About: Agnès Rötig

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

French biologist (1959-)

Attributes	Values
rdf:type	Item
description	গবেষক (bn) ഗവേഷക (ml) հետազոտող (hy) onderzoeker (nl) hulumtuese (sq) French biologist (1959-) (en) biologa francese (1959-) (it)
rdfs:label	Agnès Rötig (de) Agnès Rötig (en) Agnès Rötig (es) Agnès Rötig (fr) Agnès Rötig (it) Agnès Rötig (nl) Agnès Rötig (pt) Agnès Rötig (sl) Agnès Rötig (pt-br) Agnès Rötig (ast)
skos:prefLabel	Agnès Rötig (de) Agnès Rötig (en) Agnès Rötig (es) Agnès Rötig (fr) Agnès Rötig (it) Agnès Rötig (nl) Agnès Rötig (pt) Agnès Rötig (sl) Agnès Rötig (pt-br) Agnès Rötig (ast)
name	Agnès Rötig (de) Agnès Rötig (en) Agnès Rötig (es) Agnès Rötig (fr) Agnès Rötig (it) Agnès Rötig (nl) Agnès Rötig (pt) Agnès Rötig (sl) Agnès Rötig (pt-br) Agnès Rötig (ast)
given name	wds:Q28354286-2E7A15B2-B313-4C51-8718-0D02C71AB91C
given name	Agnès
instance of	wds:Q28354286-A6FAFFAF-7AEC-4EA0-9C24-2D1005157A76
instance of	Homo sapiens
skos:altLabel	Agnes Rotig (en) Agnes Rotig (nl) Agnes Rotig (ast)
occupation	wds:Q28354286-CA81673C-2150-4BE4-AF7A-F86DBFF3FF88
employer	wds:Q28354286-2FC9999C-33A6-40AF-91B7-420DFEFC4B4E
languages spoken, written or signed	wds:q28354286-6f486749-449a-6248-ad11-7bb237fa2bb4 wds:q28354286-ac2ca75c-4837-cbad-08fd-e6099a3a733e
sex or gender	wds:Q28354286-5C4115C8-0307-4808-80B7-257C6D735E85
ISNI	wds:Q28354286-BF6FC089-8A33-47DC-ABA0-15F73435CF25
VIAF ID	wds:Q28354286-F2D2E701-D89F-41BE-A5DA-9710A564D804
Bibliothèque nationale de France ID	wds:q28354286-ca871005-4e96-46cc-090e-6f26ee5c0c31
IdRef ID	wds:Q28354286-516260B3-BFB1-4F12-966D-32FAF8C8D90C
country of citizenship	wds:q28354286-82d91434-42f3-4637-98ce-8ddc3f3e48a3
date of birth	wds:Q28354286-74F841E1-492E-490F-878C-4133AC139F8A
educated at	wds:Q28354286-83E892D7-32E6-47B1-A737-BC801A633AD9
family name	wds:q28354286-0db1ec5f-42ba-9da8-02bf-e3e0f1ca904f
WorldCat Identities ID (superseded)	wds:Q28354286-BB95B130-0CA2-4C8F-AC4C-0DA5A816765F
VIAF ID	http://viaf.org/viaf/229691583
Bibliothèque nationale de France ID	http://data.bnf.fr/ark:/12148/cb12409173s#about
IdRef ID	http://www.idref.fr/033201218/id
occupation	biologist
employer	French National Institute of Health and Medical Research
languages spoken, written or signed	French English
sex or gender	female organism
ISNI	0000000366832283
VIAF ID	229691583
Bibliothèque nationale de France ID	12409173s
IdRef ID	033201218
country of citizenship	France
date of birth	1959-01-01 00:00:00Z (xsd:dateTime)
educated at	French National Institute of Health and Medical Research
family name	Rötig
WorldCat Identities ID (superseded)	viaf-229691583
ORCID iD	wds:Q28354286-6177B176-1C32-4F06-9CE5-43303C8C190E
Dimensions author ID	wds:Q28354286-EBF3DD70-B437-42C5-A80A-971CF171B225
ORCID iD	https://orcid.org/0000-0003-0589-0703
ORCID iD	0000-0003-0589-0703
Dimensions author ID	0600037635.42
ResearcherID	wds:Q28354286-60821AD5-FF55-425E-B37B-B9F4665BAA96
ResearcherID	G-9592-2017
is owl:sameAs of	Agnès Rötig
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28354286
is author of	Mutations in C12orf62, a factor that couples COX I synthesis with cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy Acute infantile liver failure due to mutations in the TRMU gene. Cell complementation using Genebridge 4 human:rodent hybrids for physical mapping of novel mitochondrial respiratory chain deficiency genes. Mouse models for mitochondrial diseases. Variable outcome of growth hormone administration in respiratory chain deficiency Mutations in Complex I Assembly Factor TMEM126B Result in Muscle Weakness and Isolated Complex I Deficiency Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia. A mutant mitochondrial respiratory chain assembly protein causes complex III deficiency in patients with tubulopathy, encephalopathy and liver failure. 1H MRS spectroscopy evidence of cerebellar high lactate in mitochondrial respiratory chain deficiency. Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders Selective iron chelation in Friedreich ataxia: biologic and clinical implications. Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study New evidence of a mitochondrial genetic background paradox: impact of the J haplogroup on the A3243G mutation

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