Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identify old drugs as selective bacterial β‐GUS inhibitors by structural‐based virtual screening and bio‐evaluations

13 Dec 2019

Abstract excerpt

Abstract Irinotecan (CPT‐11) is a cytotoxic drug that has wide applicability and usage in cancer treatment. Despite its success, patients suffer dose‐dependent diarrhea, limiting the drug's efficacy. No effective therapy is available for this unmet medical need. The bacterial β‐glucuronidase (β‐GUS) plays pivotal role in CPT‐11‐induced diarrhea (CID) via activating the non‐toxic SN‐38G to toxic SN‐38 inside...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cancer therapeutics and mechanisms
Share to Lung Cancer Research Studies
Share to Pneumonia and Respiratory Infections

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31834987
DOI: 10.1111/cbdd.13655

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identify old drugs as selective bacterial β‐GUS inhibitors by structural‐based virtual screening and bio‐evaluationsPMID 31834987Read ↗

Entropy-driven binding of gut bacterial β-glucuronidase inhibitors ameliorates irinotecan-induced toxicitySemantic proximity Read ↗

Inactivation of the antidiabetic drug acarbose by human intestinal microbial-mediated degradationSemantic proximity Read ↗

Amoxapine Demonstrates Incomplete Inhibition of β-Glucuronidase Activity from Human Gut MicrobiotaSemantic proximity Read ↗

Structural basis for the regulation of β-glucuronidase expression by human gut Enterobacteriaceae.Semantic proximity Read ↗

Targeting Regorafenib-Induced Toxicity through Inhibition of Gut Microbial β-GlucuronidasesSemantic proximity Read ↗

Discovery of α-Glucosidase Inhibitors from Paenibacillus sp. JNUCC 31 via Genome Mining, Metabolite Profiling, and In Silico AnalysisSemantic proximity Read ↗

Design, Synthesis, and Computational Analysis of 4-Amino-1,2,4-Triazol-3-one Schiff Base Derivatives as Potent α-Glucosidase InhibitorsSemantic proximity Read ↗

β-Glucocerebrosidase Modulators Promote Dimerization of β-Glucocerebrosidase and Reveal an Allosteric Binding Site.Semantic proximity Read ↗

Identification of pyrimidinyl piperazines as non-iminosugar glucocerebrosidase (GCase) pharmacological chaperones.Semantic proximity Read ↗

New insights into the pharmacological chaperone activity of c2-substituted glucoimidazoles for the treatment of Gaucher disease.Semantic proximity Read ↗

A bicyclic 1-deoxygalactonojirimycin derivative as a novel pharmacological chaperone for GM1 gangliosidosis.Semantic proximity Read ↗

Elucidation of the Gemcitabine Transporters of Escherichia coli K-12 and Gamma-Proteobacteria Linked to Gemcitabine-Related ChemoresistanceSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.