about
Parasite Glycobiology: A Bittersweet SymphonyStructural Insight into the Unique Substrate Binding Mechanism and Flavin Redox State of UDP-galactopyranose Mutase from Aspergillus fumigatusDepletion of UDP-Glucose and UDP-Galactose Using a Degron System Leads to Growth Cessation of Leishmania majorLeishmania UDP-sugar pyrophosphorylase: the missing link in galactose salvage?Deletion of UDP-glucose pyrophosphorylase reveals a UDP-glucose independent UDP-galactose salvage pathway in Leishmania majorLeishmania major UDP-sugar pyrophosphorylase salvages galactose for glycoconjugate biosynthesisLeishmania adleri, a lizard parasite, expresses structurally similar glycoinositolphospholipids to mammalian Leishmania.Galactofuranose in eukaryotes: aspects of biosynthesis and functional impact.The glycosylation pattern of humanized IgGI antibody (D1.3) expressed in CHO cells.A CMP-sialic acid transporter cloned from Arabidopsis thaliana.Molecular cloning of two Arabidopsis UDP-galactose transporters by complementation of a deficient Chinese hamster ovary cell line.Aspergillus fumigatus Cap59-like protein A is involved in α1,3-mannosylation of GPI-anchors.Identification, biochemical characterization, and in-vivo expression of the intracellular invertase BfrA from the pathogenic parasite Leishmania major.A single UDP-galactofuranose transporter is required for galactofuranosylation in Aspergillus fumigatus.Biosynthesis of the fungal cell wall polysaccharide galactomannan requires intraluminal GDP-mannose.Farnesol misplaces tip-localized Rho proteins and inhibits cell wall integrity signalling in Aspergillus fumigatus.Functional expression of the CMP-sialic acid transporter in Escherichia coli and its identification as a simple mobile carrier.Identification and partial characterization of two eukaryotic UDP-galactopyranose mutases.Toward an understanding of the biogenesis of the starch granule. Evidence that Chlamydomonas soluble starch synthase II controls the synthesis of intermediate size glucans of amylopectin.Apicomplexan C-Mannosyltransferases Modify Thrombospondin Type I-Containing Adhesins of the TRAP Family.The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major.Characterization of the Elongating α-d-Mannosyl Phosphate Transferase from Three Species ofLeishmaniaUsing Synthetic Acceptor Substrate Analogues†The preparation of neoglycoconjugates containing inter-saccharide phosphodiester linkages as potential anti-Leishmania vaccinesDirect investigation of the Aspergillus GDP-mannose transporter by STD NMR spectroscopy-Fucosylation of thrombospondin-like repeats is required for processing of microneme protein 2 and for efficient host cell invasion by tachyzoitesIdentification of UDP-Sugar Pyrophosphorylase Inhibitors Using Biosensor-Based Small Molecule Fragment Library ScreeningTargeted gene deletion of Leishmania major UDP-galactopyranose mutase leads to attenuated virulenceChemical characterisation of glycosylinositolphospholipids of Herpetomonas samuelpessoaiStructures of four oligosaccharides derived from the glycoinositolphospholipid of Leishmania adleri1H NMR analysis of novel sialylated and fucosylated lactose-based oligosaccharides having linear GlcNAc(beta 1-6) Gal and Neu5Ac(alpha 2-6) GlcNAc sequencesStudies on galactofuranose-containing glycostructures of the pathogenic mold Aspergillus fumigatusCharacterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesisMembrane Topological Model of Glycosyltransferases of the GT-C SuperfamilyGlycobiology of Human Fungal Pathogens: New Avenues for Drug DevelopmentProtein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparumC-Mannosylation of Toxoplasma gondii proteins promotes attachment to host cells and parasite virulence
P50
Q26777350-67651A45-D0D5-4885-8B13-C8C1C59E4E51Q27677273-DD061EBF-B2F5-43E6-A336-88E947CA2A10Q28550611-72E19E3B-4178-45F1-B455-95927CD91583Q33569844-0958AFF6-63A6-49DB-A65B-7646893DDA0FQ33979086-F24E7211-CFB6-4DA0-A9E9-509D576E1707Q36488276-B502DFD6-C033-4FCC-AC5B-B01BD401985DQ36875952-88F268BD-1413-40E6-B3CA-28387F7C702AQ37937329-8DF837AC-EF2D-4F9E-AB79-CCB38B3F520AQ38348746-556ED8AD-02B3-476A-BE95-29851E661CEBQ40015495-8731795E-0FB8-4316-871F-7E17A9B0A8FEQ40509458-B7B8651F-D4D0-4FC4-A384-F4357FBF09BAQ40540301-E41D4380-ECAA-4322-AE3A-0DEC357D684DQ40636917-986EF91E-A3D7-49D7-AE12-D6A58A7BA4AEQ41945725-E33FEACF-1EE0-41BA-8354-C5D2A17D1319Q42431094-D9CAEAE4-9417-4A06-8E84-3E697DB1A811Q43096472-AA20F5C0-0066-4D1C-A8C7-1C19EA6B23CAQ46665925-9824C48A-8973-47C1-BA61-AE2D0031EB6AQ46737594-59B5B7BE-C149-4A90-B44E-626AE55A4147Q47389489-FC9F1F0D-A8B0-4477-A32F-282FEE45FBD8Q50061912-03F11AE2-7412-4B43-A822-7F7D2B690C7BQ50456518-D9C1A513-80D7-4D7B-B252-70F79D443EE5Q58867219-0AE8A91F-52D9-4EE1-95DD-4945F77D94CBQ58867223-60A6A94A-9CB4-461D-AF18-6C1DAE06F784Q61594281-6ACF78E1-5233-4C0E-9442-D1F1EFB0EFE2Q63362965-C23B85E5-CCBE-4D61-AC9F-6F7A33C625CCQ64104362-F71F42A4-7092-4304-B227-C7AC50C48D76Q66829651-F57D8385-82E5-464F-8897-E1D129F0E233Q72173404-9F6F714A-7F84-4C7F-AD0F-968B2FB7309AQ72176454-6F672790-6079-4734-B75B-B946D08D1C5BQ73482762-BBD079B3-A024-4D2F-83CD-922CFD28C1D4Q84161643-B5500E9F-6835-49A9-99CE-04A4BC794086Q85976906-AC2D544A-3275-41FE-8D8F-ED2EDEADDAB5Q90382644-6DA5F0A5-9F97-47A9-BDF7-31BD38869115Q91037043-9C3B2AA8-D51D-4735-84E9-8655DCEE37EDQ91654553-3000546B-DB07-4938-80E0-C0F0B38212ECQ92161811-A2C241C6-3EEE-4AEB-B081-B46FFA50F419
P50
description
Forscher
@de
chercheur
@fr
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
研究者
@zh
name
Françoise H Routier
@ast
Françoise H Routier
@en
Françoise H Routier
@es
Françoise H Routier
@nl
type
label
Françoise H Routier
@ast
Françoise H Routier
@en
Françoise H Routier
@es
Françoise H Routier
@nl
prefLabel
Françoise H Routier
@ast
Françoise H Routier
@en
Françoise H Routier
@es
Françoise H Routier
@nl
P31
P496
0000-0002-7163-0590