Repository of Institute of Technology of Nuclear and Other Mineral Raw Materials
RITNMS - Repository of Institute of Technology of Nuclear and Other Mineral Raw Materials
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   RITNMS
  • Institut za tehnologiju nuklearnih i drugih mineralnih sirovina
  • Radovi istraživača / Researchers’ publications
  • View Item
  •   RITNMS
  • Institut za tehnologiju nuklearnih i drugih mineralnih sirovina
  • Radovi istraživača / Researchers’ publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs)

No Thumbnail
Authors
Mihajlović, Marija
Mitrašinović, Petar M.
Article (Published version)
Metadata
Show full item record
Abstract
Using the crystal structures of inhibitors bound to either group-2 or group-1 neuraminidases (NAs), AScore/ShapeDock (GaDock) scoring was shown to identify the binding modes in agreement with the experiment for all inhibitors docked in their own NA/inhibitor crystal structures. To investigate the effect of small changes in protein structure on predicted binding modes, in a set of 132 docking experiments (11 inhibitors docked in 12 group-2 NA structures), AScore/ShapeDock (GaDock) identified the correct binding modes of 116 complexes. In a total of 88 docking experiments (8 inhibitors docked in 11 group-1 NA structures), AScore/ShapeDock predicted 80 binding modes correctly. Flexible AScore/ShapeDock docking, as quite reproducible, is suggested to be convenient for designing novel H5N1 inhibitors.
Keywords:
inhibitors / influenza virus neuraminidase / AScore / ArgusLab 4 / 0
Source:
Molecular Simulation, 2009, 35, 4, 311-324
Publisher:
  • Taylor & Francis Ltd, Abingdon
Funding / projects:
  • Biofizička istraživanja membranskih procesa: interakcija membranskih receptora i kanala sa spoljašnjim faktorima i intracelularna regulacija (RS-143016)

DOI: 10.1080/08927020802430752

ISSN: 0892-7022

WoS: 000264134600008

Scopus: 2-s2.0-68149157302
[ Google Scholar ]
29
25
URI
https://ritnms.itnms.ac.rs/handle/123456789/147
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Institut za tehnologiju nuklearnih i drugih mineralnih sirovina
TY  - JOUR
AU  - Mihajlović, Marija
AU  - Mitrašinović, Petar M.
PY  - 2009
UR  - https://ritnms.itnms.ac.rs/handle/123456789/147
AB  - Using the crystal structures of inhibitors bound to either group-2 or group-1 neuraminidases (NAs), AScore/ShapeDock (GaDock) scoring was shown to identify the binding modes in agreement with the experiment for all inhibitors docked in their own NA/inhibitor crystal structures. To investigate the effect of small changes in protein structure on predicted binding modes, in a set of 132 docking experiments (11 inhibitors docked in 12 group-2 NA structures), AScore/ShapeDock (GaDock) identified the correct binding modes of 116 complexes. In a total of 88 docking experiments (8 inhibitors docked in 11 group-1 NA structures), AScore/ShapeDock predicted 80 binding modes correctly. Flexible AScore/ShapeDock docking, as quite reproducible, is suggested to be convenient for designing novel H5N1 inhibitors.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Molecular Simulation
T1  - Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs)
EP  - 324
IS  - 4
SP  - 311
VL  - 35
DO  - 10.1080/08927020802430752
UR  - conv_556
ER  - 
@article{
author = "Mihajlović, Marija and Mitrašinović, Petar M.",
year = "2009",
abstract = "Using the crystal structures of inhibitors bound to either group-2 or group-1 neuraminidases (NAs), AScore/ShapeDock (GaDock) scoring was shown to identify the binding modes in agreement with the experiment for all inhibitors docked in their own NA/inhibitor crystal structures. To investigate the effect of small changes in protein structure on predicted binding modes, in a set of 132 docking experiments (11 inhibitors docked in 12 group-2 NA structures), AScore/ShapeDock (GaDock) identified the correct binding modes of 116 complexes. In a total of 88 docking experiments (8 inhibitors docked in 11 group-1 NA structures), AScore/ShapeDock predicted 80 binding modes correctly. Flexible AScore/ShapeDock docking, as quite reproducible, is suggested to be convenient for designing novel H5N1 inhibitors.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Molecular Simulation",
title = "Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs)",
pages = "324-311",
number = "4",
volume = "35",
doi = "10.1080/08927020802430752",
url = "conv_556"
}
Mihajlović, M.,& Mitrašinović, P. M.. (2009). Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs). in Molecular Simulation
Taylor & Francis Ltd, Abingdon., 35(4), 311-324.
https://doi.org/10.1080/08927020802430752
conv_556
Mihajlović M, Mitrašinović PM. Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs). in Molecular Simulation. 2009;35(4):311-324.
doi:10.1080/08927020802430752
conv_556 .
Mihajlović, Marija, Mitrašinović, Petar M., "Applications of the ArgusLab4/AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs)" in Molecular Simulation, 35, no. 4 (2009):311-324,
https://doi.org/10.1080/08927020802430752 .,
conv_556 .

DSpace software copyright © 2002-2015  DuraSpace
About the RITNMS repository | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceCommunitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About the RITNMS repository | Send Feedback

OpenAIRERCUB