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Article: Analysing Complex Oral Protein Samples: Complete Workflow and Case Analysis of Salivary Pellicles

TitleAnalysing Complex Oral Protein Samples: Complete Workflow and Case Analysis of Salivary Pellicles
Authors
Keywordsdental pellicle
mass spectrometry
protein
proteogenomic
saliva
Issue Date2021
PublisherMDPI AG. The Journal's web site is located at http://www.mdpi.com/journal/jcm
Citation
Journal of Clinical Medicine, 2021, v. 10, p. article no. 2801 How to Cite?
AbstractStudies on small quantity, highly complex protein samples, such as salivary pellicle, have been enabled by recent major technological and analytical breakthroughs. Advances in mass spectrometry-based computational proteomics such as Multidimensional Protein Identification Technology have allowed precise identification and quantification of complex protein samples on a proteome-wide scale, which has enabled the determination of corresponding genes and cellular functions at the protein level. The latter was achieved via protein-protein interaction mapping with Gene Ontology annotation. In recent years, the application of these technologies has broken various barriers in small-quantity-complex-protein research such as salivary pellicle. This review provides a concise summary of contemporary proteomic techniques contributing to (1) increased complex protein (up to hundreds) identification using minute sample sizes (µg level), (2) precise protein quantification by advanced stable isotope labelling or label-free approaches and (3) the emerging concepts and techniques regarding computational integration, such as the Gene Ontology Consortium and protein-protein interaction mapping. The latter integrates the structural, genomic, and biological context of proteins and genes to predict protein interactions and functional connections in a given biological context. The same technological breakthroughs and computational integration concepts can also be applied to other low-volume oral protein complexes such as gingival crevicular or peri-implant sulcular fluids.
Persistent Identifierhttp://hdl.handle.net/10722/300907
ISSN
2023 Impact Factor: 3.0
2023 SCImago Journal Rankings: 0.882
ISI Accession Number ID
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DC FieldValueLanguage
dc.contributor.authorWEI, C-
dc.contributor.authorBurrow, MF-
dc.contributor.authorBotelho, MG-
dc.contributor.authorLeung, WK-
dc.date.accessioned2021-07-06T03:11:52Z-
dc.date.available2021-07-06T03:11:52Z-
dc.date.issued2021-
dc.identifier.citationJournal of Clinical Medicine, 2021, v. 10, p. article no. 2801-
dc.identifier.issn2077-0383-
dc.identifier.urihttp://hdl.handle.net/10722/300907-
dc.description.abstractStudies on small quantity, highly complex protein samples, such as salivary pellicle, have been enabled by recent major technological and analytical breakthroughs. Advances in mass spectrometry-based computational proteomics such as Multidimensional Protein Identification Technology have allowed precise identification and quantification of complex protein samples on a proteome-wide scale, which has enabled the determination of corresponding genes and cellular functions at the protein level. The latter was achieved via protein-protein interaction mapping with Gene Ontology annotation. In recent years, the application of these technologies has broken various barriers in small-quantity-complex-protein research such as salivary pellicle. This review provides a concise summary of contemporary proteomic techniques contributing to (1) increased complex protein (up to hundreds) identification using minute sample sizes (µg level), (2) precise protein quantification by advanced stable isotope labelling or label-free approaches and (3) the emerging concepts and techniques regarding computational integration, such as the Gene Ontology Consortium and protein-protein interaction mapping. The latter integrates the structural, genomic, and biological context of proteins and genes to predict protein interactions and functional connections in a given biological context. The same technological breakthroughs and computational integration concepts can also be applied to other low-volume oral protein complexes such as gingival crevicular or peri-implant sulcular fluids.-
dc.languageeng-
dc.publisherMDPI AG. The Journal's web site is located at http://www.mdpi.com/journal/jcm-
dc.relation.ispartofJournal of Clinical Medicine-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectdental pellicle-
dc.subjectmass spectrometry-
dc.subjectprotein-
dc.subjectproteogenomic-
dc.subjectsaliva-
dc.titleAnalysing Complex Oral Protein Samples: Complete Workflow and Case Analysis of Salivary Pellicles-
dc.typeArticle-
dc.identifier.emailBurrow, MF: mfburr58@hku.hk-
dc.identifier.emailBotelho, MG: botelho@hkucc.hku.hk-
dc.identifier.emailLeung, WK: ewkleung@hkucc.hku.hk-
dc.identifier.authorityBurrow, MF=rp01306-
dc.identifier.authorityBotelho, MG=rp00033-
dc.identifier.authorityLeung, WK=rp00019-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3390/jcm10132801-
dc.identifier.scopuseid_2-s2.0-85114077721-
dc.identifier.hkuros323245-
dc.identifier.volume10-
dc.identifier.spagearticle no. 2801-
dc.identifier.epagearticle no. 2801-
dc.identifier.isiWOS:000671237400001-
dc.publisher.placeSwitzerland-
dc.relation.projectDental and restorative materials acquired pellicle proteomics and microbiomics: A key battle front to defense against recurrent oral disease.-

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