Research graph
References from Generation of truncated derivatives through in silico enzymatic digest of peptide GV30 target MRSA both in vitro and in vivo. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1016/j.ejmech.2020.112832
10.1016/j.ejmech.2020.112832 · External reference
Multi-targeted quinazolinone-Schiff’s bases as potent bio-therapeutics
10.1016/j.rechem.2020.100067 · 2020 · External reference
Indole-based derivatives as potential antibacterial activity against methicillin-resistance Staphylococcus aureus (MRSA)
10.1016/j.ejmech.2020.112245 · 2020 · External reference
10.1016/j.micres.2018.05.002
10.1016/j.micres.2018.05.002 · External reference
A key review on oxadiazole analogs as potential methicillin-resistant Staphylococcus aureus (MRSA) activity: Structure-activity relationship studies
10.1016/j.ejmech.2021.113442 · 2021 · External reference
Antibacterial activities of sulfonyl or sulfonamide containing heterocyclic derivatives and its structure-activity relationships (SAR) studies: A critical review
2020 · External reference
Role of BP* C@ AgNPs in Bap-dependent multicellular behavior of clinically important methicillin-resistant Staphylococcus aureus (MRSA) biofilm adherence: a key virulence study
10.1016/j.micpath.2018.07.025 · 2018 · External reference
Novel TC@ AgNPs mediated biocidal mechanism against biofilm associated methicillin-resistant Staphylococcus aureus (Bap-MRSA) 090, cytotoxicity and its molecular docking studies
10.1039/c7md00486a · 2017 · External reference
Pyrazole-based analogs as potential antibacterial agents against methicillin-resistance Staphylococcus aureus (MRSA) and its SAR elucidation
2020 · External reference
Effect of low charge and high hydrophobicity on antimicrobial activity of the quinazolinone-peptide conjugates
10.1134/s1068162018020036 · 2018 · External reference
10.1038/nrmicro1098
10.1038/nrmicro1098 · External reference
10.1080/14712598.2017.1315402
10.1080/14712598.2017.1315402 · External reference
Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis
10.1016/s0021-9258(18)54469-0 · 1991 · External reference
10.1042/bsr20180710
10.1042/bsr20180710 · External reference
10.1586/14787210.2014.976613
10.1586/14787210.2014.976613 · External reference
Brevinin-1 and-2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa
10.1016/0006-291x(92)91542-x · 1992 · External reference
10.3390/app8122627
10.3390/app8122627 · External reference
An overview of Brevinin superfamily: structure, function and clinical perspectives
10.1007/978-1-4471-6458-6_10 · 2014 · External reference
Antimicrobial properties of brevinin-2-related peptide and its analogs: efficacy against multidrug-resistant Acinetobacter baumannii
10.1111/j.1747-0285.2009.00882.x · 2009 · External reference
A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica
10.1016/j.regpep.2003.12.003 · 2004 · External reference
Brevinin‐2R1 semi‐selectively kills cancer cells by a distinct mechanism, which involves the lysosomal‐mitochondrial death pathway
10.1111/j.1582-4934.2008.00129.x · 2008 · External reference
Anticancer activity of brevinin-2R peptide and its Two analogues against myelogenous leukemia cell line as natural treatments: An in vitro study
10.1007/s10989-019-09903-6 · 2020 · External reference
Peptides with antimicrobial and anti-inflammatory activities that have therapeutic potential for treatment of acne vulgaris
10.1016/j.peptides.2012.02.010 · 2012 · External reference
Brevinin-2-related peptide and its [D4K] analogue stimulate insulin release in vitro and improve glucose tolerance in mice fed a high fat diet
10.1055/s-0030-1254126 · 2010 · External reference
10.2217/fmb.11.27
10.2217/fmb.11.27 · External reference
Development of conformationally restricted analogues of bradykinin and somatostatin using constrained amino acids and different types of cyclisation
10.2174/0929867043364135 · 2004 · External reference
Protease inhibitors: Current status and future 3 prospects
10.1021/jm990412m · 2000 · External reference
10.1021/jm050488k
10.1021/jm050488k · External reference
10.1002/(sici)1097-0215(19991029)83:3<326::aid-ijc7>3.0.co;2-x
10.1002/(sici)1097-0215(19991029)83:3<326::aid-ijc7>3.0.co;2-x · External reference
10.1021/cr030024z
10.1021/cr030024z · External reference
Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity
10.3390/antibiotics9020085 · 2020 · External reference
10.1034/j.1399-3011.2001.00811.x
10.1034/j.1399-3011.2001.00811.x · External reference
Specificity of trypsin and alpha-chymotrypsin towards neutral substrates. Acta biochimica et biophysica
1976 · External reference
10.1021/cr000033x
10.1021/cr000033x · External reference
10.1021/bi7019904
10.1021/bi7019904 · External reference
Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering
10.7150/ijbs.23419 · 2018 · External reference
10.3390/ijms21249410
10.3390/ijms21249410 · External reference
Broad-spectrum antimicrobial activity and improved stability of a D-Amino acid enantiomer of DMPC-10A, the designed derivative of dermaseptin truncates
10.3390/antibiotics9090627 · 2020 · External reference
Antibacterial activity and mechanism of action of bovine lactoferricin derivatives with symmetrical amino acid sequences
10.3390/ijms19102951 · 2018 · External reference
10.1183/09031936.00007709
10.1183/09031936.00007709 · External reference
MRSA virulence and spread
10.1111/j.1462-5822.2012.01832.x · 2012 · External reference
Increased mortality associated with meticillin-resistant Staphylococcus aureus (MRSA) infection in the Intensive Care Unit: results from the EPIC II study
10.1016/j.ijantimicag.2011.05.013 · 2011 · External reference
The antimicrobial peptides and their potential clinical applications
2019 · External reference
10.1124/pr.55.1.2
10.1124/pr.55.1.2 · External reference
Colistin: still a lifesaver for the 21st century?
10.1080/17425255.2017.1230200 · 2017 · External reference
Pore formation induced by an antimicrobial peptide: electrostatic effects
10.1529/biophysj.108.136655 · 2008 · External reference
Looking for chinks in the armor of bacterial biofilms
10.1371/journal.pbio.0050307 · 2007 · External reference
10.1016/j.bioflm.2020.100027 · Admitted local publication
10.1016/j.peptides.2003.09.013
10.1016/j.peptides.2003.09.013 · External reference
Bile acid-induced liver toxicity: relation to the hydrophobic-hydrophilic balance of bile acids
10.1016/0306-9877(86)90137-4 · 1986 · External reference
Action mechanism and structural requirements of the antimicrobial peptides, gaegurins
10.1016/j.bbamem.2008.10.021 · 2009 · External reference
Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta
10.1016/s0167-4838(98)00123-x · 1998 · External reference
The technology acceptance model and the World Wide Web
10.1016/s0167-9236(00)00076-2 · 2000 · External reference
The role of C-terminal amidation in the mechanism of action of the antimicrobial peptide aurein 1.2
10.2478/ebtj-2020-0004 · 2020 · External reference
The effect of amidation on the behaviour of antimicrobial peptides
10.1007/s00249-015-1094-x · 2016 · External reference
10.4155/tde.13.104
10.4155/tde.13.104 · External reference
Trypsin cleaves exclusively C-terminal to arginine and lysine residues
10.1074/mcp.t400003-mcp200 · 2004 · External reference
10.1016/j.jconrel.2015.06.001
10.1016/j.jconrel.2015.06.001 · External reference
Effect of positive charges in the structural interaction of crabrolin isoforms with lipopolysaccharide
10.1002/psc.3271 · 2020 · External reference
10.1016/j.peptides.2003.08.023
10.1016/j.peptides.2003.08.023 · External reference
10.1128/aac.00925-06
10.1128/aac.00925-06 · External reference