 Peptide Hydrolases
"Peptide Hydrolases" 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.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
| Descriptor ID |
D010447
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| MeSH Number(s) |
D08.811.277.656
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| Concept/Terms |
Peptide Hydrolases- Peptide Hydrolases
- Proteolytic Enzymes
- Proteases
- Proteinases
- Esteroproteases
- Peptidases
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Below are MeSH descriptors whose meaning is more general than "Peptide Hydrolases".
Below are MeSH descriptors whose meaning is more specific than "Peptide Hydrolases".
This graph shows the total number of publications written about "Peptide Hydrolases" by people in UAMS Profiles by year, and whether "Peptide Hydrolases" 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 |
|---|
| 2024 | 1 | 2 | 3 | | 2023 | 1 | 0 | 1 | | 2022 | 0 | 1 | 1 | | 2021 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 | | 2018 | 3 | 0 | 3 | | 2016 | 1 | 0 | 1 | | 2015 | 1 | 1 | 2 | | 2014 | 1 | 0 | 1 | | 2013 | 0 | 1 | 1 | | 2012 | 2 | 1 | 3 | | 2010 | 2 | 1 | 3 | | 2007 | 1 | 0 | 1 | | 2006 | 1 | 0 | 1 | | 2005 | 1 | 4 | 5 | | 2003 | 0 | 1 | 1 | | 2002 | 1 | 0 | 1 | | 2000 | 1 | 0 | 1 | | 1994 | 2 | 0 | 2 | | 1992 | 0 | 1 | 1 |
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Below are the most recent publications written about "Peptide Hydrolases" by people in Profiles over the past ten years.
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Beenken KE, Campbell MJ, Smeltzer MS. The ability of sarA to limit protease production plays a key role in the pathogenesis of Staphylococcus aureus osteomyelitis irrespective of the functional status of agr. Infect Immun. 2025 01 31; 93(1):e0047324.
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Campbell MJ, Beenken KE, Ramirez AM, Smeltzer MS. Increased production of aureolysin and staphopain A is a primary determinant of the reduced virulence of Staphylococcus aureus sarA mutants in osteomyelitis. mBio. 2024 Apr 10; 15(4):e0338323.
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Kline SN, Orlando NA, Lee AJ, Wu MJ, Zhang J, Youn C, Feller LE, Pontaza C, Dikeman D, Limjunyawong N, Williams KL, Wang Y, Cihakova D, Jacobsen EA, Durum SK, Garza LA, Dong X, Archer NK. Staphylococcus aureus proteases trigger eosinophil-mediated skin inflammation. Proc Natl Acad Sci U S A. 2024 Feb 06; 121(6):e2309243121.
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Campbell MJ, Beenken KE, Ramirez AM, Smeltzer MS. The major role of sarA in limiting Staphylococcus aureus extracellular protease production in vitro is correlated with decreased virulence in diverse clinical isolates in osteomyelitis. Virulence. 2023 12; 14(1):2175496.
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Johann DJ, Shin IJ, Roberge A, Laun S, Peterson EA, Liu M, Steliga MA, Muesse J, Emmert-Buck MR, Tangrea MA. Effect of Antigen Retrieval on Genomic DNA From Immunodissected Samples. J Histochem Cytochem. 2022 09; 70(9):643-658.
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Rom JS, Beenken KE, Ramirez AM, Walker CM, Echols EJ, Smeltzer MS. Limiting protease production plays a key role in the pathogenesis of the divergent clinical isolates of Staphylococcus aureus LAC and UAMS-1. Virulence. 2021 12; 12(1):584-600.
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Ramirez AM, Beenken KE, Byrum SD, Tackett AJ, Shaw LN, Gimza BD, Smeltzer MS. SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1. Virulence. 2020 12; 11(1):1738-1762.
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G C B, Sahukhal GS, Elasri MO. Role of the msaABCR Operon in Cell Wall Biosynthesis, Autolysis, Integrity, and Antibiotic Resistance in Staphylococcus aureus. Antimicrob Agents Chemother. 2019 10; 63(10).
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Steen AD, Kevorkian RT, Bird JT, Dombrowski N, Baker BJ, Hagen SM, Mulligan KH, Schmidt JM, Webber AT, Royalty TM, Alperin MJ. Kinetics and Identities of Extracellular Peptidases in Subsurface Sediments of the White Oak River Estuary, North Carolina. Appl Environ Microbiol. 2019 10 01; 85(19).
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Byrum SD, Loughran AJ, Beenken KE, Orr LM, Storey AJ, Mackintosh SG, Edmondson RD, Tackett AJ, Smeltzer MS. Label-Free Proteomic Approach to Characterize Protease-Dependent and -Independent Effects of sarA Inactivation on the Staphylococcus aureus Exoproteome. J Proteome Res. 2018 10 05; 17(10):3384-3395.
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Lao Y, Yang K, Wang Z, Sun X, Zou Q, Yu X, Cheng J, Tong X, Yeh ETH, Yang J, Yi J. DeSUMOylation of MKK7 kinase by the SUMO2/3 protease SENP3 potentiates lipopolysaccharide-induced inflammatory signaling in macrophages. J Biol Chem. 2018 03 16; 293(11):3965-3980.
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Li J, Lu D, Dou H, Liu H, Weaver K, Wang W, Li J, Yeh ETH, Williams BO, Zheng L, Yang T. Desumoylase SENP6 maintains osteochondroprogenitor homeostasis by suppressing the p53 pathway. Nat Commun. 2018 01 10; 9(1):143.
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Balasubramanian A, Manzano M, Teramoto T, Pilankatta R, Padmanabhan R. High-throughput screening for the identification of small-molecule inhibitors of the flaviviral protease. Antiviral Res. 2016 10; 134:6-16.
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Janhsen WK, Arnold C, Hentschel J, Lehmann T, Pfister W, Baier M, B?er K, H?nniger K, Kurzai O, Hipler UC, Mainz JG. Colonization of CF patients' upper airways with S. aureus contributes more decisively to upper airway inflammation than P. aeruginosa. Med Microbiol Immunol. 2016 Oct; 205(5):485-500.
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Miyakawa K, Joshi N, Sullivan BP, Albee R, Brandenberger C, Jaeschke H, McGill MR, Scott MA, Ganey PE, Luyendyk JP, Roth RA. Platelets and protease-activated receptor-4 contribute to acetaminophen-induced liver injury in mice. Blood. 2015 Oct 08; 126(15):1835-43.
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