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http://dx.doi.org/10.25673/115074
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DC Field | Value | Language |
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dc.contributor.author | Tüting, Christian | - |
dc.contributor.author | Schmidt, Lisa | - |
dc.contributor.author | Skalidis, Ioannis | - |
dc.contributor.author | Sinz, Andrea | - |
dc.contributor.author | Kastritis, Panagiotis L. | - |
dc.date.accessioned | 2024-03-04T07:12:15Z | - |
dc.date.available | 2024-03-04T07:12:15Z | - |
dc.date.issued | 2023 | - |
dc.identifier.uri | https://opendata.uni-halle.de//handle/1981185920/117030 | - |
dc.identifier.uri | http://dx.doi.org/10.25673/115074 | - |
dc.description.abstract | Inthecellularcontext,proteinsparticipateincommunitiestoperformtheirfunction.Thedetectionandidentificationofthesecommunitiesaswellasin-communityinter-actionshaslongbeenthesubjectofinvestigation,mainlythroughproteomicsanalysiswithmassspectrometry.Withtheadventofcryogenicelectronmicroscopyandthe“resolutionrevolution,”theirvisualizationhasrecentlybeenmadepossible,evenincomplex, native samples. The advances in both fields have resulted in the genera-tionoflargeamountsofdata,whoseanalysisrequiresadvancedcomputation,oftenemployingmachinelearningapproachestoreachthedesiredoutcome.Inthiswork,wefirstperformedarobustproteomicsanalysisofmassspectrometry(MS)dataderivedfromayeastnativecellextractandusedthisinformationtoidentifyproteincommu-nitiesandinter-proteininteractions.Cryo-EManalysisofthecellextractprovidedareconstructionofabiomoleculeatmediumresolution(∼8Å(FSC=0.143)).Utiliz-ingMS-derivedproteomicsdataandsystematicfittingofAlphaFold-predictedatomicmodels, this density was assigned to the 2.6 MDa complex of yeast fatty acid syn-thase.OurproposedworkflowidentifiesproteincomplexesinnativecellextractsfromSaccharomyces cerevisiaeby combining proteomics, cryo-EM, and AI-guided proteinstructureprediction. | eng |
dc.language.iso | eng | - |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
dc.subject.ddc | 573 | - |
dc.title | Enabling cryo-EM density interpretation from yeast native cell extracts by proteomics data and AlphaFold structures | eng |
dc.type | Article | - |
local.versionType | publishedVersion | - |
local.bibliographicCitation.journaltitle | Proteomics | - |
local.bibliographicCitation.volume | 23 | - |
local.bibliographicCitation.issue | 17 | - |
local.bibliographicCitation.pagestart | 1 | - |
local.bibliographicCitation.pageend | 10 | - |
local.bibliographicCitation.publishername | Wiley VCH | - |
local.bibliographicCitation.publisherplace | Weinheim | - |
local.bibliographicCitation.doi | 10.1002/pmic.202200096 | - |
local.subject.keywords | AI-guided, computational analysis, cryo-EM, homogenates, protein structure prediction, structural proteomics | - |
local.openaccess | true | - |
dc.identifier.ppn | 1847498116 | - |
cbs.publication.displayform | 2023 | - |
local.bibliographicCitation.year | 2023 | - |
cbs.sru.importDate | 2024-03-04T07:11:41Z | - |
local.bibliographicCitation | Enthalten in Proteomics - Weinheim : Wiley VCH, 2001 | - |
local.accessrights.dnb | free | - |
Appears in Collections: | Open Access Publikationen der MLU |
Files in This Item:
File | Description | Size | Format | |
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Proteomics - 2023 - Tüting - Enabling cryo‐EM density interpretation from yeast native cell extracts by proteomics data and.pdf | 1.96 MB | Adobe PDF | View/Open |