Exploring resistance mechanisms of HCV NS3/4A protease mutations to MK5172: insight from molecular dynamics simulations and free energy calculations1. Issue 9 (11th September 2015)

Record Type:: Journal Article
Title:: Exploring resistance mechanisms of HCV NS3/4A protease mutations to MK5172: insight from molecular dynamics simulations and free energy calculations1. Issue 9 (11th September 2015)
Main Title:: Exploring resistance mechanisms of HCV NS3/4A protease mutations to MK5172: insight from molecular dynamics simulations and free energy calculations1
Authors:: Guan, Yan
Sun, Huiyong
Pan, Peichen
Li, Youyong
Li, Dan
Hou, Tingjun
Abstract:: <abstract abstract-type="toc"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <graphic position="anchor" id="ga" xlink:href="ark:/27927/pgj2fgbg33g" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" />Mutations at a number of key positions (Ala156, Asp168 and Arg155) of the HCV NS3/4A protease can induce medium to high resistance to MK5172.</p> </abstract>
Is Part Of:: Molecular bioSystems. Volume 11:Issue 9(2015:Sep.)
Journal:: Molecular bioSystems
Issue:: Volume 11:Issue 9(2015:Sep.)
Issue Display:: Volume 11, Issue 9 (2015)
Year:: 2015
Volume:: 11
Issue:: 9
Issue Sort Value:: 2015-0011-0009-0000
Page Start:: 2568
Page End:: 2578
Publication Date:: 2015-09-11
Subjects:: Molecular biology -- Periodicals
Biochemistry -- Periodicals
571.7405
Journal URLs:: http://www.rsc.org/Publishing/Journals/mb/index.asp ↗
http://www.rsc.org/ ↗
DOI:: 10.1039/c5mb00394f ↗
Languages:: English
ISSNs:: 1742-206X
Deposit Type:: Legaldeposit
View Content:: Available online (eLD content is only available in our Reading Rooms) ↗
Physical Locations:: British Library DSC - 5900.798350
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store
Ingest File:: 3207.xml