|
[1]
|
Screening and identification of bioactive components resistant to metallo-beta-lactamase from Schisandra chinensis (Turcz.) Baill. by metalloenzyme-immobilized affinity chromatography
Journal of Chromatography B,
2021
DOI:10.1016/j.jchromb.2021.122524
|
|
|
|
|
[2]
|
Screening and identification of bioactive components resistant to metallo-beta-lactamase from Schisandra chinensis (Turcz.) Baill. by metalloenzyme-immobilized affinity chromatography
Journal of Chromatography B,
2021
DOI:10.1016/j.jchromb.2021.122524
|
|
|
|
|
[3]
|
Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms
Scientific Reports,
2020
DOI:10.1038/s41598-020-68612-z
|
|
|
|
|
[4]
|
Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms
Scientific Reports,
2020
DOI:10.1038/s41598-020-68612-z
|
|
|
|
|
[5]
|
Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594
Scientific Reports,
2018
DOI:10.1038/s41598-018-19279-0
|
|
|
|
|
[6]
|
Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594
Scientific Reports,
2018
DOI:10.1038/s41598-018-19279-0
|
|
|
|
|
[7]
|
Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594
Scientific Reports,
2018
DOI:10.1038/s41598-018-19279-0
|
|
|
|
|
[8]
|
Insights into an evolutionary strategy leading to antibiotic resistance
Scientific Reports,
2017
DOI:10.1038/srep40357
|
|
|
|
|
[9]
|
Insights into an evolutionary strategy leading to antibiotic resistance
Scientific Reports,
2017
DOI:10.1038/srep40357
|
|
|
|
|
[10]
|
Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks
Journal of Inorganic Biochemistry,
2016
DOI:10.1016/j.jinorgbio.2015.12.014
|
|
|
|
|
[11]
|
β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health
JBIC Journal of Biological Inorganic Chemistry,
2015
DOI:10.1007/s00775-015-1250-x
|
|
|
|
|
[12]
|
Metallo-β-Lactamases: A Major Threat to Human Health
American Journal of Molecular Biology,
2014
DOI:10.4236/ajmb.2014.43011
|
|
|
|
|
[13]
|
Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes
American Journal of Molecular Biology,
2014
DOI:10.4236/ajmb.2014.41002
|
|
|
|
|
[14]
|
The applications of binuclear metallohydrolases in medicine: Recent advances in the design and development of novel drug leads for purple acid phosphatases, metallo-β-lactamases and arginases
European Journal of Medicinal Chemistry,
2014
DOI:10.1016/j.ejmech.2014.02.008
|
|
|
|
|
[15]
|
Metallo‐β‐lactamases and Their Biomimetic Complexes
European Journal of Inorganic Chemistry,
2014
DOI:10.1002/ejic.201402203
|
|
|
|
|
[16]
|
Metallo‐β‐lactamases and Their Biomimetic Complexes
European Journal of Inorganic Chemistry,
2014
DOI:10.1002/ejic.201402203
|
|
|
|