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  1. Article: An Enzymatic Route to the Synthesis of Tricyclic Fused Hexahydrofuranofuran P2-Ligand for a Series of Highly Potent HIV-1 Protease Inhibitors.

    Ghosh, Arun K / Sharma, Ashish / Ghazi, Somayeh

    Tetrahedron letters

    2024  Volume 140

    Abstract: We describe a stereoselective synthesis of an optically active ( ... ...

    Abstract We describe a stereoselective synthesis of an optically active (1
    Language English
    Publishing date 2024-03-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 204287-3
    ISSN 1873-3581 ; 0040-4039
    ISSN (online) 1873-3581
    ISSN 0040-4039
    DOI 10.1016/j.tetlet.2024.155013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2837: Show issues Location:
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  2. Article ; Online: In silico

    Moosavi, Fatemeh / Damghani, Tahereh / Ghazi, Somayeh / Pirhadi, Somayeh

    Journal of receptor and signal transduction research

    2022  Volume 42, Issue 6, Page(s) 549–561

    Abstract: Purpose: Cancer is a significant public health problem and ranks as a leading cause of death globally. Multidrug resistance (MDR) affects the therapeutic potential of conventional chemotherapeutic agents in cancer chemotherapy. Receptor tyrosine kinases ...

    Abstract Purpose: Cancer is a significant public health problem and ranks as a leading cause of death globally. Multidrug resistance (MDR) affects the therapeutic potential of conventional chemotherapeutic agents in cancer chemotherapy. Receptor tyrosine kinases (RTKs) are enzymes whose aberrant activation contributes to the tumorigenesis of various types of cancers. The ability of several RTKs, such as c-Met, to reverse ABC transporters mediated MDR was shown before. We aimed to explore the ability of c-Met inhibitors to circumvent MDR in cancer by inhibiting the ABCB1 transporter using
    Methods: Docking virtual screening of several potent and structurally diverse c-Met inhibitors were applied to find repurposed candidates to target the ATP binding sites and drug-substrate binding pockets of the ABCB1 transporter. The selected candidate was subjected to molecular dynamics simulations.
    Results: Based on docking findings, among 19 clinical c-Met inhibitors, several drugs, particularly golvatinib, exerted the affinity to both ATP binding sites in the nucleotide-binding domains (NBDs) as well as the drug-substrate binding site in the transmembrane domains (TMDs). Moreover, several non-clinical c-Met inhibitors obtained from the ChEMBL database had strong interactions with TMDs and NBDs, among which CHEMBL1950194 and CHEMBL2385194 compounds showed the highest binding affinity, respectively. Additionally, as a potential repositioning drug, MD simulation studies of golvatinib, corroborated the docking results.
    Conclusion: We applied docking and molecular dynamics simulations to screen the potential c-Met inhibitors as the MDR reversing agents targeting ATP and drug-substrate binding sites, and the results suggested several repurposed candidate drugs.
    MeSH term(s) Tyrosine Kinase Inhibitors ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Nucleotides/metabolism ; Nucleotides/pharmacology ; Drug Resistance, Neoplasm ; Cell Line, Tumor ; Neoplasm Proteins ; Drug Resistance, Multiple ; Binding Sites ; Adenosine Triphosphate ; Antineoplastic Agents/pharmacology
    Chemical Substances Tyrosine Kinase Inhibitors ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Nucleotides ; Neoplasm Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Antineoplastic Agents
    Language English
    Publishing date 2022-06-15
    Publishing country England
    Document type Journal Article
    ZDB-ID 1230969-2
    ISSN 1532-4281 ; 1079-9893
    ISSN (online) 1532-4281
    ISSN 1079-9893
    DOI 10.1080/10799893.2022.2086988
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    Zs.A 1643: Show issues Location:
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  3. Article ; Online: Type II c-Met inhibitors: molecular insight into crucial interactions for effective inhibition.

    Damghani, Tahereh / Elyasi, Maryam / Pirhadi, Somayeh / Haghighijoo, Zahra / Ghazi, Somayeh

    Molecular diversity

    2021  Volume 26, Issue 3, Page(s) 1411–1423

    Abstract: The c-Met tyrosine kinase plays an important role in human cancers. Preclinical studies demonstrated that c-Met is over-expressed, mutated and amplified in a variety of human tumor types and design of more potent c-Met inhibitors is a priority. In this ... ...

    Abstract The c-Met tyrosine kinase plays an important role in human cancers. Preclinical studies demonstrated that c-Met is over-expressed, mutated and amplified in a variety of human tumor types and design of more potent c-Met inhibitors is a priority. In this study, 14 molecular dynamics simulations of potent type II c-Met inhibitors were run to resolve the critical interactions responsible for high affinity of ligands towards c-Met considering the essential flexibility of protein-ligand interactions. Residues Phe1223 and Tyr1159, involved in pi-pi interactions were recognized as the most effective residues in the ligand binding in terms of binding free energies. Hydrogen bond interaction with Met1160 was also found necessary for effective type II ligand binding to c-Met.
    MeSH term(s) Humans ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Kinase Inhibitors/chemistry ; Thermodynamics
    Chemical Substances Ligands ; Protein Kinase Inhibitors
    Language English
    Publishing date 2021-07-11
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1376507-3
    ISSN 1573-501X ; 1381-1991
    ISSN (online) 1573-501X
    ISSN 1381-1991
    DOI 10.1007/s11030-021-10267-7
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4946: Show issues Location:
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  4. Article ; Online: Exploration of P1 and P4 modifications of nirmatrelvir: Design, synthesis, biological evaluation, and X-ray structural studies of SARS-CoV-2 Mpro inhibitors.

    Ghosh, Arun K / Yadav, Monika / Iddum, Satyanarayana / Ghazi, Somayeh / Lendy, Emma K / Jayashankar, Uttara / Beechboard, Sydney N / Takamatsu, Yuki / Hattori, Shin-Ichiro / Aamano, Masayuki / Higashi-Kuwata, Nobuyo / Mitsuya, Hiroaki / Mesecar, Andrew D

    European journal of medicinal chemistry

    2024  Volume 267, Page(s) 116132

    Abstract: We report the synthesis, biological evaluation, and X-ray structural studies of a series of SARS-CoV-2 Mpro inhibitors based upon the X-ray crystal structure of nirmatrelvir, an FDA approved drug that targets the main protease of SARS-CoV-2. The studies ... ...

    Abstract We report the synthesis, biological evaluation, and X-ray structural studies of a series of SARS-CoV-2 Mpro inhibitors based upon the X-ray crystal structure of nirmatrelvir, an FDA approved drug that targets the main protease of SARS-CoV-2. The studies involved examination of various P4 moieties, P1 five- and six-membered lactam rings to improve potency. In particular, the six-membered P1 lactam ring analogs exhibited high SARS-CoV-2 Mpro inhibitory activity. Several compounds effectively blocked SARS-CoV-2 replication in VeroE6 cells. One of these compounds maintained good antiviral activity against variants of concern including Delta and Omicron variants. A high-resolution X-ray crystal structure of an inhibitor bound to SARS-CoV-2 Mpro was determined to gain insight into the ligand-binding properties in the Mpro active site.
    MeSH term(s) Humans ; X-Rays ; SARS-CoV-2 ; COVID-19 ; Lactams ; Leucine ; Nitriles ; Protease Inhibitors/pharmacology ; Antiviral Agents/pharmacology ; Molecular Docking Simulation
    Chemical Substances Lactams ; Leucine (GMW67QNF9C) ; Nitriles ; Protease Inhibitors ; Antiviral Agents
    Language English
    Publishing date 2024-02-01
    Publishing country France
    Document type Journal Article
    ZDB-ID 188597-2
    ISSN 1768-3254 ; 0009-4374 ; 0223-5234
    ISSN (online) 1768-3254
    ISSN 0009-4374 ; 0223-5234
    DOI 10.1016/j.ejmech.2024.116132
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    Zs.B 784: Show issues Location:
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  5. Article ; Online: Aurones and derivatives as promising New Delhi metallo-β-lactamase (NDM-1) inhibitors.

    Caburet, Jérémy / Verdirosa, Federica / Moretti, Matis / Roulier, Brayan / Simoncelli, Giorgia / Haudecoeur, Romain / Ghazi, Somayeh / Jamet, Hélène / Docquier, Jean-Denis / Boucherle, Benjamin / Peuchmaur, Marine

    Bioorganic & medicinal chemistry

    2023  Volume 97, Page(s) 117559

    Abstract: Bacterial resistance is undoubtedly one of the main public health concerns especially with the emergence of metallo-β-lactamases (MBLs) able to hydrolytically inactivate β-lactam antibiotics. Currently, there are no inhibitors of MBLs in clinical use to ... ...

    Abstract Bacterial resistance is undoubtedly one of the main public health concerns especially with the emergence of metallo-β-lactamases (MBLs) able to hydrolytically inactivate β-lactam antibiotics. Currently, there are no inhibitors of MBLs in clinical use to rescue antibiotic action and the New Delhi metallo-β-lactamase-1 (NDM-1) is still considered as one of the most relevant targets for inhibitor development. Following a fragment-based strategy to find new NDM-1 inhibitors, we identified aurone as a promising scaffold. A series of 60 derivatives were then evaluated and two of them were identified as promising inhibitors with K
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Benzofurans ; beta-Lactamase Inhibitors/pharmacology ; beta-Lactamase Inhibitors/chemistry ; beta-Lactamases/chemistry ; Microbial Sensitivity Tests
    Chemical Substances Anti-Bacterial Agents ; aurone ; Benzofurans ; beta-Lactamase Inhibitors ; beta-lactamase NDM-1 (EC 3.5.2.6) ; beta-Lactamases (EC 3.5.2.6)
    Language English
    Publishing date 2023-12-12
    Publishing country England
    Document type Journal Article ; 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.2023.117559
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3815: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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