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dc.contributor.authorKrasny, L
dc.contributor.authorHuang, PH
dc.coverage.spatialEnglanden_US
dc.date.accessioned2021-11-25T13:02:23Z
dc.date.available2021-11-25T13:02:23Z
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/34676799en_US
dc.identifier.citationExpert Rev Proteomics, 2021, 18 (9), pp. 781 - 794en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4896
dc.identifier.eissn1744-8387en_US
dc.identifier.eissn1744-8387
dc.identifier.doi10.1080/14789450.2021.1984885en_US
dc.identifier.doi10.1080/14789450.2021.1984885
dc.description.abstractINTRODUCTION: The matrisome and adhesome comprise proteins that are found within or are associated with the extracellular matrix (ECM) and adhesion complexes, respectively. Interactions between cells and their microenvironment are mediated by key matrisome and adhesome proteins, which direct fundamental processes, including growth and development. Due to their underlying complexity, it has historically been challenging to undertake mass spectrometry (MS)-based profiling of these proteins. New developments in sample preparative workflows, informatics databases, and MS techniques have enabled in-depth proteomic characterization of the matrisome and adhesome, resulting in a comprehensive understanding of the interactomes, and cellular signaling that occur at the cell-ECM interface. AREA COVERED: This review summarizes recent advances in proteomic characterization of the matrisome and adhesome. It focuses on the importance of curated databases and discusses key strengths and limitations of different workflows. EXPERT OPINION: MS-based proteomics has shown promise in characterizing the matrisome and topology of adhesome networks in health and disease. Moving forward, it will be important to incorporate integrative analysis to define the bidirectional signaling between the matrisome and adhesome, and adopt new methods for post-translational modification and in vivo analyses to better dissect the critical roles that these proteins play in human pathophysiology.en_US
dc.format.extent781 - 794en_US
dc.languageengen_US
dc.language.isoengen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.subjectProteomicsen_US
dc.subjectadhesomeen_US
dc.subjectextracellular matrixen_US
dc.subjectintegrinsen_US
dc.subjectmass spectrometryen_US
dc.subjectmatrisomeen_US
dc.titleAdvances in the proteomic profiling of the matrisome and adhesome.en_US
dc.typeJournal Article
dcterms.dateAccepted2021-09-21
rioxxterms.versionVoRen_US
rioxxterms.versionofrecord10.1080/14789450.2021.1984885en_US
dc.relation.isPartOfExpert Rev Proteomicsen_US
pubs.issue9en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Molecular Pathology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Molecular Pathology/Molecular and Systems Oncology
pubs.publication-statusPublisheden_US
pubs.volume18en_US
pubs.embargo.termsNot knownen_US
icr.researchteamMolecular and Systems Oncology
dc.contributor.icrauthorKrasny, Lukasen_US
dc.contributor.icrauthorHuang, Paulen_US


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