High-molecular-weight penicillin-binding proteins from membranes of bacilli.

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Absence of penicillin-binding protein 4 from an apparently normal strain of Bacillus subtilis Trapping of the substrate-derived acyl enzyme intermediate of purified penicillin-binding protein 1a of Escherichia coli.Stability and synthesis of the penicillin-binding proteins during sporulation.

P2860

Q36272474-492728C9-DD24-4FDF-A4C6-62F9B1DCE67F Q36288292-5929D791-1CA5-4ACB-8809-474F5BF71D74 Q36332785-44175F4F-1927-4471-BFDE-0A5B87C52B24

P2860

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

Item

http://www.wikidata.org/entity/Q36309201

description

1981 nî lūn-bûn

@nan

1981年の論文

@ja

1981年学术文章

@wuu

1981年学术文章

@zh-cn

1981年学术文章

@zh-hans

1981年学术文章

@zh-my

1981年学术文章

@zh-sg

1981年學術文章

@yue

1981年學術文章

@zh

1981年學術文章

@zh-hant

name

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@ast

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

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type

Item

label

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@ast

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@en

prefLabel

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@ast

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@en

P1476

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

@en

P2093

Lindgren DM

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

P2860

Properties of the penicillin-binding proteins of Escherichia coli K12,

Utilization of a depsipeptide substrate for trapping acyl-enzyme intermediates of penicillin-sensitive D-alanine carboxypeptidases.

Use of model enzymes in the determination of the mode of action of penicillins and delta 3-cephalosporins.

Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins 1a, 1b, and 3

Antibody to the D-alanine carboxypeptidase of Bacillus subtilis does not cross-react with other penicillin-binding proteins.

Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.

Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis

Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis.

P304

950-955

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P31

scholarly article

P407

English

P433

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P478

148

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P50

Jack L. Strominger

David J Waxman

P577

1981-12-01T00:00:00Z

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

P698

6796565

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P932

216297

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High-molecular-weight penicillin-binding proteins from membranes of bacilli.

about

P2860

P2860

High-molecular-weight penicillin-binding proteins from membranes of bacilli.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P50

P577

P698

P932

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P50

P577

P698

P932