Yasien Sayed

Prof. Yasien Sayed

orcid

Research Focus & Metrics

Academic Career Length

24Years (2003-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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15 November 2008 in Journal of Virology
Verified
Journal Article
Closed access
SMSalerwe Mosebi
Salerwe Mosebi
LMLynn Morris
Lynn Morris
HDHeini W. Dirr
Heini W. Dirr
Yasien SayedYasien Sayed
Yasien Sayed
Human immunodeficiency virus (HIV) infections in sub-Saharan Africa represent about 56% of global infections. Study of active-site mutations (the V82A single mutation and the V82F I84V double mutation) in the less-studied South African HIV type 1 subtype C (C-SA) protease indicated that neither mutation had a significant impact on the proteolytic functioning of the protease. However, the binding affinities of, and inhibition by, saquinavir, ritonavir, indinavir, and nelfinavir were weaker for each variant than for the wild-type protease, with the double mutant exhibiting the most dramatic change. Therefore, our results show that the C-SA V82F I84V double mutation decreased the binding affinities of protease inhibitors to levels significantly lower than that required for effective inhibition.

1 December 2013 in Journal of Biomolecular Structure and Dynamics
Verified
Journal Article
Closed access
PNPrevin Naicker
Previn Naicker
IAIkechukwu Achilonu
Ikechukwu Achilonu
SFSylvia Fanucchi
Sylvia Fanucchi
MFManuel Fernandes
Manuel Fernandes
Mahmoud A. A. IbrahimMahmoud A. A. Ibrahim
Mahmoud A. A. Ibrahim
Yasien SayedYasien Sayed
Yasien Sayed
The HIV protease plays a major role in the life cycle of the virus and has long been a target in antiviral therapy. Resistance of HIV protease to protease inhibitors (PIs) is problematic for the effective treatment of HIV infection. The South African HIV-1 subtype C protease (C-SA PR), which contains eight polymorphisms relative to the consensus HIV-1 subtype B protease, was expressed in Escherichia coli, purified, and crystallized. The crystal structure of the C-SA PR was resolved at 2.7 Å, which is the first crystal structure of a HIV-1 subtype C protease that predominates in Africa. Structural analyses of the C-SA PR in comparison to HIV-1 subtype B proteases indicated that polymorphisms at position 36 of the homodimeric HIV-1 protease may impact on the stability of the hinge region of the protease, and hence the dynamics of the flap region. Molecular dynamics simulations showed that the flap region of the C-SA PR displays a wider range of movements over time as compared to the subtype B proteases. Reduced stability in the hinge region resulting from the absent E35-R57 salt bridge in the C-SA PR, most likely contributes to the increased flexibility of the flaps which may be associated with reduced susceptibility to PIs. An animated interactive 3D complement (I3DC) is available in Proteopedia at http://proteopedia.org/w/Journal:JBSD:36

29 January 2016 in Chemical Biology & Drug Design
Verified
Journal Article
Closed access
PDF file
HLHusain A. Lockhat
Husain A. Lockhat
José Rogério A. SilvaJosé Rogério A. Silva
José Rogério A. Silva
CAClaudio Alves
Claudio Alves
TGThavendran Govender
Thavendran Govender
JLJeronimo Lameira
Jeronimo Lameira
Gerhardus - Gert Hendrik KrugerGerhardus - Gert Hendrik Kruger
Gerhardus - Gert Hendrik Kruger

1 June 2018 in Journal of Molecular Graphics and Modelling
Verified
Journal Article
Closed access
JZJake Zondagh
Jake Zondagh
VBVijayakumar Balakrishnan
Vijayakumar Balakrishnan
IAIkechukwu Achilonu
Ikechukwu Achilonu
HDHeini W. Dirr
Heini W. Dirr
Yasien SayedYasien Sayed
Yasien Sayed


6 November 2003
Verified
Journal Article
Closed access
AVAdrian Velazquez-Campoy
Adrian Velazquez-Campoy
SVSonia Vega
Sonia Vega
EFErin Fleming
Erin Fleming
UBUsman Bacha
Usman Bacha
Yasien SayedYasien Sayed
Yasien Sayed
EFErnesto Freire
Ernesto Freire