About: Olivier Berteau

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

researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) onderzoeker (nl) biochimiste français (fr)
exact match	wds:Q39062184-7A7C8225-F03E-474A-A992-EFBC5B5DB517
exact match	https://scigraph.springernature.com/person.0655525676.45
rdfs:label	Olivier Berteau (en) Olivier Berteau (es) Olivier Berteau (fr) Olivier Berteau (it) Olivier Berteau (nl) Olivier Berteau (sl) Olivier Berteau (ast)
skos:prefLabel	Olivier Berteau (en) Olivier Berteau (es) Olivier Berteau (fr) Olivier Berteau (it) Olivier Berteau (nl) Olivier Berteau (sl) Olivier Berteau (ast)
name	Olivier Berteau (en) Olivier Berteau (es) Olivier Berteau (fr) Olivier Berteau (it) Olivier Berteau (nl) Olivier Berteau (sl) Olivier Berteau (ast)
Scopus author ID	wds:Q39062184-6C927672-733C-49D3-A28F-A306D320B257
Scopus author ID	56347467500
given name	wds:Q39062184-27B16537-F12E-4519-9693-FA5C1547092B
given name	Olivier
instance of	wds:Q39062184-255521AA-2490-4F23-B239-0B07C4AB2542
instance of	Homo sapiens
Loop ID	wds:Q39062184-05538927-F876-4E87-8059-2B260D59A1CE
Loop ID	393264
occupation	wds:Q39062184-72D1D343-4D8F-4912-A43E-25FA9FD292A0
employer	wds:Q39062184-B89C7510-67ED-4380-8881-447C257DD33A
sex or gender	wds:Q39062184-3C8F7A97-33CD-40F2-A1B4-98D3538AAE42
ISNI	wds:Q39062184-688A041C-F54F-49AA-B113-4E51A075760C
VIAF ID	wds:Q39062184-7B4619AD-85F3-43C6-8D18-60A7C6B94F86
IdRef ID	wds:Q39062184-3D176833-B3FA-4B2E-9EBB-0CEA6119E6B9
country of citizenship	wds:Q39062184-20382e36-4705-2975-3f2d-21ec9dd5302e
date of birth	wds:Q39062184-E5A155F8-A1E1-4145-B96D-59B88E122B5C
educated at	wds:Q39062184-9d5ca5fb-4def-125c-f169-175426c6f933
family name	wds:Q39062184-96ebf0e0-4729-45f5-0547-a3689e82261a
VIAF ID	http://viaf.org/viaf/204789572
IdRef ID	http://www.idref.fr/077259718/id
occupation	researcher
employer	National Institute for Agricultural Research
sex or gender	male
ISNI	0000000358224798
VIAF ID	204789572
IdRef ID	077259718
country of citizenship	France
date of birth	1973-01-01 00:00:00Z (xsd:dateTime)
educated at	Université Sorbonne Paris Nord
family name	Berteau
ORCID iD	wds:Q39062184-2D48B0C4-60D3-4BFD-AD04-47251AF12E3D
Dimensions author ID	wds:Q39062184-AE4A719B-0BAF-45CB-A6FF-AAD3B4221E44
ORCID iD	https://orcid.org/0000-0002-3434-5168
ORCID iD	0000-0002-3434-5168
Dimensions author ID	0655525676.45
ResearcherID	wds:Q39062184-19D42B41-593D-467A-AF6F-9A547AC44A84
ResearcherID	AAF-9080-2019
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q39062184 https://fr.wikipedia.org/wiki/Olivier_Berteau
is author of	Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate Mechanistic investigations of anaerobic sulfatase-maturating enzyme: direct Cbeta H-atom abstraction catalyzed by a radical AdoMet enzyme Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes Anaerobic Sulfatase-Maturating Enzymes: Radical SAM Enzymes Able To Catalyze in Vitro Sulfatase Post-translational Modification An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily A metagenomic β-glucuronidase uncovers a core adaptive function of the human intestinal microbiome. The spore photoproduct lyase repairs the 5S- and not the 5R-configured spore photoproduct DNA lesion Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes. Sulfatases and a radical S-adenosyl-L-methionine (AdoMet) enzyme are key for mucosal foraging and fitness of the prominent human gut symbiont, Bacteroides thetaiotaomicron. Dinucleotide spore photoproduct, a minimal substrate of the DNA repair spore photoproduct lyase enzyme from Bacillus subtilis A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes Anaerobic sulfatase-maturating enzyme--a mechanistic link with glycyl radical-activating enzymes? Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR. DNA repair and free radicals, new insights into the mechanism of spore photoproduct lyase revealed by single amino acid substitution Characterization of glycosaminoglycan (GAG) sulfatases from the human gut symbiont Bacteroides thetaiotaomicron reveals the first GAG-specific bacterial endosulfatase Sulfatases and radical SAM enzymes: emerging themes in glycosaminoglycan metabolism and the human microbiota Insights into the catalysis of a lysine-tryptophan bond in bacterial peptides by a SPASM domain radical S-adenosylmethionine (SAM) peptide cyclase DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From Biochemistry to Structural Investigations The B12-Radical SAM Enzyme PoyC Catalyzes Valine Cβ-Methylation during Polytheonamide Biosynthesis Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs).

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