scholarly journals 1.6 Å Crystal structure of a PA2721 protein from pseudomonas aeruginosa-A potential drug-resistance protein

2006 ◽  
Vol 63 (4) ◽  
pp. 1102-1105 ◽  
Author(s):  
B. Nocek ◽  
M. Cuff ◽  
E. Evdokimova ◽  
A. Edwards ◽  
A. Joachimiak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Drug Resistance ◽  
Potential Drug ◽  
Resistance Protein

scholarly journals An In Vitro Coumarin-Antibiotic Combination Treatment of Pseudomonas aeruginosa Biofilms

2021 ◽  
Vol 16 (1) ◽  
pp. 1934578X2098774
Author(s):  
Jinpeng Zou ◽  
Yang Liu ◽  
Ruiwei Guo ◽  
Yu Tang ◽  
Zhengrong Shi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Drug Resistance ◽  
Combination Treatment ◽  
Crude Extract ◽  
Biofilm Formation ◽  
Bacterial Resistance ◽  
Antibacterial Properties ◽  
Biofilm Growth ◽  
Antibiotic Combination

The drug resistance of Pseudomonas aeruginosa is a worldwide problem due to its great threat to human health. A crude extract of Angelica dahurica has been proved to have antibacterial properties, which suggested that it may be able to inhibit the biofilm formation of P. aeruginosa; initial exploration had shown that the crude extract could inhibit the growth of P. aeruginosa effectively. After the adaptive dose of coumarin was confirmed to be a potential treatment for the bacteria’s drug resistance, “coumarin-antibiotic combination treatments” (3 coumarins—simple coumarin, imperatorin, and isoimperatorin—combined with 2 antibiotics—ampicillin and ceftazidime) were examined to determine their capability to inhibit P. aeruginosa. The final results showed that (1) coumarin with either ampicillin or ceftazidime significantly inhibited the biofilm formation of P. aeruginosa; (2) coumarin could directly destroy mature biofilms; and (3) the combination treatment can synergistically enhance the inhibition of biofilm formation, which could significantly reduce the usage of antibiotics and bacterial resistance. To sum up, a coumarin-antibiotic combination treatment may be a potential way to inhibit the biofilm growth of P. aeruginosa and provides a reference for antibiotic resistance treatment.

scholarly journals Insights into Class D β-Lactamases Are Revealed by the Crystal Structure of the OXA10 Enzyme from Pseudomonas aeruginosa

Structure ◽  
2000 ◽  
Vol 8 (12) ◽  
pp. 1289-1298 ◽  
Author(s):  
Laurent Maveyraud ◽  
Dasantila Golemi ◽  
Lakshmi P. Kotra ◽  
Samuel Tranier ◽  
Sergei Vakulenko ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Class D

scholarly journals PP-006 Analyse of drug-resistance about clinical isolated Pseudomonas aeruginosa

2009 ◽  
Vol 13 ◽  
pp. S52
Author(s):  
Lie Huang ◽  
Qin Hu ◽  
Runxiang Wu ◽  
Dongmei Zeng ◽  
Xuedong Lu
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Drug Resistance

scholarly journals Crystal Structure of the Outer Membrane Protein OpdK from Pseudomonas aeruginosa

Structure ◽  
2008 ◽  
Vol 16 (7) ◽  
pp. 1027-1035 ◽  
Author(s):  
Shyamasri Biswas ◽  
Mohammad M. Mohammad ◽  
Liviu Movileanu ◽  
Bert van den Berg
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein

Drug-Resistance Patterns of Clinical Isolates of Pseudomonas aeruginosa with Reference to Their Lipopolysaccharide Compositions

Chemotherapy ◽  
1997 ◽  
Vol 43 (5) ◽  
pp. 323-331 ◽  
Author(s):  
Miyuki Hasegawa ◽  
Intetsu Kobayashi ◽  
Takeshi Saika ◽  
Minoru Nishida
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Drug Resistance ◽  
Clinical Isolates ◽  
Resistance Patterns

scholarly journals MiR-331-3p Links to Drug Resistance of Pancreatic Cancer Cells by Activating WNT/β-Catenin Signal via ST7L

2020 ◽  
Vol 19 ◽  
pp. 153303382094580
Author(s):  
Ting Zhan ◽  
Xiaoli Chen ◽  
Xia Tian ◽  
Zheng Han ◽  
Meng Liu ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Drug Resistance ◽  
Multidrug Resistance ◽  
Cancer Cells ◽  
Breast Cancer Resistance Protein ◽  
Cancer Resistance ◽  
Multidrug Resistance Protein 1 ◽  
Pancreatic Cancer Cells ◽  
Resistance Protein ◽  
Multidrug Resistance Related Protein

Background: Pancreatic cancer is an aggressive type of cancer with poor prognosis, short survival rate, and high mortality. Drug resistance is a major cause of treatment failure in the disease. MiR-331-3p has been reported to play an important role in several cancers. We previously showed that miR-331-3p is upregulated in pancreatic cancer and promotes pancreatic cancer cell proliferation and epithelial-to-mesenchymal transition–mediated metastasis by targeting ST7L. However, it is uncertain whether miR-331-3p is involved in drug resistance. Methods: We investigated the relationship between miR-331-3p and pancreatic cancer drug resistance. As part of this, microRNA mimics or inhibitors were transfected into pancreatic cancer cells. Quantitative polymerase chain reaction was used to detect miR-331-3p expression, and flow cytometry was used to detect cell apoptosis. The Cell Counting Kit-8 assay was used to measure the IC50 values of gemcitabine in pancreatic cancer cells. The expression of multidrug resistance protein 1, multidrug resistance-related protein 1, breast cancer resistance protein, β-Catenin, c-Myc, Cyclin D1, Bcl-2, and Caspase-3 was evaluated by Western blotting. Results: We confirmed that miR-331-3p is upregulated in gemcitabine-treated pancreatic cancer cells and plasma from chemotherapy patients. We also confirmed that miR-331-3p inhibition decreased drug resistance by regulating cell apoptosis and multidrug resistance protein 1, multidrug resistance-related protein 1, and breast cancer resistance protein expression in pancreatic cancer cells, whereas miR-331-3p overexpression had the opposite effect. We further demonstrated that miR-331-3p effects in drug resistance were partially reversed by ST7L overexpression. In addition, overexpression of miR-331-3p activated Wnt/β-catenin signaling in pancreatic cancer cells, and ST7L overexpression restored activation of Wnt/β-catenin signaling. Conclusions: Taken together, our data demonstrate that miR-331-3p contributes to drug resistance by activating Wnt/β-catenin signaling via ST7L in pancreatic cancer cells. These data provide a theoretical basis for new targeted therapies in the future.

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