 - 3425. [Abstract] [Full Text] [PDF]
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T. Asano, N. Tanaka, G. Yang, N. Hayashi, and S. Komatsu Genome-wide Identification of the Rice Calcium-dependent Protein Kinase and its Closely Related Kinase Gene Families: Comprehensive Analysis of the CDPKs Gene Family in Rice Plant Cell Physiol., February 1, 2005; 46(2): 356 - 366. [Abstract] [Full Text] [PDF]
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Y. Chen, Y. Zhang, Y. Yin, G. Gao, S. Li, Y. Jiang, X. Gu, and J. Luo SPD--a web-based secreted protein database Nucleic Acids Res., January 1, 2005; 33(suppl_1): D169 - D173. [Abstract] [Full Text] [PDF]
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Q. J. Su, L. Lu, S. Saxonov, and D. L. Brutlag eBLOCKs: enumerating conserved protein blocks to achieve maximal sensitivity and specificity Nucleic Acids Res., January 1, 2005; 33(suppl_1): D178 - D182. [Abstract] [Full Text] [PDF]
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D. Guo, K. Hu, Y. Lei, Y. Wang, T. Ma, and D. He Identification and Characterization of a Novel Cytoplasm Protein ICF45 That Is Involved in Cell Cycle Regulation J. Biol. Chem., December 17, 2004; 279(51): 53498 - 53505. [Abstract] [Full Text] [PDF]
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A. E. Whitfield, D. E. Ullman, and T. L. German Expression and Characterization of a Soluble Form of Tomato Spotted Wilt Virus Glycoprotein GN J. Virol., December 1, 2004; 78(23): 13197 - 13206. [Abstract] [Full Text] [PDF]
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J. L. McMurry, J. S. Van Arnam, M. Kihara, and R. M. Macnab Analysis of the Cytoplasmic Domains of Salmonella FlhA and Interactions with Components of the Flagellar Export Machinery J. Bacteriol., November 15, 2004; 186(22): 7586 - 7592. [Abstract] [Full Text] [PDF]
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W. J. Song, Q. W. Qin, J. Qiu, C. H. Huang, F. Wang, and C. L. Hew Functional Genomics Analysis of Singapore Grouper Iridovirus: Complete Sequence Determination and Proteomic Analysis J. Virol., November 15, 2004; 78(22): 12576 - 12590. [Abstract] [Full Text] [PDF]
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F. C. Minion, E. J. Lefkowitz, M. L. Madsen, B. J. Cleary, S. M. Swartzell, and G. G. Mahairas The Genome Sequence of Mycoplasma hyopneumoniae Strain 232, the Agent of Swine Mycoplasmosis J. Bacteriol., November 1, 2004; 186(21): 7123 - 7133. [Abstract] [Full Text] [PDF]
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A. Teplyakov, G. Obmolova, E. Sarikaya, S. Pullalarevu, W. Krajewski, A. Galkin, A. J. Howard, O. Herzberg, and G. L. Gilliland Crystal Structure of the YgfZ Protein from Escherichia coli Suggests a Folate-Dependent Regulatory Role in One-Carbon Metabolism J. Bacteriol., November 1, 2004; 186(21): 7134 - 7140. [Abstract] [Full Text] [PDF]
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P. Malik and J. B. Clements Protein kinase CK2 phosphorylation regulates the interaction of Kaposi's sarcoma-associated herpesvirus regulatory protein ORF57 with its multifunctional partner hnRNP K Nucleic Acids Res., October 14, 2004; 32(18): 5553 - 5569. [Abstract] [Full Text] [PDF]
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I. Alam, A. Dress, M. Rehmsmeier, and G. Fuellen Comparative homology agreement search: An effective combination of homology-search methods PNAS, September 21, 2004; 101(38): 13814 - 13819. [Abstract] [Full Text] [PDF]
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J. A. Schmidt, G. F. Browning, and P. F. Markham Mycoplasma hyopneumoniae p65 Surface Lipoprotein Is a Lipolytic Enzyme with a Preference for Shorter-Chain Fatty Acids J. Bacteriol., September 1, 2004; 186(17): 5790 - 5798. [Abstract] [Full Text] [PDF]
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H. M. Kivela, R. Daugelavicius, R. H. Hankkio, J. K. H. Bamford, and D. H. Bamford Penetration of Membrane-Containing Double-Stranded-DNA Bacteriophage PM2 into Pseudoalteromonas Hosts J. Bacteriol., August 15, 2004; 186(16): 5342 - 5354. [Abstract] [Full Text] [PDF]
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J. N. Bragg, D. M. Lawrence, and A. O. Jackson The N-Terminal 85 Amino Acids of the Barley Stripe Mosaic Virus {gamma}b Pathogenesis Protein Contain Three Zinc-Binding Motifs J. Virol., July 15, 2004; 78(14): 7379 - 7391. [Abstract] [Full Text] [PDF]
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I. Niedick, N. Froese, A. Oumard, P. P. Mueller, M. Nourbakhsh, H. Hauser, and M. Koster Nucleolar localization and mobility analysis of the NF-{kappa}B repressing factor NRF J. Cell Sci., July 15, 2004; 117(16): 3447 - 3458. [Abstract] [Full Text] [PDF]
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J. M. Cliff, I. N. J. Andrade, R. Mistry, C. L. Clayton, M. G. Lennon, A. P. Lewis, K. Duncan, P. T. Lukey, and H. M. Dockrell Differential Gene Expression Identifies Novel Markers of CD4+ and CD8+ T Cell Activation Following Stimulation by Mycobacterium tuberculosis J. Immunol., July 1, 2004; 173(1): 485 - 493. [Abstract] [Full Text] [PDF]
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P. K. Papasaikas, P. G. Bagos, Z. I. Litou, V. J. Promponas, and S. J. Hamodrakas PRED-GPCR: GPCR recognition and family classification server Nucleic Acids Res., July 1, 2004; 32(suppl_2): W380 - W382. [Abstract] [Full Text] [PDF]
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