About: Peter Tessarz

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher (ORCID 0000-0002-6953-9835)

Attributes	Values
rdf:type	Item
description	研究者 (ja) onderzoeker (nl) researcher (ORCID 0000-0002-6953-9835) (en)
rdfs:label	Peter Tessarz (en) Peter Tessarz (nl)
skos:prefLabel	Peter Tessarz (en) Peter Tessarz (nl)
name	Peter Tessarz (en) Peter Tessarz (nl)
given name	wds:Q92475972-57EA0E7D-C559-4A46-B098-30DB14C95406
given name	Peter
instance of	wds:Q92475972-BB97263F-2CE0-4929-A67B-DD187A1C24B4
instance of	Homo sapiens
occupation	wds:Q92475972-E86D76DE-26AF-4B40-BC13-7B81832A9287
employer	wds:Q92475972-1687690B-F2D1-4393-8B0E-B81EC2F01D90 wds:Q92475972-36DBECEB-085D-4410-9C7A-6DE49FE4B2D1 wds:Q92475972-8C125F40-2D8C-40DC-A9D2-5ED3E1C7FCC1
sex or gender	wds:Q92475972-2867931D-D13A-4F04-BF27-384222E8ABC2
VIAF ID	wds:Q92475972-91141365-b713-416e-9331-290add40b177
GND ID	wds:Q92475972-ab6dc148-abc3-4e8d-825e-4285b59b728d
educated at	wds:Q92475972-A174920E-5C59-4FAA-BAC5-B0A88E866798
VIAF ID	http://viaf.org/viaf/55370776
GND ID	https://d-nb.info/gnd/135703662
occupation	researcher
employer	Gurdon Institute Max Planck Institute for Biology of Ageing
sex or gender	male
VIAF ID	55370776
GND ID	135703662
educated at	Universität Heidelberg Zentrum für Molekulare Biologie
ORCID iD	wds:Q92475972-C1A4C1E9-FC47-47D3-AEE0-9CA4B93AAB08
Dimensions author ID	wds:Q92475972-98A9E64E-F561-4947-BDF4-7F1C2EF79A24
ORCID iD	https://orcid.org/0000-0002-6953-9835
ORCID iD	0000-0002-6953-9835
Dimensions author ID	0736630606.42
ResearcherID	wds:Q92475972-0188B1A0-CF7A-4ABC-BA07-1506091F86E7
ResearcherID	I-9035-2014
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q92475972
is author of	Common and specific mechanisms of AAA+ proteins involved in protein quality control Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation Substrate recognition by the AAA+ chaperone ClpB. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Novel insights into the mechanism of chaperone-assisted protein disaggregation The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins Ageing and sources of transcriptional heterogeneity Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis NET-prism enables RNA polymerase-dedicated transcriptional interrogation at nucleotide resolution Transcriptional repression by FACT is linked to regulation of chromatin accessibility at the promoter of ES cells The impact of genomic variation on protein phosphorylation states and regulatory networks The RNA-binding protein Puf5 contributes to buffering of mRNA upon chromatin-mediated changes in nascent transcription Long-lived macrophage reprogramming drives spike protein-mediated inflammasome activation in COVID-19 Histone N-terminal acetyltransferase NAA40 links one-carbon metabolism to chemoresistance
is author of	wds:Q43578585-BD8D3030-D160-40CB-B7F0-27D01BA9712E wds:Q92876957-2B94C6D8-B601-47E2-9DAD-1CD284AD8E9A wds:Q112304528-77F6AAB6-E994-4F2E-8BD6-36AB4944BC72 wds:Q112641636-EDD79CD3-2352-4397-BE6C-304049CB8C1C wds:Q112644397-551E182A-279A-4E8B-9583-378757405DB1 wds:Q44945731-3E648B8B-D909-4C1E-8F6E-C0C2AFF75573 wds:Q112718417-16DF57EB-B350-41AB-8A31-B3F72F3B15A0 wds:Q37061511-D2D4FA05-4F29-4B87-9623-AF096818D504 wds:Q36275416-28EEB7FC-FE66-4D93-89BB-FF8C241585BC wds:Q112640967-3521541E-00E2-4413-A0BA-DA4CD011BB0F wds:Q93229409-740B5254-FEE6-41EB-B4A6-A49E9A5B04CE wds:Q41349152-5DA91AA0-7B1B-4140-90BD-1DF64D8F6AA8 wds:Q92475975-0773DFC4-11EC-41C8-BBAE-9B1B02E5E23D wds:Q34369100-C3309BA4-7B12-44A4-8796-06D3CE247AF1

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