About: Nathalie Juge

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

About: Nathalie Juge Goto Sponge NotDistinct Permalink

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) ikertzailea (eu) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) chercheuse (fr) investigadora (es) ഗവേഷക (ml) araştırmacı (tr) wetenschapper (nl) дослідниця (uk) 研究者 (zh) հետազոտող (hy) researcher (en-ca) researcher (en-gb) researcher (en-us) hulumtuese (sq) ricercatrice (it) investigadora (ca) investigadora (gl) investigadora (pt) investigadora (ast)
rdfs:label	Nathalie Juge (en) Nathalie Juge (es) Nathalie Juge (nl) Nathalie Juge (sl) Nathalie Juge (ast)
skos:prefLabel	Nathalie Juge (en) Nathalie Juge (es) Nathalie Juge (nl) Nathalie Juge (sl) Nathalie Juge (ast)
name	Nathalie Juge (en) Nathalie Juge (es) Nathalie Juge (nl) Nathalie Juge (sl) Nathalie Juge (ast)
Scopus author ID	wds:Q28358713-85A58A52-15FE-45B4-8643-A0F1E772F5AE
Scopus author ID	7004217528
given name	wds:Q28358713-B7871D73-BFAF-4A39-9166-13AB5E36B96B
given name	Nathalie
instance of	wds:Q28358713-605A7276-F3F1-4A1D-BE47-D9012AE6DA4B
instance of	Homo sapiens
occupation	wds:Q28358713-23E830DC-3C1F-4248-948A-799632C39C2B
employer	wds:Q28358713-14390ED1-717D-43E1-8AB1-FAE1A13CA5FE
sex or gender	wds:Q28358713-CEA34505-88EF-403E-8092-4A8CEF250A86
VIAF ID	wds:Q28358713-E6F4FEEC-0350-40F3-B64E-0EBED4F5D22C
IdRef ID	wds:Q28358713-e53e0d63-0541-416e-a71c-e956689199ab
WorldCat Identities ID (superseded)	wds:Q28358713-E43CDD67-68BA-45F9-8B66-6C2A821DC289
VIAF ID	http://viaf.org/viaf/158149196475474791677
IdRef ID	http://www.idref.fr/07230815X/id
occupation	researcher
employer	Quadram Institute Bioscience
sex or gender	female organism
VIAF ID	158149196475474791677
IdRef ID	07230815X
WorldCat Identities ID (superseded)	viaf-158149196475474791677
ORCID iD	wds:Q28358713-286E0140-69CD-4D50-AF03-B4E2C4E0F55A
ORCID iD	https://orcid.org/0000-0001-8515-1315
ORCID iD	0000-0001-8515-1315
is owl:sameAs of	Nathalie Juge
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28358713
is author of	Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum, var. Soisson) Cross-inhibitory activity of cereal protein inhibitors against alpha-amylases and xylanases The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases. The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri XIP-I, a xylanase inhibitor protein from wheat: a novel protein function Utilisation of mucin glycans by the human gut symbiont Ruminococcus gnavus is strain-dependent Secretion, purification, and characterisation of barley alpha-amylase produced by heterologous gene expression in Aspergillus niger. The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase The pan-genome of Lactobacillus reuteri strains originating from the pig gastrointestinal tract Strain-specific diversity of mucus-binding proteins in the adhesion and aggregation properties of Lactobacillus reuteri. Interactions defining the specificity between fungal xylanases and the xylanase-inhibiting protein XIP-I from wheat Substrate (aglycone) specificity of human cytosolic beta-glucosidase Molecular characterization of host-specific biofilm formation in a vertebrate gut symbiont Hydrolytic fate of deoxynivalenol-3-glucoside during digestion Molecular basis for chemoprevention by sulforaphane: a comprehensive review. Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases Domain B protruding at the third beta strand of the alpha/beta barrel in barley alpha-amylase confers distinct isozyme-specific properties. Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylose by barley alpha-amylase. The activity of barley alpha-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose 1 1Edited by R. Huber Factors affecting xylanase functionality in the degradation of arabinoxylans. Comparative characterization of complete and truncated forms of Lactobacillus amylovorus alpha-amylase and role of the C-terminal direct repeats in raw-starch binding. The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger. Mucin glycan foraging in the human gut microbiome. High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris. Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-xylanase inhibitor Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18 Genome sequence of the vertebrate gut symbiont Lactobacillus reuteri ATCC 53608. Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont Structural insights into bacterial recognition of intestinal mucins. Sialidases from gut bacteria: a mini-review γδ T-cell-deficient mice show alterations in mucin expression, glycosylation, and goblet cells but maintain an intact mucus layer Crystal Structure of a Mucus-binding Protein Repeat Reveals an Unexpected Functional Immunoglobulin Binding Activity Structural basis for adaptation of lactobacilli to gastrointestinal mucus

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, 180 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software