LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 4 of total 4

Search options

  1. Article: A review of global initiatives to fight antibiotic resistance and recent antibiotics׳ discovery.

    Chaudhary, Arpana Sagwal

    Acta pharmaceutica Sinica. B

    2016  Volume 6, Issue 6, Page(s) 552–556

    Abstract: Data from across the world have shown an overall decline in the antibiotic pipeline and continually rising resistance to all first-line and last-resort antibiotics. The gaps in our knowledge of existing prevalence and mechanisms of antibiotic resistance ( ...

    Abstract Data from across the world have shown an overall decline in the antibiotic pipeline and continually rising resistance to all first-line and last-resort antibiotics. The gaps in our knowledge of existing prevalence and mechanisms of antibiotic resistance (ABR) are all too well known. Several decades of antibiotic abuse in humans, animals, and agricultural practices have created health emergency situations and huge socio-economic impact. This paper discusses key findings of the studies conducted by several national and international collaborative organizations on the current state of affairs in ABR. Alongside, a brief overview of the antibacterial agents׳ discovery in recent years approved by the US FDA is discussed.
    Language English
    Publishing date 2016-07-15
    Publishing country Netherlands
    Document type Journal Article
    ISSN 2211-3835
    ISSN 2211-3835
    DOI 10.1016/j.apsb.2016.06.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: A review of global initiatives to fight antibiotic resistance and recent antibiotics׳ discovery

    Arpana Sagwal Chaudhary

    Acta Pharmaceutica Sinica B, Vol 6, Iss 6, Pp 552-

    2016  Volume 556

    Abstract: Data from across the world have shown an overall decline in the antibiotic pipeline and continually rising resistance to all first-line and last-resort antibiotics. The gaps in our knowledge of existing prevalence and mechanisms of antibiotic resistance ( ...

    Abstract Data from across the world have shown an overall decline in the antibiotic pipeline and continually rising resistance to all first-line and last-resort antibiotics. The gaps in our knowledge of existing prevalence and mechanisms of antibiotic resistance (ABR) are all too well known. Several decades of antibiotic abuse in humans, animals, and agricultural practices have created health emergency situations and huge socio-economic impact. This paper discusses key findings of the studies conducted by several national and international collaborative organizations on the current state of affairs in ABR. Alongside, a brief overview of the antibacterial agents׳ discovery in recent years approved by the US FDA is discussed.
    Keywords Antibiotic drug resistance ; Antibacterial drug resistance ; Antimicrobial drugs ; Medicine ; R ; Therapeutics. Pharmacology ; RM1-950
    Language English
    Publishing date 2016-10-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Evaluation of small molecule SecA inhibitors against methicillin-resistant Staphylococcus aureus.

    Jin, Jinshan / Cui, Jianmei / Chaudhary, Arpana Sagwal / Hsieh, Ying-Hsin / Damera, Krishna / Zhang, Hao / Yang, Hsiuchin / Wang, Binghe / Tai, Phang C

    Bioorganic & medicinal chemistry

    2015  Volume 23, Issue 21, Page(s) 7061–7068

    Abstract: Due to the emergence and rapid spread of drug resistance in bacteria, there is an urgent need for the development of novel antimicrobials. SecA, a key component of the general bacterial secretion system required for viability and virulence, is an ... ...

    Abstract Due to the emergence and rapid spread of drug resistance in bacteria, there is an urgent need for the development of novel antimicrobials. SecA, a key component of the general bacterial secretion system required for viability and virulence, is an attractive antimicrobial target. Earlier we reported that systematical dissection of a SecA inhibitor, Rose Bengal (RB), led to the development of novel small molecule SecA inhibitors active against Escherichia coli and Bacillus subtilis. In this study, two potent RB analogs were further evaluated for activities against methicillin-resistant Staphylococcus aureus (MRSA) strains and for their mechanism of actions. These analogs showed inhibition on the ATPase activities of S. aureus SecA1 (SaSecA1) and SecA2 (SaSecA2), and inhibition of SaSecA1-dependent protein-conducting channel. Moreover, these inhibitors reduce the secretion of three toxins from S. aureus and exert potent bacteriostatic effects against three MRSA strains. Our best inhibitor SCA-50 showed potent concentration-dependent bactericidal activity against MRSA Mu50 strain and very importantly, 2-60 fold more potent inhibitory effect on MRSA Mu50 than all the commonly used antibiotics including vancomycin, which is considered the last resort option in treating MRSA-related infections. Protein pull down experiments further confirmed SaSecA1 as a target. Deletion or overexpression of NorA and MepA efflux pumps had minimal effect on the antimicrobial activities against S. aureus, indicating that the effects of SecA inhibitors were not affected by the presence of these efflux pumps. Our studies show that these small molecule analogs target SecA functions, have potent antimicrobial activities, reduce the secretion of toxins, and have the ability to overcome the effect efflux pumps, which are responsible for multi-drug resistance. Thus, targeting SecA is an attractive antimicrobial strategy against MRSA.
    MeSH term(s) Adenosine Triphosphatases/antagonists & inhibitors ; Adenosine Triphosphatases/metabolism ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/pharmacology ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/metabolism ; Binding Sites ; Drug Evaluation, Preclinical ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Kinetics ; Light ; Membrane Transport Proteins/metabolism ; Methicillin-Resistant Staphylococcus aureus/drug effects ; Methicillin-Resistant Staphylococcus aureus/enzymology ; Microbial Sensitivity Tests ; Molecular Docking Simulation ; Oxidation-Reduction ; Protein Structure, Tertiary ; Rose Bengal/chemistry ; Rose Bengal/pharmacology ; SEC Translocation Channels ; Staphylococcus aureus/drug effects
    Chemical Substances Anti-Bacterial Agents ; Anti-Infective Agents ; Bacterial Proteins ; Enzyme Inhibitors ; Membrane Transport Proteins ; SEC Translocation Channels ; SecA protein, Bacteria (119129-39-4) ; Rose Bengal (1ZPG1ELY14) ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2015-11-01
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1161284-8
    ISSN 1464-3391 ; 0968-0896
    ISSN (online) 1464-3391
    ISSN 0968-0896
    DOI 10.1016/j.bmc.2015.09.027
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3815: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors.

    Cui, Jianmei / Jin, Jinshan / Chaudhary, Arpana Sagwal / Hsieh, Ying-hsin / Zhang, Hao / Dai, Chaofeng / Damera, Krishna / Chen, Weixuan / Tai, Phang C / Wang, Binghe

    ChemMedChem

    2015  Volume 11, Issue 1, Page(s) 43–56

    Abstract: SecA, a key component of the bacterial Sec-dependent secretion pathway, is an attractive target for the development of new antimicrobial agents. Through a combination of virtual screening and experimental exploration of the surrounding chemical space, we ...

    Abstract SecA, a key component of the bacterial Sec-dependent secretion pathway, is an attractive target for the development of new antimicrobial agents. Through a combination of virtual screening and experimental exploration of the surrounding chemical space, we identified a hit bistriazole SecA inhibitor, SCA-21, and studied a series of analogues by systematic dissections of the core scaffold. Evaluation of these analogues allowed us to establish an initial structure-activity relationship in SecA inhibition. The best compounds in this group are potent inhibitors of SecA-dependent protein-conducting channel activity and protein translocation activity at low- to sub-micromolar concentrations. They also have minimal inhibitory concentration (MIC) values against various strains of bacteria that correlate well with the SecA and protein translocation inhibition data. These compounds are effective against methicillin-resistant Staphylococcus aureus strains with various levels of efflux pump activity, indicating the capacity of SecA inhibitors to null the effect of multidrug resistance. Results from studies of drug-affinity-responsive target stability and protein pull-down assays are consistent with SecA as a target for these compounds.
    MeSH term(s) Adenosine Triphosphatases/antagonists & inhibitors ; Adenosine Triphosphatases/metabolism ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/metabolism ; Dose-Response Relationship, Drug ; Drug Design ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Membrane Transport Proteins/metabolism ; Methicillin-Resistant Staphylococcus aureus/drug effects ; Methicillin-Resistant Staphylococcus aureus/enzymology ; Microbial Sensitivity Tests ; Molecular Structure ; Pyrimidines/chemistry ; Pyrimidines/pharmacology ; SEC Translocation Channels ; SecA Proteins ; Structure-Activity Relationship ; Triazoles/chemistry ; Triazoles/pharmacology
    Chemical Substances Bacterial Proteins ; Enzyme Inhibitors ; Membrane Transport Proteins ; Pyrimidines ; SEC Translocation Channels ; Triazoles ; Adenosine Triphosphatases (EC 3.6.1.-) ; SecA Proteins (EC 7.4.2.4) ; pyrimidine (K8CXK5Q32L)
    Language English
    Publishing date 2015-11-26
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2218496-X
    ISSN 1860-7187 ; 1860-7179
    ISSN (online) 1860-7187
    ISSN 1860-7179
    DOI 10.1002/cmdc.201500447
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6280: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top