Muramidase
"Muramidase" 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.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
Descriptor ID |
D009113
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MeSH Number(s) |
D08.811.277.450.642
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Concept/Terms |
Muramidase- Muramidase
- N-Acetylmuramide Glycanhydrolase
- Glycanhydrolase, N-Acetylmuramide
- N Acetylmuramide Glycanhydrolase
- Lysozyme
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Below are MeSH descriptors whose meaning is more general than "Muramidase".
Below are MeSH descriptors whose meaning is more specific than "Muramidase".
This graph shows the total number of publications written about "Muramidase" by people in this website by year, and whether "Muramidase" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
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1997 | 1 | 0 | 1 | 1998 | 1 | 1 | 2 | 1999 | 2 | 1 | 3 | 2000 | 2 | 1 | 3 | 2001 | 1 | 0 | 1 | 2002 | 0 | 2 | 2 | 2006 | 0 | 1 | 1 | 2007 | 0 | 1 | 1 | 2008 | 1 | 0 | 1 | 2009 | 1 | 2 | 3 | 2010 | 2 | 1 | 3 | 2011 | 2 | 0 | 2 | 2012 | 1 | 2 | 3 | 2013 | 1 | 0 | 1 | 2014 | 0 | 3 | 3 | 2015 | 2 | 3 | 5 | 2016 | 2 | 0 | 2 | 2017 | 1 | 2 | 3 | 2020 | 2 | 0 | 2 | 2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Muramidase" by people in Profiles.
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Witeof AE, McClary WD, Rea LT, Yang Q, Davis MM, Funke HH, Catalano CE, Randolph TW. Atomic-Layer Deposition Processes Applied to Phage ? and a Phage-like Particle Platform Yield Thermostable, Single-Shot Vaccines. J Pharm Sci. 2022 05; 111(5):1354-1362.
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Shirts MR, Ferguson AL. Statistically Optimal Continuous Free Energy Surfaces from Biased Simulations and Multistate Reweighting. J Chem Theory Comput. 2020 Jul 14; 16(7):4107-4125.
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Ayyappan P, Harms RZ, Seifert JA, Bemis EA, Feser ML, Deane KD, Demoruelle MK, Mikuls TR, Holers VM, Sarvetnick NE. Heightened Levels of Antimicrobial Response Factors in Patients With Rheumatoid Arthritis. Front Immunol. 2020; 11:427.
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Carmali S, Murata H, Matyjaszewski K, Russell AJ. Tailoring Site Specificity of Bioconjugation Using Step-Wise Atom-Transfer Radical Polymerization on Proteins. Biomacromolecules. 2018 10 08; 19(10):4044-4051.
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Wu C, Su H, Karydis A, Anderson KM, Ghadri N, Tang S, Wang Y, Bumgardner JD. Mechanically stable surface-hydrophobilized chitosan nanofibrous barrier membranes for guided bone regeneration. Biomed Mater. 2017 Nov 10; 13(1):015004.
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Ellison MA, Gearheart CM, Porter CC, Ambruso DR. IFN-? alters the expression of diverse immunity related genes in a cell culture model designed to represent maturing neutrophils. PLoS One. 2017; 12(10):e0185956.
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Chisholm CF, Soucie KR, Song JS, Strauch P, Torres RM, Carpenter JF, Ragheb JA, Randolph TW. Immunogenicity of Structurally Perturbed Hen Egg Lysozyme Adsorbed to Silicone Oil Microdroplets in Wild-Type and Transgenic Mouse Models. J Pharm Sci. 2017 06; 106(6):1519-1527.
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Riederer MS, Requist BD, Payne KA, Way JD, Krebs MD. Injectable and microporous scaffold of densely-packed, growth factor-encapsulating chitosan microgels. Carbohydr Polym. 2016 11 05; 152:792-801.
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Panja S, Halder M. Exploration of electrostatic interaction in the hydrophobic pocket of lysozyme: Importance of ligand-induced perturbation of the secondary structure on the mode of binding of exogenous ligand and possible consequences. J Photochem Photobiol B. 2016 Aug; 161:253-65.
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Weltz JS, Schwartz DK, Kaar JL. Surface-Mediated Protein Unfolding as a Search Process for Denaturing Sites. ACS Nano. 2016 Jan 26; 10(1):730-8.
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