Two distinct alpha-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates.
about
Proteinaceous Molecules Mediating Bifidobacterium-Host InteractionsLactobacillus adhesion to mucusThe impact of the milk glycobiome on the neonate gut microbiotaBifidobacterium longum subsp. infantis ATCC 15697 -Fucosidases Are Active on Fucosylated Human Milk OligosaccharidesCrystal Structures of a Glycoside Hydrolase Family 20 Lacto-N-biosidase from Bifidobacterium bifidum1,3-1,4- -L-Fucosynthase That Specifically Introduces Lewis a/x Antigens into Type-1/2 ChainsOligosaccharide binding proteins from Bifidobacterium longum subsp. infantis reveal a preference for host glycansChemical characterization of oligosaccharides in the milk of six species of New and Old World monkeysEvolutionary glycomics: characterization of milk oligosaccharides in primates.Consumption of human milk glycoconjugates by infant-associated bifidobacteria: mechanisms and implications.Nursing our microbiota: molecular linkages between bifidobacteria and milk oligosaccharides.Bifidobacterium bifidum as an example of a specialized human gut commensal.Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foragingThe structure of a glycoside hydrolase 29 family member from a rumen bacterium reveals unique, dual carbohydrate-binding domains.Cross-feeding by Bifidobacterium breve UCC2003 during co-cultivation with Bifidobacterium bifidum PRL2010 in a mucin-based mediumAlpha-L-fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus.Colonization resistance and microbial ecophysiology: using gnotobiotic mouse models and single-cell technology to explore the intestinal jungle.An infant-associated bacterial commensal utilizes breast milk sialyloligosaccharides.Utilisation of mucin glycans by the human gut symbiont Ruminococcus gnavus is strain-dependentHow do bifidobacteria counteract environmental challenges? Mechanisms involved and physiological consequences.Physiology of consumption of human milk oligosaccharides by infant gut-associated bifidobacteria.Maternal fucosyltransferase 2 status affects the gut bifidobacterial communities of breastfed infantsα-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to novel glycoside hydrolase family 129 is implicated in alternative mucin degradation pathway.Comparative genomic analyses of 17 clinical isolates of Gardnerella vaginalis provide evidence of multiple genetically isolated clades consistent with subspeciation into genovars.In Vitro Fermentation of caprine milk oligosaccharides by bifidobacteria isolated from breast-fed infantsBifidobacterial enzymes involved in the metabolism of human milk oligosaccharides.Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expressionConsumption of a Bifidobacterium bifidum Strain for 4 Weeks Modulates Dominant Intestinal Bacterial Taxa and Fecal Butyrate in Healthy AdultsA novel gene cluster allows preferential utilization of fucosylated milk oligosaccharides in Bifidobacterium longum subsp. longum SC596.Algal fucoidan: structural and size-dependent bioactivities and their perspectives.How a sugary bug gets through the day: recent developments in understanding fundamental processes impacting Campylobacter jejuni pathogenesis.Technological advances in bifidobacterial molecular genetics: application to functional genomics and medical treatments.Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans.Solubilization and Iterative Saturation Mutagenesis of α1,3-fucosyltransferase from Helicobacter pylori to enhance its catalytic efficiency.α-N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes α-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin.Bifidobacterial α-galactosidase with unique carbohydrate-binding module specifically acts on blood group B antigen.Glycoside hydrolase family 89 alpha-N-acetylglucosaminidase from Clostridium perfringens specifically acts on GlcNAc alpha1,4Gal beta1R at the non-reducing terminus of O-glycans in gastric mucin.Mucin glycan foraging in the human gut microbiome.Host-derived glycans serve as selected nutrients for the gut microbe: human milk oligosaccharides and bifidobacteria.The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.
P2860
Q26740603-2852973F-5A4F-479B-90AB-91108E9DDCEDQ26827553-186AC12F-2669-48DD-8DD8-9C39EBB5046FQ26860976-CB3C4B57-30E5-469E-91FB-D7ACA0813132Q27675939-C6691EB3-97DD-4FA2-A17F-81E7E6BCCA6EQ27676765-C02E7DF7-CC09-4726-96E6-161BC74B5135Q27678219-6F43CAD1-7943-43DA-8785-705A737C9016Q28477426-DFCCF656-F883-49B7-8C48-324FCDC4278DQ28744229-8865A6DE-9475-4028-8511-432BD2674CD0Q33788219-65A6240F-4EF3-4CBD-BD4E-EFE7A650FE68Q33852500-AE50B943-CAD9-4826-A975-164E664615AFQ33987598-B982367A-D589-4080-9AA0-FF5DD68B5EE1Q34073166-0507CED7-FEC4-4110-8F1E-DAE893A9771FQ34320513-40380E34-BC4E-44AE-9914-4509EBC74949Q34542128-AAADBC33-EB9D-4857-82A8-BFCBF96E2779Q34611971-DAD06D4B-BE0D-4415-AC1A-131D43B4902EQ34669987-68AD5133-EDBC-4CCF-AA8A-882F0DD138E7Q34714359-33DD2E23-C4A3-4E3C-88A5-AC4EAE719D48Q34751990-223179CF-B54D-407C-A1A6-6C21F2E5C38AQ35034645-1E6E94D2-D737-4A5E-A50B-BEDB32427B2CQ35132155-734E8093-5092-4205-A298-292D98CD8F9FQ35266351-D513F6BD-2F95-45E9-BB74-F218CE4929B0Q35545529-D9F4D443-534D-4072-A19D-CD9592BE7079Q35643847-B721C74F-C92F-4296-B165-43634D058AA7Q36156238-EBD9C687-4E0D-4DCE-BF5A-5CED8066E403Q36782192-B665193F-5ADB-4C5D-8EE0-989AF77DB379Q36830452-41268CC0-D3A5-4059-8719-77AA3B4C841AQ37132084-F75C53DC-7C79-4EE7-A0C9-0AEC243D87E8Q37287065-70BCB8B5-328C-4266-8ADC-09D9A8D52957Q37348745-E4EFE408-6001-41C7-A280-5637D8041557Q37956919-2A068412-EB90-4DFB-8FBF-550CF1D1AFE7Q38007349-BA7DF624-7A02-4A94-B2FB-1564A86FC4BEQ38220830-01C51EDF-3873-4DA7-A507-982825DC9D62Q38289549-94A78AAF-0DC8-41BD-84F6-F49FE52FE8B2Q38294196-BAF75905-C1C1-4726-A3A6-759A6A766DEAQ38303147-A37B1D21-9541-4D94-8DB4-07236F0CA304Q38320578-E8B75F91-6B25-4E77-9D86-F5C7921F7C96Q38338535-E94BD6BB-C7FD-4C90-A558-D218604A2BB4Q38411042-044D4D35-2DB2-463E-B1F6-DE1B3B1D53E2Q38720798-0B5843C1-BE30-4EC5-9F32-A72CC64EDC90Q38762828-91409EC1-BD95-4D88-B9DD-0DDE27EFAA30
P2860
Two distinct alpha-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
Two distinct alpha-L-fucosidas ...... ccharides and glycoconjugates.
@en
type
label
Two distinct alpha-L-fucosidas ...... ccharides and glycoconjugates.
@en
prefLabel
Two distinct alpha-L-fucosidas ...... ccharides and glycoconjugates.
@en
P2093
P2860
P356
P1433
P1476
Two distinct alpha-L-fucosidas ...... accharides and glycoconjugates
@en
P2093
Akiko Miyake
Erina Yoshida
Hidehiko Kumagai
Kenji Yamamoto
Masashi Kiyohara
P2860
P304
P356
10.1093/GLYCOB/CWP082
P577
2009-06-11T00:00:00Z