About: Manon Couture

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

researcher and university professor

Attributes	Values
rdf:type	Item
field of work	wds:Q41083485-c940ba34-4849-9fee-d637-756d7d884c82
field of work	microbiology
description	wetenschapper (nl) дослідник (uk) հետազոտող (hy) researcher and university professor (en) chercheuse et professeure d'université (fr)
rdfs:label	Manon Couture (en) Manon Couture (es) Manon Couture (fr) Manon Couture (nl) Manon Couture (sl) Manon Couture (ast)
skos:prefLabel	Manon Couture (en) Manon Couture (es) Manon Couture (fr) Manon Couture (nl) Manon Couture (sl) Manon Couture (ast)
name	Manon Couture (en) Manon Couture (es) Manon Couture (fr) Manon Couture (nl) Manon Couture (sl) Manon Couture (ast)
LinkedIn personal profile ID	wds:Q41083485-9f787d70-4f13-aa27-5510-a973eb63a2d4
LinkedIn personal profile ID	manon-couture-4b83893b
Scopus author ID	wds:Q41083485-A19DD6CE-5DCD-4D78-BA27-69E711FAB60F
Scopus author ID	7006417950
given name	wds:Q41083485-B109FA63-9DE6-40E8-8CC9-3866CF317EAF
given name	Manon
instance of	wds:Q41083485-288FAC28-C9B8-4CF4-9D69-2809ED7E8FBE
instance of	Homo sapiens
ResearchGate profile ID	wds:Q41083485-25e95d44-4dab-b2f1-a229-d0aa6b1b2c21
ResearchGate profile ID	Manon_Couture
occupation	wds:Q41083485-8146b905-4f6d-03a5-6255-242a4dfc84b6
employer	wds:Q41083485-C6A5218E-E167-4AA3-B2C5-EAB2BFCECD4C
sex or gender	wds:Q41083485-3C7B7F37-B43B-4FB3-BA9D-B16FDF6297EE
VIAF ID	wds:Q41083485-124f9863-4c88-833c-0ce2-c5a8006c97ea
country of citizenship	wds:Q41083485-73283f06-4da7-a8a6-2eb4-9a1bbeb63a64
date of birth	wds:Q41083485-5F673257-464E-4F29-B0CD-61D94353175E
educated at	wds:Q41083485-98efdbd3-4783-e216-cd79-a62228b57351
family name	wds:Q41083485-EDE99BF0-9986-498C-BE46-17A3BA619DEF
WorldCat Identities ID (superseded)	wds:Q41083485-7eee1795-4648-0549-180a-218fd5228a0e
VIAF ID	http://viaf.org/viaf/7331163335753703270001
occupation	university teacher
employer	Laval University
sex or gender	female organism
VIAF ID	7331163335753703270001
country of citizenship	Malawi
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
educated at	Laval University
family name	Couture
WorldCat Identities ID (superseded)	viaf-7331163335753703270001
ORCID iD	wds:Q41083485-80686005-461A-40E6-B817-3A0EF09E6121
ORCID iD	https://orcid.org/0000-0001-8296-8055
ORCID iD	0000-0001-8296-8055
ResearcherID	wds:Q41083485-8FE53666-7853-474C-99A6-09304BFF7C58
Publons author ID	wds:Q41083485-ef16c512-e14b-4bff-a48f-db3a49b04ce3
ResearcherID	F-8326-2015
Publons author ID	2404750
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q41083485
is author of	Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function Trp180 of endothelial NOS and Trp56 of bacterial saNOS modulate sigma bonding of the axial cysteine to the heme. The Heme Environment of Mouse Neuroglobin The roles of Tyr(CD1) and Trp(G8) in Mycobacterium tuberculosis truncated hemoglobin O in ligand binding and on the heme distal site architecture Peroxidase activity and involvement in the oxidative stress response of roseobacter denitrificans truncated hemoglobin Identification of the Ligands to the Ferric Heme ofChlamydomonasChloroplast Hemoglobin: Evidence for Ligation of Tyrosine-63 (B10) to the Heme† Simultaneous observation of the O—O and Fe—O2 stretching modes in oxyhemoglobins A weak Fe-O bond in the oxygenated complex of the nitric-oxide synthase of Staphylococcus aureus. The Conserved Trp–Cys Hydrogen Bond Dampens the “Push Effect” of the Heme Cysteinate Proximal Ligand during the First Catalytic Cycle of Nitric Oxide Synthase Substrate-specific Interactions with the Heme-bound Oxygen Molecule of Nitric-oxide Synthase The Ferrous Dioxygen Complex of the Oxygenase Domain of Neuronal Nitric-oxide Synthase Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues A Cooperative Oxygen Binding Hemoglobin fromMycobacterium tuberculosis Ligand-protein interactions in nitric oxide synthase. Flavoenzyme CrmK-mediated substrate recycling in caerulomycin biosynthesis Synthesis of β-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases An alternative reaction for heme degradation catalyzed by the Escherichia coli O157:H7 ChuS protein: Release of hematinic acid, tripyrrole and Fe(III). Cytochrome b5 from Giardia lamblia. Interactions between substrates and the haem-bound nitric oxide of ferric and ferrous bacterial nitric oxide synthases Kinetic studies of HPr, HPr(H15D), HPr(H15E), and HPr(His approximately P) phosphorylation by the Streptococcus salivarius HPr(Ser) kinase/phosphorylase. Synthesis of HPr(Ser-P)(His∼P) by Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System ofStreptococcussalivarius†
is author of	wds:Q35556614-0EAFE1A2-2DCC-4D99-8459-4C2C6452C2D1 wds:Q59421127-19BF5434-F18D-44D4-B901-7D5DDA1B7F7D wds:Q62026439-5C2AC9BE-5F8E-4366-9465-B7F36F630A01 wds:Q42700056-4BC45055-A692-4438-8AF7-AC4E167BD927 wds:Q41083444-5009012C-553C-468E-A65C-23DFE9422619 wds:Q34610144-88551A5D-FF08-45CF-B9AA-4B9A299AF30B wds:Q44196484-8301BFE9-3F53-47FC-A2DC-7B2B80FD8D15 wds:Q45962075-D30B5878-607E-445D-96B0-61ACA4944CB4 wds:Q54323485-254F7B1E-EDD3-4588-872C-F5F4766041C3 wds:Q62026433-C2090614-106A-47D7-892E-9662DE76D5E3 wds:Q27648409-0ADFBF14-C21A-4009-A9F5-F9AF29838146 wds:Q62026427-035E1DBC-DF83-49DF-93A0-C514D9D1E46F wds:Q62026432-AB602BF0-2933-4645-B70F-8BF569E413A9 wds:Q62026442-0993DC0A-190F-41A1-BBF9-CC5929DFEF5D

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