About: Ronald Hay

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

molecular biologist

Attributes	Values
rdf:type	Item
description	molecular biologist (en) moleculair bioloog (nl)
rdfs:label	Ronald Hay (en) Ronald Hay (es) Ronald Hay (fr) Ronald Hay (nl) Ronald Hay (sq) Ronald Hay (ast)
skos:prefLabel	Ronald Hay (en) Ronald Hay (es) Ronald Hay (fr) Ronald Hay (nl) Ronald Hay (sq) Ronald Hay (ast)
name	Ronald Hay (en) Ronald Hay (es) Ronald Hay (fr) Ronald Hay (nl) Ronald Hay (sq) Ronald Hay (ast)
Scopus author ID	wds:Q21165834-12D369AC-5AE9-43BA-AC33-6C04BD061AA4
AE member ID	wds:Q21165834-31E537EF-7040-4E0B-AD5A-200EF3B95451
EMBO member ID	wds:Q21165834-E32DCE69-395B-420E-BB14-4B9FA649D87B
Scopus author ID	7202248496
AE member ID	Hay_Ronald_Thomas
EMBO member ID	ronald-t-hay
given name	wds:Q21165834-4EFD736C-178E-4392-863B-84455CCF5398
given name	Ronald
instance of	wds:Q21165834-ECE39E0C-D163-4403-B7D8-AA5AF8468EFD
instance of	Homo sapiens
award received	wds:Q21165834-1928fbf4-4d45-8eab-6be8-4a4ae1dafe66 wds:Q21165834-6E1167A5-DBFD-4CC9-9854-734530DF1E41 wds:Q21165834-865E1AF5-AF11-460C-AF33-37D53ED3E53D wds:Q21165834-ffb3ae69-4972-df0f-e87b-b900f97c9945
award received	Novartis Medal and Prize Fellow of the Royal Society Fellow of the Academy of Medical Sciences Fellow of the Royal Society of Edinburgh
Fellow of the Royal Society ID	wds:Q21165834-685b6cb4-4e80-c1e9-9503-69583959eb0a
Fellow of the Royal Society ID	11600
skos:altLabel	Ron Hay (en) Ronald Thomas Hay (en)
occupation	wds:Q21165834-cf002dd9-4cf1-ef01-5243-c042ebccb8f7
employer	wds:Q21165834-2436A26A-C2B6-4A6F-9436-0190CE914A5D wds:Q21165834-36B0105A-E82C-401D-8BBF-AED45E05F3A3 wds:Q21165834-7E883033-8483-4138-AF05-0FF91DF5077C wds:Q21165834-FBD4558C-74D7-402E-BBE9-3456C533F9E2
sex or gender	wds:Q21165834-BDF00D90-E933-47E9-BFE1-737AA56F69AA
member of	wds:Q21165834-1D119711-02B0-49E2-AC19-1EA2DB0BB351 wds:Q21165834-1F17847D-A363-42A9-A383-9C3945F4629F
Who's Who UK ID	wds:Q21165834-60adc4e6-418e-5e3d-8c25-6e98823b8db4
date of birth	wds:Q21165834-82AB1157-CB55-4694-911C-0E6A77961282
educated at	wds:Q21165834-61EBDFA4-621D-4B9F-94A8-0686106BE881
family name	wds:Q21165834-0878D51A-3711-462F-9D2E-D75FB631FB99
occupation	molecular biologist
employer	University of Dundee MRC-University of Glasgow Centre For Virus Research Harvard Medical School University of St Andrews
sex or gender	male
member of	Academia Europaea Royal Society
Who's Who UK ID	U255637
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
educated at	University of Glasgow
family name	Hay
ORCID iD	wds:Q21165834-b17927bc-473f-ba61-8b29-01bbf208e633
ORCID iD	https://orcid.org/0000-0001-7113-9024
ORCID iD	0000-0001-7113-9024
Gateway to Research person ID	wds:Q21165834-07B358B4-CC34-42A1-987B-729078AE5DB3
Gateway to Research person ID	ADFBB240-800A-4DB1-866A-C8772541CDF7
ResearcherID	wds:Q21165834-B64FC0D1-F9B2-4335-985C-280993C5C20B
Publons author ID	wds:Q21165834-35116891-f737-4378-bdc0-aba1a43de598
ResearcherID	F-9338-2011
Publons author ID	2777043
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q21165834
is author of	SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1 Ribosomal proteins are targets for the NEDD8 pathway Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics SUMO-1 modification of human transcription factor (TF) IID complex subunits: inhibition of TFIID promoter-binding activity through SUMO-1 modification of hsTAF5 betaTrCP-mediated proteolysis of NF-kappaB1 p105 requires phosphorylation of p105 serines 927 and 932. Recognition of the adenovirus type 2 origin of DNA replication by the virally encoded DNA polymerase and preterminal proteins System-wide changes to SUMO modifications in response to heat shock SUMO-specific proteases: a twist in the tail Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans Proteome-wide identification of SUMO2 modification sites p75-mediated NF-kappaB activation enhances the survival response of developing sensory neurons to nerve growth factor. Replication of adenovirus type 4 DNA by a Purified fraction from infected Cells Adenovirus DNA polymerase: domain organisation and interaction with preterminal protein The DNA-binding Domain of Nuclear Factor I is Sufficient to Cooperate with the Adenovirus Type 2 DNA-binding Protein in Viral DNA Replication SUMO protease SENP1 induces isomerization of the scissile peptide bond FRET-based in vitro assays for the analysis of SUMO protease activities Characterization of IκBα Nuclear Import Pathway Purification and identification of endogenous polySUMO conjugates Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers Nuclear Retention of IκBα Protects It from Signal-induced Degradation and Inhibits Nuclear Factor κB Transcriptional Activation Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH) Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62

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