Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity (scientific article published on 13 December 2010)

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Q24286950

Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein

Q27639039

Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein

Q27730770

Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly

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Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors

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Genetic correlates of in vivo viral resistance to indinavir, a human immunodeficiency virus type 1 protease inhibitor

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Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors

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A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism

Q28469113

HIV-1 subtype B protease and reverse transcriptase amino acid covariation

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Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss

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In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector

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In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors

Q29620622

Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1.

Q35548279

HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity.

Q37447762

Amino acid insertions near Gag cleavage sites restore the otherwise compromised replication of human immunodeficiency virus type 1 variants resistant to protease inhibitors

Q37583389

Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease

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Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1.

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Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo.

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The role of lysine residue at amino acid position 165 of human immunodeficiency virus type 1 CRF01_AE Gag in reducing viral drug susceptibility to protease inhibitors.

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Amino acid substitutions in Gag protein at non-cleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors

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Gag mutations can impact virological response to dual-boosted protease inhibitor combinations in antiretroviral-naïve HIV-infected patients

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Full-length HIV-1 Gag determines protease inhibitor susceptibility within in vitro assays

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A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle

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Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1.

Q42546416

Ordered accumulation of mutations in HIV protease confers resistance to ritonavir

Q42555782

Protease inhibitor resistance analysis in the MONARK trial comparing first-line lopinavir-ritonavir monotherapy to lopinavir-ritonavir plus zidovudine and lamivudine triple therapy

Q43102710

In vivo gene transfer to the mouse eye using an HIV-based lentiviral vector; efficient long-term transduction of corneal endothelium and retinal pigment epithelium

Q43917989

Impact of amino acid variations in Gag and protease of HIV type 1 CRF01_AE strains on drug susceptibility of virus to protease inhibitors

Q45381734

Resistance of human immunodeficiency virus type 1 to protease inhibitors: selection of resistance mutations in the presence and absence of the drug.

Q45771435

British HIV Association guidelines for the treatment of HIV-1-infected adults with antiretroviral therapy 2008

Q57180178

Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy

Q73271748

P433

issue

P407

language of work or name

English

Q1860

P1104

number of pages

P304

page(s)

1106-1113

P577

publication date

2010-12-13

P1433

published in

Antimicrobial Agents and Chemotherapy

Q578004

P1476

title

Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity

P478

volume

Reverse relations

cites work (P2860)

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