<div class="csl-bib-body">
<div class="csl-entry">Conibear, A. C. (2024, June 3). <i>Deciphering the impact of phosphorylation on the structure and chaperoning of Heat Shock Protein 90</i> [Conference Presentation]. 9th Chemical Protein Synthesis Conference, Nagoya, Japan.</div>
</div>
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/207444
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dc.description.abstract
Human heat shock protein 90 (Hsp90) is a molecular chaperone important for the folding, stabilization and quality control of many important client proteins.1 Its role as a hub at the intersection of several fundamental cellular pathways makes it a therapeutic target for pathologies such as neurological disease, cancer and protein folding disorders.2 Hsp90 is also posttranslationally modified at many sites,3 however the structural and functional role of these modifications, individually and in combination, are poorly resolved. Here we use expressed protein selenoester ligation4, 5 to access site-specifically phosphorylated variants of the Hsp90 C-terminal domain, which forms the dimerization interface of the Hsp90 homodimer. The phosphorylations caused only minor conformational changes in the intrinsically-disordered C-terminus, but modulated the chaperone activity. We also extended the semi-synthesis strategy towards Hsp90 variants with modifications in the middle domains. Access to site-specifically modified variants of this large and challenging protein will allow us to elucidate the roles of the posttranslational modifications systematically and investigate their impacts on various client proteins and therapeutics.
en
dc.description.sponsorship
FWF - Österr. Wissenschaftsfonds
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dc.language.iso
en
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dc.subject
phosphorylation
en
dc.subject
posttranslational modifications
en
dc.subject
protein semi-synthesis
en
dc.subject
chaperones
en
dc.subject
heat shock protein 90
en
dc.title
Deciphering the impact of phosphorylation on the structure and chaperoning of Heat Shock Protein 90
en
dc.type
Presentation
en
dc.type
Vortrag
de
dc.relation.grantno
P 36101-B
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dc.type.category
Conference Presentation
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tuw.publication.invited
invited
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tuw.project.title
Posttranslationale Modifikation von HMGN1 in DNA-Verpackung
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tuw.researchTopic.id
M6
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tuw.researchTopic.id
M8
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tuw.researchTopic.name
Biological and Bioactive Materials
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tuw.researchTopic.name
Structure-Property Relationsship
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tuw.researchTopic.value
70
-
tuw.researchTopic.value
30
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tuw.publication.orgunit
E163-03-2 - Forschungsgruppe Molekulare Chemie und Chemische Biologie
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tuw.author.orcid
0000-0002-5482-6225
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tuw.event.name
9th Chemical Protein Synthesis Conference
en
tuw.event.startdate
02-06-2024
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tuw.event.enddate
05-06-2024
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tuw.event.online
On Site
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tuw.event.type
Event for scientific audience
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tuw.event.place
Nagoya
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tuw.event.country
JP
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tuw.event.presenter
Conibear, Anne Claire
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tuw.event.track
Single Track
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wb.sciencebranch
Chemie
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wb.sciencebranch
Chemische Verfahrenstechnik
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wb.sciencebranch
Pharmazie, Pharmakologie, Toxikologie
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wb.sciencebranch.oefos
1040
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wb.sciencebranch.oefos
2040
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wb.sciencebranch.oefos
3012
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wb.sciencebranch.value
60
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wb.sciencebranch.value
20
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wb.sciencebranch.value
20
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item.languageiso639-1
en
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item.openairetype
conference paper not in proceedings
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item.grantfulltext
none
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item.fulltext
no Fulltext
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item.cerifentitytype
Publications
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item.openairecristype
http://purl.org/coar/resource_type/c_18cp
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crisitem.author.dept
E163-03-2 - Forschungsgruppe Molekulare Chemie und Chemische Biologie
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crisitem.author.orcid
0000-0002-5482-6225
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crisitem.author.parentorg
E163-03 - Forschungsbereich Organische und Biologische Chemie
