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1

S., A. Abdullahi, H. Arzai A., Yusuf I., et al. "Molecular Detection of New Delhi Metallo Beta Lactamase 1 (NDM-1) Producing Bacterial Isolates in Kano- Northwestern Nigeria." Annual Research & Review in Biology 14, no. 4 (2017): 1–6. https://doi.org/10.9734/ARRB/2017/33477.

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New Delhi Metallo Beta Lactamase 1 (NDM-1) is an enzyme with zinc ions at its active site that cleaves the amide bond of β-lactam ring and provides resistance against major classes of β-lactam antibiotics. The molecular detection of NDM-1 producing bacterial isolates from tertiary Hospitals in Kano was investigated. A total of 500 bacterial isolates of <em>Enterobacteriaceae </em>and <em>Pseudomonas aeruginosa</em> from samples of blood, urine, catheter tip were screened for NDM-1 over a period of 12 months. The isolates were screened preliminarily for carbapenemases using meropenem (10 µg) an
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2

He, Song, and Jin Yuan. "Homology Analysis of New Delhi metallo-B-lactamase (NDM-1) Gene Sequences from Enterobacter." Acta Informatica Medica 20, no. 2 (2012): 118. http://dx.doi.org/10.5455/aim.2012.20.118-128.

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3

Ahsan, Sunjukta, Anindita Bhowmik, Sharmistha Goswami, and Nasir Uddin. "Detection of New Delhi Metallo b Lactamase gene in Uropathogenic E. coli." Bangladesh Journal of Microbiology 36, no. 1 (2019): 29–33. http://dx.doi.org/10.3329/bjm.v36i1.44280.

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The rapid dissemination of antibiotic resistant E. coli is now a worldwide problem. In this study, a total of twenty E. coli obtained from stool were selected to determine resistance to beta lactam antibiotics. Beta–Lactamase are enzymes produced by bacteria that provide multi resistance to beta lactam antibiotics such as penicillin, cephalosporin, cephamycin and carbapenems. Of these isolates (n = 20), 35% were found resistant to Amoxicillin Clavulanate, 5% to Imipenem, 50% to Ceftriaxone and 75% to Ampicillin. PCR amplification confirmed the presence of the New Delhi beta-lactamase gene (bla
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4

Hussein, Zeyad, Haider Kadhim, and Jabbar Hassan. "DETECTION OF NEW DELHI METALLO-BETA-LACTAMASE-1 (BLANDM-1) IN CARBAPENEM-RESISTANT PSEUDOMONAS AERUGINOSA ISOLATED FROM CLINICAL SAMPLES IN WASIT HOSPITALS." Iraqi Journal of Medical Sciences 16, no. 3 (2018): 239–46. http://dx.doi.org/10.22578/ijms.16.3.3.

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Background:Pseudomonas aeruginosa (P. aeruginosa) infections are clinical problem, it is a difficult to treat because of high resistant to many antibiotics (Multi-drug resistant) and a high risk of emergence of resistance during therapy. Carbapenems are therapeutic choice against infections caused by Gram-negative bacilli including strains of P. aeruginosa. New Delhi metallo-β-lactamase-1 (blaNDM-1) gene, an acquired class B carbapenemase. Dissemination predominantly involves transfer of the blaNDM-1 gene among promiscuous plasmids and clonal outbreaks. Bacteria with NDM-1 are typically resist
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Moreira, Mirna Giselle, Lidia Miranda Barreto, Vera Lúcia dos Santos, Andrea Souza Monteiro, Vandack Nobre, and Simone Gonçalves dos Santos. "Rapid detection of the New Delhi metallo-b-lactamase 1 (NDM-1) gene by loop-mediated isothermal amplification (LAMP)." Journal of Clinical Laboratory Analysis 32, no. 4 (2017): e22323. http://dx.doi.org/10.1002/jcla.22323.

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6

Alfei, Silvana, та Guendalina Zuccari. "Recommendations to Synthetize Old and New β-Lactamases Inhibitors: A Review to Encourage Further Production". Pharmaceuticals 15, № 3 (2022): 384. http://dx.doi.org/10.3390/ph15030384.

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The increasing emergence of bacteria producing β-lactamases enzymes (BLEs), able to inactivate the available β-lactam antibiotics (BLAs), causing the hydrolytic opening of their β-lactam ring, is one of the global major warnings. According to Ambler classification, BLEs are grouped in serine-BLEs (SBLEs) of class A, C, and D, and metal-BLEs (MBLEs) of class B. A current strategy to restore no longer functioning BLAs consists of associating them to β-lactamase enzymes inhibitors (BLEsIs), which, interacting with BLEs, prevent them hydrolyzing to the associated antibiotic. Worryingly, the inhibi
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7

Sharma, Shubhangi, and Anshu Sharma. "Study of New Delhi Metallo Beta Lactamase and Oxacillinase beta Lactamase coexistence in Carbapenem Resistant Klebsiella Pneumoniae Obtained from Bloodstream Infections." International Journal of Health Sciences and Research 15, no. 1 (2025): 56–62. https://doi.org/10.52403/ijhsr.20250108.

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Background: Carbapenem‑resistant Klebsiella pneumoniae(CRkp) is of utmost clinical importance because they challenge the armamentarium of the treating clinicians, hampering current treatment strategies. This study aimed to compare the outcomes of oxacillinases β-lactamases (OXA-48) and New Delhi metallo-β-lactamase (NDM-1)-producing CRKP isolates, the two most common carbapenemases reported from Worldwide including India, obtained from patients with bloodstream infections in an ICU in a tertiary care center in southern part of Rajasthan and to compare the different laboratory methods for their
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8

Biedenbach, D., S. Bouchillon, M. Hackel та ін. "Dissemination of NDM Metallo-β-Lactamase Genes among Clinical Isolates of Enterobacteriaceae Collected during the SMART Global Surveillance Study from 2008 to 2012". Antimicrobial Agents and Chemotherapy 59, № 2 (2014): 826–30. http://dx.doi.org/10.1128/aac.03938-14.

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ABSTRACTThe prevalence of carbapenemase enzymes continues to increase. Among the Ambler class B enzymes is the New Delhi metallo-β-lactamase (NDM). This particular enzyme is capable of hydrolyzing nearly all β-lactam antimicrobial agents and has spread rapidly, becoming a global problem. Therapeutic treatment options for patients infected with isolates which produce this enzyme are difficult to manage, as cross-resistance to other antimicrobial classes is common. The Study for Monitoring Antimicrobial Resistance Trends (SMART) is a global surveillance study evaluating the antimicrobial suscept
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9

Alfei, Silvana, та Anna Maria Schito. "β-Lactam Antibiotics and β-Lactamase Enzymes Inhibitors, Part 2: Our Limited Resources". Pharmaceuticals 15, № 4 (2022): 476. http://dx.doi.org/10.3390/ph15040476.

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β-lactam antibiotics (BLAs) are crucial molecules among antibacterial drugs, but the increasing emergence of resistance to them, developed by bacteria producing β-lactamase enzymes (BLEs), is becoming one of the major warnings to the global public health. Since only a small number of novel antibiotics are in development, a current clinical approach to limit this phenomenon consists of administering proper combinations of β-lactam antibiotics (BLAs) and β-lactamase inhibitors (BLEsIs). Unfortunately, while few clinically approved BLEsIs are capable of inhibiting most class-A and -C serine β-lac
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10

Wang, Yanling, Xiaodi Sun, Fanrong Kong, et al. "Specific NDM-1 Inhibitor of Isoliquiritin Enhances the Activity of Meropenem against NDM-1-positive Enterobacteriaceae in vitro." International Journal of Environmental Research and Public Health 17, no. 6 (2020): 2162. http://dx.doi.org/10.3390/ijerph17062162.

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NDM-1-positive Enterobacteriaceae have caused serious clinical infections, with high mortality rates. Carbapenem was the ultimate expectation for the treatment of such infections in clinical practice. However, since the discovery of plasmid-mediated New Delhi metallo-β-lactamase-1 (NDM-1), the efficient therapeutic effects of carbapenems have been increasingly restricted. Here, we identified isoliquiritin, a novel specific inhibitor of the NDM-1 enzyme that restored the activity of carbapenem against NDM-1-producing E. coli isolates and K. pneumoniae isolates without affecting the growth of ba
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11

Krivitskaya, Alexandra V., та Maria G. Khrenova. "Boronic Acids as Prospective Inhibitors of Metallo-β-Lactamases: Efficient Chemical Reaction in the Enzymatic Active Site Revealed by Molecular Modeling". Molecules 26, № 7 (2021): 2026. http://dx.doi.org/10.3390/molecules26072026.

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Boronic acids are prospective compounds in inhibition of metallo-β-lactamases as they form covalent adducts with the catalytic hydroxide anion in the enzymatic active site upon binding. We compare this chemical reaction in the active site of the New Delhi metallo-β-lactamase (NDM-1) with the hydrolysis of the antibacterial drug imipenem. The nucleophilic attack occurs with the energy barrier of 14 kcal/mol for imipenem and simultaneously upon binding a boronic acid inhibitor. A boron atom of an inhibitor exhibits stronger electrophilic properties than the carbonyl carbon atom of imipenem in a
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12

VonBank, Brittany, Sean O’Malley, Paula Snippes Vagnone та ін. "2462. Public Health Response to Contain the First Outbreak of New Delhi Metallo-β-Lactamase-Producing Klebsiella pneumoniae in Minnesota". Open Forum Infectious Diseases 6, Supplement_2 (2019): S852. http://dx.doi.org/10.1093/ofid/ofz360.2140.

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Abstract Background Carbapenem-resistant Enterobacteriaceae (CRE) producing the New Delhi-metallo-β-lactamase (NDM) carbapenemase are uncommon in the United States but are a serious threat for untreatable antibiotic-resistant infections. In Minnesota (MN), NDM-CRE is typically associated with receipt of healthcare abroad. We describe the public health response to contain the first outbreak of NDM-CRE in MN. Methods CRE is reportable, with isolate submission to the MN Department of Health (MDH) for MALDI-TOF identification, phenotypic carbapenemase production testing, and PCR for carbapenemase
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13

McNamara, Kiara, Caroline Habrun, W. Wyatt Wilson та ін. "New Delhi metallo-β-lactamase–producing Escherichia coli among dogs at an animal rescue facility—Wisconsin, 2022". Antimicrobial Stewardship & Healthcare Epidemiology 3, S2 (2023): s90. http://dx.doi.org/10.1017/ash.2023.354.

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Background: New Delhi Metallo-β-lactamase (NDM)–producing Escherichia coli are highly resistant organisms that spread quickly. In the United States, organisms with blaNDM are rare and mostly associated with healthcare settings. However, in other countries, blaNDM can be relatively common and are found in community settings. State veterinary and public health partners detected NDM E. coli in a dog from Iran living at a Wisconsin animal rescue facility (ARF), where 40% of dogs had international origins. We investigated to determine spread among dog and human contacts and prevent further transmis
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14

Smith, Nicholas M., Liang Chen, Katie Rose Boissonneault, et al. "1325. Things that go Bump in the Night: Combating Klebsiella pneumoniae co-producing New Delhi metallo-beta-lactamase (NDM) and Mobile Colistin Resistance (MCR)." Open Forum Infectious Diseases 7, Supplement_1 (2020): S673. http://dx.doi.org/10.1093/ofid/ofaa439.1507.

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Abstract Background The scourge of MBLs among Gram negatives, such New Delhi Metallo-beta-lactamase-producing Klebsiella pneumoniae, has resulted in an overwhelming need for new treatmens. Worryingly, additional acquisition of plasmid-mediated polymyxin resistance through the mcr gene can produce strains resistant to all last line agents. The novel combination of aztreonam (ATM, which is not an MBL substrate) with avibactam (AVI, to inhibit extended spectrum beta-lactamases that inactivate ATM) has been proposed to restore ATM activity. Methods K. pneumoniae SZ04 harboring blaNDM-5, blaCTX-M-5
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15

Lim, Tze-Peng, Jun-Yuan Ho, Jocelyn Qi-Min Teo, et al. "In Vitro Susceptibility to Ceftazidime-Avibactam and Comparator Antimicrobial Agents of Carbapenem-Resistant Enterobacterales Isolates." Microorganisms 11, no. 9 (2023): 2158. http://dx.doi.org/10.3390/microorganisms11092158.

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The emergence of carbapenem-resistant Enterobacterales (CRE) has been recognized as a significant concern globally. Ceftazidime/avibactam (CZA) is a novel β-lactam/β-lactamase inhibitor that has demonstrated activity against isolates producing class A, C, and D β-lactamases. Here-in, we evaluated the in vitro activity of CZA and comparator antimicrobial agents against 858 CRE isolates, arising from the Southeast Asian region, collected from a large tertiary hospital in Singapore. These CRE isolates mainly comprised Klebsiella pneumoniae (50.5%), Escherichia coli (29.4%), and Enterobacter cloac
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16

Kim, Young Ah, Se Ju Lee, Yoon Soo Park, et al. "Risk Factors for Carbapenemase-Producing Enterobacterales Infection or Colonization in a Korean Intensive Care Unit: A Case–Control Study." Antibiotics 9, no. 10 (2020): 680. http://dx.doi.org/10.3390/antibiotics9100680.

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The purpose of this study is to identify the factors related to the infection and/or colonization of carbapenemase-producing Enterobacterales (CPE) based on clinical and microbiological data for patients in the intensive care unit (ICU). All patients admitted to medical ICU were screened for CPE on admission and weekly, and this 1:2 case–control study included patients with CPE identified by screening or clinical cultures from 2017 to 2018. The clonal relatedness was evaluated by pulsed-field gel electrophoresis (PFGE). A total of 45 CPE patients were identified with a prevalence of 3.8%. The
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17

Alnimr, Amani M. "Predictive role of culture-based MIC testing vs. genotyping for carbapenem-resistant Enterobacterales in a non-universal screening, highly resourced setting." Electronic Journal of General Medicine 20, no. 4 (2023): em495. http://dx.doi.org/10.29333/ejgm/13181.

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A lack of evidence of accuracy for various testing modalities for carbapenem-resistant Enterobacterales (CRE) reduces the efficiency of screening and delays the isolation of carriers. This study examined the performance of phenotypic detection of CRE in comparison to molecular testing. A cross-sectional study was conducted in an academic medical institution in Saudi Arabia on CRE-screened patients during a 36-month period (April 1, 2019, through March 31, 2022). Cases were followed up for their susceptibility status by the phenotypic gradient method and genotypes. Of 3,116 samples tested, 359
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18

Li, Xin, Daniel Goodman, Sarah A. Mihalov, and Matthew Oswald. "Poster 118 New Delhi Metallo-B-Lactamase (NDM-1) Producing Klebsiella Pneumoniae Urinary Tract Infection (UTI) in Acute Inpatient Rehabilitation After Right Hip Open Reduction Internal Fixation Revision (ORIF): A Case Report." PM&R 6, no. 9 (2014): S224—S225. http://dx.doi.org/10.1016/j.pmrj.2014.08.512.

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19

Bhaskar, Emmanuel. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 749. http://dx.doi.org/10.1016/s1473-3099(10)70238-3.

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20

Sirohi, Bhawna. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 750. http://dx.doi.org/10.1016/s1473-3099(10)70240-1.

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21

Tempe, Deepak K. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 750–51. http://dx.doi.org/10.1016/s1473-3099(10)70241-3.

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22

Goel, Neeraj, та Chand Wattal. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 751. http://dx.doi.org/10.1016/s1473-3099(10)70242-5.

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23

Gibb, Alan P., та Alison K. McCallum. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 751–52. http://dx.doi.org/10.1016/s1473-3099(10)70243-7.

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24

de Costa, Ayesha, та Dileep Mavalankar. "New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 11 (2010): 752. http://dx.doi.org/10.1016/s1473-3099(10)70244-9.

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Lorenc, Karol, Magdalena Kozioł, Alicja Sobek, et al. "Cefiderocol - a promising new antibiotic for the antibiotic-resistant pathogens of the highest epidemiological priority." Journal of Education, Health and Sport 9, no. 5 (2019): 81–88. https://doi.org/10.5281/zenodo.2667284.

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<strong>Lorenc Karol, Kozioł Magdalena, Sobek Alicja, Pawlicki Mateusz, Łopuszyńska Anna, Misztal Zofia, Lewicki Marcin, Smoleń&nbsp;Agata. </strong><strong>Cefiderocol - a promising new antibiotic for the </strong><strong>antibiotic-resistant </strong><strong>pathogens of the highest epidemiological priority</strong><strong>. </strong><strong>Journal of Education, Health and Sport. 2019;9(5):</strong><strong>81</strong><strong>-8</strong><strong>8</strong><strong>. eISSN 2391-8306. DOI</strong><strong> </strong><strong>http://dx.doi.org/10.5281/zenodo.2667284</strong> <strong>http://ojs.ukw.e
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26

Walsh, T. R. "New Delhi metallo- -lactamase-1: detection and prevention." Canadian Medical Association Journal 183, no. 11 (2011): 1240–41. http://dx.doi.org/10.1503/cmaj.111100.

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Walsh, Timothy R., Mark A. Toleman, Jayanta B. Sarma, Seema Irfan, Neil Woodford та David M. Livermore. "New Delhi metallo-β-lactamase 1 – Authors' reply". Lancet Infectious Diseases 10, № 11 (2010): 752–54. http://dx.doi.org/10.1016/s1473-3099(10)70245-0.

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28

Green, Victoria L., Anil Verma, Raymond J. Owens, Simon E. V. Phillips та Stephen B. Carr. "Structure of New Delhi metallo-β-lactamase 1 (NDM-1)". Acta Crystallographica Section F Structural Biology and Crystallization Communications 67, № 10 (2011): 1160–64. http://dx.doi.org/10.1107/s1744309111029654.

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29

Shakil, S., E. I. Azhar, S. Tabrez та ін. "New Delhi Metallo-β-Lactamase (NDM-1): An Updates". Journal of Chemotherapy 23, № 5 (2011): 263–65. http://dx.doi.org/10.1179/joc.2011.23.5.263.

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Koh, Tse Hsien, Cheng Teng Khoo, Limin Wijaya та ін. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 828. http://dx.doi.org/10.1016/s1473-3099(10)70274-7.

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Göttig, Stephan, Yvonne Pfeifer, Thomas A. Wichelhaus та ін. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 828–29. http://dx.doi.org/10.1016/s1473-3099(10)70275-9.

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32

Hammerum, Anette M., Mark A. Toleman, Frank Hansen та ін. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 829–30. http://dx.doi.org/10.1016/s1473-3099(10)70276-0.

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33

Leverstein-Van Hall, Maurine A., James Cohen Stuart, Guido M. Voets, Dik Versteeg, Thijs Tersmette та Ad C. Fluit. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 830–31. http://dx.doi.org/10.1016/s1473-3099(10)70277-2.

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Bogaerts, Pierre, Alexia Verroken, Beatrice Jans, Olivier Denis та Youri Glupczynski. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 831–32. http://dx.doi.org/10.1016/s1473-3099(10)70278-4.

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Poirel, Laurent, Cécile Hombrouck-Alet, Claire Freneaux, Sandrine Bernabeu та Patrice Nordmann. "Global spread of New Delhi metallo-β-lactamase 1". Lancet Infectious Diseases 10, № 12 (2010): 832. http://dx.doi.org/10.1016/s1473-3099(10)70279-6.

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Thomas, Pei W., Min Zheng, Shanshan Wu та ін. "Characterization of Purified New Delhi Metallo-β-lactamase-1". Biochemistry 50, № 46 (2011): 10102–13. http://dx.doi.org/10.1021/bi201449r.

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Pillai, D. R., A. McGeer, and D. E. Low. "New Delhi metallo- -lactamase-1 in Enterobacteriaceae: emerging resistance." Canadian Medical Association Journal 183, no. 1 (2011): 59–64. http://dx.doi.org/10.1503/cmaj.101487.

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Ghosh, Amit, Anirban Sarkar, Goutam Chowdhury, Gururajaperumal Pazhani, and Thandavarayan Ramamurthy. "Overview on the New Delhi Metallo-B-lactamase (NDM)-producers." Proceedings of the Indian National Science Academy 80, no. 3 (2014): 547. http://dx.doi.org/10.16943/ptinsa/2014/v80i3/55132.

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Rolain, J. M., P. Parola, and G. Cornaglia. "New Delhi metallo-beta-lactamase (NDM-1): towards a new pandemia?" Clinical Microbiology and Infection 16, no. 12 (2010): 1699–701. http://dx.doi.org/10.1111/j.1469-0691.2010.03385.x.

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Huang, Jinwei, Minghua Wang, Hui Ding та ін. "New Delhi Metallo-β-Lactamase-1 in Carbapenem-ResistantSalmonellaStrain, China". Emerging Infectious Diseases 19, № 12 (2013): 2049–51. http://dx.doi.org/10.3201/eid1912.130051.

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41

Li, Jun-Jie, L. Silvia Munoz-Price, Caressa N. Spychala, Dennise DePascale та Yohei Doi. "New Delhi Metallo-β-Lactamase-1–ProducingKlebsiella pneumoniae, Florida, USA1". Emerging Infectious Diseases 22, № 4 (2016): 744–46. http://dx.doi.org/10.3201/eid2204.151176.

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Paget, James T., та Timothy S. Burge. "Keeping New Delhi Metallo-β-lactamase-1 at the Door". Journal of Burn Care & Research 35, № 2 (2014): e125-e127. http://dx.doi.org/10.1097/bcr.0b013e3182920d41.

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43

Thomas, Chris S., Doug R. Braun, Jose Luis Olmos, et al. "Pyridine-2,6-Dithiocarboxylic Acid and Its Metal Complexes: New Inhibitors of New Delhi Metallo -Lactamase-1." Marine Drugs 18, no. 6 (2020): 295. http://dx.doi.org/10.3390/md18060295.

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Carbapenem-resistant Enterobacteriaceae continue to threaten human health worldwide with few effective treatment options. New Delhi metallo--lactamase (NDM) enzymes are a contributing element that drive resistance to many -lactam- and carbapenem-based antimicrobials. Many NDM inhibitors are known, yet none are clinically viable. In this study, we present and characterize a new class of NDM-1 inhibitors based on a pyridine-2,6-dithiocarboxylic acid metal complex scaffold. These complexes display varied and unique activity profiles against NDM-1 in kinetic assays and serve to increase the effect
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44

Gan, Maoluo, Yufeng Liu, Yinlei Bai та ін. "Polyketides with New Delhi Metallo-β-lactamase 1 Inhibitory Activity fromPenicilliumsp." Journal of Natural Products 76, № 9 (2013): 1535–40. http://dx.doi.org/10.1021/np4000944.

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45

Ahmad, Nayeem, Syed Manazir Ali та Asad U. Khan. "First reported New Delhi metallo-β-lactamase-1-producing Cedecea lapagei". International Journal of Antimicrobial Agents 49, № 1 (2017): 118–19. http://dx.doi.org/10.1016/j.ijantimicag.2016.10.001.

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Ge, Ying, Peng-Wei Kang, Jia-Qi Li та ін. "Thiosemicarbazones exhibit inhibitory efficacy against New Delhi metallo-β-lactamase-1 (NDM-1)". Journal of Antibiotics 74, № 9 (2021): 574–79. http://dx.doi.org/10.1038/s41429-021-00440-3.

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47

Shen, Bingzheng, Yan Yu, Hui Chen та ін. "Inhibitor Discovery of Full-Length New Delhi Metallo-β-Lactamase-1 (NDM-1)". PLoS ONE 8, № 5 (2013): e62955. http://dx.doi.org/10.1371/journal.pone.0062955.

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48

Liu, Xiao-Long, Yang Xiang, Cheng Chen та Ke-Wu Yang. "Azolylthioacetamides as potential inhibitors of New Delhi metallo-β-lactamase-1 (NDM-1)". Journal of Antibiotics 72, № 2 (2018): 118–21. http://dx.doi.org/10.1038/s41429-018-0121-4.

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Hsueh, Po-Ren. "New Delhi Metallo-β-lactamase-1 (NDM-1): An Emerging Threat Among Enterobacteriaceae". Journal of the Formosan Medical Association 109, № 10 (2010): 685–87. http://dx.doi.org/10.1016/s0929-6646(10)60111-8.

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Shen, Bingzheng, Chengliang Zhu, Xiang Gao, Gang Liu, Jinchun Song та Yan Yu. "Oligopeptides as full-length New Delhi metallo-β-lactamase-1 (NDM-1) inhibitors". PLOS ONE 12, № 5 (2017): e0177293. http://dx.doi.org/10.1371/journal.pone.0177293.

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