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 |
|---|
| 1998 | 0 | 1 | 1 |
| 1999 | 0 | 2 | 2 |
| 2003 | 0 | 2 | 2 |
| 2005 | 0 | 1 | 1 |
| 2006 | 1 | 0 | 1 |
| 2008 | 0 | 1 | 1 |
| 2010 | 0 | 2 | 2 |
| 2014 | 1 | 0 | 1 |
| 2015 | 1 | 0 | 1 |
| 2017 | 1 | 0 | 1 |
| 2020 | 0 | 1 | 1 |
| 2024 | 1 | 0 | 1 |
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Below are the most recent publications written about "Penicillin-Binding Proteins" by people in Profiles.
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Synergistic effects of novel penicillin-binding protein 1A amino acid substitutions contribute to high-level amoxicillin resistance of Helicobacter pylori. mSphere. 2024 Aug 28; 9(8):e0008924.
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Reduced In Vitro Susceptibility of Streptococcus pyogenes to ?-Lactam Antibiotics Associated with Mutations in the pbp2x Gene Is Geographically Widespread. J Clin Microbiol. 2020 03 25; 58(4).
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BLIP-II Employs Differential Hotspot Residues To Bind Structurally Similar Staphylococcus aureus PBP2a and Class A ?-Lactamases. Biochemistry. 2017 02 28; 56(8):1075-1084.
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Aptamer-Phage Reporters for Ultrasensitive Lateral Flow Assays. Anal Chem. 2015 Dec 01; 87(23):11660-5.
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PBP2a mutations causing high-level Ceftaroline resistance in clinical methicillin-resistant Staphylococcus aureus isolates. Antimicrob Agents Chemother. 2014 Nov; 58(11):6668-74.
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Mini-bronchoalveolar lavage quantitative polymerase chain reaction for diagnosis of methicillin-resistant Staphylococcus aureus pneumonia. Crit Care Med. 2010 Jul; 38(7):1536-41.
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Rapid detection of Staphylococcus aureus Panton-Valentine leukocidin in clinical specimens by enzyme-linked immunosorbent assay and immunochromatographic tests. J Clin Microbiol. 2010 Apr; 48(4):1384-90.
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Group B streptococcus exploits lipid rafts and phosphoinositide 3-kinase/Akt signaling pathway to invade human endometrial cells. Am J Obstet Gynecol. 2008 Nov; 199(5):548.e1-9.
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Analysis of mutations in the pbp genes of penicillin-non-susceptible pneumococci from Turkey. Clin Microbiol Infect. 2006 Feb; 12(2):150-5.
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Common beta-lactamases inhibit bacterial biofilm formation. Mol Microbiol. 2005 Nov; 58(4):1012-24.