Substitutions at Phe61 in the beta3-beta4 hairpin of HIV-1 reverse transcriptase reveal a role for the Fingers subdomain in strand displacement DNA synthesis (Q44260045)

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English	Substitutions at Phe61 in the beta3-beta4 hairpin of HIV-1 reverse transcriptase reveal a role for the Fingers subdomain in strand displacement DNA synthesis	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 December 2017

Substitutions at Phe61 in the beta3-beta4 hairpin of HIV-1 reverse transcriptase reveal a role for the Fingers subdomain in strand displacement DNA synthesis (English)

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Europe PubMed Central

PubMed publication ID

1 December 2017

Vinayaka R. Prasad

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Vinayaka R Prasad

3

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author name string

Timothy S Fisher

1

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Europe PubMed Central

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1 December 2017

Tom Darden

2

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Europe PubMed Central

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1 December 2017

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publication date

1 January 2003

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Europe PubMed Central

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1 December 2017

Journal of Molecular Biology

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Europe PubMed Central

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1 December 2017

325

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Europe PubMed Central

PubMed publication ID

1 December 2017

3

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Europe PubMed Central

PubMed publication ID

1 December 2017

443-459

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Europe PubMed Central

PubMed publication ID

1 December 2017

Linker insertion mutagenesis of the human immunodeficiency virus reverse transcriptase expressed in bacteria: definition of the minimal polymerase domain

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Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor

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Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA

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Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer

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Reduced frameshift fidelity and processivity of HIV-1 reverse transcriptase mutants containing alanine substitutions in helix H of the thumb subdomain.

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A minor groove binding track in reverse transcriptase

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Insertions into the β3-β4 Hairpin Loop of HIV-1 Reverse Transcriptase Reveal a Role for Fingers Subdomain in Processive Polymerization

1 reference

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The K65R mutation confers increased DNA polymerase processivity to HIV-1 reverse transcriptase

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New human immunodeficiency virus, type 1 reverse transcriptase (HIV-1 RT) mutants with increased fidelity of DNA synthesis. Accuracy, template binding, and processivity

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HIV-1 Reverse Transcription A Termination Step at the Center of the Genome

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HIV-1 genome nuclear import is mediated by a central DNA flap

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Mechanism of inhibition of the avian myeloblastosis virus deoxyribonucleic acid polymerase by adriamycin

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Characterization of RNA strand displacement synthesis by Moloney murine leukemia virus reverse transcriptase

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Substitutions of Phe61 located in the vicinity of template 5'-overhang influence polymerase fidelity and nucleoside analog sensitivity of HIV-1 reverse transcriptase

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Properties of strand displacement synthesis by Moloney murine leukemia virus reverse transcriptase: mechanistic implications

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Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism

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Mutated K65R recombinant reverse transcriptase of human immunodeficiency virus type 1 shows diminished chain termination in the presence of 2',3'-dideoxycytidine 5'-triphosphate and other drugs

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K65R mutation of human immunodeficiency virus type 1 reverse transcriptase encodes cross-resistance to 9-(2-phosphonylmethoxyethyl)adenine

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An expanded model of replicating human immunodeficiency virus reverse transcriptase

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Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes

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Insights into DNA polymerization mechanisms from structure and function analysis of HIV-1 reverse transcriptase

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Nucleotide-induced stable complex formation by HIV-1 reverse transcriptase

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Cross-linking of the fingers subdomain of human immunodeficiency virus type 1 reverse transcriptase to template-primer

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Compression of the DNA minor groove is responsible for termination of DNA synthesis by HIV-1 reverse transcriptase

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Structural alterations in the DNA ahead of the primer terminus during displacement synthesis by reverse transcriptases

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Mechanisms of helicase-catalyzed DNA unwinding

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Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA

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Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

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Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7

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The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Identifiers

10.1016/S0022-2836(02)01225-1

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

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