Penicillin-Binding Proteins
"Penicillin-Binding Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Bacterial proteins that share the property of binding irreversibly to PENICILLINS and other ANTIBACTERIAL AGENTS derived from LACTAMS. The penicillin-binding proteins are primarily enzymes involved in CELL WALL biosynthesis including MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; PEPTIDE SYNTHASES; TRANSPEPTIDASES; and HEXOSYLTRANSFERASES.
| Descriptor ID |
D046915
|
| MeSH Number(s) |
D08.811.710 D12.776.097.545
|
| Concept/Terms |
Penicillin-Binding Proteins- Penicillin-Binding Proteins
- Penicillin Binding Proteins
- Proteins, Penicillin-Binding
- Penicillin-Binding Protein
- Penicillin Binding Protein
|
Below are MeSH descriptors whose meaning is more general than "Penicillin-Binding Proteins".
Below are MeSH descriptors whose meaning is more specific than "Penicillin-Binding Proteins".
This graph shows the total number of publications written about "Penicillin-Binding Proteins" by people in this website by year, and whether "Penicillin-Binding Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2001 | 0 | 1 | 1 |
| 2005 | 3 | 0 | 3 |
| 2008 | 1 | 0 | 1 |
| 2010 | 2 | 0 | 2 |
| 2012 | 2 | 1 | 3 |
| 2016 | 1 | 0 | 1 |
| 2017 | 1 | 0 | 1 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Penicillin-Binding Proteins" by people in Profiles.
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Recognition of the ?-lactam carboxylate triggers acylation of Neisseria gonorrhoeae penicillin-binding protein 2. J Biol Chem. 2019 09 20; 294(38):14020-14032.
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Alanine 501 Mutations in Penicillin-Binding Protein 2 from Neisseria gonorrhoeae: Structure, Mechanism, and Effects on Cephalosporin Resistance and Biological Fitness. Biochemistry. 2017 02 28; 56(8):1140-1150.
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Penicillin-Binding Protein 3 Is Essential for Growth of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2017 01; 61(1).
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High-throughput screening for novel inhibitors of Neisseria gonorrhoeae penicillin-binding protein 2. PLoS One. 2012; 7(9):e44918.
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Guidelines for reporting novel mecA gene homologues. Antimicrob Agents Chemother. 2012 Oct; 56(10):4997-9.
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The role of the ?5-a11 loop in the active-site dynamics of acylated penicillin-binding protein A from Mycobacterium tuberculosis. J Mol Biol. 2012 May 18; 418(5):316-30.
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Crystal structures of covalent complexes of ?-lactam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity. Biochemistry. 2010 Sep 21; 49(37):8094-104.
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Unusual conformation of the SxN motif in the crystal structure of penicillin-binding protein A from Mycobacterium tuberculosis. J Mol Biol. 2010 Apr 23; 398(1):54-65.
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Crystal structures of penicillin-binding protein 2 from penicillin-susceptible and -resistant strains of Neisseria gonorrhoeae reveal an unexpectedly subtle mechanism for antibiotic resistance. J Biol Chem. 2009 Jan 09; 284(2):1202-12.
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A large displacement of the SXN motif of Cys115-modified penicillin-binding protein 5 from Escherichia coli. Biochem J. 2005 Nov 15; 392(Pt 1):55-63.