dc.contributor.author | Gentzel, M | |
dc.contributor.author | Pardo, M | |
dc.contributor.author | Subramaniam, S | |
dc.contributor.author | Stewart, AF | |
dc.contributor.author | Choudhary, JS | |
dc.date.accessioned | 2019-06-04T09:57:48Z | |
dc.date.issued | 2019-07-15 | |
dc.identifier.citation | Methods (San Diego, Calif.), 2019, 164-165 pp. 67 - 72 | |
dc.identifier.issn | 1046-2023 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/3249 | |
dc.identifier.eissn | 1095-9130 | |
dc.identifier.doi | 10.1016/j.ymeth.2019.03.028 | |
dc.description.abstract | The identification of bona fide protein-protein interactions and the mapping of proteomes was greatly enhanced by protein tagging for generic affinity purification methods and analysis by mass spectrometry (AP-MS). The high quality of AP-MS data permitted the development of proteomic navigation by sequential tagging of identified interactions. However AP-MS is laborious and limited to relatively high affinity protein-protein interactions. Proximity labeling, first with the biotin ligase BirA, termed BioID, and then with ascorbate peroxidase, termed APEX, permits a greater reach into the proteome than AP-MS enabling both the identification of a wider field and weaker protein-protein interactions. This additional reach comes with the need for stringent controls. Proximity labeling also permits experiments in living cells allowing spatiotemporal investigations of the proteome. Here we discuss proximity labeling with accompanying methodological descriptions for E. coli and mammalian cells. | |
dc.format | Print-Electronic | |
dc.format.extent | 67 - 72 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | |
dc.rights.uri | https://www.rioxx.net/licenses/under-embargo-all-rights-reserved | |
dc.subject | Cell Line | |
dc.subject | Animals | |
dc.subject | Escherichia coli | |
dc.subject | Hydrogen Peroxide | |
dc.subject | Biotin | |
dc.subject | Carbon-Nitrogen Ligases | |
dc.subject | Escherichia coli Proteins | |
dc.subject | Repressor Proteins | |
dc.subject | Staining and Labeling | |
dc.subject | Biotinylation | |
dc.subject | Protein Interaction Mapping | |
dc.subject | Proteomics | |
dc.subject | Mass Spectrometry | |
dc.subject | Ascorbate Peroxidases | |
dc.subject | Spatio-Temporal Analysis | |
dc.title | Proteomic navigation using proximity-labeling. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2019-03-29 | |
rioxxterms.versionofrecord | 10.1016/j.ymeth.2019.03.028 | |
rioxxterms.licenseref.uri | https://www.rioxx.net/licenses/under-embargo-all-rights-reserved | |
rioxxterms.licenseref.startdate | 2019-07 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Methods (San Diego, Calif.) | |
pubs.notes | Not known | |
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/Cancer Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology/Functional Proteomics Group | |
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/Cancer Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Biology/Functional Proteomics Group | |
pubs.publication-status | Published | |
pubs.volume | 164-165 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Functional Proteomics Group | |
dc.contributor.icrauthor | Pardo Calvo, Maria Mercedes | |
dc.contributor.icrauthor | Choudhary, Jyoti | |