PROLIX: Rapid Mining of Protein–Ligand Interactions in Large Crystal Structure Databases-Reference-Cited by-同舟云学术

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PROLIX: Rapid Mining of Protein–Ligand Interactions in Large Crystal Structure Databases

Published:2012-06-01 Issue:6 Volume:52 Page:1450-1461
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Weisel Martin¹,Bitter Hans-Marcus²,Diederich François³,So W. Venus⁴,Kondru Rama¹

Affiliation:

1. Discovery Chemistry, Hoffmann-La Roche, Inc., 340 Kingsland Street, Nutley, New Jersey 07110, United States

2. Translational Research Sciences, Hoffmann-La Roche, Inc., 340 Kingsland Street, Nutley, New Jersey 07110, United States

3. Laboratorium für Organische Chemie, ETH Zürich, Wolfgang-Pauli-Strasse 10, HCI, 8093 Zürich, Switzerland

4. Pharma Research & Early Development Informatics, Hoffmann-La Roche, Inc., 340 Kingsland Street, Nutley, New Jersey 07110, United States

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ci300034x

Reference49 articles.

1. High-throughput crystallography to enhance drug discovery

2. High-Throughput Nuclear Magnetic Resonance-Based Screening

3. The Protein Data Bank

4. Protein‐Ligand Interactions

5. A new test set for validating predictions of protein-ligand interaction

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2. Identification of Catechins’ Binding Sites in Monomeric Aβ42 through Ensemble Docking and MD Simulations;International Journal of Molecular Sciences;2023-05-03

3. fingeRNAt—A novel tool for high-throughput analysis of nucleic acid-ligand interactions;PLOS Computational Biology;2022-06-02

4. Identification of Catechins Binding Pockets in Monomeric Aβ₄₂ Through Ensemble Docking and MD Simulations;2022-02-10

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