Quantitative analysis of the intra- and inter-subject variability of the whole salivary proteome
Background and Objective Interest in human saliva is increasing for disease‐specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins. Material and Me...
Saved in:
| Published in | Journal of periodontal research Vol. 48; no. 3; pp. 392 - 403 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Blackwell Publishing Ltd
01.06.2013
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Background and Objective
Interest in human saliva is increasing for disease‐specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins.
Material and Methods
We compared intra‐ and inter‐subject variabilities using complementary gel‐based (two‐dimensional difference gel electrophoresis, 2‐D DIGE) and gel‐free (liquid chromatography tandem mass spectrometry, LC‐MS/MS) proteomics profiling of saliva. Unstimulated whole saliva of four subjects was examined at three different time‐points (08.00 h, 12.00 h and 17.00 h) and variability of the saliva proteome was analyzed on two successive days by LC‐MS/MS.
Results
In the 2‐D DIGE experiment, the median coefficient of variation (CV) for intra‐subject variability was significantly lower (CV of 0.39) than that for inter‐subject variability (CV of 0.57; CV of technical replicates 0.17). LC‐MS/MS data confirmed the significantly lower variation within subjects over time (CV of 0.37) than the inter‐subject variability (CV of 0.53; CV of technical replicates 0.11), and that the inter‐subject variability was not time‐dependent.
Conclusion
Both techniques revealed similar trends of variations on technical, intra‐ and inter‐subject level but provided peptide and protein focused information and should thus be used as complementary approaches. The data presented indicate that 2‐D DIGE as well as LC‐MS/MS approaches are suitable for biomarker screening in saliva. |
|---|---|
| AbstractList | Background and Objective
Interest in human saliva is increasing for disease‐specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins.
Material and Methods
We compared intra‐ and inter‐subject variabilities using complementary gel‐based (two‐dimensional difference gel electrophoresis, 2‐D DIGE) and gel‐free (liquid chromatography tandem mass spectrometry, LC‐MS/MS) proteomics profiling of saliva. Unstimulated whole saliva of four subjects was examined at three different time‐points (08.00 h, 12.00 h and 17.00 h) and variability of the saliva proteome was analyzed on two successive days by LC‐MS/MS.
Results
In the 2‐D DIGE experiment, the median coefficient of variation (CV) for intra‐subject variability was significantly lower (CV of 0.39) than that for inter‐subject variability (CV of 0.57; CV of technical replicates 0.17). LC‐MS/MS data confirmed the significantly lower variation within subjects over time (CV of 0.37) than the inter‐subject variability (CV of 0.53; CV of technical replicates 0.11), and that the inter‐subject variability was not time‐dependent.
Conclusion
Both techniques revealed similar trends of variations on technical, intra‐ and inter‐subject level but provided peptide and protein focused information and should thus be used as complementary approaches. The data presented indicate that 2‐D DIGE as well as LC‐MS/MS approaches are suitable for biomarker screening in saliva. Interest in human saliva is increasing for disease-specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins.BACKGROUND AND OBJECTIVEInterest in human saliva is increasing for disease-specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins.We compared intra- and inter-subject variabilities using complementary gel-based (two-dimensional difference gel electrophoresis, 2-D DIGE) and gel-free (liquid chromatography tandem mass spectrometry, LC-MS/MS) proteomics profiling of saliva. Unstimulated whole saliva of four subjects was examined at three different time-points (08.00 h, 12.00 h and 17.00 h) and variability of the saliva proteome was analyzed on two successive days by LC-MS/MS.MATERIAL AND METHODSWe compared intra- and inter-subject variabilities using complementary gel-based (two-dimensional difference gel electrophoresis, 2-D DIGE) and gel-free (liquid chromatography tandem mass spectrometry, LC-MS/MS) proteomics profiling of saliva. Unstimulated whole saliva of four subjects was examined at three different time-points (08.00 h, 12.00 h and 17.00 h) and variability of the saliva proteome was analyzed on two successive days by LC-MS/MS.In the 2-D DIGE experiment, the median coefficient of variation (CV) for intra-subject variability was significantly lower (CV of 0.39) than that for inter-subject variability (CV of 0.57; CV of technical replicates 0.17). LC-MS/MS data confirmed the significantly lower variation within subjects over time (CV of 0.37) than the inter-subject variability (CV of 0.53; CV of technical replicates 0.11), and that the inter-subject variability was not time-dependent.RESULTSIn the 2-D DIGE experiment, the median coefficient of variation (CV) for intra-subject variability was significantly lower (CV of 0.39) than that for inter-subject variability (CV of 0.57; CV of technical replicates 0.17). LC-MS/MS data confirmed the significantly lower variation within subjects over time (CV of 0.37) than the inter-subject variability (CV of 0.53; CV of technical replicates 0.11), and that the inter-subject variability was not time-dependent.Both techniques revealed similar trends of variations on technical, intra- and inter-subject level but provided peptide and protein focused information and should thus be used as complementary approaches. The data presented indicate that 2-D DIGE as well as LC-MS/MS approaches are suitable for biomarker screening in saliva.CONCLUSIONBoth techniques revealed similar trends of variations on technical, intra- and inter-subject level but provided peptide and protein focused information and should thus be used as complementary approaches. The data presented indicate that 2-D DIGE as well as LC-MS/MS approaches are suitable for biomarker screening in saliva. Interest in human saliva is increasing for disease-specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with physiological and environmental factors over time and it comprises human as well as bacterial proteins. We compared intra- and inter-subject variabilities using complementary gel-based (two-dimensional difference gel electrophoresis, 2-D DIGE) and gel-free (liquid chromatography tandem mass spectrometry, LC-MS/MS) proteomics profiling of saliva. Unstimulated whole saliva of four subjects was examined at three different time-points (08.00 h, 12.00 h and 17.00 h) and variability of the saliva proteome was analyzed on two successive days by LC-MS/MS. In the 2-D DIGE experiment, the median coefficient of variation (CV) for intra-subject variability was significantly lower (CV of 0.39) than that for inter-subject variability (CV of 0.57; CV of technical replicates 0.17). LC-MS/MS data confirmed the significantly lower variation within subjects over time (CV of 0.37) than the inter-subject variability (CV of 0.53; CV of technical replicates 0.11), and that the inter-subject variability was not time-dependent. Both techniques revealed similar trends of variations on technical, intra- and inter-subject level but provided peptide and protein focused information and should thus be used as complementary approaches. The data presented indicate that 2-D DIGE as well as LC-MS/MS approaches are suitable for biomarker screening in saliva. |
| Author | Hammer, E. Kocher, T. Völker, U. Gesell-Salazar, M. Dinh, K. H. D. Holtfreter, B. Steil, L. Schurmann, C. Jehmlich, N. Dhople, V. M. |
| Author_xml | – sequence: 1 givenname: N. surname: Jehmlich fullname: Jehmlich, N. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 2 givenname: K. H. D. surname: Dinh fullname: Dinh, K. H. D. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 3 givenname: M. surname: Gesell-Salazar fullname: Gesell-Salazar, M. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 4 givenname: E. surname: Hammer fullname: Hammer, E. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 5 givenname: L. surname: Steil fullname: Steil, L. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 6 givenname: V. M. surname: Dhople fullname: Dhople, V. M. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 7 givenname: C. surname: Schurmann fullname: Schurmann, C. organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany – sequence: 8 givenname: B. surname: Holtfreter fullname: Holtfreter, B. organization: Unit of Periodontology, Department of Restorative Dentistry, Periodontology and Endodontology, University Medicine Greifswald, Ernst-Moritz-Arndt-University, Greifswald, Germany – sequence: 9 givenname: T. surname: Kocher fullname: Kocher, T. organization: Unit of Periodontology, Department of Restorative Dentistry, Periodontology and Endodontology, University Medicine Greifswald, Ernst-Moritz-Arndt-University, Greifswald, Germany – sequence: 10 givenname: U. surname: Völker fullname: Völker, U. email: voelker@uni-greifswald.de organization: Department of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23164135$$D View this record in MEDLINE/PubMed |
| BookMark | eNp1kMtO4zAYRi3ECArDghdAWcIixfckS8T9MqAZDSo74yR_hIubgO1Q-va4tJ0FGrzx7XyfrbOF1tuuBYR2CR6SOA7HDoaEYirW0IBIjFOcSbGOBhhTmjKe80205f0Yx73Mig20SRmRnDAxQI-_e90GE3Qwb5DoVtuZNz7pmiQ8QWLa4HQaj-v5Elzq-3IMVUjetDO6NNaE2YqdPnUWEq-tiZez5MV1AboJ_EQ_Gm097CznbXR_dvr3-CK9uTu_PD66SSsmmUhLgUkpdSYElVrImlFclDwH3mCZ87IpGBUZkzWvtGS0ICB13TDd1DktC8EF20b7i9748GsPPqiJ8RVYq1voeq8I40IQnhc8ontLtC8nUKsXZybxy2plJQKHC6BynfcOGlV9GurmOoxVBKu5dxW9q0_vMXHwJbEq_R-7bJ8aC7PvQXX153SVSBcJ4wO8_0to96xkxjKhRrfn6mR0hkfXD7_ULfsAhUOguQ |
| CitedBy_id | crossref_primary_10_1002_pmic_201800425 crossref_primary_10_1371_journal_pone_0191307 crossref_primary_10_1039_C4NR00319E crossref_primary_10_1016_j_foodhyd_2022_107681 crossref_primary_10_1111_jcpe_12130 crossref_primary_10_1002_pmic_201600230 crossref_primary_10_1039_D3AN00850A crossref_primary_10_1093_database_baab065 crossref_primary_10_1007_s10266_017_0302_9 crossref_primary_10_1021_acs_jproteome_7b00133 crossref_primary_10_1002_prca_201600142 crossref_primary_10_1016_j_jprot_2015_04_030 crossref_primary_10_1039_D3MO00144J crossref_primary_10_1186_2001_1326_3_3 crossref_primary_10_3390_cells12050747 crossref_primary_10_1039_C7NR02140B crossref_primary_10_1080_08927014_2014_977268 crossref_primary_10_1002_prca_201700039 crossref_primary_10_1016_j_dib_2016_05_053 crossref_primary_10_1016_j_jprot_2015_08_006 crossref_primary_10_1074_mcp_RA120_002174 crossref_primary_10_1007_s00702_015_1489_y crossref_primary_10_1016_j_jaci_2016_03_045 crossref_primary_10_1021_acs_jproteome_9b00037 crossref_primary_10_1371_journal_pone_0113683 crossref_primary_10_1177_00220345211014432 crossref_primary_10_1016_j_cca_2015_12_005 crossref_primary_10_1128_mSphere_00215_16 crossref_primary_10_14712_fb2020066020072 crossref_primary_10_1016_j_jprot_2017_12_003 crossref_primary_10_1016_j_jprot_2019_103629 |
| Cites_doi | 10.1021/pr8003776 10.1177/154405910708600802 10.1002/pmic.200400907 10.1002/pmic.200500125 10.1002/sim.4780090710 10.1373/clinchem.2010.153767 10.1016/j.jprot.2008.04.004 10.1111/j.1537-2995.2007.01255.x 10.1016/j.jprot.2009.05.004 10.1590/S0103-64402003000100005 10.1021/pr900675w 10.1111/j.1601-0825.2010.01700.x 10.1111/j.1601-0825.2010.01773.x 10.1586/epr.11.80 10.1074/mcp.M110.000992 10.1074/mcp.M111.012112 10.4137/BMI.S607 10.1016/j.jprot.2010.02.018 10.1074/mcp.M700146-MCP200 10.1158/1078-0432.CCR-07-5037 10.1021/pr060189z 10.1002/pmic.200800626 10.1111/j.1537-2995.2008.01856.x 10.1021/pr049953c 10.1021/pr901096u 10.1016/j.archoralbio.2011.09.016 10.1016/j.bbapap.2007.04.017 10.1586/14789450.4.4.531 10.1021/ac050161r 10.1196/annals.1384.015 10.1007/BF03168467 10.1016/j.jim.2011.07.013 10.1002/pmic.200300426 10.1021/pr100835s 10.1021/pr060065m 10.1016/j.cca.2012.02.020 10.1002/pmic.200600783 10.1111/j.1600-051X.2009.01525.x 10.1021/pr100857t 10.1016/S0003-9969(03)00182-1 |
| ContentType | Journal Article |
| Copyright | 2012 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd 2012 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd. |
| Copyright_xml | – notice: 2012 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd – notice: 2012 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd. |
| DBID | BSCLL AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1111/jre.12025 |
| DatabaseName | Istex CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Dentistry |
| EISSN | 1600-0765 |
| EndPage | 403 |
| ExternalDocumentID | 23164135 10_1111_jre_12025 JRE12025 ark_67375_WNG_DWF0WKXM_N |
| Genre | article Research Support, Non-U.S. Gov't Journal Article |
| GrantInformation_xml | – fundername: Federal Ministry of Education and Research and the Ministry of Cultural Affairs of the Federal State of Mecklenburg–West Pomerania funderid: 03IS2061A |
| GroupedDBID | --- .3N .GA .GJ .Y3 05W 0R~ 10A 1OB 1OC 29L 31~ 33P 34H 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52V 52W 52X 53G 5GY 5HH 5LA 5RE 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AAKAS AANLZ AAONW AASGY AAWTL AAXRX AAZKR ABCQN ABCUV ABEML ABJNI ABLJU ABPVW ABQWH ABXGK ACAHQ ACBWZ ACCFJ ACCZN ACGFS ACGOF ACMXC ACPOU ACPRK ACSCC ACXBN ACXQS ADBBV ADBTR ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZCM ADZMN AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFEBI AFFNX AFFPM AFGKR AFPWT AFZJQ AHBTC AHEFC AIACR AITYG AIURR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMXJE BROTX BRXPI BSCLL BY8 C45 CAG COF CS3 CWXXS D-E D-F DC6 DCZOG DPXWK DR2 DRFUL DRMAN DRSTM DU5 EBD EBS EJD F00 F01 F04 F5P FEDTE FUBAC FZ0 G-S G.N GODZA H.T H.X HF~ HGLYW HVGLF HZI HZ~ IHE IX1 J0M K48 KBYEO LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRMAN MRSTM MSFUL MSMAN MSSTM MXFUL MXMAN MXSTM N04 N05 N9A NF~ O66 O9- OIG OVD P2P P2W P2X P4D PALCI Q.N Q11 QB0 R.K RIWAO RJQFR ROL RX1 SAMSI SUPJJ TEORI UB1 W8V W99 WBKPD WBNRW WIH WIJ WIK WOHZO WPGGZ WQJ WRC WXSBR XG1 YFH ZGI ZZTAW ~IA ~WT AAHQN AAIPD AAMNL AANHP AAYCA ACRPL ACYXJ ADNMO AFWVQ ALVPJ AAYXX AEYWJ AGHNM AGQPQ AGYGG CITATION AAMMB AEFGJ AGXDD AIDQK AIDYY CGR CUY CVF ECM EIF NPM 7X8 |
| ID | FETCH-LOGICAL-c3635-b501b6a75526a56d3209b48e4f0684bf9325736d4ca63291e6adf3afd82b95453 |
| IEDL.DBID | DR2 |
| ISSN | 0022-3484 1600-0765 |
| IngestDate | Thu Jul 10 19:31:27 EDT 2025 Mon Jul 21 06:09:12 EDT 2025 Tue Jul 01 04:30:52 EDT 2025 Thu Apr 24 22:59:51 EDT 2025 Wed Jan 22 16:23:13 EST 2025 Wed Oct 30 10:00:50 EDT 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 3 |
| Language | English |
| License | http://onlinelibrary.wiley.com/termsAndConditions#vor 2012 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c3635-b501b6a75526a56d3209b48e4f0684bf9325736d4ca63291e6adf3afd82b95453 |
| Notes | ark:/67375/WNG-DWF0WKXM-N Figure S1. For identification of protein spots of whole saliva a pool of 400 μg protein was separated by 2-DE and stained with coomassie brilliant blue.Figure S2. Subject ordered standard deviation of spot volumes of the 2-DIGE experiment.Figure S3. Subject ordered standard deviation of protein intensities of the LC-MS/MS experiment.Table S1. MALDI protein identification_n106.xlsx.Table S2. LC-MS protein identification list with corresponding proteins.Table S3. Pearson correlation coefficient (R2) of protein intensities.Table S4. Table of analysis of variance (ANOVA) values of the gel-based and gel-free approaches. Federal Ministry of Education and Research and the Ministry of Cultural Affairs of the Federal State of Mecklenburg-West Pomerania - No. 03IS2061A istex:C378D764D48447D013D539B1A1FF7A101AA8CC43 ArticleID:JRE12025 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| PMID | 23164135 |
| PQID | 1345514894 |
| PQPubID | 23479 |
| PageCount | 12 |
| ParticipantIDs | proquest_miscellaneous_1345514894 pubmed_primary_23164135 crossref_citationtrail_10_1111_jre_12025 crossref_primary_10_1111_jre_12025 wiley_primary_10_1111_jre_12025_JRE12025 istex_primary_ark_67375_WNG_DWF0WKXM_N |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2013-06 June 2013 2013-06-00 2013-Jun 20130601 |
| PublicationDateYYYYMMDD | 2013-06-01 |
| PublicationDate_xml | – month: 06 year: 2013 text: 2013-06 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Journal of periodontal research |
| PublicationTitleAlternate | J Periodontal Res |
| PublicationYear | 2013 |
| Publisher | Blackwell Publishing Ltd |
| Publisher_xml | – name: Blackwell Publishing Ltd |
| References | Hu S, Arellano M, Boontheung P et al. Salivary proteomics for oral cancer biomarker discovery. Clin Cancer Res 2008;14:6246-6252. Hochberg Y, Benjamini Y. More powerful procedures for multiple significance testing. Stat Med 1990;9:811-818. Krief G, Deutsch O, Gariba S, Zaks B, Aframian DJ, Palmon A. Improved visualization of low abundance oral fluid proteins after triple depletion of alpha amylase, albumin and IgG. Oral Dis 2011;17:45-52. Haigh BJ, Stewart KW, Whelan JR, Barnett MP, Smolenski GA, Wheeler TT. Alterations in the salivary proteome associated with periodontitis. J Clin Periodontol 2010;37:241-247. Ghafouri B, Tagesson C, Lindahl M. Mapping of proteins in human saliva using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics 2003;3:1003-1015. Afkarian M, Bhasin M, Dillon ST et al. Optimizing a proteomics platform for urine biomarker discovery. Mol Cell Proteomics 2010;9:2195-2204. Quintana M, Palicki O, Lucchi G et al. Inter-individual variability of protein patterns in saliva of healthy adults. J Proteomics 2009;72:822-830. Punyadeera C, Dimeski G, Kostner K, Beyerlein P, Cooper-White J. One-step homogeneous C-reactive protein assay for saliva. J Immunol Methods 2011;373:19-25. Neyraud E, Palicki O, Schwartz C, Nicklaus S, Feron G. Variability of human saliva composition: Possible relationships with fat perception and liking. Arch Oral Biol 2012;57:556-566. Gusman H, Leone C, Helmerhorst EJ et al. Human salivary gland-specific daily variations in histatin concentrations determined by a novel quantitation technique. Arch Oral Biol 2004;49:11-22. Spielmann N, Wong D. Saliva: diagnostics and therapeutic perspectives. Oral Dis 2011;17:345-354. Hammer E, Bien S, Salazar MG et al. Proteomic analysis of doxorubicin-induced changes in the proteome of HepG2cells combining 2-D DIGE and LC-MS/MS approaches. Proteomics 2010;10:99-114. Bandhakavi S, Van RS, Tawfik PN et al. Hexapeptide libraries for enhanced protein PTM identification and relative abundance profiling in whole human saliva. J Proteome Res 2011;10:1052-1061. Ruhl S. The scientific exploration of saliva in the post-proteomic era: from database back to basic function. Expert Rev Proteomics 2012;9:85-96. R_Development_Core_Team. R: A language and environment for statistical computing, R Development Core Team. Vienna: R Foundation for Statistical Computing, 2008. Hardt M, Witkowska HE, Webb S et al. Assessing the effects of diurnal variation on the composition of human parotid saliva: quantitative analysis of native peptides using iTRAQ reagents. Anal Chem 2005;77:4947-4954. Pfaffe T, Cooper-White J, Beyerlein P, Kostner K, Punyadeera C. Diagnostic potential of saliva: current state and future applications. Clin Chem 2011;57:675-687. Guo T, Rudnick PA, Wang W, Lee CS, Devoe DL, Balgley BM. Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS. J Proteome Res 2006;5:1469-1478. Schulz BL, Cooper-White J, Punyadeera CK. Saliva proteome research: current status and future outlook. Crit Rev Biotechnol 2012; ??: ??-??. Xiao H, Zhang L, Zhou H, Lee JM, Garon EB, Wong DTW. Proteomic analysis of human saliva from lung cancer patients using two-dimensional difference gel electrophoresis and mass spectrometry. Mol Cell Proteomics 2012; 11: M111.012112. Neyraud E, Sayd T, Morzel M, Dransfield E. Proteomic analysis of human whole and parotid salivas following stimulation by different tastes. J Proteome Res 2006;5:2474-2480. Bandhakavi S, Stone MD, Onsongo G, Van RS, Griffin TJ. A dynamic range compression and three-dimensional peptide fractionation analysis platform expands proteome coverage and the diagnostic potential of whole saliva. J Proteome Res 2009;8:5590-5600. Thiele T, Steil L, Gebhard S et al. Profiling of alterations in platelet proteins during storage of platelet concentrates. Transfusion 2007;47:1221-1233. Helmerhorst EJ, Oppenheim FG. Saliva: a dynamic proteome. J Dent Res 2007;86:680-693. Castagnola M, Picciotti PM, Messana I et al. Potential applications of human saliva as diagnostic fluid. Acta Otorhinolaryngol Ital 2011;31:347-357. Eymann C, Dreisbach A, Albrecht D et al. A comprehensive proteome map of growing Bacillus subtilis cells. Proteomics 2004;4:2849-2876. Dowling P, Wormald R, Meleady P, Henry M, Curran A, Clynes M. Analysis of the saliva proteome from patients with head and neck squamous cell carcinoma reveals differences in abundance levels of proteins associated with tumour progression and metastasis. J Proteomics 2008;71:168-175. Rao PV, Reddy AP, Lu X et al. Proteomic identification of salivary biomarkers of type-2 diabetes. J Proteome Res 2009;8:239-245. Hu S, Loo JA, Wong DT. Human saliva proteome analysis. Ann N Y Acad Sci 2007;1098:323-329. Giusti L, Baldini C, Bazzichi L et al. Proteome analysis of whole saliva: a new tool for rheumatic diseases-the example of Sjogren's syndrome. Proteomics 2007;7:1634-1643. Esser D, Alvarez-Llamas G, de VM, Weening D, Vonk RJ, Roelofsen H. Sample stability and protein composition of saliva: implications for its use as a diagnostic fluid. Biomark Insights 2008;3:25-27. Millea KM, Krull IS, Chakraborty AB, Gebler JC, Berger SJ. Comparative profiling of human saliva by intact protein LC/ESI-TOF mass spectrometry. Biochim Biophys Acta 2007;1774:897-906. Xie H, Onsongo G, Popko J et al. Proteomics analysis of cells in whole saliva from oral cancer patients via value-added three-dimensional peptide fractionation and tandem mass spectrometry. Mol Cell Proteomics 2008;7:486-498. Goncalves LR, Soares MR, Nogueira FC et al. Comparative proteomic analysis of whole saliva from chronic periodontitis patients. J Proteomics 2010;73:1334-1341. Steil L, Thiele T, Hammer E et al. Proteomic characterization of freeze-dried human plasma: providing treatment of bleeding disorders without the need for a cold chain. Transfusion 2008;48:2356-2363. Morales-Bozo I, Urztua-Orellana B, Dominguez P, Aguilera S, Lopez-Solis R. Patterns and variability in electrophoretic polypeptide profiles of human saliva in a healthy population. J Physiol Biochem 2006;62:179-188. Karanam NK, Grabarczyk P, Hammer E et al. Proteome analysis reveals new mechanisms of Bcl11b-loss driven apoptosis. J Proteome Res 2010;9:3799-3811. Lopez ME, Colloca ME, Paez RG, Schallmach JN, Koss MA, Chervonagura A. Salivary characteristics of diabetic children. Braz Dent J 2003;14:26-31. Messana I, Cabras T, Inzitari R et al. Characterization of the human salivary basic proline-rich protein complex by a proteomic approach. J Proteome Res 2004;3:792-800. Nagaraj N, Mann M. Quantitative analysis of the intra- and inter-individual variability of the normal urinary proteome. J Proteome Res 2011;10:637-645. Walz A, Stuhler K, Wattenberg A et al. Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis. Proteomics 2006;6:1631-1639. Topkas E, Keith P, Dimeski G, Cooper-White J, Punyadeera C. Evaluation of saliva collection devices for the analysis of proteins. Clin Chim Acta 2012;413:1066-1070. Hu S, Loo JA, Wong DT. Human saliva proteome analysis and disease biomarker discovery. Expert Rev Proteomics 2007;4:531-538. 2010; 10 2010; 37 2004; 49 2011; 31 2008; 14 2004; 4 2003; 14 2008 2004; 3 2006; 5 2008; 7 2006; 6 2011; 10 2011; 57 2008; 3 2011; 17 2012; 57 2008; 71 2012; 11 2012; ?? 2011; 373 2006; 62 2007; 1774 2009; 72 2007; 1098 2003; 3 2008; 48 2007; 7 2009; 8 2007; 4 2007; 86 2012; 413 1990; 9 2005; 77 2010; 73 2007; 47 2010; 9 2012; 9 e_1_2_7_6_1 e_1_2_7_5_1 e_1_2_7_4_1 e_1_2_7_9_1 e_1_2_7_8_1 e_1_2_7_7_1 e_1_2_7_19_1 e_1_2_7_18_1 e_1_2_7_17_1 e_1_2_7_16_1 e_1_2_7_40_1 e_1_2_7_2_1 e_1_2_7_15_1 e_1_2_7_41_1 e_1_2_7_14_1 e_1_2_7_42_1 e_1_2_7_13_1 e_1_2_7_43_1 e_1_2_7_12_1 e_1_2_7_44_1 e_1_2_7_11_1 e_1_2_7_10_1 e_1_2_7_26_1 e_1_2_7_27_1 e_1_2_7_29_1 R_Development_Core_Team (e_1_2_7_37_1) 2008 Schulz BL (e_1_2_7_28_1) 2012 e_1_2_7_30_1 e_1_2_7_25_1 e_1_2_7_31_1 e_1_2_7_24_1 e_1_2_7_32_1 e_1_2_7_23_1 e_1_2_7_33_1 e_1_2_7_22_1 e_1_2_7_34_1 e_1_2_7_21_1 e_1_2_7_35_1 e_1_2_7_20_1 e_1_2_7_36_1 e_1_2_7_38_1 e_1_2_7_39_1 Castagnola M (e_1_2_7_3_1) 2011; 31 |
| References_xml | – reference: Giusti L, Baldini C, Bazzichi L et al. Proteome analysis of whole saliva: a new tool for rheumatic diseases-the example of Sjogren's syndrome. Proteomics 2007;7:1634-1643. – reference: Topkas E, Keith P, Dimeski G, Cooper-White J, Punyadeera C. Evaluation of saliva collection devices for the analysis of proteins. Clin Chim Acta 2012;413:1066-1070. – reference: Dowling P, Wormald R, Meleady P, Henry M, Curran A, Clynes M. Analysis of the saliva proteome from patients with head and neck squamous cell carcinoma reveals differences in abundance levels of proteins associated with tumour progression and metastasis. J Proteomics 2008;71:168-175. – reference: Millea KM, Krull IS, Chakraborty AB, Gebler JC, Berger SJ. Comparative profiling of human saliva by intact protein LC/ESI-TOF mass spectrometry. Biochim Biophys Acta 2007;1774:897-906. – reference: Goncalves LR, Soares MR, Nogueira FC et al. Comparative proteomic analysis of whole saliva from chronic periodontitis patients. J Proteomics 2010;73:1334-1341. – reference: Xie H, Onsongo G, Popko J et al. Proteomics analysis of cells in whole saliva from oral cancer patients via value-added three-dimensional peptide fractionation and tandem mass spectrometry. Mol Cell Proteomics 2008;7:486-498. – reference: Morales-Bozo I, Urztua-Orellana B, Dominguez P, Aguilera S, Lopez-Solis R. Patterns and variability in electrophoretic polypeptide profiles of human saliva in a healthy population. J Physiol Biochem 2006;62:179-188. – reference: R_Development_Core_Team. R: A language and environment for statistical computing, R Development Core Team. Vienna: R Foundation for Statistical Computing, 2008. – reference: Xiao H, Zhang L, Zhou H, Lee JM, Garon EB, Wong DTW. Proteomic analysis of human saliva from lung cancer patients using two-dimensional difference gel electrophoresis and mass spectrometry. Mol Cell Proteomics 2012; 11: M111.012112. – reference: Krief G, Deutsch O, Gariba S, Zaks B, Aframian DJ, Palmon A. Improved visualization of low abundance oral fluid proteins after triple depletion of alpha amylase, albumin and IgG. Oral Dis 2011;17:45-52. – reference: Haigh BJ, Stewart KW, Whelan JR, Barnett MP, Smolenski GA, Wheeler TT. Alterations in the salivary proteome associated with periodontitis. J Clin Periodontol 2010;37:241-247. – reference: Thiele T, Steil L, Gebhard S et al. Profiling of alterations in platelet proteins during storage of platelet concentrates. Transfusion 2007;47:1221-1233. – reference: Guo T, Rudnick PA, Wang W, Lee CS, Devoe DL, Balgley BM. Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS. J Proteome Res 2006;5:1469-1478. – reference: Messana I, Cabras T, Inzitari R et al. Characterization of the human salivary basic proline-rich protein complex by a proteomic approach. J Proteome Res 2004;3:792-800. – reference: Quintana M, Palicki O, Lucchi G et al. Inter-individual variability of protein patterns in saliva of healthy adults. J Proteomics 2009;72:822-830. – reference: Hu S, Loo JA, Wong DT. Human saliva proteome analysis. Ann N Y Acad Sci 2007;1098:323-329. – reference: Hardt M, Witkowska HE, Webb S et al. Assessing the effects of diurnal variation on the composition of human parotid saliva: quantitative analysis of native peptides using iTRAQ reagents. Anal Chem 2005;77:4947-4954. – reference: Ruhl S. The scientific exploration of saliva in the post-proteomic era: from database back to basic function. Expert Rev Proteomics 2012;9:85-96. – reference: Steil L, Thiele T, Hammer E et al. Proteomic characterization of freeze-dried human plasma: providing treatment of bleeding disorders without the need for a cold chain. Transfusion 2008;48:2356-2363. – reference: Rao PV, Reddy AP, Lu X et al. Proteomic identification of salivary biomarkers of type-2 diabetes. J Proteome Res 2009;8:239-245. – reference: Nagaraj N, Mann M. Quantitative analysis of the intra- and inter-individual variability of the normal urinary proteome. J Proteome Res 2011;10:637-645. – reference: Walz A, Stuhler K, Wattenberg A et al. Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis. Proteomics 2006;6:1631-1639. – reference: Hu S, Arellano M, Boontheung P et al. Salivary proteomics for oral cancer biomarker discovery. Clin Cancer Res 2008;14:6246-6252. – reference: Schulz BL, Cooper-White J, Punyadeera CK. Saliva proteome research: current status and future outlook. Crit Rev Biotechnol 2012; ??: ??-??. – reference: Hammer E, Bien S, Salazar MG et al. Proteomic analysis of doxorubicin-induced changes in the proteome of HepG2cells combining 2-D DIGE and LC-MS/MS approaches. Proteomics 2010;10:99-114. – reference: Neyraud E, Palicki O, Schwartz C, Nicklaus S, Feron G. Variability of human saliva composition: Possible relationships with fat perception and liking. Arch Oral Biol 2012;57:556-566. – reference: Esser D, Alvarez-Llamas G, de VM, Weening D, Vonk RJ, Roelofsen H. Sample stability and protein composition of saliva: implications for its use as a diagnostic fluid. Biomark Insights 2008;3:25-27. – reference: Neyraud E, Sayd T, Morzel M, Dransfield E. Proteomic analysis of human whole and parotid salivas following stimulation by different tastes. J Proteome Res 2006;5:2474-2480. – reference: Ghafouri B, Tagesson C, Lindahl M. Mapping of proteins in human saliva using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics 2003;3:1003-1015. – reference: Afkarian M, Bhasin M, Dillon ST et al. Optimizing a proteomics platform for urine biomarker discovery. Mol Cell Proteomics 2010;9:2195-2204. – reference: Hu S, Loo JA, Wong DT. Human saliva proteome analysis and disease biomarker discovery. Expert Rev Proteomics 2007;4:531-538. – reference: Helmerhorst EJ, Oppenheim FG. Saliva: a dynamic proteome. J Dent Res 2007;86:680-693. – reference: Pfaffe T, Cooper-White J, Beyerlein P, Kostner K, Punyadeera C. Diagnostic potential of saliva: current state and future applications. Clin Chem 2011;57:675-687. – reference: Lopez ME, Colloca ME, Paez RG, Schallmach JN, Koss MA, Chervonagura A. Salivary characteristics of diabetic children. Braz Dent J 2003;14:26-31. – reference: Karanam NK, Grabarczyk P, Hammer E et al. Proteome analysis reveals new mechanisms of Bcl11b-loss driven apoptosis. J Proteome Res 2010;9:3799-3811. – reference: Gusman H, Leone C, Helmerhorst EJ et al. Human salivary gland-specific daily variations in histatin concentrations determined by a novel quantitation technique. Arch Oral Biol 2004;49:11-22. – reference: Spielmann N, Wong D. Saliva: diagnostics and therapeutic perspectives. Oral Dis 2011;17:345-354. – reference: Eymann C, Dreisbach A, Albrecht D et al. A comprehensive proteome map of growing Bacillus subtilis cells. Proteomics 2004;4:2849-2876. – reference: Bandhakavi S, Van RS, Tawfik PN et al. Hexapeptide libraries for enhanced protein PTM identification and relative abundance profiling in whole human saliva. J Proteome Res 2011;10:1052-1061. – reference: Hochberg Y, Benjamini Y. More powerful procedures for multiple significance testing. Stat Med 1990;9:811-818. – reference: Castagnola M, Picciotti PM, Messana I et al. Potential applications of human saliva as diagnostic fluid. Acta Otorhinolaryngol Ital 2011;31:347-357. – reference: Punyadeera C, Dimeski G, Kostner K, Beyerlein P, Cooper-White J. One-step homogeneous C-reactive protein assay for saliva. J Immunol Methods 2011;373:19-25. – reference: Bandhakavi S, Stone MD, Onsongo G, Van RS, Griffin TJ. A dynamic range compression and three-dimensional peptide fractionation analysis platform expands proteome coverage and the diagnostic potential of whole saliva. J Proteome Res 2009;8:5590-5600. – volume: 11 start-page: M111.012112 year: 2012 article-title: Proteomic analysis of human saliva from lung cancer patients using two‐dimensional difference gel electrophoresis and mass spectrometry publication-title: Mol Cell Proteomics – volume: 72 start-page: 822 year: 2009 end-page: 830 article-title: Inter‐individual variability of protein patterns in saliva of healthy adults publication-title: J Proteomics – volume: 14 start-page: 26 year: 2003 end-page: 31 article-title: Salivary characteristics of diabetic children publication-title: Braz Dent J – volume: 14 start-page: 6246 year: 2008 end-page: 6252 article-title: Salivary proteomics for oral cancer biomarker discovery publication-title: Clin Cancer Res – volume: 413 start-page: 1066 year: 2012 end-page: 1070 article-title: Evaluation of saliva collection devices for the analysis of proteins publication-title: Clin Chim Acta – volume: 9 start-page: 811 year: 1990 end-page: 818 article-title: More powerful procedures for multiple significance testing publication-title: Stat Med – volume: ?? start-page: ?? year: 2012 end-page: ?? article-title: Saliva proteome research: current status and future outlook publication-title: Crit Rev Biotechnol – volume: 62 start-page: 179 year: 2006 end-page: 188 article-title: Patterns and variability in electrophoretic polypeptide profiles of human saliva in a healthy population publication-title: J Physiol Biochem – volume: 1098 start-page: 323 year: 2007 end-page: 329 article-title: Human saliva proteome analysis publication-title: Ann N Y Acad Sci – volume: 31 start-page: 347 year: 2011 end-page: 357 article-title: Potential applications of human saliva as diagnostic fluid publication-title: Acta Otorhinolaryngol Ital – volume: 3 start-page: 25 year: 2008 end-page: 27 article-title: Sample stability and protein composition of saliva: implications for its use as a diagnostic fluid publication-title: Biomark Insights – volume: 17 start-page: 45 year: 2011 end-page: 52 article-title: Improved visualization of low abundance oral fluid proteins after triple depletion of alpha amylase, albumin and IgG publication-title: Oral Dis – volume: 37 start-page: 241 year: 2010 end-page: 247 article-title: Alterations in the salivary proteome associated with periodontitis publication-title: J Clin Periodontol – volume: 8 start-page: 239 year: 2009 end-page: 245 article-title: Proteomic identification of salivary biomarkers of type‐2 diabetes publication-title: J Proteome Res – volume: 57 start-page: 675 year: 2011 end-page: 687 article-title: Diagnostic potential of saliva: current state and future applications publication-title: Clin Chem – volume: 48 start-page: 2356 year: 2008 end-page: 2363 article-title: Proteomic characterization of freeze‐dried human plasma: providing treatment of bleeding disorders without the need for a cold chain publication-title: Transfusion – volume: 4 start-page: 2849 year: 2004 end-page: 2876 article-title: A comprehensive proteome map of growing Bacillus subtilis cells publication-title: Proteomics – volume: 9 start-page: 3799 year: 2010 end-page: 3811 article-title: Proteome analysis reveals new mechanisms of Bcl11b‐loss driven apoptosis publication-title: J Proteome Res – volume: 10 start-page: 1052 year: 2011 end-page: 1061 article-title: Hexapeptide libraries for enhanced protein PTM identification and relative abundance profiling in whole human saliva publication-title: J Proteome Res – volume: 373 start-page: 19 year: 2011 end-page: 25 article-title: One‐step homogeneous C‐reactive protein assay for saliva publication-title: J Immunol Methods – volume: 57 start-page: 556 year: 2012 end-page: 566 article-title: Variability of human saliva composition: Possible relationships with fat perception and liking publication-title: Arch Oral Biol – volume: 8 start-page: 5590 year: 2009 end-page: 5600 article-title: A dynamic range compression and three‐dimensional peptide fractionation analysis platform expands proteome coverage and the diagnostic potential of whole saliva publication-title: J Proteome Res – volume: 77 start-page: 4947 year: 2005 end-page: 4954 article-title: Assessing the effects of diurnal variation on the composition of human parotid saliva: quantitative analysis of native peptides using iTRAQ reagents publication-title: Anal Chem – volume: 73 start-page: 1334 year: 2010 end-page: 1341 article-title: Comparative proteomic analysis of whole saliva from chronic periodontitis patients publication-title: J Proteomics – volume: 17 start-page: 345 year: 2011 end-page: 354 article-title: Saliva: diagnostics and therapeutic perspectives publication-title: Oral Dis – volume: 49 start-page: 11 year: 2004 end-page: 22 article-title: Human salivary gland‐specific daily variations in histatin concentrations determined by a novel quantitation technique publication-title: Arch Oral Biol – volume: 7 start-page: 1634 year: 2007 end-page: 1643 article-title: Proteome analysis of whole saliva: a new tool for rheumatic diseases–the example of Sjogren's syndrome publication-title: Proteomics – volume: 5 start-page: 1469 year: 2006 end-page: 1478 article-title: Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed‐phase liquid chromatography coupled with ESI‐tandem MS publication-title: J Proteome Res – volume: 9 start-page: 2195 year: 2010 end-page: 2204 article-title: Optimizing a proteomics platform for urine biomarker discovery publication-title: Mol Cell Proteomics – volume: 10 start-page: 637 year: 2011 end-page: 645 article-title: Quantitative analysis of the intra‐ and inter‐individual variability of the normal urinary proteome publication-title: J Proteome Res – volume: 1774 start-page: 897 year: 2007 end-page: 906 article-title: Comparative profiling of human saliva by intact protein LC/ESI‐TOF mass spectrometry publication-title: Biochim Biophys Acta – volume: 3 start-page: 792 year: 2004 end-page: 800 article-title: Characterization of the human salivary basic proline‐rich protein complex by a proteomic approach publication-title: J Proteome Res – volume: 5 start-page: 2474 year: 2006 end-page: 2480 article-title: Proteomic analysis of human whole and parotid salivas following stimulation by different tastes publication-title: J Proteome Res – volume: 10 start-page: 99 year: 2010 end-page: 114 article-title: Proteomic analysis of doxorubicin‐induced changes in the proteome of HepG2cells combining 2‐D DIGE and LC‐MS/MS approaches publication-title: Proteomics – volume: 71 start-page: 168 year: 2008 end-page: 175 article-title: Analysis of the saliva proteome from patients with head and neck squamous cell carcinoma reveals differences in abundance levels of proteins associated with tumour progression and metastasis publication-title: J Proteomics – year: 2008 – volume: 7 start-page: 486 year: 2008 end-page: 498 article-title: Proteomics analysis of cells in whole saliva from oral cancer patients via value‐added three‐dimensional peptide fractionation and tandem mass spectrometry publication-title: Mol Cell Proteomics – volume: 86 start-page: 680 year: 2007 end-page: 693 article-title: Saliva: a dynamic proteome publication-title: J Dent Res – volume: 4 start-page: 531 year: 2007 end-page: 538 article-title: Human saliva proteome analysis and disease biomarker discovery publication-title: Expert Rev Proteomics – volume: 9 start-page: 85 year: 2012 end-page: 96 article-title: The scientific exploration of saliva in the post‐proteomic era: from database back to basic function publication-title: Expert Rev Proteomics – volume: 47 start-page: 1221 year: 2007 end-page: 1233 article-title: Profiling of alterations in platelet proteins during storage of platelet concentrates publication-title: Transfusion – volume: 3 start-page: 1003 year: 2003 end-page: 1015 article-title: Mapping of proteins in human saliva using two‐dimensional gel electrophoresis and peptide mass fingerprinting publication-title: Proteomics – volume: 6 start-page: 1631 year: 2006 end-page: 1639 article-title: Proteome analysis of glandular parotid and submandibular‐sublingual saliva in comparison to whole human saliva by two‐dimensional gel electrophoresis publication-title: Proteomics – ident: e_1_2_7_11_1 doi: 10.1021/pr8003776 – ident: e_1_2_7_25_1 doi: 10.1177/154405910708600802 – ident: e_1_2_7_35_1 doi: 10.1002/pmic.200400907 – ident: e_1_2_7_16_1 doi: 10.1002/pmic.200500125 – ident: e_1_2_7_34_1 doi: 10.1002/sim.4780090710 – volume-title: R: A language and environment for statistical computing, R Development Core Team year: 2008 ident: e_1_2_7_37_1 – ident: e_1_2_7_8_1 doi: 10.1373/clinchem.2010.153767 – ident: e_1_2_7_13_1 doi: 10.1016/j.jprot.2008.04.004 – ident: e_1_2_7_32_1 doi: 10.1111/j.1537-2995.2007.01255.x – ident: e_1_2_7_27_1 doi: 10.1016/j.jprot.2009.05.004 – ident: e_1_2_7_10_1 doi: 10.1590/S0103-64402003000100005 – ident: e_1_2_7_24_1 doi: 10.1021/pr900675w – start-page: ?? year: 2012 ident: e_1_2_7_28_1 article-title: Saliva proteome research: current status and future outlook publication-title: Crit Rev Biotechnol – ident: e_1_2_7_19_1 doi: 10.1111/j.1601-0825.2010.01700.x – ident: e_1_2_7_2_1 doi: 10.1111/j.1601-0825.2010.01773.x – ident: e_1_2_7_18_1 doi: 10.1586/epr.11.80 – ident: e_1_2_7_30_1 doi: 10.1074/mcp.M110.000992 – volume: 31 start-page: 347 year: 2011 ident: e_1_2_7_3_1 article-title: Potential applications of human saliva as diagnostic fluid publication-title: Acta Otorhinolaryngol Ital – ident: e_1_2_7_15_1 doi: 10.1074/mcp.M111.012112 – ident: e_1_2_7_26_1 doi: 10.4137/BMI.S607 – ident: e_1_2_7_6_1 doi: 10.1016/j.jprot.2010.02.018 – ident: e_1_2_7_23_1 doi: 10.1074/mcp.M700146-MCP200 – ident: e_1_2_7_14_1 doi: 10.1158/1078-0432.CCR-07-5037 – ident: e_1_2_7_43_1 doi: 10.1021/pr060189z – ident: e_1_2_7_31_1 doi: 10.1002/pmic.200800626 – ident: e_1_2_7_33_1 doi: 10.1111/j.1537-2995.2008.01856.x – ident: e_1_2_7_40_1 doi: 10.1021/pr049953c – ident: e_1_2_7_36_1 doi: 10.1021/pr901096u – ident: e_1_2_7_44_1 doi: 10.1016/j.archoralbio.2011.09.016 – ident: e_1_2_7_41_1 doi: 10.1016/j.bbapap.2007.04.017 – ident: e_1_2_7_4_1 doi: 10.1586/14789450.4.4.531 – ident: e_1_2_7_20_1 doi: 10.1021/ac050161r – ident: e_1_2_7_7_1 doi: 10.1196/annals.1384.015 – ident: e_1_2_7_42_1 doi: 10.1007/BF03168467 – ident: e_1_2_7_5_1 doi: 10.1016/j.jim.2011.07.013 – ident: e_1_2_7_21_1 doi: 10.1002/pmic.200300426 – ident: e_1_2_7_38_1 doi: 10.1021/pr100835s – ident: e_1_2_7_22_1 doi: 10.1021/pr060065m – ident: e_1_2_7_29_1 doi: 10.1016/j.cca.2012.02.020 – ident: e_1_2_7_9_1 doi: 10.1002/pmic.200600783 – ident: e_1_2_7_12_1 doi: 10.1111/j.1600-051X.2009.01525.x – ident: e_1_2_7_17_1 doi: 10.1021/pr100857t – ident: e_1_2_7_39_1 doi: 10.1016/S0003-9969(03)00182-1 |
| SSID | ssj0002679 |
| Score | 2.1971729 |
| Snippet | Background and Objective
Interest in human saliva is increasing for disease‐specific biomarker discovery studies. However, protein composition of whole saliva... Interest in human saliva is increasing for disease-specific biomarker discovery studies. However, protein composition of whole saliva can grossly vary with... |
| SourceID | proquest pubmed crossref wiley istex |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 392 |
| SubjectTerms | 2-D DIGE Adult Analysis of Variance Electrophoresis, Gel, Two-Dimensional Evaluation Studies as Topic Female Gene Expression Profiling Genetic Variation Humans intra- and inter-subject variability LC-MS/MS Male Middle Aged proteome Proteomics - methods Salivary Proteins and Peptides - analysis Salivary Proteins and Peptides - genetics Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Statistics, Nonparametric whole saliva |
| Title | Quantitative analysis of the intra- and inter-subject variability of the whole salivary proteome |
| URI | https://api.istex.fr/ark:/67375/WNG-DWF0WKXM-N/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fjre.12025 https://www.ncbi.nlm.nih.gov/pubmed/23164135 https://www.proquest.com/docview/1345514894 |
| Volume | 48 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3NbtQwEB5V5QCXllIKWygyFap6ySo_jpOIE6LdVkVdiarV7qGSZSe2hArZKrsplBOPwDPyJMw4P7SoSKi3WJkkjmfG_myPvwF4g0NIYJPQeAhGY49bazydptwzIuEWhxelHX3x8VgcnvGjaTxdgrfdWZiGH6JfcCPPcP01ObjS85tOXplhgFN3OmBOsVoEiE7-UEeFIsl6pnCe8pZVyEXxdE_eGoseULN-uwto3satbuAZrcJ5V-Um3uRiWC_0MP_-F5vjPf_pMay0gJS9ayxoDZZM-QQe7lEQEeWBW4fiY61KdxQNO0amWhITNrMMsSP7RIvDv378xBsFFUyFhXmtaXmHXeFEvOEBv-7kv1I-XjZXtANVXTNHEzH7Yp7C2Wj_9P2h1-Zm8PIIMYqnYz_QQqGCQ6FiUUShn2meGm59kXJtERbGSSQKnisRoT0YoQobKVukoc4QtUUbsFzOSvMcGGKGnHKPBhkaScozYijMbZAkOs8Rv9oB7HZaknlLXE75Mz7LfgJTGemabQDbvehlw9Zxl9COU3UvoaoLCm9LYjkZH8i9yciffJgey_EAXne2INHpaCdFlWZWz2UQcUKaacYH8Kwxkv5tCJgFIgP8zK5T9b8rIo9O9t3F5v-LvoBHYZOQw_ODl7C8qGqzhbBooV85-_8NR08IoA |
| linkProvider | Wiley-Blackwell |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6V9lAuvCnL0yCEeskqD8dJJC6Idlna7kpUrXYvyLITW0Kl2Sq7AcqJn8Bv5Jcw4zygqEiIW6xMEsczY3-2x98APMchJLBJaDwEo7HHrTWeTlPuGZFwi8OL0o6-eDIV42O-N4_na_CyOwvT8EP0C27kGa6_JgenBenfvbwywwDn7vEV2KCM3m5CdfiLPCoUSdZzhfOUt7xCLo6ne_TCaLRBDfvlMqh5Ebm6oWd0Hd53lW4iTk6G9UoP869_8Dn-71_dgGstJmWvGiO6CWumvAWbOxRHRKngbkPxrlalO42GfSNTLY8JW1iG8JF9oPXhH9--442CCqbCwrLWtMLDPuFcvKECP-_kP1NKXrZUtAlVnTPHFLE4NXfgeLR79HrstekZvDxCmOLp2A-0UKjjUKhYFFHoZ5qnhltfpFxbRIZxEomC50pEaBJGqMJGyhZpqDMEbtFdWC8XpbkHDGFDTulHgwztJOUZkRTmNkgSnecIYe0Atjs1ybzlLqcUGh9lP4epjHTNNoBnvehZQ9hxmdALp-teQlUnFOGWxHI2fSN3ZiN_tj-fyOkAnnbGINHvaDNFlWZRL2UQcQKbacYHsNVYSf82xMwCwQF-Ztvp-u8VkXuHu-7i_r-LPoHN8dHkQB68ne4_gKthk5_D84OHsL6qavMIUdJKP3bO8BO_Nwy7 |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VVgIuQIGWhUINQqiXrPJwHEc9IbZLnyuoqHYPlSw7sSVUyFbZDVBO_IT-Rn5Jx84DiopU9RYrk8TxzNif7fE3AK9xCAlMEmoPwWjsUWO0pzinnmYJNTi8SOXoiw9GbPuI7k7iyQJstmdhan6IbsHNeobrr62Dn-bmbycvdT_AqXt8C5Yo87k16cHhH-6okCVpRxVOOW1ohVwYT_vopcFoybbrj6uQ5mXg6kae4X04butcB5yc9Ku56mc__6FzvOFPPYB7DSIlb2sTWoYFXTyEOwMbRWQTwT2C_GMlC3cWDXtGIhsWEzI1BMEj-WxXh3__OscbuS3oEguzStn1HfINZ-I1EfhZK__dJuQlM2m3oMoz4ngipl_1Yzgabn16t-01yRm8LEKQ4qnYDxSTqOGQyZjlUeininJNjc84VQZxYZxELKeZZBEahGYyN5E0OQ9VirAtWoHFYlroJ0AQNGQ2-WiQopVwmlqKwswESaKyDAGs6cFGqyWRNczlNoHGF9HNYEotXLP14FUnelrTdVwl9MapupOQ5YmNb0tiMR69F4Px0B_vTQ7EqAcvW1sQ6HV2K0UWelrNRBBRCzV5SnuwWhtJ9zZEzAyhAX5mw6n6_xURu4db7uLp9UXX4faHwVDs74z2nsHdsE7O4fnBGizOy0o_R4g0Vy-cK1wAsfwLcw |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Quantitative+analysis+of+the+intra-+and+inter-subject+variability+of+the+whole+salivary+proteome&rft.jtitle=Journal+of+periodontal+research&rft.au=Jehmlich%2C+N.&rft.au=Dinh%2C+K.+H.+D.&rft.au=Gesell-Salazar%2C+M.&rft.au=Hammer%2C+E.&rft.date=2013-06-01&rft.pub=Blackwell+Publishing+Ltd&rft.issn=0022-3484&rft.eissn=1600-0765&rft.volume=48&rft.issue=3&rft.spage=392&rft.epage=403&rft_id=info:doi/10.1111%2Fjre.12025&rft.externalDBID=n%2Fa&rft.externalDocID=ark_67375_WNG_DWF0WKXM_N |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-3484&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-3484&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-3484&client=summon |