For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
11
views
62
references
 Top references
cited by
9
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
1 collections
    0
    shares
      301
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Diagnostic potential of saliva proteome analysis: a review and guide to clinical practice

      review-article

      Read this article at

      SciELOPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Abstract: Proteomic techniques have become popular in medicine and dentistry because of their widespread use in analyzing bodily fluids such as blood, saliva, urine, and gingival crevicular fluids as well as hard tissues such as enamel, dentine, and cementum. This review is a guide to proteomic techniques in general dentistry, summarizing techniques and their clinical application in understanding and diagnosing diseases and their use in identifying biomarkers of various diseases.

          Related collections

          Most cited references62

          • Record: found
          • Abstract: found
          • Article: not found

          Proteomics. Tissue-based map of the human proteome.

          Mathias Uhlén, Linn Fagerberg, Björn Hallström … (2015)
          Resolving the molecular details of proteome variation in the different tissues and organs of the human body will greatly increase our knowledge of human biology and disease. Here, we present a map of the human tissue proteome based on an integrated omics approach that involves quantitative transcriptomics at the tissue and organ level, combined with tissue microarray-based immunohistochemistry, to achieve spatial localization of proteins down to the single-cell level. Our tissue-based analysis detected more than 90% of the putative protein-coding genes. We used this approach to explore the human secretome, the membrane proteome, the druggable proteome, the cancer proteome, and the metabolic functions in 32 different tissues and organs. All the data are integrated in an interactive Web-based database that allows exploration of individual proteins, as well as navigation of global expression patterns, in all major tissues and organs in the human body. Copyright © 2015, American Association for the Advancement of Science.
          Article 0 comments Cited 3974 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Large-scale analysis of the yeast proteome by multidimensional protein identification technology.

            Michael Washburn, Dirk Wolters, John R R Yates (2001)
            We describe a largely unbiased method for rapid and large-scale proteome analysis by multidimensional liquid chromatography, tandem mass spectrometry, and database searching by the SEQUEST algorithm, named multidimensional protein identification technology (MudPIT). MudPIT was applied to the proteome of the Saccharomyces cerevisiae strain BJ5460 grown to mid-log phase and yielded the largest proteome analysis to date. A total of 1,484 proteins were detected and identified. Categorization of these hits demonstrated the ability of this technology to detect and identify proteins rarely seen in proteome analysis, including low-abundance proteins like transcription factors and protein kinases. Furthermore, we identified 131 proteins with three or more predicted transmembrane domains, which allowed us to map the soluble domains of many of the integral membrane proteins. MudPIT is useful for proteome analysis and may be specifically applied to integral membrane proteins to obtain detailed biochemical information on this unwieldy class of proteins.
            Article 0 comments Cited 619 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Current two-dimensional electrophoresis technology for proteomics.

              Angelika Görg, Walter W Weiss, Michael J Dunn (2004)
              Two-dimensional gel electrophoresis (2-DE) with immobilized pH gradients (IPGs) combined with protein identification by mass spectrometry (MS) is currently the workhorse for proteomics. In spite of promising alternative or complementary technologies (e.g. multidimensional protein identification technology, stable isotope labelling, protein or antibody arrays) that have emerged recently, 2-DE is currently the only technique that can be routinely applied for parallel quantitative expression profiling of large sets of complex protein mixtures such as whole cell lysates. 2-DE enables the separation of complex mixtures of proteins according to isoelectric point (pI), molecular mass (Mr), solubility, and relative abundance. Furthermore, it delivers a map of intact proteins, which reflects changes in protein expression level, isoforms or post-translational modifications. This is in contrast to liquid chromatography-tandem mass spectrometry based methods, which perform analysis on peptides, where Mr and pI information is lost, and where stable isotope labelling is required for quantitative analysis. Today's 2-DE technology with IPGs (Görg et al., Electrophoresis 2000, 21, 1037-1053), has overcome the former limitations of carrier ampholyte based 2-DE (O'Farrell, J. Biol. Chem. 1975, 250, 4007-4021) with respect to reproducibility, handling, resolution, and separation of very acidic and/or basic proteins. The development of IPGs between pH 2.5-12 has enabled the analysis of very alkaline proteins and the construction of the corresponding databases. Narrow-overlapping IPGs provide increased resolution (delta pI = 0.001) and, in combination with prefractionation methods, the detection of low abundance proteins. Depending on the gel size and pH gradient used, 2-DE can resolve more than 5000 proteins simultaneously (approximately 2000 proteins routinely), and detect and quantify < 1 ng of protein per spot. In this article we describe the current 2-DE/MS workflow including the following topics: sample preparation, protein solubilization, and prefractionation; protein separation by 2-DE with IPGs; protein detection and quantitation; computer assisted analysis of 2-DE patterns; protein identification and characterization by MS; two-dimensional protein databases.
              Article 0 comments Cited 250 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Camilla Vieira Esteves: Role: ND
                Wladimir Gushiken de Campos: Role: ND
                Milena Monteiro de Souza: Role: ND
                Silvia Vanessa Lourenço: Role: ND
                Walter Luiz Siqueira: Role: ND
                Celso Augusto Lemos-Júnior: Role: ND
                Journal
                Journal ID (publisher-id): bor
                Title: Brazilian Oral Research
                Abbreviated Title: Braz. oral res.
                Publisher: Sociedade Brasileira de Pesquisa Odontológica - SBPqO (São Paulo, SP, Brazil )
                ISSN (Print): 1806-8324
                ISSN (Electronic): 1807-3107
                Publication date (Print and electronic): May 2019
                Volume: 33
                Issue: 0
                Electronic Location Identifier: e043
                Affiliations
                [3] São Paulo São Paulo orgnameUniversidade de São Paulo orgdiv1School of Dentistry orgdiv2Department of General Pathology Brazil
                [1] São Paulo São Paulo orgnameUniversidade de São Paulo orgdiv1School of Dentistry orgdiv2Department of Stomatology Brazil
                [2] São Paulo São Paulo orgnameUniversidade de São Paulo orgdiv1School of Medicine orgdiv2Department of Dermatology Brazil
                [4] London Ontario orgnameThe University of Western Ontario orgdiv1Schulich School of Medicine & Dentistry Canada
                Article
                Publisher ID: S1806-83242019000100600
                DOI: 10.1590/1807-3107bor-2019.vol33.0043
                PubMed ID: 31508727
                SO-VID: 0d61a204-245d-45d0-b83b-7bd229a5147c
                License:

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                Date received : 17 September 2018
                Date accepted : 25 April 2019
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 72, Pages: 0
                Product

                SciELO Brazil

                Categories
                Subject: Critical Review

                Keywords: Proteomics,Mass Spectrometry,Diagnosis,Electrophoresis, Polyacrylamide Gel,Saliva
                Data availability:
                Keywords: Proteomics, Mass Spectrometry, Diagnosis, Electrophoresis, Polyacrylamide Gel, Saliva

                Comments

                Comment on this article

                scite_

                Similar content301

                See all similar

                Cited by9

                See all cited by

                Most referenced authors1,432

                See all reference authors