 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 |
|---|
| 2021 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 | | 2019 | 1 | 1 | 2 | | 2018 | 3 | 0 | 3 | | 2016 | 1 | 1 | 2 | | 2015 | 2 | 1 | 3 | | 2014 | 1 | 0 | 1 | | 2013 | 0 | 2 | 2 | | 2012 | 2 | 1 | 3 | | 2010 | 2 | 1 | 3 | | 2006 | 1 | 0 | 1 | | 2005 | 1 | 4 | 5 | | 2003 | 0 | 2 | 2 | | 2002 | 2 | 1 | 3 | | 2000 | 1 | 0 | 1 | | 1994 | 2 | 0 | 2 | | 1992 | 0 | 1 | 1 | | 1989 | 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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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, Böer K, Hünniger 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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Atwood DN, Loughran AJ, Courtney AP, Anthony AC, Meeker DG, Spencer HJ, Gupta RK, Lee CY, Beenken KE, Smeltzer MS. Comparative impact of diverse regulatory loci on Staphylococcus aureus biofilm formation. Microbiologyopen. 2015 Jun; 4(3):436-51.
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Sahukhal GS, Batte JL, Elasri MO. msaABCR operon positively regulates biofilm development by repressing proteases and autolysis in Staphylococcus aureus. FEMS Microbiol Lett. 2015 Feb; 362(4).
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Beenken KE, Mrak LN, Zielinska AK, Atwood DN, Loughran AJ, Griffin LM, Matthews KA, Anthony AM, Spencer HJ, Skinner RA, Post GR, Lee CY, Smeltzer MS. Impact of the functional status of saeRS on in vivo phenotypes of Staphylococcus aureus sarA mutants. Mol Microbiol. 2014 Jun; 92(6):1299-312.
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Snowden JN, Beaver M, Beenken K, Smeltzer M, Horswill AR, Kielian T. Staphylococcus aureus sarA regulates inflammation and colonization during central nervous system biofilm formation. PLoS One. 2013; 8(12):e84089.
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Zhang Y, Wei C, Jiang W, Wang L, Li C, Wang Y, Dow JM, Sun W. The HD-GYP domain protein RpfG of Xanthomonas oryzae pv. oryzicola regulates synthesis of extracellular polysaccharides that contribute to biofilm formation and virulence on rice. PLoS One. 2013; 8(3):e59428.
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Zielinska AK, Beenken KE, Mrak LN, Spencer HJ, Post GR, Skinner RA, Tackett AJ, Horswill AR, Smeltzer MS. sarA-mediated repression of protease production plays a key role in the pathogenesis of Staphylococcus aureus USA300 isolates. Mol Microbiol. 2012 Dec; 86(5):1183-96.
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Khan RZ, Badros A. Role of carfilzomib in the treatment of multiple myeloma. Expert Rev Hematol. 2012 Aug; 5(4):361-72.
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Mrak LN, Zielinska AK, Beenken KE, Mrak IN, Atwood DN, Griffin LM, Lee CY, Smeltzer MS. saeRS and sarA act synergistically to repress protease production and promote biofilm formation in Staphylococcus aureus. PLoS One. 2012; 7(6):e38453.
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