About: Britt-Marie Sjöberg

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Britt-Marie Sjöberg Goto Sponge Distinct Permalink

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

Swedish biochemist

Attributes	Values
rdf:type	Item
description	Zweeds academicus (nl) académica sueca (ast) Swedish biochemist (en) bithcheimiceoir Sualannach (ga)
rdfs:label	Britt-Marie Sjöberg (ca) Britt-Marie Sjöberg (en) Britt-Marie Sjöberg (es) Britt-Marie Sjöberg (fi) Britt-Marie Sjöberg (fr) Britt-Marie Sjöberg (ga) Britt-Marie Sjöberg (it) Britt-Marie Sjöberg (nl) Britt-Marie Sjöberg (sl) Britt-Marie Sjöberg (sq) Britt-Marie Sjöberg (sv) Britt-Marie Sjöberg (ast)
skos:prefLabel	Britt-Marie Sjöberg (ca) Britt-Marie Sjöberg (en) Britt-Marie Sjöberg (es) Britt-Marie Sjöberg (fi) Britt-Marie Sjöberg (fr) Britt-Marie Sjöberg (ga) Britt-Marie Sjöberg (it) Britt-Marie Sjöberg (nl) Britt-Marie Sjöberg (sl) Britt-Marie Sjöberg (sq) Britt-Marie Sjöberg (sv) Britt-Marie Sjöberg (ast)
name	Britt-Marie Sjöberg (ca) Britt-Marie Sjöberg (en) Britt-Marie Sjöberg (es) Britt-Marie Sjöberg (fi) Britt-Marie Sjöberg (fr) Britt-Marie Sjöberg (ga) Britt-Marie Sjöberg (it) Britt-Marie Sjöberg (nl) Britt-Marie Sjöberg (sl) Britt-Marie Sjöberg (sq) Britt-Marie Sjöberg (sv) Britt-Marie Sjöberg (ast)
Scopus author ID	wds:Q4978874-0074d2b7-453f-d8df-32df-27d98c19e777
AE member ID	wds:Q4978874-8C6F563B-EDA4-46F3-9168-F2F70CADE789
Scopus author ID	7102349759
AE member ID	Sjöberg_Britt-Marie
given name	wds:Q4978874-298E7AEF-E240-44C0-AB79-DA0A1EF6529D
given name	Britt
instance of	wds:Q4978874-3217DC8C-2CDD-452A-85CF-B023F13FA101
instance of	Homo sapiens
occupation	wds:Q4978874-0409097e-ce82-40b7-ba12-2d5a289efab3 wds:Q4978874-533dad2a-44f8-5a8a-11c6-5faaa9be9b32
employer	wds:Q4978874-D044FA35-8362-4FC7-87CC-4CE4CFAD6A45 wds:Q4978874-D9C35FAE-EDBA-42AC-BEFA-012BA869A721 wds:Q4978874-F7994EA4-5C95-46F6-B90C-B41424ED29F6
sex or gender	wds:q4978874-FEEAEE03-2B8A-4E0E-9B53-750E82E05CAE
country of citizenship	wds:Q4978874-F31BDA3F-E331-4029-A297-CDC2CDB39416
member of	wds:Q4978874-9857CC15-8121-4DA2-B904-F2C01272B038 wds:Q4978874-DDD4021B-529E-42FE-8D1C-6AFD277C9BF5
date of birth	wds:Q4978874-DCA8BC05-E673-462E-9F39-E5A193317AD1
educated at	wds:Q4978874-11307AEB-D0B9-44AB-A2FA-AB6EF686E5B9
family name	wds:Q4978874-D255E5FD-C028-44BE-A3ED-C393B73E631F
occupation	biochemist academic
employer	Stockholm University Karolinska Institutet Swedish University of Agricultural Sciences
sex or gender	female organism
country of citizenship	Sweden
member of	Royal Swedish Academy of Sciences Academia Europaea
date of birth	1944-01-01 00:00:00Z (xsd:dateTime)
educated at	Karolinska Institutet
family name	Sjöberg
ORCID iD	wds:Q4978874-D1252B5A-7F4F-449C-B40D-6EF69E1D7CA2
Dimensions author ID	wds:Q4978874-D553C3C3-B126-4307-9EFB-926616E55065
ORCID iD	https://orcid.org/0000-0001-5953-3360
ORCID iD	0000-0001-5953-3360
Dimensions author ID	01025556763.64
is owl:sameAs of	Britt-Marie Sjöberg
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q4978874 https://sv.wikipedia.org/wiki/Britt-Marie_Sj%C3%B6berg
is author of	Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F. Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4. Cysteines Involved in Radical Generation and Catalysis of Class III Anaerobic Ribonucleotide Reductase Cysteinyl and Substrate Radical Formation in Active Site Mutant E441Q ofEscherichia coliClass I Ribonucleotide Reductase Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase Structural and mutational studies of the carboxylate cluster in iron-free ribonucleotide reductase R2. In vivo assay for low-activity mutant forms of Escherichia coli ribonucleotide reductase Preserved catalytic activity in an engineered ribonucleotide reductase R2 protein with a nonphysiological radical transfer pathway. The importance of hydrogen bond connections between the participating residues. Kinetics of transient radicals in Escherichia coli ribonucleotide reductase. Formation of a new tyrosyl radical in mutant protein R2. The conserved serine 211 is essential for reduction of the dinuclear iron center in protein R2 of Escherichia coli ribonucleotide reductase. Three-dimensional structure of the free radical protein of ribonucleotide reductase A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined x-ray diffraction and EPR/ENDOR studies Residues Important for Radical Stability in Ribonucleotide Reductase fromEscherichia coli Shift in ribonucleotide reductase gene expression in Pseudomonas aeruginosa during infection. Localization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4. Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins Trisodium Phosphonoformate, a New Antiviral Compound Identification of the stable free radical tyrosine residue in ribonucleotide reductase. Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 195 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software