Fluorescent analogs of UDP-glucose and their use in characterizing substrate binding by toxin A from Clostridium difficile.

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Biophysical Characterization and Activity of Lymphostatin, a Multifunctional Virulence Factor of Attaching and Effacing Escherichia coli.Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects.

P2860

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P2860

Fluorescent analogs of UDP-glucose and their use in characterizing substrate binding by toxin A from Clostridium difficile.

Item

http://www.wikidata.org/entity/Q44075211

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh

2002年學術文章

@zh-hant

name

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@en

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@nl

type

Item

label

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@en

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@nl

prefLabel

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@en

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@nl

P1476

Fluorescent analogs of UDP-glu ...... A from Clostridium difficile.

@en

P2093

Amy Kerzmann

http://www.w3.org/2001/XMLSchema#string

Sudeep Bhattacharyya

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of the catalytic domain of Clostridium novyi alpha-toxin

Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms

T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism

X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily

Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs

High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding

Structure of UDP complex of UDP-galactose:beta-galactoside-alpha -1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C terminus

Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases

Clostridium difficile toxins A and B are cation-dependent UDP-glucose hydrolases with differing catalytic activities.

Clostridial enterocolitis.

P304

3425-3432

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P31

scholarly article

P356

10.1046/J.1432-1033.2002.03013.X

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

269

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P50

Andrew L. Feig

P577

2002-07-01T00:00:00Z

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P5875

11247362

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P698

12135481

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P921

Clostridium difficile

glucose

glycobiology

Fluorescent analogs of UDP-glucose and their use in characterizing substrate binding by toxin A from Clostridium difficile.

about

P2860

P2860

Fluorescent analogs of UDP-glucose and their use in characterizing substrate binding by toxin A from Clostridium difficile.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921