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
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MeSH Number(s) |
D08.811.710 D12.776.097.545
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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 |
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1998 | 1 | 0 | 1 |
2015 | 1 | 1 | 2 |
2022 | 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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Melzer ES, Kado T, Garc?a-Heredia A, Gupta KR, Meniche X, Morita YS, Sassetti CM, Rego EH, Siegrist MS. Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria. J Bacteriol. 2022 06 21; 204(6):e0054021.
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Syed MA, Shah SHH, Sherafzal Y, Shafi-Ur-Rehman S, Khan MA, Barrett JB, Woodley TA, Jamil B, Abbasi SA, Jackson CR. Detection and Molecular Characterization of Methicillin-Resistant Staphylococcus aureus from Table Eggs in Haripur, Pakistan. Foodborne Pathog Dis. 2018 02; 15(2):86-93.
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Proulx MK, Palace SG, Gandra S, Torres B, Weir S, Stiles T, Ellison RT, Goguen JD. Reversion From Methicillin Susceptibility to Methicillin Resistance in Staphylococcus aureus During Treatment of Bacteremia. J Infect Dis. 2016 Mar 15; 213(6):1041-8.
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Kieser KJ, Boutte CC, Kester JC, Baer CE, Barczak AK, Meniche X, Chao MC, Rego EH, Sassetti CM, Fortune SM, Rubin EJ. Phosphorylation of the Peptidoglycan Synthase PonA1 Governs the Rate of Polar Elongation in Mycobacteria. PLoS Pathog. 2015 Jun; 11(6):e1005010.
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Cho H, Adrio JL, Luengo JM, Wolfe S, Ocran S, Hintermann G, Piret JM, Demain AL. Elucidation of conditions allowing conversion of penicillin G and other penicillins to deacetoxycephalosporins by resting cells and extracts of Streptomyces clavuligerus NP1. Proc Natl Acad Sci U S A. 1998 Sep 29; 95(20):11544-8.
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Xiao XF, Wolfe S, Demain AL. Purification and characterization of cephalosporin 7 alpha-hydroxylase from Streptomyces clavuligerus. Biochem J. 1991 Dec 01; 280 ( Pt 2):471-4.
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Shen YQ, Wolfe S, Demain AL. Enzymatic conversion of the unnatural tripeptide delta-(D-alpha-aminoadipyl)-L-cysteinyl-D-valine to beta-lactam antibiotics. J Antibiot (Tokyo). 1984 Sep; 37(9):1044-8.
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Kupka J, Shen YQ, Wolfe S, Demain AL. Studies on the ring-cyclization and ring-expansion enzymes of beta-lactam biosynthesis in Cephalosporium acremonium. Can J Microbiol. 1983 May; 29(5):488-96.