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.
View timeline visualization
| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 3 | 3 |
| 2001 | 0 | 3 | 3 |
| 2003 | 1 | 2 | 3 |
| 2004 | 1 | 2 | 3 |
| 2005 | 0 | 1 | 1 |
| 2006 | 1 | 1 | 2 |
| 2007 | 0 | 1 | 1 |
| 2008 | 1 | 1 | 2 |
| 2009 | 2 | 2 | 4 |
| 2010 | 0 | 5 | 5 |
| 2012 | 1 | 0 | 1 |
| 2013 | 1 | 1 | 2 |
| 2014 | 2 | 0 | 2 |
| 2015 | 3 | 1 | 4 |
| 2016 | 0 | 5 | 5 |
| 2017 | 4 | 2 | 6 |
| 2018 | 3 | 1 | 4 |
| 2019 | 0 | 1 | 1 |
| 2022 | 0 | 1 | 1 |
| 2024 | 1 | 0 | 1 |
Below are the most recent publications written about "Penicillin-Binding Proteins" by people in Profiles.
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Molecular motor tug-of-war regulates elongasome cell wall synthesis dynamics in Bacillus subtilis. Nat Commun. 2024 Jun 26; 15(1):5411.
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Altered PBP4 and GdpP functions synergistically mediate MRSA-like high-level, broad-spectrum β-lactam resistance in Staphylococcus aureus. mBio. 2024 May 08; 15(5):e0288923.
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The NaHCO3-Responsive Phenotype in Methicillin-Resistant Staphylococcus aureus (MRSA) Is Influenced by mecA Genotype. Antimicrob Agents Chemother. 2022 06 21; 66(6):e0025222.
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Bicarbonate Resensitization of Methicillin-Resistant Staphylococcus aureus to β-Lactam Antibiotics. Antimicrob Agents Chemother. 2019 07; 63(7).
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Movement dynamics of divisome proteins and PBP2x:FtsW in cells of Streptococcus pneumoniae. Proc Natl Acad Sci U S A. 2019 02 19; 116(8):3211-3220.
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Structural and kinetic analyses of penicillin-binding protein 4 (PBP4)-mediated antibiotic resistance in Staphylococcus aureus. J Biol Chem. 2018 12 21; 293(51):19854-19865.
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A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery. PLoS Genet. 2018 10; 14(10):e1007726.
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PBP4 activity and its overexpression are necessary for PBP4-mediated high-level β-lactam resistance. J Antimicrob Chemother. 2018 05 01; 73(5):1177-1180.
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Evaluation of Oxacillin and Cefoxitin Disk Diffusion and MIC Breakpoints Established by the Clinical and Laboratory Standards Institute for Detection of mecA-Mediated Oxacillin Resistance in Staphylococcus schleiferi. J Clin Microbiol. 2018 02; 56(2).
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Identification of a Functionally Unique Family of Penicillin-Binding Proteins. J Am Chem Soc. 2017 12 13; 139(49):17727-17730.